ID 2B11_HUMAN Reviewed; 266 AA. AC P04229; A4F5N0; A8K098; O62869; P13758; Q06662; Q30116; Q30117; AC Q5Y7E9; Q7M2H4; Q95461; Q9BCL7; Q9GIK5; Q9MXZ0; Q9MXZ5; Q9TQ91; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 12-SEP-2018, entry version 179. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-1 beta chain; DE AltName: Full=MHC class II antigen DRB1*1; DE Short=DR-1; DE Short=DR1; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01). RX PubMed=2998758; RA Tonnelle C., Demars R., Long E.O.; RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of RT expression."; RL EMBO J. 4:2839-2847(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:01). RX PubMed=3858829; DOI=10.1073/pnas.82.10.3405; RA Bell J.I., Estess P., St John T., Saiki R., Watling D.L., Erlich H.A., RA McDevitt H.O.; RT "DNA sequence and characterization of human class II major RT histocompatibility complex beta chains from the DR1 haplotype."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3405-3409(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*01:03). RX PubMed=1688595; RA Coppin H.L., Avoustin P., Fabron J., Huchenq A., Garnier J.-M., RA Thomsen M., De Preval C.; RT "Evolution of the HLA-DR1 gene family. Structural and functional RT analysis of the new allele 'DR-BON'."; RL J. Immunol. 144:984-989(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*01:01), AND VARIANT RP ARG-262. RX PubMed=17345114; DOI=10.1007/s00251-007-0196-8; RA von Salome J., Gyllensten U., Bergstroem T.F.; RT "Full-length sequence analysis of the HLA-DRB1 locus suggests a recent RT origin of alleles."; RL Immunogenetics 59:261-271(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29. RC TISSUE=B-cell; RX PubMed=8462990; DOI=10.1007/BF00216386; RA Louis P., Eliaou J.F., Kerlan-Candon S., Pinet V., Vincent R., RA Clot J.; RT "Polymorphism in the regulatory region of HLA-DRB genes correlating RT with haplotype evolution."; RL Immunogenetics 38:21-26(1993). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*01:04). RA Middleton D., Versluis L.F., Tilanus M.G.J.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [9] RP PROTEIN SEQUENCE OF 30-64. RC TISSUE=B-cell; RX PubMed=6600932; DOI=10.1021/bi00270a027; RA Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J., RA Reisfeld R.A.; RT "N-terminal amino acid sequences of the alpha and beta chains of HLA- RT DR1 and HLA-DR2 antigens."; RL Biochemistry 22:185-188(1983). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:06). RX PubMed=10203026; DOI=10.1034/j.1399-0039.1999.530313.x; RA Palou E., Mongay L., Arias M.T., Isart F., Suarez B., Masso M., RA Fabregat V., Martorell J., Gaya A.; RT "Identification of a novel DRB1-allele (DRB1*0106) by sequence-based RT typing."; RL Tissue Antigens 53:308-310(1999). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07). RX PubMed=12753659; DOI=10.1034/j.1399-0039.2003.00034.x; RA Voorter C.E.M., Hepkema B.G., Lems S.P.M., van den Berg-Loonen E.M.; RT "Identification of three new DRB1 alleles, DRB1*0107, *0425 and *13012 RT and confirmation of DRB4*01033."; RL Tissue Antigens 61:398-402(2003). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:05). RA Kashiwase K., Akaza T., Juji T.; RT "HLA-DRB1 new alleles."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*01:07). RA Dormoy A., Froelich N., Leisenbach R., Tongio M.M.; RT "A new HLA-DRB1*01 allele."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*01:02). RC TISSUE=Blood; RA Hashemi S., Couture C., Cole R., Buyse I.; RT "Identification and sequencing of a novel DRB1*01 allele."; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-266 (ALLELE DRB1*01:02). RX PubMed=2453563; RA Hurley C.K., Ziff B.L., Silver J., Gregersen P.K., Hartzman R., RA Johnson A.H.; RT "Polymorphism of the HLA-DR1 haplotype in American blacks. RT Identification of a DR1 beta-chain determinant recognized in the mixed RT lymphocyte reaction."; RL J. Immunol. 140:4019-4023(1988). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (ALLELES DRB1*01:01 AND RP DRB1*01:02). RC TISSUE=Blood; RA Arnaiz-Villena A.; RT "HLA class II polymorphism."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [17] RP DISEASE. RX PubMed=14508706; DOI=10.1086/378097; RA Rossman M.D., Thompson B., Frederick M., Maliarik M., Iannuzzi M.C., RA Rybicki B.A., Pandey J.P., Newman L.S., Magira E., Beznik-Cizman B., RA Monos D.; RT "HLA-DRB1*1101: a significant risk factor for sarcoidosis in blacks RT and whites."; RL Am. J. Hum. Genet. 73:720-735(2003). RN [18] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [19] RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH EPSTEIN-BARR RP VIRUS GP42 PROTEIN. RX PubMed=9151859; RA Li Q., Spriggs M.K., Kovats S., Turk S.M., Comeau M.R., Nepom B., RA Hutt-Fletcher L.M.; RT "Epstein-Barr virus uses HLA class II as a cofactor for infection of B RT lymphocytes."; RL J. Virol. 71:4657-4662(1997). RN [20] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [21] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [22] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [23] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [24] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [25] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [26] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219. RX PubMed=8316295; DOI=10.1038/364033a0; RA Brown J.H., Jardetzky T.S., Gorga J.C., Stern L.J., Urban R.G., RA Strominger J.L., Wiley D.C.; RT "Three-dimensional structure of the human class II histocompatibility RT antigen HLA-DR1."; RL Nature 364:33-39(1993). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 32-219. RX PubMed=8145819; DOI=10.1038/368215a0; RA Stern L.J., Brown J.H., Jardetzky T.J., Gorga J.C., Urban R.G., RA Strominger J.L., Wiley D.C.; RT "Crystal structure of the human class II MHC protein HLA-DR1 complexed RT with an influenza virus peptide."; RL Nature 368:215-221(1994). RN [29] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH SEB. RX PubMed=8152483; DOI=10.1038/368711a0; RA Jardetzky T.S., Brown J.H., Gorga J.C., Stern L.J., Urban R.G., RA Chi Y.I., Stauffacher C., Strominger J.L., Wiley D.C.; RT "Three-dimensional structure of a human class II histocompatibility RT molecule complexed with superantigen."; RL Nature 368:711-718(1994). RN [30] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 28-207 IN COMPLEX WITH RP EPSTEIN-BARR VIRUS BZLF2/GP42, AND FUNCTION (MICROBIAL INFECTION). RX PubMed=11864610; DOI=10.1016/S1097-2765(02)00465-3; RA Mullen M.M., Haan K.M., Longnecker R., Jardetzky T.S.; RT "Structure of the Epstein-Barr virus gp42 protein bound to the MHC RT class II receptor HLA-DR1."; RL Mol. Cell 9:375-385(2002). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- FUNCTION: (Microbial infection) Acts as a receptor for Epstein- CC Barr virus on lymphocytes. {ECO:0000269|PubMed:11864610, CC ECO:0000269|PubMed:9151859}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBUNIT: (Microbial infection) Interacts with Epstein-Barr virus CC gp42 protein (PubMed:11864610, PubMed:9151859). CC {ECO:0000269|PubMed:11864610, ECO:0000269|PubMed:9151859}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-1 are known: CC DRB1*01:01; DRB1*01:02; DRB1*01:03; DRB1*01:04; DRB1*01:05; CC DRB1*01:06; DRB1*01:07; DRB1*01:08; DRB1*01:09; DRB1*01:10; CC DRB1*01:11; DRB1*01:12; DRB1*01:13; DRB1*01:14; DRB1*01:15; CC DRB1*01:16; DRB1*01:17; DRB1*01:18; DRB1*01:19; DRB1*01:20 and CC DRB1*01:21. The sequence shown is that of DRB1*01:01. CC -!- DISEASE: Sarcoidosis 1 (SS1) [MIM:181000]: An idiopathic, CC systemic, inflammatory disease characterized by the formation of CC immune granulomas in involved organs. Granulomas predominantly CC invade the lungs and the lymphatic system, but also skin, liver, CC spleen, eyes and other organs may be involved. Note=Disease CC susceptibility is associated with variations affecting the gene CC represented in this entry. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X03069; CAA26873.1; -; mRNA. DR EMBL; M11161; AAA59781.1; -; mRNA. DR EMBL; M33600; AAA59782.1; -; mRNA. DR EMBL; AY663400; AAU87993.1; -; Genomic_DNA. DR EMBL; AM419948; CAL99240.1; -; Genomic_DNA. DR EMBL; AK289463; BAF82152.1; -; mRNA. DR EMBL; X64547; CAA45845.1; -; Genomic_DNA. DR EMBL; X99896; CAA68171.1; -; mRNA. DR EMBL; AF089723; AAD51131.1; -; Genomic_DNA. DR EMBL; AJ276206; CAC27123.1; -; Genomic_DNA. DR EMBL; AB015184; BAA28761.1; -; Genomic_DNA. DR EMBL; AJ303118; CAC19693.1; -; Genomic_DNA. DR EMBL; Z50871; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M21008; AAA59780.1; -; mRNA. DR EMBL; AF029288; AAF65497.1; -; Genomic_DNA. DR EMBL; AF029293; AAF65502.1; -; Genomic_DNA. DR PIR; A19197; A19197. DR PIR; D24669; HLHU1B. DR PIR; I56072; I56072. DR PIR; PH0147; PH0147. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 1AQD; X-ray; 2.45 A; B/E/H/K=30-227. DR PDB; 1DLH; X-ray; 2.80 A; B/E=32-219. DR PDB; 1FYT; X-ray; 2.60 A; B=30-221. DR PDB; 1HXY; X-ray; 2.60 A; B=30-219. DR PDB; 1JWM; X-ray; 2.70 A; B=30-219. DR PDB; 1JWS; X-ray; 2.60 A; B=30-219. DR PDB; 1JWU; X-ray; 2.30 A; B=30-219. DR PDB; 1KG0; X-ray; 2.65 A; B=32-219. DR PDB; 1KLG; X-ray; 2.40 A; B=30-219. DR PDB; 1KLU; X-ray; 1.93 A; B=30-219. DR PDB; 1LO5; X-ray; 3.20 A; B=30-219. DR PDB; 1PYW; X-ray; 2.10 A; B=30-219. DR PDB; 1R5I; X-ray; 2.60 A; B/F=30-219. DR PDB; 1SEB; X-ray; 2.70 A; B/F=30-221. DR PDB; 1SJE; X-ray; 2.45 A; B=30-219. DR PDB; 1SJH; X-ray; 2.25 A; B=30-219. DR PDB; 1T5W; X-ray; 2.40 A; B/E=30-219. DR PDB; 1T5X; X-ray; 2.50 A; B=30-219. DR PDB; 2FSE; X-ray; 3.10 A; B/D=33-219. DR PDB; 2G9H; X-ray; 2.00 A; B=30-219. DR PDB; 2IAM; X-ray; 2.80 A; B=30-219. DR PDB; 2IAN; X-ray; 2.80 A; B/G/L/Q=30-219. DR PDB; 2ICW; X-ray; 2.41 A; B/E=30-219. DR PDB; 2IPK; X-ray; 2.30 A; B=30-219. DR PDB; 2OJE; X-ray; 3.00 A; B/F=30-219. DR PDB; 2XN9; X-ray; 2.30 A; E=30-219. DR PDB; 3L6F; X-ray; 2.10 A; B=30-221. DR PDB; 3PDO; X-ray; 1.95 A; B=30-227. DR PDB; 3PGC; X-ray; 2.66 A; B/E=30-227. DR PDB; 3PGD; X-ray; 2.72 A; B/E=30-227. DR PDB; 3QXA; X-ray; 2.71 A; B/E=30-219. DR PDB; 3QXD; X-ray; 2.30 A; B/E=30-219. DR PDB; 3S4S; X-ray; 2.40 A; B/E=30-221. DR PDB; 3S5L; X-ray; 2.10 A; B/E=30-221. DR PDB; 4AEN; X-ray; 2.20 A; B=30-227. DR PDB; 4AH2; X-ray; 2.36 A; B=30-227. DR PDB; 4C56; X-ray; 2.90 A; E/K=30-219. DR PDB; 4E41; X-ray; 2.60 A; B/G=30-219. DR PDB; 4FQX; X-ray; 2.60 A; B=30-221. DR PDB; 4GBX; X-ray; 3.00 A; B=30-220. DR PDB; 4I5B; X-ray; 2.12 A; B/E=31-222. DR PDB; 4OV5; X-ray; 2.20 A; B/E/H/K/N/Q=30-219. DR PDB; 4X5W; X-ray; 1.34 A; B=30-227. DR PDB; 4X5X; X-ray; 3.20 A; B/D=30-227. DR PDB; 6CQJ; X-ray; 2.75 A; B/E/H=31-219. DR PDB; 6CQR; X-ray; 3.04 A; B/G=30-219. DR PDBsum; 1AQD; -. DR PDBsum; 1DLH; -. DR PDBsum; 1FYT; -. DR PDBsum; 1HXY; -. DR PDBsum; 1JWM; -. DR PDBsum; 1JWS; -. DR PDBsum; 1JWU; -. DR PDBsum; 1KG0; -. DR PDBsum; 1KLG; -. DR PDBsum; 1KLU; -. DR PDBsum; 1LO5; -. DR PDBsum; 1PYW; -. DR PDBsum; 1R5I; -. DR PDBsum; 1SEB; -. DR PDBsum; 1SJE; -. DR PDBsum; 1SJH; -. DR PDBsum; 1T5W; -. DR PDBsum; 1T5X; -. DR PDBsum; 2FSE; -. DR PDBsum; 2G9H; -. DR PDBsum; 2IAM; -. DR PDBsum; 2IAN; -. DR PDBsum; 2ICW; -. DR PDBsum; 2IPK; -. DR PDBsum; 2OJE; -. DR PDBsum; 2XN9; -. DR PDBsum; 3L6F; -. DR PDBsum; 3PDO; -. DR PDBsum; 3PGC; -. DR PDBsum; 3PGD; -. DR PDBsum; 3QXA; -. DR PDBsum; 3QXD; -. DR PDBsum; 3S4S; -. DR PDBsum; 3S5L; -. DR PDBsum; 4AEN; -. DR PDBsum; 4AH2; -. DR PDBsum; 4C56; -. DR PDBsum; 4E41; -. DR PDBsum; 4FQX; -. DR PDBsum; 4GBX; -. DR PDBsum; 4I5B; -. DR PDBsum; 4OV5; -. DR PDBsum; 4X5W; -. DR PDBsum; 4X5X; -. DR PDBsum; 6CQJ; -. DR PDBsum; 6CQR; -. DR ProteinModelPortal; P04229; -. DR SMR; P04229; -. DR DIP; DIP-6143N; -. DR IntAct; P04229; 7. DR MINT; P04229; -. DR BindingDB; P04229; -. DR ChEMBL; CHEMBL1943; -. DR DrugBank; DB05259; Glatiramer Acetate. DR iPTMnet; P04229; -. DR PhosphoSitePlus; P04229; -. DR SwissPalm; P04229; -. DR DMDM; 34395916; -. DR PeptideAtlas; P04229; -. DR PRIDE; P04229; -. DR Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126. DR DisGeNET; 3123; -. DR EuPathDB; HostDB:ENSG00000196126.10; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; CAB015400; -. DR HPA; CAB034021; -. DR HPA; HPA043151; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR MIM; 181000; phenotype. DR neXtProt; NX_P04229; -. DR Orphanet; 703; Bullous pemphigoid. DR Orphanet; 555; Celiac disease. DR Orphanet; 243377; Diabetes mellitus type 1. DR Orphanet; 220393; Diffuse cutaneous systemic sclerosis. DR Orphanet; 545; Follicular lymphoma. DR Orphanet; 220402; Limited cutaneous systemic sclerosis. DR Orphanet; 220407; Limited systemic sclerosis. DR Orphanet; 802; Multiple sclerosis. DR Orphanet; 83465; Narcolepsy without cataplexy. DR Orphanet; 2073; Narcolepsy-cataplexy. DR Orphanet; 284130; Rheumatoid arthritis. DR Orphanet; 797; Sarcoidosis. DR Orphanet; 536; Systemic lupus erythematosus. DR HOVERGEN; HBG012730; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR EvolutionaryTrace; P04229; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000196126; Expressed in 94 organ(s), highest expression level in spleen. DR CleanEx; HS_HLA-DRB1; -. DR ExpressionAtlas; P04229; baseline and differential. DR Genevisible; P04229; HS. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB. DR GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB. DR GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Endosome; Glycoprotein; Golgi apparatus; KW Host cell receptor for virus entry; Host-virus interaction; Immunity; KW Lysosome; Membrane; MHC II; Polymorphism; Receptor; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 {ECO:0000269|PubMed:6600932}. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-1 beta chain. FT /FTId=PRO_0000018949. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 5 5 K -> R (in dbSNP:rs707953). FT /FTId=VAR_056527. FT VARIANT 29 29 A -> S (in dbSNP:rs9270299). FT /FTId=VAR_033378. FT VARIANT 33 33 R -> Q (in dbSNP:rs1141741). FT /FTId=VAR_033380. FT VARIANT 39 39 Q -> E (in allele DRB1*01:07). FT /FTId=VAR_016740. FT VARIANT 66 66 S -> Y (in dbSNP:rs16822820). FT /FTId=VAR_033381. FT VARIANT 74 74 G -> R (in allele DRB1*01:05). FT /FTId=VAR_016741. FT VARIANT 89 89 Y -> S (in dbSNP:rs1059586). FT /FTId=VAR_033383. FT VARIANT 96 96 L -> I (in allele DRB1*01:03). FT /FTId=VAR_016710. FT VARIANT 99 99 Q -> D (in allele DRB1*01:03; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016711. FT VARIANT 99 99 Q -> E (in dbSNP:rs17881965). FT /FTId=VAR_033384. FT VARIANT 99 99 Q -> H (in dbSNP:rs17879599). FT /FTId=VAR_033385. FT VARIANT 100 100 R -> A (in allele DRB1*01:06; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016742. FT VARIANT 100 100 R -> E (in allele DRB1*01:03; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016712. FT VARIANT 102 102 A -> G (in dbSNP:rs17878857). FT /FTId=VAR_033386. FT VARIANT 103 103 A -> E (in dbSNP:rs16822805). FT /FTId=VAR_033387. FT VARIANT 106 106 T -> N (in allele DRB1*01:04). FT /FTId=VAR_016713. FT VARIANT 107 107 Y -> H (in dbSNP:rs16822512). FT /FTId=VAR_033388. FT VARIANT 114 114 V -> A (in allele DRB1*01:02; FT dbSNP:rs17424145). FT /FTId=VAR_016714. FT VARIANT 115 115 G -> V (in allele DRB1*01:02, allele FT DRB1*01:04 and allele DRB1*01:06). FT /FTId=VAR_016715. FT VARIANT 164 164 G -> D (in dbSNP:rs1059633). FT /FTId=VAR_033389. FT VARIANT 171 171 V -> M (in dbSNP:rs701829). FT /FTId=VAR_033391. FT VARIANT 195 195 R -> Q (in dbSNP:rs3205588). FT /FTId=VAR_033393. FT VARIANT 253 253 Q -> E (in allele DRB1*01:02). FT /FTId=VAR_016716. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT {ECO:0000269|PubMed:17345114}. FT /FTId=VAR_056528. FT CONFLICT 25 25 P -> R (in Ref. 2; AAA59781). FT {ECO:0000305}. FT CONFLICT 36 36 F -> S (in Ref. 9; AA sequence). FT {ECO:0000305}. FT CONFLICT 58 59 RC -> LF (in Ref. 9; AA sequence). FT {ECO:0000305}. FT CONFLICT 80 80 T -> E (in Ref. 2; AAA59781). FT {ECO:0000305}. FT CONFLICT 100 103 RRAA -> KRGQ (in Ref. 2; AAA59781). FT {ECO:0000305}. FT CONFLICT 192 192 T -> I (in Ref. 2; AAA59781). FT {ECO:0000305}. FT STRAND 36 47 {ECO:0000244|PDB:4X5W}. FT TURN 48 51 {ECO:0000244|PDB:4X5W}. FT STRAND 52 61 {ECO:0000244|PDB:4X5W}. FT STRAND 64 70 {ECO:0000244|PDB:4X5W}. FT TURN 71 73 {ECO:0000244|PDB:4X5W}. FT STRAND 75 80 {ECO:0000244|PDB:4X5W}. FT HELIX 81 83 {ECO:0000244|PDB:4X5W}. FT HELIX 84 91 {ECO:0000244|PDB:4X5W}. FT HELIX 94 106 {ECO:0000244|PDB:4X5W}. FT HELIX 108 115 {ECO:0000244|PDB:4X5W}. FT HELIX 116 118 {ECO:0000244|PDB:4X5W}. FT TURN 119 121 {ECO:0000244|PDB:4X5W}. FT STRAND 127 132 {ECO:0000244|PDB:4X5W}. FT STRAND 135 139 {ECO:0000244|PDB:3PDO}. FT STRAND 144 154 {ECO:0000244|PDB:4X5W}. FT STRAND 157 162 {ECO:0000244|PDB:4X5W}. FT STRAND 165 167 {ECO:0000244|PDB:4X5W}. FT STRAND 171 173 {ECO:0000244|PDB:4X5W}. FT STRAND 180 182 {ECO:0000244|PDB:4X5W}. FT STRAND 184 190 {ECO:0000244|PDB:4X5W}. FT STRAND 199 205 {ECO:0000244|PDB:4X5W}. FT STRAND 213 218 {ECO:0000244|PDB:4X5W}. SQ SEQUENCE 266 AA; 29914 MW; CC9CC7E2D0DD036C CRC64; MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQL KFECHFFNGT ERVRLLERCI YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQR RAAVDTYCRH NYGVGESFTV QRRVEPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B13_HUMAN Reviewed; 266 AA. AC P01912; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 12-SEP-2018, entry version 166. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-3 chain; DE AltName: Full=Clone P2-beta-3; DE AltName: Full=MHC class II antigen DRB1*3; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*03:01). RX PubMed=6589154; RA Peterson P.A., Gustafsson K., Wiman K.G., Emmoth E., Larhammar D., RA Boehme J., Hyldig-Nielsen J.J., Ronne H., Rask L.; RT "Mutations and selection in the generation of class II RT histocompatibility antigen polymorphism."; RL EMBO J. 3:1655-1660(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*03:01). RX PubMed=6415003; DOI=10.1016/0198-8859(83)90087-3; RA Larhammar D., Andersson G., Andersson M., Bill P., Boehme J., RA Claesson L., Denaro M., Emmoth E., Gustafsson K., Hammarling U., RA Heldin E., Hyldig-Nielsen J.-J., Lind P., Schenning L., Servenius B., RA Widmark E., Rask L., Peterson P.A.; RT "Molecular analysis of human class II transplantation antigens and RT their genes."; RL Hum. Immunol. 8:95-103(1983). RN [3] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [4] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [5] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [6] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [7] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [8] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [9] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 34-220 OF HLA-DRA/HLA-DRB1 RP HETERODIMER IN COMPLEX WITH CD74 PEPTIDE (CLIP), SUBUNIT, AND RP DISULFIDE BONDS. RX PubMed=7477400; DOI=10.1038/378457a0; RA Ghosh P., Amaya M., Mellins E., Wiley D.C.; RT "The structure of an intermediate in class II MHC maturation: CLIP RT bound to HLA-DR3."; RL Nature 378:457-462(1995). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC {ECO:0000269|PubMed:7477400}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-3 are known: CC DRB1*03:01; DRB1*03:02; DRB1*03:03; DRB1*03:04; DRB1*03:05; CC DRB1*03:06; DRB1*03:07; DRB1*03:08; DRB1*03:09; DRB1*03:10; CC DRB1*03:11; DRB1*03:12; DRB1*03:13; DRB1*03:14; DRB1*03:15; CC DRB1*03:16; DRB1*03:17; DRB1*03:18; DRB1*03:19; DRB1*03:20; CC DRB1*03:21; DRB1*03:22; DRB1*03:23; DRB1*03:24; DRB1*03:25; CC DRB1*03:26; DRB1*03:27; DRB1*03:28; DRB1*03:29; DRB1*03:30; CC DRB1*03:31; DRB1*03:32; DRB1*03:33; DRB1*03:34; DRB1*03:35; CC DRB1*03:36; DRB1*03:37; DRB1*03:38; DRB1*03:39; DRB1*03:40 and CC DRB1*03:41. The sequence shown is that of DRB1*03:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X00699; CAA25295.1; -; mRNA. DR PIR; I37546; HLHU3D. DR RefSeq; NP_001230894.1; NM_001243965.1. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 1A6A; X-ray; 2.75 A; B=34-220. DR PDBsum; 1A6A; -. DR ProteinModelPortal; P01912; -. DR SMR; P01912; -. DR BioGrid; 109368; 39. DR DIP; DIP-6064N; -. DR IntAct; P01912; 8. DR MINT; P01912; -. DR ChEMBL; CHEMBL3988561; -. DR iPTMnet; P01912; -. DR DMDM; 1708116; -. DR PeptideAtlas; P01912; -. DR PRIDE; P01912; -. DR DNASU; 3123; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR GeneID; 3123; -. DR KEGG; hsa:3123; -. DR CTD; 3123; -. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_P01912; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR PhylomeDB; P01912; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SIGNOR; P01912; -. DR ChiTaRS; HLA-DRB1; human. DR EvolutionaryTrace; P01912; -. DR GenomeRNAi; 3123; -. DR Proteomes; UP000005640; Chromosome 6. DR CleanEx; HS_HLA-DRB1; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; IDA:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-3 chain. FT /FTId=PRO_0000018965. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 123 Beta-1. FT REGION 124 217 Beta-2. FT REGION 218 227 Connecting peptide. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:7477400}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:7477400}. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P20039}. FT VARIANT 55 55 Y -> F (in dbSNP:rs1059569). FT /FTId=VAR_050371. FT VARIANT 106 106 N -> T (in dbSNP:rs9269941). FT /FTId=VAR_050372. FT VARIANT 164 164 G -> S (in dbSNP:rs1059633). FT /FTId=VAR_050373. FT STRAND 37 47 {ECO:0000244|PDB:1A6A}. FT TURN 48 51 {ECO:0000244|PDB:1A6A}. FT STRAND 52 61 {ECO:0000244|PDB:1A6A}. FT STRAND 64 70 {ECO:0000244|PDB:1A6A}. FT TURN 71 73 {ECO:0000244|PDB:1A6A}. FT STRAND 75 80 {ECO:0000244|PDB:1A6A}. FT HELIX 81 83 {ECO:0000244|PDB:1A6A}. FT HELIX 84 92 {ECO:0000244|PDB:1A6A}. FT HELIX 94 101 {ECO:0000244|PDB:1A6A}. FT HELIX 103 106 {ECO:0000244|PDB:1A6A}. FT HELIX 108 115 {ECO:0000244|PDB:1A6A}. FT TURN 116 121 {ECO:0000244|PDB:1A6A}. FT STRAND 127 134 {ECO:0000244|PDB:1A6A}. FT STRAND 138 140 {ECO:0000244|PDB:1A6A}. FT STRAND 143 150 {ECO:0000244|PDB:1A6A}. FT STRAND 152 154 {ECO:0000244|PDB:1A6A}. FT STRAND 157 162 {ECO:0000244|PDB:1A6A}. FT STRAND 180 182 {ECO:0000244|PDB:1A6A}. FT STRAND 184 187 {ECO:0000244|PDB:1A6A}. FT STRAND 189 191 {ECO:0000244|PDB:1A6A}. FT STRAND 199 205 {ECO:0000244|PDB:1A6A}. FT STRAND 213 218 {ECO:0000244|PDB:1A6A}. SQ SEQUENCE 266 AA; 30120 MW; 37329B097C6BEEB4 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRYLDRYF HNQEENVRFD SDVGEFRAVT ELGRPDAEYW NSQKDLLEQK RGRVDNYCRH NYGVVESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B14_HUMAN Reviewed; 266 AA. AC P13760; O19717; O19739; P13759; Q29875; Q30145; Q9GIX9; Q9GIY4; AC Q9MY13; Q9XRY5; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 12-SEP-2018, entry version 176. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-4 beta chain; DE AltName: Full=MHC class II antigen DRB1*4; DE Short=DR-4; DE Short=DR4; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*04:01). RX PubMed=3036826; RA Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., RA Rask L.; RT "Class II genes of the human major histocompatibility complex. RT Organization and evolutionary relationship of the DR beta genes."; RL J. Biol. Chem. 262:8748-8758(1987). RN [2] RP ERRATUM, AND SEQUENCE REVISION. RA Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., RA Rask L.; RL J. Biol. Chem. 263:8551-8551(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*04:01). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*04:01). RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:01). RX PubMed=3860851; DOI=10.1073/pnas.82.15.5165; RA Spies T., Sorrentino R., Boss J.M., Okada K., Strominger J.L.; RT "Structural organization of the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 82:5165-5169(1985). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:01). RX PubMed=9098937; DOI=10.1111/j.1399-0039.1997.tb02751.x; RA Thonnard J., Gervais T., Heusterpreute M., Mersch G., De Canck I., RA De Greef C., Demanet C., Van Waeyenberge C.; RT "A new silent mutation at codon 35 in exon 2 yielding a DRB1*04012 RT allele."; RL Tissue Antigens 49:274-276(1997). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:02). RX PubMed=12358860; DOI=10.1046/j.1365-2370.2002.00354.x; RA Ramon D., Corell A., Cox S.T., Soteriou B., Madrigal J.A., RA Marsh S.G.E.; RT "Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041 RT alleles."; RL Eur. J. Immunogenet. 29:453-455(2002). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-115 (ALLELE DRB1*04:03). RC TISSUE=Blood; RA Arnaiz-Villena A.; RT "HLA class II polymorphism."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-122 (ALLELE DRB1*04:03). RA Greville W.D., van Eijck A., Dunckley H.; RT "New HLA class II (DRB1) alleles detected by sequencing-based RT typing."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*04:03). RA Guttridge M.G., Hammond L.; RT "Confirmatory sequence of HLA-DRB1*04032."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:04). RX PubMed=3875800; DOI=10.1038/317166a0; RA Cairns J.S., Curtsinger J.M., Dahl C.A., Freeman S., Alter B.J., RA Bach F.H.; RT "Sequence polymorphism of HLA DR beta 1 alleles relating to T-cell- RT recognized determinants."; RL Nature 317:166-168(1985). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-123 (ALLELE DRB1*04:04). RX PubMed=3458223; DOI=10.1073/pnas.83.8.2642; RA Gregersen P.K., Shen M., Song Q.-L., Merryman P., Degar S., Seki T., RA Maccari J., Goldberg D., Murphy H., Schwenzer J., Wang C.Y., RA Winchester R.J., Nepom G.T., Silver J.; RT "Molecular diversity of HLA-DR4 haplotypes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2642-2646(1986). RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*04:11). RA Zhao W., Fernandez-Vina M.A., Stastny P.; RT "Full cDNA sequence of HLA-DRB1*0411."; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [14] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [15] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [16] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [17] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [18] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [19] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [20] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH A COLLAGEN RP PEPTIDE. RX PubMed=9354468; DOI=10.1016/S1074-7613(00)80369-6; RA Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.; RT "X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed RT with a peptide from human collagen II."; RL Immunity 7:473-481(1997). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- INTERACTION: CC P0A6Y8:dnaK (xeno); NbExp=5; IntAct=EBI-1033104, EBI-542092; CC P0DMV8:HSPA1A; NbExp=10; IntAct=EBI-1033104, EBI-11052499; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-4 are known: CC DRB1*04:01, DRB1*04:02, DRB1*04:03, DRB1*04:04, DRB1*04:05, CC DRB1*04:06, DRB1*04:07, DRB1*04:08, DRB1*04:09, DRB1*04:10, CC DRB1*04:11, DRB1*04:12, DRB1*04:13, DRB1*04:14, DRB1*04:15, CC DRB1*04:16, DRB1*04:17, DRB1*04:18, DRB1*04:19, DRB1*04:20, CC DRB1*04:21, DRB1*04:22, DRB1*04:23, DRB1*04:24, DRB1*04:25, CC DRB1*04:26, DRB1*04:27, DRB1*04:28, DRB1*04:29, DRB1*04:30, CC DRB1*04:31, DRB1*04:32, DRB1*04:33, DRB1*04:34, DRB1*04:35, CC DRB1*04:36, DRB1*04:37, DRB1*04:38, DRB1*04:39, DRB1*04:40, CC DRB1*04:41, DRB1*04:42, DRB1*04:43, DRB1*04:44, DRB1*04:45, CC DRB1*04:46, DRB1*04:47, DRB1*04:48, DRB1*04:49, DRB1*04:50, CC DRB1*04:51, DRB1*04:52, DRB1*04:53, DRB1*04:54, DRB1*04:55, CC DRB1*04:56, DRB1*04:57, DRB1*04:58, DRB1*04:59, DRB1*04:60, CC DRB1*04:61, DRB1*04:62, DRB1*04:63, DRB1*04:64, DRB1*04:65, CC DRB1*04:66, DRB1*04:67, DRB1*04:68, DRB1*04:69, DRB1*04:70, CC DRB1*04:71, DRB1*04:72, DRB1*04:73, DRB1*04:74, DRB1*04:75, CC DRB1*04:76, DRB1*04:77 and DRB1*04:78. The sequence shown is that CC of DRB1*04:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M20548; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M20549; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M20550; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL137064; CAC19360.1; -; Genomic_DNA. DR EMBL; M17381; AAA59805.1; -; mRNA. DR EMBL; K02776; AAA59808.1; -; Genomic_DNA. DR EMBL; X96851; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ297586; CAC08826.2; -; mRNA. DR EMBL; AF029269; AAF65479.1; -; Genomic_DNA. DR EMBL; AF112876; AAD29581.1; -; Genomic_DNA. DR EMBL; AJ295845; CAC08181.1; -; Genomic_DNA. DR EMBL; X02902; CAA26660.1; -; mRNA. DR EMBL; M15069; AAA59809.1; -; mRNA. DR EMBL; L42143; AAA67104.1; -; mRNA. DR PIR; A94681; A29310. DR PIR; I79419; I79419. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 1D5M; X-ray; 2.00 A; B=30-221. DR PDB; 1D5X; X-ray; 2.45 A; B=30-221. DR PDB; 1D5Z; X-ray; 2.00 A; B=30-221. DR PDB; 1D6E; X-ray; 2.45 A; B=30-221. DR PDB; 1J8H; X-ray; 2.40 A; B=30-221. DR PDB; 2SEB; X-ray; 2.50 A; B=30-221. DR PDB; 3O6F; X-ray; 2.80 A; B/F=31-221. DR PDB; 3T0E; X-ray; 4.00 A; B=30-221. DR PDB; 4IS6; X-ray; 2.50 A; B=30-221. DR PDB; 4MCY; X-ray; 2.30 A; B=30-219. DR PDB; 4MCZ; X-ray; 2.41 A; B=30-219. DR PDB; 4MD0; X-ray; 2.19 A; B=30-219. DR PDB; 4MD4; X-ray; 1.95 A; B=30-219. DR PDB; 4MD5; X-ray; 1.65 A; B=30-219. DR PDB; 4MDI; X-ray; 2.00 A; B=30-219. DR PDB; 4MDJ; X-ray; 1.70 A; B=30-219. DR PDB; 4Y19; X-ray; 2.50 A; B=30-219. DR PDB; 4Y1A; X-ray; 4.00 A; B=30-219. DR PDB; 5JLZ; X-ray; 1.99 A; B/D=30-219. DR PDB; 5LAX; X-ray; 2.60 A; B/D=30-219. DR PDB; 5NI9; X-ray; 1.33 A; B=30-219. DR PDB; 5NIG; X-ray; 1.35 A; B=30-219. DR PDB; 6BIJ; X-ray; 2.10 A; B=31-219. DR PDB; 6BIL; X-ray; 2.40 A; B=30-219. DR PDB; 6BIN; X-ray; 2.50 A; B=30-219. DR PDB; 6BIR; X-ray; 2.30 A; B=30-219. DR PDB; 6BIV; X-ray; 2.90 A; A=30-219. DR PDB; 6BIX; X-ray; 2.20 A; B=30-219. DR PDB; 6BIY; X-ray; 2.05 A; B=30-219. DR PDB; 6BIZ; X-ray; 2.10 A; B=30-219. DR PDBsum; 1D5M; -. DR PDBsum; 1D5X; -. DR PDBsum; 1D5Z; -. DR PDBsum; 1D6E; -. DR PDBsum; 1J8H; -. DR PDBsum; 2SEB; -. DR PDBsum; 3O6F; -. DR PDBsum; 3T0E; -. DR PDBsum; 4IS6; -. DR PDBsum; 4MCY; -. DR PDBsum; 4MCZ; -. DR PDBsum; 4MD0; -. DR PDBsum; 4MD4; -. DR PDBsum; 4MD5; -. DR PDBsum; 4MDI; -. DR PDBsum; 4MDJ; -. DR PDBsum; 4Y19; -. DR PDBsum; 4Y1A; -. DR PDBsum; 5JLZ; -. DR PDBsum; 5LAX; -. DR PDBsum; 5NI9; -. DR PDBsum; 5NIG; -. DR PDBsum; 6BIJ; -. DR PDBsum; 6BIL; -. DR PDBsum; 6BIN; -. DR PDBsum; 6BIR; -. DR PDBsum; 6BIV; -. DR PDBsum; 6BIX; -. DR PDBsum; 6BIY; -. DR PDBsum; 6BIZ; -. DR ProteinModelPortal; P13760; -. DR SMR; P13760; -. DR IntAct; P13760; 11. DR ChEMBL; CHEMBL3988561; -. DR iPTMnet; P13760; -. DR PhosphoSitePlus; P13760; -. DR DMDM; 122253; -. DR EPD; P13760; -. DR MaxQB; P13760; -. DR PeptideAtlas; P13760; -. DR PRIDE; P13760; -. DR Ensembl; ENST00000419393; ENSP00000403458; ENSG00000228080. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR H-InvDB; HIX0207659; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; HPA043151; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_P13760; -. DR HOVERGEN; HBG012730; -. DR PhylomeDB; P13760; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR EvolutionaryTrace; P13760; -. DR Proteomes; UP000005640; Chromosome 6. DR CleanEx; HS_HLA-DRB1; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0042609; F:CD4 receptor binding; IPI:CAFA. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IDA:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IDA:UniProtKB. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:CAFA. DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:CAFA. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0033674; P:positive regulation of kinase activity; IDA:CAFA. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:CAFA. DR GO; GO:0045657; P:positive regulation of monocyte differentiation; IDA:CAFA. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:CAFA. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CAFA. DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:CAFA. DR GO; GO:0051290; P:protein heterotetramerization; IDA:CAFA. DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB. DR GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB. DR GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-4 beta chain. FT /FTId=PRO_0000018950. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 5 5 K -> R (in dbSNP:rs707953). FT /FTId=VAR_056529. FT VARIANT 86 86 D -> S (in allele DRB1*04:11; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016673. FT VARIANT 96 96 L -> I (in allele DRB1*04:02). FT /FTId=VAR_016674. FT VARIANT 99 99 Q -> D (in allele DRB1*04:02; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016675. FT VARIANT 100 100 K -> E (in allele DRB1*04:02). FT /FTId=VAR_016676. FT VARIANT 100 100 K -> R (in allele DRB1*04:03, allele FT DRB1*04:04 and allele DRB1*04:11). FT /FTId=VAR_016677. FT VARIANT 103 103 A -> E (in allele DRB1*04:03 and allele FT DRB1*04:11). FT /FTId=VAR_016678. FT VARIANT 115 115 G -> V (in allele DRB1*04:02, allele FT DRB1*04:03, allele DRB1*04:04 and allele FT DRB1*04:11). FT /FTId=VAR_016679. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_056531. FT CONFLICT 154 154 G -> A (in Ref. 4; AAA59805). FT {ECO:0000305}. FT STRAND 36 47 {ECO:0000244|PDB:4MD5}. FT TURN 48 51 {ECO:0000244|PDB:4MD5}. FT STRAND 52 61 {ECO:0000244|PDB:4MD5}. FT STRAND 64 70 {ECO:0000244|PDB:4MD5}. FT TURN 71 73 {ECO:0000244|PDB:4MD5}. FT STRAND 74 80 {ECO:0000244|PDB:4MD5}. FT HELIX 81 83 {ECO:0000244|PDB:4MD5}. FT HELIX 84 91 {ECO:0000244|PDB:4MD5}. FT HELIX 94 106 {ECO:0000244|PDB:4MD5}. FT HELIX 108 115 {ECO:0000244|PDB:4MD5}. FT HELIX 116 118 {ECO:0000244|PDB:4MD5}. FT TURN 119 121 {ECO:0000244|PDB:4MD5}. FT STRAND 127 133 {ECO:0000244|PDB:4MD5}. FT STRAND 135 137 {ECO:0000244|PDB:6BIY}. FT STRAND 143 154 {ECO:0000244|PDB:4MD5}. FT STRAND 157 162 {ECO:0000244|PDB:4MD5}. FT STRAND 165 167 {ECO:0000244|PDB:4MD5}. FT STRAND 171 173 {ECO:0000244|PDB:4MD5}. FT STRAND 180 182 {ECO:0000244|PDB:4MD5}. FT STRAND 184 191 {ECO:0000244|PDB:4MD5}. FT STRAND 199 205 {ECO:0000244|PDB:4MD5}. FT STRAND 213 218 {ECO:0000244|PDB:4MD5}. SQ SEQUENCE 266 AA; 30112 MW; 8116E91DA38294E5 CRC64; MVCLKFPGGS CMAALTVTLM VLSSPLALAG DTRPRFLEQV KHECHFFNGT ERVRFLDRYF YHQEEYVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQK RAAVDTYCRH NYGVGESFTV QRRVYPEVTV YPAKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKTG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSLT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B17_HUMAN Reviewed; 266 AA. AC P13761; B0UYW1; O46699; O46872; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 12-SEP-2018, entry version 161. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-7 beta chain; DE AltName: Full=MHC class II antigen DRB1*7; DE Short=DR-7; DE Short=DR7; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*07:01). RX PubMed=3110774; DOI=10.1073/pnas.84.14.4929; RA Young J.A.T., Wilkinson D., Bodmer W.F., Trowsdale J.; RT "Sequence and evolution of HLA-DR7- and -DRw53-associated beta-chain RT genes."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4929-4933(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB1*07:01). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB1*07:03). RC TISSUE=Blood; RA Buyse I.M., Couture C., Ouellet S., Hashemi-tavoularis S.; RT "Identification of novel DR7, DRB5 and DQB1*03 alleles using the RT CANTYPE assay."; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-117 (ALLELE DRB1*07:04). RC TISSUE=Blood; RX PubMed=11144299; DOI=10.1034/j.1399-0039.2000.560514.x; RA Darke C., Guttridge M.G., Street J., Thompson J., Thomas M.; RT "Molecular, serological and genetic studies on two new HLA-DRB1 RT alleles -- HLA-DRB1*0704 and HLA-DRB1*1507."; RL Tissue Antigens 56:467-469(2000). RN [6] RP ASSOCIATION WITH SUSCEPTIBILITY TO HEPATITIS C VIRUS. RX PubMed=10609818; DOI=10.1016/S0140-6736(99)91443-5; RG Hepatitis C European Network for Cooperative Research; RA Thursz M., Yallop R., Goldin R., Trepo C., Thomas H.C.; RT "Influence of MHC class II genotype on outcome of infection with RT hepatitis C virus."; RL Lancet 354:2119-2124(1999). RN [7] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [8] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [9] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [10] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [11] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [12] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [13] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-7 are known: CC DRB1*07:01, DRB1*07:03, DRB1*07:04, DRB1*07:05, DRB1*07:06, CC DRB1*07:07, DRB1*07:08, DRB1*07:09, DRB1*07:11, DRB1*07:12, CC DRB1*07:13, DRB1*07:14, DRB1*07:15, DRB1*07:16 and DRB1*07:17. The CC sequence shown is that of DRB1*07:01. CC -!- POLYMORPHISM: Allele DRB1*07:01 is associated with persistent CC hepatitis C virus (HCV) infections [MIM:609532]. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M16941; AAA36282.1; -; mRNA. DR EMBL; CR753309; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753835; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001023; AAH01023.1; -; mRNA. DR EMBL; Y13785; CAA74112.1; -; Genomic_DNA. DR EMBL; Y16224; CAA76123.1; -; Genomic_DNA. DR PIR; A28031; A28031. DR RefSeq; XP_011546040.1; XM_011547738.2. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; P13761; -. DR SMR; P13761; -. DR IntAct; P13761; 1. DR ChEMBL; CHEMBL3988561; -. DR DMDM; 122256; -. DR MaxQB; P13761; -. DR PeptideAtlas; P13761; -. DR PRIDE; P13761; -. DR Ensembl; ENST00000437784; ENSP00000405960; ENSG00000229074. DR Ensembl; ENST00000444645; ENSP00000409322; ENSG00000236884. DR UCSC; uc011gjy.3; human. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; HPA043151; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR MIM; 609532; phenotype. DR neXtProt; NX_P13761; -. DR HOVERGEN; HBG012730; -. DR PhylomeDB; P13761; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR CleanEx; HS_HLA-DRB1; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; IMP:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; IDA:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; IDA:UniProtKB. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IDA:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IMP:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:UniProtKB. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB. DR GO; GO:2001179; P:regulation of interleukin-10 secretion; IDA:UniProtKB. DR GO; GO:0032673; P:regulation of interleukin-4 production; IDA:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0042088; P:T-helper 1 type immune response; IMP:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-7 beta chain. FT /FTId=PRO_0000018951. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 216 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 5 5 K -> R (in dbSNP:rs707953). FT /FTId=VAR_056532. FT VARIANT 58 58 R -> S (in allele DRB1*07:03; FT dbSNP:rs17878437). FT /FTId=VAR_016680. FT VARIANT 106 106 T -> N (in allele DRB1*07:04; FT dbSNP:rs9269941). FT /FTId=VAR_016681. FT VARIANT 107 107 V -> Y (in allele DRB1*07:04; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016682. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_056534. SQ SEQUENCE 266 AA; 29822 MW; 439B6AFA553F162C CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALAG DTQPRFLWQG KYKCHFFNGT ERVQFLERLF YNQEEFVRFD SDVGEYRAVT ELGRPVAESW NSQKDILEDR RGQVDTVCRH NYGVGESFTV QRRVHPEVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVM SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B18_HUMAN Reviewed; 266 AA. AC Q30134; O19718; O19788; Q29968; Q30108; Q30115; Q9BCP0; Q9BCP1; AC Q9BCP2; Q9BD33; Q9TQ37; Q9UIM9; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2003, sequence version 2. DT 18-JUL-2018, entry version 135. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-8 beta chain; DE AltName: Full=MHC class II antigen DRB1*8; DE Short=DR-8; DE Short=DR8; DE Short=DRw8; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*08:02). RX PubMed=2497068; DOI=10.1007/BF00352840; RA Jonsson A.K., Andersson L., Rask L.; RT "A cellular and functional split in the DRw8 haplotype is due to a RT single amino acid replacement (DR beta ser 57- asp 57)."; RL Immunogenetics 29:308-316(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21. RX PubMed=8106268; DOI=10.1016/0198-8859(93)90531-5; RA Emery P., Mach B., Reith W.; RT "The different level of expression of HLA-DRB1 and -DRB3 genes is RT controlled by conserved isotypic differences in promoter sequence."; RL Hum. Immunol. 38:137-147(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-115 (ALLELE DRB1*08:01). RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123. RX PubMed=1979063; RA Van Kerckhove C., Melin-Aldana H., Elma M.S., Luyrink L., Donnelly P., RA Taylor J., Maksymowych W.P., Lovell D.J., Choi E., Glass D.N.; RT "A distinct HLA-DRw8 haplotype characterizes patients with juvenile RT rheumatoid arthritis."; RL Immunogenetics 32:304-308(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*08:01). RA Dormoy A., Froelich N., Weschler B., Tongio M.M.; RT "A new DRB1*08 allele."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*08:04). RC TISSUE=Blood; RA Hurley C.K., Tang T., Li L.; RT "Human leukocyte antigen class II DRB1*0804 variant."; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-208 (ALLELE DRB1*08:01). RA Greville W.D.; RT "SBT of DRB1*0801, exons two and three."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-115 (ALLELE DRB1*08:03). RX PubMed=2592019; DOI=10.1007/BF02421173; RA Abe A., Ito I., Ohkubo M., Kaneko T., Ito K., Kato H., Kashiwagi N., RA Obata F.; RT "Two distinct subtypes of the HLA-DRw12 haplotypes in the Japanese RT population detected by nucleotide sequence analysis and RT oligonucleotide genotyping."; RL Immunogenetics 30:422-426(1989). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-120 (ALLELE DRB1*08:01). RA Eberle M., Asu U., Taylor M., Hunter J.B., Fuller T.C., Maurer D.; RT "Identification of a putative DR8 founder haplotype containing a novel RT DRB1*08 allele."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 47-122 (ALLELE DRB1*08:04). RC TISSUE=Blood; RX PubMed=8023844; RA Titus-Trachtenberg E.A., Rickards O., De Stefano G.F., Erlich H.A.; RT "Analysis of HLA class II haplotypes in the Cayapa Indians of Ecuador: RT a novel DRB1 allele reveals evidence for convergent evolution and RT balancing selection at position 86."; RL Am. J. Hum. Genet. 55:160-167(1994). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-217. RX PubMed=2471740; RA Gorski J.; RT "HLA-DR beta-chain polymorphism. Second domain polymorphism reflects RT evolutionary relatedness of alleles and may explain public serologic RT epitopes."; RL J. Immunol. 143:329-333(1989). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 256-266. RX PubMed=3458223; DOI=10.1073/pnas.83.8.2642; RA Gregersen P.K., Shen M., Song Q.-L., Merryman P., Degar S., Seki T., RA Maccari J., Goldberg D., Murphy H., Schwenzer J., Wang C.Y., RA Winchester R.J., Nepom G.T., Silver J.; RT "Molecular diversity of HLA-DR4 haplotypes."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2642-2646(1986). RN [13] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [14] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [15] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [16] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [17] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [18] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [19] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- INTERACTION: CC P0A6Y8:dnaK (xeno); NbExp=7; IntAct=EBI-13952091, EBI-542092; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-8 are known: CC DRB1*08:01 (Dw8.1), DRB1*08:02 (Dw8.2; DRB1L), DRB1*08:03 (Dw8.3); CC DRB1*08:04; DRB1*08:05, DRB1*08:06, DRB1*08:07, DRB1*08:08, CC DRB1*08:09, DRB1*08:10, DRB1*08:11, DRB1*08:12, DRB1*08:13, CC DRB1*08:14, DRB1*08:15, DRB1*08:16, DRB1*08:17, DRB1*08:18, CC DRB1*08:19, DRB1*08:20, DRB1*08:21, DRB1*08:22, DRB1*08:23, CC DRB1*08:24, DRB1*08:25, DRB1*08:26, DRB1*08:27, DRB1*08:28, CC DRB1*08:29, DRB1*08:30, DRB1*08:31, DRB1*08:32, DRB1*08:33, CC DRB1*08:34, DRB1*08:35 and DRB1*08:36. The sequence shown is that CC of DRB1*08:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M26038; AAA59794.1; -; mRNA. DR EMBL; S69987; AAD14052.1; -; Genomic_DNA. DR EMBL; M17386; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M60216; AAA36298.1; -; Genomic_DNA. DR EMBL; AJ249626; CAB56284.1; -; Genomic_DNA. DR EMBL; AF330103; AAK08504.1; -; Genomic_DNA. DR EMBL; AH010612; AAK31608.1; -; Genomic_DNA. DR EMBL; AH010613; AAK31609.1; -; Genomic_DNA. DR EMBL; AH010614; AAK31610.1; -; Genomic_DNA. DR EMBL; M27511; AAA59817.1; -; Genomic_DNA. DR EMBL; AF144105; AAD38374.1; -; Genomic_DNA. DR EMBL; L10402; AAA51400.1; -; Genomic_DNA. DR EMBL; M15074; AAA59810.1; -; mRNA. DR PIR; A45856; A45856. DR PIR; F60748; F60748. DR PIR; I51875; I51875. DR PIR; I54473; I54473. DR PIR; I68778; I68778. DR PIR; PH0160; PH0160. DR PIR; PT0161; PT0161. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q30134; -. DR SMR; Q30134; -. DR IntAct; Q30134; 2. DR ChEMBL; CHEMBL3988561; -. DR DMDM; 34395492; -. DR PeptideAtlas; Q30134; -. DR PRIDE; Q30134; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; HPA043151; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_Q30134; -. DR HOVERGEN; HBG012730; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR CleanEx; HS_HLA-DRB1; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-8 beta chain. FT /FTId=PRO_0000018952. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P20039}. FT VARIANT 86 86 S -> D (in allele DRB1*08:02 and allele FT DRB1*08:04; requires 2 nucleotide FT substitutions). FT /FTId=VAR_016683. FT VARIANT 96 96 F -> I (in allele DRB1*08:03). FT /FTId=VAR_016684. FT VARIANT 115 115 G -> V (in allele DRB1*08:04). FT /FTId=VAR_016685. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_056536. SQ SEQUENCE 266 AA; 30004 MW; D452D1C3A75CEA31 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TGECYFFNGT ERVRFLDRYF YNQEEYVRFD SDVGEYRAVT ELGRPSAEYW NSQKDFLEDR RALVDTYCRH NYGVGESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWSAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B19_HUMAN Reviewed; 266 AA. AC Q9TQE0; Q30149; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 18-JUL-2018, entry version 142. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-9 beta chain; DE AltName: Full=MHC class II antigen DRB1*9; DE Short=DR-9; DE Short=DR9; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*09:01). RC TISSUE=Blood; RX PubMed=9777332; DOI=10.1046/j.1365-2370.1998.00105.x; RA Martinez-Quiles N., Martin-Villa J.M., Ferre-Lopez S., RA Moreno-Pelayo M.A., Martinez-Laso J., Perez-Blas M., Alegre R., RA Arnaiz-Villena A.; RT "Complete cDNA sequence of the HLA-DRB1*09012 allele."; RL Eur. J. Immunogenet. 25:307-309(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-115 (ALLELE DRB1*09:01). RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-115. RX PubMed=2023919; DOI=10.1073/pnas.88.9.3686; RA Gyllensten U.B., Sundvall M., Erlich H.A.; RT "Allelic diversity is generated by intraexon sequence exchange at the RT DRB1 locus of primates."; RL Proc. Natl. Acad. Sci. U.S.A. 88:3686-3690(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 45-266. RX PubMed=3466180; DOI=10.1073/pnas.83.23.9149; RA Gregersen P.K., Moriuchi T., Karr R.W., Obata F., Moriuchi J., RA Maccari J., Goldberg D., Winchester R.J., Silver J.; RT "Polymorphism of HLA-DR beta chains in DR4, -7, and -9 haplotypes: RT implications for the mechanisms of allelic variation."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9149-9153(1986). RN [5] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [6] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [7] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [8] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [9] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [10] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [11] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-9 are known: CC DRB1*09:01, DRB1*09:02, DRB1*09:03, DRB1*09:04, DRB1*09:05, CC DRB1*09:06, DRB1*09:07 and DRB1*09:08. The sequence shown is that CC of DRB1*09:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; U66826; AAD43829.1; -; mRNA. DR EMBL; M17387; AAA36297.1; -; mRNA. DR PIR; A25925; A25925. DR PIR; C28515; C28515. DR UniGene; Hs.485130; -. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q9TQE0; -. DR SMR; Q9TQE0; -. DR IntAct; Q9TQE0; 1. DR ChEMBL; CHEMBL3988561; -. DR iPTMnet; Q9TQE0; -. DR PhosphoSitePlus; Q9TQE0; -. DR DMDM; 34395508; -. DR MaxQB; Q9TQE0; -. DR PeptideAtlas; Q9TQE0; -. DR PRIDE; Q9TQE0; -. DR Ensembl; ENST00000437784; ENSP00000405960; ENSG00000229074. DR Ensembl; ENST00000444645; ENSP00000409322; ENSG00000236884. DR UCSC; uc063vvt.1; human. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR H-InvDB; HIX0166371; -. DR H-InvDB; HIX0166636; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; HPA043151; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_Q9TQE0; -. DR HOVERGEN; HBG012730; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR CleanEx; HS_HLA-DRB1; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB. DR GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB. DR GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-9 beta chain. FT /FTId=PRO_0000018953. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 216 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 5 5 K -> R (in dbSNP:rs707953). FT /FTId=VAR_056537. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_056539. SQ SEQUENCE 266 AA; 29826 MW; AD46B4AD27BAD8F2 CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALAG DTQPRFLKQD KFECHFFNGT ERVRYLHRGI YNQEENVRFD SDVGEYRAVT ELGRPVAESW NSQKDFLERR RAEVDTVCRH NYGVGESFTV QRRVHPEVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVM SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B1A_HUMAN Reviewed; 266 AA. AC Q30167; P01914; Q9MYF5; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 23-MAR-2010, sequence version 2. DT 23-MAY-2018, entry version 129. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-10 beta chain; DE AltName: Full=DRw10; DE AltName: Full=MHC class II antigen DRB1*10; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*10:01). RX PubMed=6589154; RA Peterson P.A., Gustafsson K., Wiman K.G., Emmoth E., Larhammar D., RA Boehme J., Hyldig-Nielsen J.J., Ronne H., Rask L.; RT "Mutations and selection in the generation of class II RT histocompatibility antigen polymorphism."; RL EMBO J. 3:1655-1660(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*10:01). RX PubMed=2450924; RA Merryman P., Gregersen P.K., Lee S., Silver J., Nunez-Roldan A., RA Crapper R., Winchester R.; RT "Nucleotide sequence of a DRw10 beta chain cDNA clone. Identity of the RT third D region with that of the DRw53 allele of the beta 2 locus and RT as the probable site encoding a polymorphic MHC class II epitope."; RL J. Immunol. 140:2447-2452(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*10:01). RX PubMed=6415003; DOI=10.1016/0198-8859(83)90087-3; RA Larhammar D., Andersson G., Andersson M., Bill P., Boehme J., RA Claesson L., Denaro M., Emmoth E., Gustafsson K., Hammarling U., RA Heldin E., Hyldig-Nielsen J.-J., Lind P., Schenning L., Servenius B., RA Widmark E., Rask L., Peterson P.A.; RT "Molecular analysis of human class II transplantation antigens and RT their genes."; RL Hum. Immunol. 8:95-103(1983). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*10:01). RA Woelpl A.; RT "Sequence of an HLA-DRB gene."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [6] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [7] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [8] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [9] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [10] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [11] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route; where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules; and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments; exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides; autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs; other cells of the gastrointestinal tract; such CC as epithelial cells; express MHC class II molecules and CD74 and CC act as APCs; which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen; three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs; CD74 undergoes a sequential CC degradation by various proteases; including CTSS and CTSL; leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells; the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules; increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-10 are known: CC DRB1*10:01; DRB1*10:02 and DRB1*10:03. The sequence shown is that CC of DRB1*10:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X00700; CAA25296.1; -; mRNA. DR EMBL; M20138; AAA59832.1; -; mRNA. DR EMBL; AF225565; AAF65542.1; -; Genomic_DNA. DR PIR; A27614; HLHU4D. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q30167; -. DR SMR; Q30167; -. DR ChEMBL; CHEMBL3580495; -. DR DMDM; 292494999; -. DR PeptideAtlas; Q30167; -. DR PRIDE; Q30167; -. DR Ensembl; ENST00000419393; ENSP00000403458; ENSG00000228080. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; HPA043151; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_Q30167; -. DR HOVERGEN; HBG012730; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR CleanEx; HS_HLA-DRB1; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-10 beta chain. FT /FTId=PRO_0000018954. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 216 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P20039}. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_056541. FT CONFLICT 180 180 G -> E (in Ref. 2; AAA59832). FT {ECO:0000305}. SQ SEQUENCE 266 AA; 30002 MW; 45AB410F8AC21750 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEEV KFECHFFNGT ERVRLLERRV HNQEEYARYD SDVGEYRAVT ELGRPDAEYW NSQKDLLERR RAAVDTYCRH NYGVGESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKTG VVSTGLIQNG DWTFQTLVML ETVPQSGEVY TCQVEHPSVM SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLP PTGFLS // ID 2B1B_HUMAN Reviewed; 266 AA. AC P20039; Q30006; Q9GIX8; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 12-SEP-2018, entry version 148. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-11 beta chain; DE AltName: Full=DR-5; DE Short=DR5; DE AltName: Full=DRw11; DE AltName: Full=MHC class II antigen DRB1*11; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*11:01). RX PubMed=3456344; RA Tieber V.L., Abruzzini L.F., Didier D.K., Schwartz B.D., Rotwein P.; RT "Complete characterization and sequence of an HLA class II DR beta RT chain cDNA from the DR5 haplotype."; RL J. Biol. Chem. 261:2738-2742(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*11:03). RX PubMed=3137159; DOI=10.1007/BF00375861; RA Steimle V., Hinkkanen A., Schlesier M., Epplen J.T.; RT "A novel HLA-DR beta I sequence from the DRw11 haplotype."; RL Immunogenetics 28:208-210(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*11:04). RX PubMed=12358860; DOI=10.1046/j.1365-2370.2002.00354.x; RA Ramon D., Corell A., Cox S.T., Soteriou B., Madrigal J.A., RA Marsh S.G.E.; RT "Complete cDNA sequences of the HLA-DRB1*0402 and DRB1*11041 RT alleles."; RL Eur. J. Immunogenet. 29:453-455(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-217. RX PubMed=2471740; RA Gorski J.; RT "HLA-DR beta-chain polymorphism. Second domain polymorphism reflects RT evolutionary relatedness of alleles and may explain public serologic RT epitopes."; RL J. Immunol. 143:329-333(1989). RN [5] RP ASSOCIATION WITH SUSCEPTIBILITY TO HEPATITIS C VIRUS. RX PubMed=10609818; DOI=10.1016/S0140-6736(99)91443-5; RG Hepatitis C European Network for Cooperative Research; RA Thursz M., Yallop R., Goldin R., Trepo C., Thomas H.C.; RT "Influence of MHC class II genotype on outcome of infection with RT hepatitis C virus."; RL Lancet 354:2119-2124(1999). RN [6] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [7] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [8] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [9] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [10] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [11] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [12] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-11 are known: CC DRB1*11:01, DRB1*11:03, DRB1*11:04, DRB1*11:05, DRB1*11:06, CC DRB1*11:07, DRB1*11:08, DRB1*11:09, DRB1*11:10, DRB1*11:11, CC DRB1*11:12, DRB1*11:13, DRB1*11:14, DRB1*11:15, DRB1*11:16, CC DRB1*11:17, DRB1*11:18, DRB1*11:19, DRB1*11:20, DRB1*11:21, CC DRB1*11:22, DRB1*11:23, DRB1*11:24, DRB1*11:25, DRB1*11:26, CC DRB1*11:27, DRB1*11:28, DRB1*11:29, DRB1*11:30, DRB1*11:31, CC DRB1*11:32, DRB1*11:33, DRB1*11:34, DRB1*11:35, DRB1*11:36, CC DRB1*11:37, DRB1*11:38, DRB1*11:39, DRB1*11:40, DRB1*11:41, CC DRB1*11:42, DRB1*11:43, DRB1*11:44, DRB1*11:45, DRB1*11:46, CC DRB1*11:47, DRB1*11:48, DRB1*11:49, DRB1*11:50, DRB1*11:51, CC DRB1*11:52, DRB1*11:53, DRB1*11:54, DRB1*11:55, DRB1*11:56, CC DRB1*11:57, DRB1*11:58, DRB1*11:59, DRB1*11:60, DRB1*11:61, CC DRB1*11:62, DRB1*11:63, DRB1*11:64, DRB1*11:65, DRB1*11:66, CC DRB1*11:67, DRB1*11:68, DRB1*11:69, DRB1*11:70 and DRB1*11:72. The CC sequence shown is that of DRB1*11:01. CC -!- POLYMORPHISM: Allele DRB1*11:01 is associated with self-limiting CC hepatitis C virus (HCV) infections [MIM:609532]. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M11867; AAA36274.1; -; mRNA. DR EMBL; M22050; AAA59713.1; -; Genomic_DNA. DR EMBL; M21966; AAA59713.1; JOINED; Genomic_DNA. DR EMBL; M22047; AAA59713.1; JOINED; Genomic_DNA. DR EMBL; M22048; AAA59713.1; JOINED; Genomic_DNA. DR EMBL; M22049; AAA59713.1; JOINED; Genomic_DNA. DR EMBL; AJ297587; CAC08827.1; -; mRNA. DR PIR; A25324; A25324. DR PIR; F60748; F60748. DR PIR; I54448; I54448. DR PIR; PH0153; PH0153. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 6CPL; X-ray; 2.45 A; B=30-219. DR PDB; 6CPN; X-ray; 2.00 A; B=30-219. DR PDB; 6CQL; X-ray; 2.40 A; B=30-219. DR PDB; 6CQN; X-ray; 2.50 A; B=30-219. DR PDBsum; 6CPL; -. DR PDBsum; 6CPN; -. DR PDBsum; 6CQL; -. DR PDBsum; 6CQN; -. DR ProteinModelPortal; P20039; -. DR SMR; P20039; -. DR IntAct; P20039; 1. DR ChEMBL; CHEMBL3988561; -. DR iPTMnet; P20039; -. DR DMDM; 122254; -. DR MaxQB; P20039; -. DR PeptideAtlas; P20039; -. DR PRIDE; P20039; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; HPA043151; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR MIM; 609532; phenotype. DR neXtProt; NX_P20039; -. DR HOVERGEN; HBG012730; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR CleanEx; HS_HLA-DRB1; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-11 beta chain. FT /FTId=PRO_0000018955. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000269|PubMed:18305173}. FT VARIANT 55 55 F -> Y (in dbSNP:rs1059569). FT /FTId=VAR_056542. FT VARIANT 100 100 R -> E (in allele DRB1*11:03; requires 2 FT nucleotide substitutions). FT /FTId=VAR_016717. FT VARIANT 115 115 G -> V (in allele DRB1*11:03 and allele FT DRB1*11:04). FT /FTId=VAR_016718. FT STRAND 36 47 {ECO:0000244|PDB:6CPN}. FT TURN 48 51 {ECO:0000244|PDB:6CPN}. FT STRAND 52 61 {ECO:0000244|PDB:6CPN}. FT STRAND 64 70 {ECO:0000244|PDB:6CPN}. FT TURN 71 73 {ECO:0000244|PDB:6CPN}. FT STRAND 75 80 {ECO:0000244|PDB:6CPN}. FT HELIX 81 83 {ECO:0000244|PDB:6CPN}. FT HELIX 84 91 {ECO:0000244|PDB:6CPN}. FT HELIX 94 106 {ECO:0000244|PDB:6CPN}. FT HELIX 108 115 {ECO:0000244|PDB:6CPN}. FT HELIX 116 118 {ECO:0000244|PDB:6CPN}. FT TURN 119 121 {ECO:0000244|PDB:6CPN}. FT STRAND 127 133 {ECO:0000244|PDB:6CPN}. FT STRAND 140 154 {ECO:0000244|PDB:6CPN}. FT STRAND 157 162 {ECO:0000244|PDB:6CPN}. FT STRAND 165 167 {ECO:0000244|PDB:6CPL}. FT STRAND 171 173 {ECO:0000244|PDB:6CPN}. FT STRAND 180 182 {ECO:0000244|PDB:6CPN}. FT STRAND 184 192 {ECO:0000244|PDB:6CPN}. FT STRAND 199 205 {ECO:0000244|PDB:6CPN}. FT STRAND 213 218 {ECO:0000244|PDB:6CPN}. SQ SEQUENCE 266 AA; 30160 MW; 6CFC0D44391B1059 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRFLDRYF YNQEEYVRFD SDVGEFRAVT ELGRPDEEYW NSQKDFLEDR RAAVDTYCRH NYGVGESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B1C_HUMAN Reviewed; 266 AA. AC Q95IE3; A7LA26; B0LUZ6; B6VCX2; B7UDB2; O19585; Q19AF2; Q29771; AC Q2L9H4; Q2MZ92; Q5EER6; Q5NDB9; Q5UT58; Q5Y7G0; Q768U4; Q7YP04; AC Q861H8; Q95IT6; Q9BD40; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 18-JUL-2018, entry version 116. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-12 beta chain; DE AltName: Full=MHC class II antigen DRB1*12; DE Short=DR-12; DE Short=DR12; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*12:01). RX PubMed=12028552; DOI=10.1034/j.1399-0039.2002.590221.x; RA Zanone R., Bettens F., Tiercy J.M.; RT "Sequence of a new DR12 allele with two silent mutations that affect RT PCR-SSP typing."; RL Tissue Antigens 59:165-167(2002). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*12:10). RX PubMed=15361134; DOI=10.1111/j.1399-0039.2004.00309.x; RA Kim E., Lee E.J., Lim Y.H., Lee J.Y., Koh I.S., Kimm K., Ji G.E., RA Kwack K.; RT "Identification of a novel HLA-DRB1*12 allele (DRB1*1210) in the RT Korean population."; RL Tissue Antigens 64:518-519(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*12:17). RX PubMed=19493243; DOI=10.1111/j.1399-0039.2009.01224.x; RA Park M.H., Kim Y., Lee J.Y.; RT "Identification of a novel HLA-DRB1 allele, HLA-DRB1*1217, in a Korean RT individual."; RL Tissue Antigens 73:627-628(2009). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-262 (ALLELE DRB1*12:01). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-208 (ALLELE DRB1*12:07). RX PubMed=12028551; DOI=10.1034/j.1399-0039.2002.590220.x; RA Dunckley H., Le T., Dodd R., Hogbin J.P., Strickland J., Chapman G., RA Greville W.D.; RT "Description of a novel HLA-DRB1 allele, DRB1*1207."; RL Tissue Antigens 59:162-164(2002). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:11). RC TISSUE=Peripheral blood; RX PubMed=16690413; DOI=10.1016/j.humimm.2005.05.002; RA Horn P.A., DeLuca D.S., Jindra P., Blasczyk R.; RT "The replacement mutation in HLA-DRB1*1211 affects a likely keystone RT position."; RL Hum. Immunol. 66:1254-1257(2005). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:08). RX PubMed=12144630; DOI=10.1034/j.1399-0039.2002.590513.x; RA Sheldon M.H., Bunce M., Dunn P.P., Day S., Lee G.D., Park Y.J., RA Bang B.K., Kim B.K., Oh E.J.; RT "Identification of two new alleles in a single Korean individual, HLA- RT B*1568 and HLA-DRB1*1208."; RL Tissue Antigens 59:430-432(2002). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:15). RX PubMed=19046299; DOI=10.1111/j.1744-313X.2008.00785.x; RA Lee H.L., Chu C.C., Trejaut J.A., Yang K.L., Lin M.; RT "Identification of two novel HLA-DRB1 alleles, HLA-DRB1*1214 and HLA- RT DRB1*1215, in two Taiwanese individuals."; RL Int. J. Immunogenet. 35:423-426(2008). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:19). RX PubMed=19624612; DOI=10.1111/j.1399-0039.2009.01316.x; RA Nie X.M., Fang Y.H., Zhang Y., He W.D., Zhu C.F.; RT "A novel HLA-DRB1 allele, DRB1*1219, was identified by sequence-based RT typing in a Chinese leukaemia family."; RL Tissue Antigens 74:352-354(2009). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:18). RX PubMed=19508407; DOI=10.1111/j.1399-0039.2009.01294.x; RA Gao S.Q., Deng Z.H., Xu Y.P.; RT "Identification of a novel HLA-DRB1*12 allele, DRB1*1218, in Chinese RT population."; RL Tissue Antigens 74:265-267(2009). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:05). RA Kashiwase K., Tokunaga K., Akaza T., Tadokoro K., Juji T.; RT "Sequence of new allele."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:09). RA Ono A.; RT "A new HLA-DR12V allele detected by PCR-RFLP."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:04). RA Gedil M.A., Steiner N.K., Hurley C.K.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:12). RA Zhu F., Lu Q., Zhang W.; RT "Identification a novel HLA-DRB1*12 in Chinese by sequence-based RT typed."; RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:13). RA Hur S.S., Lee M.N., Park S.Y., Kwon O.J.; RT "Novel HLA-DRB1*120201 variant allele."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:14). RA Chu C.-C.; RT "A novel HLA-DRB1 allele."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*12:16). RA Zhang C., Liu J.; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*12:03). RX PubMed=8851733; DOI=10.1111/j.1399-0039.1996.tb02532.x; RA Hashemi S., Couture C., Buyse I., Cole R., Aye M.T.; RT "Sequence analysis of three novel HLA-DRB1 alleles: DRB1*1113, RT DRB1*1114 and DRB1*12032."; RL Tissue Antigens 47:155-158(1996). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELE DRB1*12:02). RA Lo B.; RT "HLA class II DRB1*120201 confirmatory sequence."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 88-197 (ALLELE DRB1*12:06). RX PubMed=10372549; DOI=10.1034/j.1399-0039.1999.530510.x; RA Maeng C.Y., Kim K.H., Kang J.H., Han H., Kim K.L.; RT "A novel HLA-DR12 allele (DRB1*1206) found in a Korean B-cell line."; RL Tissue Antigens 53:516-518(1999). RN [21] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [22] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [23] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [24] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [25] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [26] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [27] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-12 are known: CC DRB1*12:01, DRB1*12:02, DRB1*12:03, DRB1*12:04, DRB1*12:05, CC DRB1*12:06, DRB1*12:07, DRB1*12:08, DRB1*12:09, DRB1*12:10, CC DRB1*12:11, DRB1*12:12, DRB1*12:13, DRB1*12:14, DRB1*12:15, CC DRB1*12:16, DRB1*12:17, DRB1*12:18 and DRB1*12:19. The sequence CC shown is that of DRB1*12:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AJ302075; CAC44379.1; -; mRNA. DR EMBL; AY626551; AAV34808.1; -; mRNA. DR EMBL; EU375850; ABY78039.1; -; mRNA. DR EMBL; AY663396; AAU87983.1; -; Genomic_DNA. DR EMBL; AH010330; AAK07563.1; -; Genomic_DNA. DR EMBL; AJ870921; CAI35044.1; -; Genomic_DNA. DR EMBL; AY033428; AAK55114.1; -; Genomic_DNA. DR EMBL; DQ533486; ABF74752.1; -; Genomic_DNA. DR EMBL; FJ374889; ACJ09136.1; -; Genomic_DNA. DR EMBL; FJ481086; ACK77491.1; -; Genomic_DNA. DR EMBL; D86503; BAA13098.1; -; Genomic_DNA. DR EMBL; AB112911; BAD02942.1; -; Genomic_DNA. DR EMBL; AY339246; AAQ18913.1; -; Genomic_DNA. DR EMBL; AY899825; AAW82078.1; -; Genomic_DNA. DR EMBL; DQ250650; ABC59072.1; -; Genomic_DNA. DR EMBL; DQ343834; ABC70992.1; -; Genomic_DNA. DR EMBL; EF688603; ABS11697.1; -; Genomic_DNA. DR EMBL; X83455; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY174091; AAO20088.1; -; Genomic_DNA. DR EMBL; AF017439; AAB70553.1; -; mRNA. DR PIR; C60748; C60748. DR PIR; F60748; F60748. DR PIR; PH0154; PH0154. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.728; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q95IE3; -. DR SMR; Q95IE3; -. DR ChEMBL; CHEMBL3988561; -. DR DMDM; 74760669; -. DR PeptideAtlas; Q95IE3; -. DR PRIDE; Q95IE3; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR Ensembl; ENST00000412634; ENSP00000408795; ENSG00000228080. DR Ensembl; ENST00000415796; ENSP00000412168; ENSG00000206306. DR Ensembl; ENST00000419393; ENSP00000403458; ENSG00000228080. DR Ensembl; ENST00000428566; ENSP00000392280; ENSG00000206240. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MalaCards; HLA-DRB1; -. DR neXtProt; NX_Q95IE3; -. DR HOVERGEN; HBG012730; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-12 beta chain. FT /FTId=PRO_0000391832. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 5 5 R -> K (in allele DRB1*12:17). FT /FTId=VAR_062818. FT VARIANT 13 13 A -> T (in allele DRB1*12:17). FT /FTId=VAR_062819. FT VARIANT 14 14 V -> A (in allele DRB1*12:17). FT /FTId=VAR_062820. FT VARIANT 14 14 V -> I (in allele DRB1*12:10). FT /FTId=VAR_062821. FT VARIANT 54 54 R -> L (in allele DRB1*12:13). FT /FTId=VAR_062822. FT VARIANT 55 55 L -> F (in allele DRB1*12:08). FT /FTId=VAR_062823. FT VARIANT 66 66 L -> F (in allele DRB1*12:05, allele FT DRB1*12:14 and allele DRB1*12:15). FT /FTId=VAR_062824. FT VARIANT 67 67 L -> V (in allele DRB1*12:14). FT /FTId=VAR_062825. FT VARIANT 76 76 F -> L (in allele DRB1*12:11). FT /FTId=VAR_062826. FT VARIANT 86 86 V -> D (in allele DRB1*12:04 and allele FT DRB1*12:09). FT /FTId=VAR_062827. FT VARIANT 87 87 A -> E (in allele DRB1*12:04). FT /FTId=VAR_062828. FT VARIANT 88 88 E -> Q (in allele DRB1*12:18). FT /FTId=VAR_062829. FT VARIANT 89 89 S -> Y (in allele DRB1*12:04 and allele FT DRB1*12:09). FT /FTId=VAR_062830. FT VARIANT 96 96 I -> F (in allele DRB1*12:02, allele FT DRB1*12:13, allele DRB1*12:15, allele FT DRB1*12:16, allele DRB1*12:18 and allele FT DRB1*12:19). FT /FTId=VAR_062831. FT VARIANT 96 96 I -> L (in allele DRB1*12:12). FT /FTId=VAR_062832. FT VARIANT 98 98 E -> G (in allele DRB1*12:07). FT /FTId=VAR_062833. FT VARIANT 114 114 A -> V (in allele DRB1*12:03, allele FT DRB1*12:16 and allele DRB1*12:19). FT /FTId=VAR_062834. FT VARIANT 115 115 V -> G (in allele DRB1*12:16). FT /FTId=VAR_062835. FT VARIANT 125 125 H -> E (in allele DRB1*12:17; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062836. FT VARIANT 169 169 T -> A (in allele DRB1*12:17). FT /FTId=VAR_062837. FT VARIANT 178 178 H -> Q (in allele DRB1*12:06 and allele FT DRB1*12:17). FT /FTId=VAR_062838. FT VARIANT 262 262 R -> T (in allele DRB1*12:17; FT dbSNP:rs9269744). FT /FTId=VAR_062839. SQ SEQUENCE 266 AA; 29878 MW; FFDD0001C2F0BAF9 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TGECYFFNGT ERVRLLERHF HNQEELLRFD SDVGEFRAVT ELGRPVAESW NSQKDILEDR RAAVDTYCRH NYGAVESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B1D_HUMAN Reviewed; 266 AA. AC Q5Y7A7; A0MWF2; A2ICT1; A4ZXA5; A4ZXA6; A7UHG2; A7X5K7; A8YQE9; AC B0BK85; B3VTQ3; B5A8Y2; B5A8Y3; B5B9V6; B5QSK8; C0LAB5; O02930; AC O62889; O78047; P79545; Q14280; Q14QT2; Q19K86; Q1G0Z9; Q1KLJ6; AC Q29673; Q29720; Q29722; Q29806; Q29833; Q29874; Q29886; Q2MF40; AC Q2YHQ2; Q30112; Q3LA93; Q3LA94; Q3LA95; Q3LA96; Q3LA97; Q3LA98; AC Q3LA99; Q3LAA0; Q3LAA1; Q3LAA2; Q3MQ60; Q53IG1; Q56FP2; Q56FP3; AC Q58F52; Q5K3W2; Q5UBA2; Q5W3L4; Q6REE2; Q6U387; Q701T1; Q70Q85; AC Q768U2; Q7YP03; Q7YQ26; Q7YQA3; Q860E5; Q860H8; Q860Z3; Q861G6; AC Q861H0; Q861H4; Q8HWQ6; Q8WMA0; Q95389; Q95HL1; Q96HZ9; Q9BCP5; AC Q9BD21; Q9GIP3; Q9GJ25; Q9GJ60; Q9GJF8; Q9GJF9; Q9GJG0; Q9MY45; AC Q9MY56; Q9TPW3; Q9TPW9; Q9TPX4; Q9UBY1; Q9UIN0; Q9XRX1; Q9Y453; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 18-JUL-2018, entry version 109. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-13 beta chain; DE AltName: Full=MHC class II antigen DRB1*13; DE Short=DR-13; DE Short=DR13; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*13:01 AND DRB1*13:02). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*13:05). RX PubMed=15896200; DOI=10.1111/j.1399-0039.2005.00407.x; RA Vilches C., Sepulveda S., Balas A., Solis R., Aviles M.J., RA Estefania E., Gomez-Lozano N., Vicario J.L., DePablo R.; RT "Complete coding sequences and haplotypic associations of HLA-B*0707, RT -B*1524, -B*4405, -B*4802, -DRB1*0409, -DRB1*0411, -DRB1*1115, RT - DRB1*1305, and the novel allele -DRB1*0709. Group-specific RT amplification of cDNA from DRB1 alleles associated to DRB3 and DRB4."; RL Tissue Antigens 65:529-538(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*13:27 AND DRB1*13:56). RX PubMed=17174751; DOI=10.1016/j.humimm.2006.09.002; RA Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., RA de Pablo R., Garcia-Sanchez F., Vicario J.L.; RT "Group-specific amplification of cDNA from DRB1 genes. Complete coding RT sequences of partially defined alleles and identification of the new RT alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."; RL Hum. Immunol. 67:1008-1016(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*13:02). RC TISSUE=Blood; RA Arnaiz-Villena A., Martinez-Quiles N., De Juan-Echavarri D., RA Martin-Villa M., Martinez-Laso J.; RT "New complete sequences of MHC-DR in Spanish family with systemic RT lupus erythematosus."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB1*13:01). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB1*13:02). RC TISSUE=B-cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-148 (ALLELE DRB1*13:21). RC TISSUE=Leukocyte; RA Maurer D.H.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-123 (ALLELE DRB1*13:19). RC TISSUE=Blood; RX PubMed=7652736; DOI=10.1111/j.1399-0039.1995.tb02458.x; RA Robbins F., Tang T., Yao H., Ng J., Hartzman R.J., Hurley C.K.; RT "Direct sequencing of SSP-PCR-amplified cDNA to identify new alleles RT in the DR52-associated DRB1 group: identification of DRB1*1115, RT DRB1*1117 and DRB1*1319."; RL Tissue Antigens 45:302-308(1995). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-130 (ALLELE DRB1*13:04). RX PubMed=2212675; RA Lee K.W., Johnson A.H., Hurley C.K.; RT "Two divergent routes of evolution gave rise to the DRw13 RT haplotypes."; RL J. Immunol. 145:3119-3125(1990). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB1*13:87). RA Ogrzewalla K., Tillmann G., Scheibelhut N., Lauber J., Enczmann J.; RT "A novel HLA-DRB1*13 allele identified by sequence-based typing."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-216 (ALLELES DRB1*13:03; RP DRB1*13:06; DRB1*13:08; DRB1*13:10; DRB1*13:11; DRB1*13:14; RP DRB1*13:17; DRB1*13:20; DRB1*13:29 AND DRB1*13:36). RC TISSUE=Peripheral blood; RX PubMed=17767557; DOI=10.1111/j.1399-0039.2007.00918.x; RA Horn P.A., Albis-Camps M., Verboom M., Bunce M., Yousaf K., RA Williams S., Blasczyk R.; RT "The nature of diversity of HLA-DRB1 exon 3."; RL Tissue Antigens 70:335-337(2007). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-124 (ALLELE DRB1*13:12). RA Hu C.J.; RT "DR variant with a DR5-like-haplotype found in Taiwan."; RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:18). RX PubMed=8575826; DOI=10.1007/s002510050054; RA Dormoy A., Delbosc A., Galy-Floc'h M., Tongio M.M.; RT "A new HLA-DRB1(*)13 allele (DRB1(*)1318) with a short DRB1(*)08 RT sequence."; RL Immunogenetics 43:240-241(1996). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:22). RX PubMed=9271638; DOI=10.1007/s002510050302; RA Duran K.J., Maeda H., Otten H.G., Vries R.D., Schreuder G.M., RA Tilanus M.G.; RT "Two newly identified HLA-DRB1 alleles: DRB1*1322 and DRB1*1327."; RL Immunogenetics 46:442-443(1997). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*13:42 AND RP DRB1*13:43), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELES RP DRB1*13:35; DRB1*13:37 AND DRB1*13:49), AND NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 35-115 (ALLELE DRB1*13:38). RX PubMed=11972885; DOI=10.1034/j.1399-0039.2002.590115.x; RA Tang T.F., Lin Y.-S., Robbins F.M., Li L., Sintasath D., RA Coquillard G., Huang A., Heine U., Ng J., Hartzman R.J., Hurley C.K.; RT "Description of fourteen new DRB alleles found in a stem cell donor RT registry."; RL Tissue Antigens 59:63-65(2002). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:46). RX PubMed=12028548; DOI=10.1034/j.1399-0039.2002.590217.x; RA Greville W.D., Chapman G., Hogbin J.-P., Kennedy A., Dunckley H.; RT "Novel HLA-DRB1 alleles discovered during routine sequencing based RT typing, DRB1*03052, DRB1*04032, DRB1*1139 and DRB1*1346."; RL Tissue Antigens 59:154-156(2002). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:44). RX PubMed=12028549; DOI=10.1034/j.1399-0039.2002.590218.x; RA Kennedy A., Le T., Chapman G., Greville W.D., Dunckley H.; RT "Identification of two new HLA-DRB1 alleles, DRB1*1138 and RT DRB1*1344."; RL Tissue Antigens 59:157-158(2002). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:60). RX PubMed=15140048; DOI=10.1111/j.0001-2815.2004.00226.x; RA Testa G.V., Bunce M., Sheldon M.H., Dunn P.P., Day S., Marques S.B.; RT "Identification of a new allele, HLA-DRB1*1360, on a DRB5 haplotype in RT a Brazilian individual."; RL Tissue Antigens 63:617-618(2004). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:57). RX PubMed=15245379; DOI=10.1111/j.1399-0039.2004.00261.x; RA Danzer M., Leitner D., Gangl E., Fae I., Fischer G.F., Gabriel C.; RT "A novel HLA-DRB1*13 allele (DRB1*1357) identified by polymerase chain RT reaction with sequence-specific primers and direct sequencing."; RL Tissue Antigens 64:213-214(2004). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:50). RX PubMed=15304013; DOI=10.1111/j.0001-2815.2004.00282.x; RA Chen Z.X., Tsan S.G., Dang C.W., Chu C.C., Lin M., Lee Y.J.; RT "Identification of two new HLA-DRB1 alleles: HLA-DRB1*1350 and RT DRB1*140502."; RL Tissue Antigens 64:300-303(2004). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:51). RX PubMed=15304015; DOI=10.1111/j.0001-2815.2004.00275.x; RA Chu C.C., Lee H.L., Hsieh N.K., Trejaut J., Lin M.; RT "Two novel HLA-DRB1 alleles identified using a sequence-based typing: RT HLA-DRB1*1443 and HLA-DRB1*1351*."; RL Tissue Antigens 64:308-310(2004). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:66). RX PubMed=15982265; DOI=10.1111/j.1399-0039.2005.00427.x; RA Milia S., Lai S., Valentini T., Testi M., Cappai L., Moscetti A., RA Mariani M., Alba F., Carcassi C.; RT "Identification of a new allele, HLA-DRB1*1366*."; RL Tissue Antigens 66:69-71(2005). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:64). RC TISSUE=Peripheral blood; RX PubMed=16029439; DOI=10.1111/j.1399-0039.2005.00440.x; RA Czachurski D., Scollo A., Skambraks A., Perichon A.M., Scherer S., RA Tran T.H., Opelz G., Grappiolo I., Mytilineos J.; RT "Description and characterization of two new HLA alleles, B*4051 and RT DRB1*1364, identified by sequence-based typing."; RL Tissue Antigens 66:151-155(2005). RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:68). RX PubMed=16101838; DOI=10.1111/j.1399-0039.2005.00451.x; RA Caggiari L., Simula M.P., Marzotto A., Caragnano A., Luchetti M., RA Gabrielli A., De Re V.; RT "Identification of a novel human DRB1*13 allele by sequence-based DRB RT typing."; RL Tissue Antigens 66:246-247(2005). RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:70). RC TISSUE=Peripheral blood; RX PubMed=16634878; DOI=10.1111/j.1399-0039.2006.00580.x; RA Horn P.A., Zingsem J., Eckstein R., Blasczyk R.; RT "Novel HLA-DRB1*1370 allele identified in a cord blood donor and her RT mother."; RL Tissue Antigens 67:345-347(2006). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:77). RC TISSUE=Blood; RA Tavoularis S., Conrod V., Ribeiro E.; RT "Identification of three novel DRB1 alleles."; RL Hum. Immunol. 68:S63-S63(2007). RN [27] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:75). RX PubMed=17257328; DOI=10.1111/j.1399-0039.2006.00750.x; RA Sanchez-Gordo F., Balas A., Ortiz M., Prat I., Vicario J.L.; RT "A new human leukocyte antigen DRB1 allele, HLA-DRB1*1375."; RL Tissue Antigens 69:204-205(2007). RN [28] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:71). RX PubMed=17493158; DOI=10.1111/j.1399-0039.2006.00753.x; RA McWhinnie A.J., Shah A., Peat J., Tavarozzi F., Little A.M.; RT "Description of HLA-DRB1*1371 allele, which has the 3' intron 1 RT sequence and HLA-DQB1 association normally seen with a DRB1*0301 RT allele."; RL Tissue Antigens 69:284-285(2007). RN [29] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:76). RX PubMed=17498272; DOI=10.1111/j.1399-0039.2007.00835.x; RA Abdeen H., McErlean C., Moraes M.E., Torres M., Campiotto S., RA Galvao S., Gouvea C., Middleton D.; RT "Identification of three novel alleles of HLA-DRB1 and HLA-A in the RT Brazilian population."; RL Tissue Antigens 69:607-610(2007). RN [30] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:82). RC TISSUE=Blood; RX PubMed=19744147; DOI=10.1111/j.1399-0039.2009.01334.x; RA Anholts J.D., Aneq M., Dirks H.L., Tas A., Verduyn W., Oudshoorn M.; RT "Thirty-six novel HLA alleles: 7 HLA-A, 11 HLA-B, 15 HLA-C and 3 HLA- RT DRB1."; RL Tissue Antigens 74:424-428(2009). RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:32). RC TISSUE=Peripheral blood; RA Lester S., Laham N., Humphreys I., McCluskey J.; RT "A new DRB1*13 allele detected by PCR-SSOP and confirmed by RT sequencing."; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:34). RA Erne G., Schmid C., Schwarz K., Woelpl A.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [33] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:39). RA Park M.H., Whang D.H., Kang S.J.; RT "A new HLA-DRB1*13 allele in a Korean individual."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [34] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:14). RC TISSUE=Peripheral blood; RA Guttridge M.G.; RT "Sequence confirmation of HLA-DRB1*1314."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [35] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:41). RA Bois M., Dormoy A., Alcalay D.; RT "Characterization of a new HLA-DRB1*13 class II allele."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [36] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:48). RC TISSUE=Peripheral blood; RA Moine A.; RT "A new HLA DRB1* allele close to DRB1*1304."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [37] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:47). RA Kashiwase K., Shimizu M., Juji T., Tanaka H., Ishikawa Y.; RT "HLA-DRB1-1307V for exon2."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [38] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:07). RA Tamouza R., Keyhani M., Poirier J.C., Schaeffer V., Fortier C., RA Labie D., Charron D.; RT "New HLA-DRB1*13."; RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases. RN [39] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:01). RA Voorter C.E., van den Berg-Loonen E.M.; RT "New HLA DRB1*13 allele identified by sequence-based typing."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [40] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*13:01 AND RP DRB1*13:16). RA Rizzo M., Gedil M.A., Steiner N.K., Hurley C.K.; RT "Complete exon 2 sequence for HLA-DRB1*1316."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [41] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:69). RA Rodriguez-Marino S., Coquillard G.J.; RT "Novel HLA-DRB1*1301 Variant."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [42] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:58). RA Chen D.-F., Dong L., Janzen M., Rabson A., Fraser P.; RT "Novel HLA-DRB1*13 alleles detected by PCR-SSOP and confirmed by RT single allele specific sequencing."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [43] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:54). RA Ono A.; RT "A new HLA-DR12V allele detected by PCR-RFLP."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [44] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:61). RA Lazaro A.M., Gedil M.A., Rizzo M., Hurley C.K.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [45] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*13:62 AND RP DRB1*13:63). RA Hirv K., Krauss A., Schwarz K.; RT "Characterization of a new HLA-DRB1 allele by direct sequencing."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [46] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:59). RA Bendukidze N.; RT "Rare DRB1*1359 alleles confirmatory testing."; RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases. RN [47] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:65). RA Czachurski D.; RT "Hochaufloesende Typisierung von HLA-Klasse I und Klasse II mittels RT Sequenzanalyse. Einfluss auf das Transplantatueberleben."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [48] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:67). RC TISSUE=Peripheral blood; RA Binder T.M.C., Mosebach M., Kuehnl P., Heim M.U., Blasczyk R., RA Eiermann T.H.; RT "A new HLA-DRB1*13 variant similar to DRB1*130201 and DRB3*020101."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [49] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:74). RC TISSUE=Peripheral blood; RA Dunne C., Crowley J.; RT "Sequence of new HLA-DRB1*13 allele DRB1*13XX."; RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases. RN [50] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:79). RC TISSUE=Blood; RA Duignan P., Varney M., Holdsworth R.; RT "New DRB1*13 allele found in cord blood."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [51] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:78). RA Moore J., Bowman S., Varney M., Tait B.; RT "New HLA DR13 sequence found in bone marrow donor."; RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases. RN [52] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*13:83). RA Horn P.A., Blasczyk R.; RT "A novel HLA-DRB1*13 allele."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. RN [53] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*13:31; RP DRB1*13:72; DRB1*13:73; DRB1*13:80; DRB1*13:81; DRB1*13:84; RP DRB1*13:85; DRB1*13:86 AND DRB1*13:88). RA Lazaro A.M., Xiao Y., Cao K., Shan X., Zhang B., Masaberg C., RA Hurley C.K.; RT "Novel HLA-class II allele."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [54] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELES DRB1*13:23 AND RP DRB1*13:24). RX PubMed=9243754; DOI=10.1111/j.1399-0039.1997.tb02832.x; RA Ellis J.M., Robbins F., Wang J., Tang T., Heine U., Mason J.M., RA Sese D., Milford E., Hurley C.K.; RT "Identification of four new DR52-associated DRB1 alleles: DRB1*1424, RT *1425, *1323 and *1324."; RL Tissue Antigens 50:42-46(1997). RN [55] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-120 (ALLELE DRB1*13:13). RC TISSUE=Blood; RA Hurley C.K., Noreen H., Lin Y.S.; RT "DRB1*1313."; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [56] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-120 (ALLELE DRB1*13:52). RA Rodriguez-Marino S., Coquillard G.; RT "Characterization of a new DRB1*13011 variant allele."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [57] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-116 (ALLELE DRB1*13:25). RX PubMed=9008317; DOI=10.1111/j.1399-0039.1996.tb02698.x; RA Poli F., Bianchi P., Crespiatico L., Sirchia G.; RT "Identification of a new DRB1 allele (DRB1*1325) by PCR-SSP and DNA RT sequencing."; RL Tissue Antigens 48:714-716(1996). RN [58] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB1*13:33). RC TISSUE=Blood; RX PubMed=9694360; DOI=10.1111/j.1399-0039.1998.tb03010.x; RA Buyse I.M., Ouellet S., Hashemi-Tavoularis S.; RT "Identification of novel DRB1*13 (DRB1*1333), DRB1*04 (DRB1*0426) and RT DRB5* (DRB5*0109) alleles."; RL Tissue Antigens 51:658-662(1998). RN [59] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELE DRB1*13:40). RC TISSUE=Cervix; RX PubMed=11019927; DOI=10.1034/j.1399-0039.2000.560218.x; RA Maciag P.C., Junes K.S., Villa L.L., Petzl-Erler M.L.; RT "Identification of a novel allele, DRB1*1340, in two Brazilian RT individuals."; RL Tissue Antigens 56:194-196(2000). RN [60] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELE DRB1*13:53). RC TISSUE=Peripheral blood; RA Poli F., Longhi E., Frison S.; RT "Identification of a new HLA DRB1*13 by SBT."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [61] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELES DRB1*13:15 AND RP DRB1*13:55). RA Lo B.; RT "Confirmatory Sequence of HLA Class II DRB1*1315."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [62] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-120 (ALLELE DRB1*13:09). RC TISSUE=Blood; RX PubMed=8023320; DOI=10.1111/j.1399-0039.1994.tb02298.x; RA Yunis J.J., Kineke E., Yunis E.J.; RT "Characterization of a new DRB1 allele, DRB1*1309, by PCR-SSOP and RT sequencing."; RL Tissue Antigens 43:54-57(1994). RN [63] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB1*13:30). RA Greville W.D., Bowman S.; RT "New HLA class II (DRB1) allele from Melbourne BTS."; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [64] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-119 (ALLELE DRB1*13:28). RA Varney M.D., Tait B.D.; RT "Identification of a novel DPB allele."; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [65] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB1*13:26). RX PubMed=9027974; DOI=10.1111/j.1399-0039.1997.tb02718.x; RA Voorter C.E.M., de Bruyn-Geraets D., Verduyn W., Schreuder G.M.T., RA van den Berg-Loonen E.M.; RT "Identification of a new HLA-DRB1*13 allele (DRB1*1326) with a short RT DRB1*16 sequence."; RL Tissue Antigens 49:88-91(1997). RN [66] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB1*13:45). RX PubMed=12028550; DOI=10.1034/j.1399-0039.2002.590219.x; RA Bengtsson M., Jansson I.E., Danielsson F., Henrysson H., Kallsten K.; RT "Identification of a novel HLA DRB1 exon 2 sequence, DRB1*1345."; RL Tissue Antigens 59:159-161(2002). RN [67] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [68] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [69] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [70] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [71] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [72] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [73] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-13 are known: CC DRB1*13:01, DRB1*13:02, DRB1*13:03, DRB1*13:04, DRB1*13:05, CC DRB1*13:06, DRB1*13:07, DRB1*13:08, DRB1*13:09, DRB1*13:10, CC DRB1*13:11, DRB1*13:12, DRB1*13:13, DRB1*13:14, DRB1*13:15, CC DRB1*13:16, DRB1*13:17, DRB1*13:18, DRB1*13:19, DRB1*13:20, CC DRB1*13:21, DRB1*13:22, DRB1*13:23, DRB1*13:24, DRB1*13:25, CC DRB1*13:26, DRB1*13:27, DRB1*13:28, DRB1*13:29, DRB1*13:30, CC DRB1*13:31, DRB1*13:32, DRB1*13:33, DRB1*13:34, DRB1*13:35, CC DRB1*13:36, DRB1*13:37, DRB1*13:38, DRB1*13:39, DRB1*13:40, CC DRB1*13:41, DRB1*13:42, DRB1*13:43, DRB1*13:44, DRB1*13:45, CC DRB1*13:46, DRB1*13:47, DRB1*13:48, DRB1*13:49, DRB1*13:50, CC DRB1*13:51, DRB1*13:52, DRB1*13:53, DRB1*13:54, DRB1*13:55, CC DRB1*13:56, DRB1*13:57, DRB1*13:58, DRB1*13:59, DRB1*13:60, CC DRB1*13:61, DRB1*13:62, DRB1*13:63, DRB1*13:64, DRB1*13:65, CC DRB1*13:66, DRB1*13:67, DRB1*13:68, DRB1*13:69, DRB1*13:70, CC DRB1*13:71, DRB1*13:72, DRB1*13:73, DRB1*13:74, DRB1*13:75, CC DRB1*13:76, DRB1*13:77, DRB1*13:78, DRB1*13:79, DRB1*13:80, CC DRB1*13:81, DRB1*13:82, DRB1*13:83, DRB1*13:84, DRB1*13:85, CC DRB1*13:86, DRB1*13:87 and DRB1*13:88. The sequence shown is that CC of DRB1*13:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB40418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY663413; AAU88029.1; -; Genomic_DNA. DR EMBL; AY663415; AAU88035.1; -; Genomic_DNA. DR EMBL; AJ697893; CAG27026.1; -; mRNA. DR EMBL; AY961069; AAX63457.1; -; mRNA. DR EMBL; AY961070; AAX63458.2; -; mRNA. DR EMBL; L76133; AAL40069.1; -; mRNA. DR EMBL; AK293020; BAF85709.1; -; mRNA. DR EMBL; BC007920; AAH07920.1; -; mRNA. DR EMBL; L41992; AAA65914.1; -; Genomic_DNA. DR EMBL; U17381; AAC50167.1; -; mRNA. DR EMBL; M59803; AAA64237.1; -; mRNA. DR EMBL; FM196526; CAQ86517.1; -; Genomic_DNA. DR EMBL; AM109988; CAJ33595.1; -; Genomic_DNA. DR EMBL; AM109989; CAJ33596.1; -; Genomic_DNA. DR EMBL; AM109990; CAJ33597.1; -; Genomic_DNA. DR EMBL; AM109991; CAJ33598.1; -; Genomic_DNA. DR EMBL; AM109992; CAJ33599.1; -; Genomic_DNA. DR EMBL; AM109993; CAJ33600.1; -; Genomic_DNA. DR EMBL; AM109994; CAJ33601.1; -; Genomic_DNA. DR EMBL; AM109995; CAJ33602.1; -; Genomic_DNA. DR EMBL; AM109996; CAJ33603.1; -; Genomic_DNA. DR EMBL; AM109997; CAJ33604.1; -; Genomic_DNA. DR EMBL; D29836; BAA06216.1; -; Genomic_DNA. DR EMBL; Z48631; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X86326; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF136155; AAD27646.1; -; Genomic_DNA. DR EMBL; AF164346; AAD47814.1; -; Genomic_DNA. DR EMBL; AF169239; AAD51315.1; -; Genomic_DNA. DR EMBL; AF243537; AAG00414.1; -; Genomic_DNA. DR EMBL; AF243538; AAG00415.1; -; Genomic_DNA. DR EMBL; AF352295; AAK27712.1; -; Genomic_DNA. DR EMBL; AF306862; AAG42258.1; -; Genomic_DNA. DR EMBL; AF247533; AAF99607.1; -; Genomic_DNA. DR EMBL; AY178845; AAO18733.1; -; Genomic_DNA. DR EMBL; AJ555156; CAD87537.1; -; Genomic_DNA. DR EMBL; AY048687; AAL12226.1; -; Genomic_DNA. DR EMBL; AF441789; AAL35834.1; -; Genomic_DNA. DR EMBL; AY765349; AAV35213.1; -; Genomic_DNA. DR EMBL; AJ634529; CAG25408.1; -; Genomic_DNA. DR EMBL; AY963587; AAX51706.1; -; Genomic_DNA. DR EMBL; AM086025; CAJ30431.1; -; Genomic_DNA. DR EMBL; AM494414; CAM36736.1; -; Genomic_DNA. DR EMBL; EF053230; ABK33462.1; -; Genomic_DNA. DR EMBL; AM158254; CAJ43560.1; -; Genomic_DNA. DR EMBL; EF196873; ABM69041.1; -; Genomic_DNA. DR EMBL; AM904556; CAP17407.1; -; Genomic_DNA. DR EMBL; U97554; AAB58309.1; -; Genomic_DNA. DR EMBL; AF048688; AAC05271.1; -; Genomic_DNA. DR EMBL; AF170582; AAD50971.1; -; Genomic_DNA. DR EMBL; AJ245717; CAB53346.1; -; Genomic_DNA. DR EMBL; AJ249591; CAB56840.1; -; Genomic_DNA. DR EMBL; AJ401236; CAB96577.1; -; Genomic_DNA. DR EMBL; AB049459; BAB16298.1; -; Genomic_DNA. DR EMBL; AF305212; AAG22826.1; -; Genomic_DNA. DR EMBL; AJ271206; CAC27122.1; -; Genomic_DNA. DR EMBL; AY178184; AAO21939.1; -; Genomic_DNA. DR EMBL; AY277392; AAP34696.1; -; Genomic_DNA. DR EMBL; AY225520; AAO67727.1; -; Genomic_DNA. DR EMBL; AY259126; AAP21612.1; -; Genomic_DNA. DR EMBL; AB112913; BAD02944.1; -; Genomic_DNA. DR EMBL; AY339247; AAQ18914.1; -; Genomic_DNA. DR EMBL; AY379480; AAQ85128.1; -; Genomic_DNA. DR EMBL; AY502108; AAR89455.1; -; Genomic_DNA. DR EMBL; AJ627565; CAF28889.1; -; Genomic_DNA. DR EMBL; AJ783982; CAH04455.1; -; Genomic_DNA. DR EMBL; AJ853708; CAH68606.1; -; Genomic_DNA. DR EMBL; AM279417; CAK50561.1; -; Genomic_DNA. DR EMBL; EF493833; ABP68561.1; -; Genomic_DNA. DR EMBL; EF493832; ABP68560.1; -; Genomic_DNA. DR EMBL; AM931066; CAP62371.1; -; Genomic_DNA. DR EMBL; DQ473293; ABF18979.1; -; Genomic_DNA. DR EMBL; DQ514602; ABF60565.1; -; Genomic_DNA. DR EMBL; DQ525629; ABF74594.1; -; Genomic_DNA. DR EMBL; EU029803; ABU86862.1; -; Genomic_DNA. DR EMBL; EU071684; ABS87343.1; -; Genomic_DNA. DR EMBL; EU812541; ACE88700.1; -; Genomic_DNA. DR EMBL; EU826130; ACF36162.1; -; Genomic_DNA. DR EMBL; EU826129; ACF36161.1; -; Genomic_DNA. DR EMBL; FJ688163; ACN56340.1; -; Genomic_DNA. DR EMBL; U36827; AAC51629.1; -; Genomic_DNA. DR EMBL; U36825; AAC51628.1; -; Genomic_DNA. DR EMBL; U79025; AAB52235.1; -; Genomic_DNA. DR EMBL; AF499445; AAP68877.1; -; Genomic_DNA. DR EMBL; X93924; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ001254; CAA04628.1; -; Genomic_DNA. DR EMBL; AJ237964; CAB40418.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ488066; CAD32373.1; -; Genomic_DNA. DR EMBL; AY174182; AAO17054.1; -; Genomic_DNA. DR EMBL; AY179366; AAO23237.1; -; Genomic_DNA. DR EMBL; L23534; AAA62591.1; -; Genomic_DNA. DR EMBL; U72264; AAB17276.1; -; Genomic_DNA. DR EMBL; X97407; CAA66060.1; -; Genomic_DNA. DR EMBL; X96396; CAA65260.1; -; Genomic_DNA. DR EMBL; AJ276873; CAB82169.1; -; Genomic_DNA. DR PIR; D25239; D25239. DR PIR; I38899; I38899. DR PIR; I59647; I59647. DR PIR; I72484; I72484. DR PIR; PH0155; PH0155. DR PIR; S03439; S03439. DR UniGene; Hs.485130; -. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q5Y7A7; -. DR SMR; Q5Y7A7; -. DR IntAct; Q5Y7A7; 1. DR ChEMBL; CHEMBL3988561; -. DR DMDM; 74757225; -. DR EPD; Q5Y7A7; -. DR MaxQB; Q5Y7A7; -. DR PeptideAtlas; Q5Y7A7; -. DR PRIDE; Q5Y7A7; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR Ensembl; ENST00000415796; ENSP00000412168; ENSG00000206306. DR Ensembl; ENST00000428566; ENSP00000392280; ENSG00000206240. DR DisGeNET; 3123; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_Q5Y7A7; -. DR HOVERGEN; HBG012730; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-13 beta chain. FT /FTId=PRO_0000392290. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P20039}. FT VARIANT 39 39 Y -> L (in allele DRB1*13:67; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062866. FT VARIANT 40 40 S -> L (in allele DRB1*13:67). FT /FTId=VAR_062867. FT VARIANT 41 41 T -> K (in allele DRB1*13:67). FT /FTId=VAR_062868. FT VARIANT 42 42 S -> G (in allele DRB1*13:17). FT /FTId=VAR_062869. FT VARIANT 45 45 H -> Q (in allele DRB1*13:72). FT /FTId=VAR_062871. FT VARIANT 45 45 H -> Y (in allele DRB1*13:17). FT /FTId=VAR_062870. FT VARIANT 54 54 R -> L (in allele DRB1*13:73). FT /FTId=VAR_062872. FT VARIANT 55 55 F -> Y (in allele DRB1*13:27, allele FT DRB1*13:41 and allele DRB1*13:71). FT /FTId=VAR_062873. FT VARIANT 56 56 L -> Q (in allele DRB1*13:59). FT /FTId=VAR_062874. FT VARIANT 57 57 D -> E (in allele DRB1*13:15, allele FT DRB1*13:19, allele DRB1*13:26, allele FT DRB1*13:53, allele DRB1*13:57, allele FT DRB1*13:85 and allele DRB1*13:86). FT /FTId=VAR_062875. FT VARIANT 61 61 H -> Y (in allele DRB1*13:03, allele FT DRB1*13:07, allele DRB1*13:04, allele FT DRB1*13:11, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:14, allele FT DRB1*13:17, allele DRB1*13:21, allele FT DRB1*13:22, allele DRB1*13:23, allele FT DRB1*13:24, allele DRB1*13:25, allele FT DRB1*13:30, allele DRB1*13:33, allele FT DRB1*13:37, allele DRB1*13:38, allele FT DRB1*13:44, allele DRB1*13:45, allele FT DRB1*13:46, allele DRB1*13:47, allele FT DRB1*13:48, allele DRB1*13:49, allele FT DRB1*13:50, allele DRB1*13:54, allele FT DRB1*13:55, allele DRB1*13:58, allele FT DRB1*13:60, allele DRB1*13:62, allele FT DRB1*13:66, allele DRB1*13:69, allele FT DRB1*13:70, allele DRB1*13:75, allele FT DRB1*13:81, allele DRB1*13:82, allele FT DRB1*13:86 and allele DRB1*13:88). FT /FTId=VAR_062876. FT VARIANT 66 66 N -> D (in allele DRB1*13:62 and allele FT DRB1*13:68). FT /FTId=VAR_062880. FT VARIANT 66 66 N -> F (in allele DRB1*13:08, allele FT DRB1*13:19, allele DRB1*13:57, allele FT DRB1*13:64, allele DRB1*13:72, allele FT DRB1*13:76 and allele DRB1*13:83; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062878. FT VARIANT 66 66 N -> I (in allele DRB1*13:87). FT /FTId=VAR_062881. FT VARIANT 66 66 N -> S (in allele DRB1*13:60 and allele FT DRB1*13:84). FT /FTId=VAR_062879. FT VARIANT 66 66 N -> Y (in allele DRB1*13:03, allele FT DRB1*13:07, allele DRB1*13:04, allele FT DRB1*13:11, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:14, allele FT DRB1*13:17, allele DRB1*13:21, allele FT DRB1*13:22, allele DRB1*13:23, allele FT DRB1*13:24, allele DRB1*13:25, allele FT DRB1*13:30, allele DRB1*13:33, allele FT DRB1*13:37, allele DRB1*13:38, allele FT DRB1*13:44, allele DRB1*13:45, allele FT DRB1*13:46, allele DRB1*13:47, allele FT DRB1*13:48, allele DRB1*13:49, allele FT DRB1*13:52, allele DRB1*13:54, allele FT DRB1*13:55, allele DRB1*13:58, allele FT DRB1*13:66, allele DRB1*13:70, allele FT DRB1*13:75, allele DRB1*13:81, allele FT DRB1*13:82, allele DRB1*13:86 and allele FT DRB1*13:88). FT /FTId=VAR_062877. FT VARIANT 67 67 V -> L (in allele DRB1*13:34, allele FT DRB1*13:62 and allele DRB1*13:64). FT /FTId=VAR_062882. FT VARIANT 76 76 F -> Y (in allele DRB1*13:03, allele FT DRB1*13:07, allele DRB1*13:08, allele FT DRB1*13:12, allele DRB1*13:13, allele FT DRB1*13:19, allele DRB1*13:26, allele FT DRB1*13:32, allele DRB1*13:33, allele FT DRB1*13:36, allele DRB1*13:37, allele FT DRB1*13:38, allele DRB1*13:40, allele FT DRB1*13:47, allele DRB1*13:48, allele FT DRB1*13:49, allele DRB1*13:53, allele FT DRB1*13:55, allele DRB1*13:58, allele FT DRB1*13:60, allele DRB1*13:65, allele FT DRB1*13:70, allele DRB1*13:72, allele FT DRB1*13:76, allele DRB1*13:81, allele FT DRB1*13:84, allele DRB1*13:85 and allele FT DRB1*13:88). FT /FTId=VAR_062883. FT VARIANT 77 77 R -> L (in allele DRB1*13:35). FT /FTId=VAR_062884. FT VARIANT 77 77 R -> W (in allele DRB1*13:80). FT /FTId=VAR_062885. FT VARIANT 79 79 V -> L (in allele DRB1*13:51). FT /FTId=VAR_062886. FT VARIANT 86 86 D -> A (in allele DRB1*13:43 and allele FT DRB1*13:45). FT /FTId=VAR_062889. FT VARIANT 86 86 D -> S (in allele DRB1*13:03, allele FT DRB1*13:04, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:21, allele FT DRB1*13:30, allele DRB1*13:32, allele FT DRB1*13:33, allele DRB1*13:38, allele FT DRB1*13:48, allele DRB1*13:49, allele FT DRB1*13:55, allele DRB1*13:58, allele FT DRB1*13:65, allele DRB1*13:66, allele FT DRB1*13:75, allele DRB1*13:81 and allele FT DRB1*13:88; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062887. FT VARIANT 86 86 D -> V (in allele DRB1*13:31, allele FT DRB1*13:46, allele DRB1*13:54 and allele FT DRB1*13:77). FT /FTId=VAR_062888. FT VARIANT 89 89 Y -> H (in allele DRB1*13:43 and allele FT DRB1*13:45). FT /FTId=VAR_062891. FT VARIANT 89 89 Y -> S (in allele DRB1*13:39, allele FT DRB1*13:54, allele DRB1*13:77, allele FT DRB1*13:78 and allele DRB1*13:79). FT /FTId=VAR_062890. FT VARIANT 96 96 I -> F (in allele DRB1*13:07, allele FT DRB1*13:05, allele DRB1*13:11, allele FT DRB1*13:14, allele DRB1*13:18, allele FT DRB1*13:21, allele DRB1*13:24, allele FT DRB1*13:26, allele DRB1*13:42, allele FT DRB1*13:46, allele DRB1*13:47, allele FT DRB1*13:49, allele DRB1*13:50, allele FT DRB1*13:54, allele DRB1*13:55, allele FT DRB1*13:62, allele DRB1*13:63 and allele FT DRB1*13:75). FT /FTId=VAR_062892. FT VARIANT 96 96 I -> L (in allele DRB1*13:20, allele FT DRB1*13:25, allele DRB1*13:29, allele FT DRB1*13:43, allele DRB1*13:44, allele FT DRB1*13:56, allele DRB1*13:60, allele FT DRB1*13:71, allele DRB1*13:78, allele FT DRB1*13:86 and allele DRB1*13:88). FT /FTId=VAR_062893. FT VARIANT 97 97 L -> R (in allele DRB1*13:74). FT /FTId=VAR_062894. FT VARIANT 99 99 D -> Q (in allele DRB1*13:09, allele FT DRB1*13:44 and allele DRB1*13:86; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062895. FT VARIANT 100 100 E -> A (in allele DRB1*13:09). FT /FTId=VAR_062898. FT VARIANT 100 100 E -> K (in allele DRB1*13:03, allele FT DRB1*13:10, allele DRB1*13:33, allele FT DRB1*13:37, allele DRB1*13:66, allele FT DRB1*13:81, allele DRB1*13:85 and allele FT DRB1*13:88). FT /FTId=VAR_062897. FT VARIANT 100 100 E -> R (in allele DRB1*13:07, allele FT DRB1*13:05, allele DRB1*13:06, allele FT DRB1*13:11, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:14, allele FT DRB1*13:18, allele DRB1*13:21, allele FT DRB1*13:25, allele DRB1*13:26, allele FT DRB1*13:30, allele DRB1*13:42, allele FT DRB1*13:44, allele DRB1*13:46, allele FT DRB1*13:47, allele DRB1*13:49, allele FT DRB1*13:50, allele DRB1*13:55, allele FT DRB1*13:56, allele DRB1*13:58, allele FT DRB1*13:60, allele DRB1*13:62, allele FT DRB1*13:77, allele DRB1*13:82 and allele FT DRB1*13:86; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062896. FT VARIANT 103 103 A -> E (in allele DRB1*13:76). FT /FTId=VAR_062900. FT VARIANT 103 103 A -> L (in allele DRB1*13:13, allele FT DRB1*13:18, allele DRB1*13:47 and allele FT DRB1*13:55; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062899. FT VARIANT 106 106 T -> N (in allele DRB1*13:33 and allele FT DRB1*13:61). FT /FTId=VAR_062901. FT VARIANT 113 113 G -> R (in allele DRB1*13:28). FT /FTId=VAR_062902. FT VARIANT 114 114 V -> A (in allele DRB1*13:58 and allele FT DRB1*13:81). FT /FTId=VAR_062903. FT VARIANT 115 115 V -> D (in allele DRB1*13:16). FT /FTId=VAR_062905. FT VARIANT 115 115 V -> G (in allele DRB1*13:02, allele FT DRB1*13:03, allele DRB1*13:07, allele FT DRB1*13:05, allele DRB1*13:12, allele FT DRB1*13:13, allele DRB1*13:14, allele FT DRB1*13:21, allele DRB1*13:23, allele FT DRB1*13:25, allele DRB1*13:26, allele FT DRB1*13:29, allele DRB1*13:30, allele FT DRB1*13:31, allele DRB1*13:33, allele FT DRB1*13:34, allele DRB1*13:36, allele FT DRB1*13:37, allele DRB1*13:38, allele FT DRB1*13:39, allele DRB1*13:41, allele FT DRB1*13:45, allele DRB1*13:46, allele FT DRB1*13:47, allele DRB1*13:49, allele FT DRB1*13:50, allele DRB1*13:55, allele FT DRB1*13:56, allele DRB1*13:60, allele FT DRB1*13:62, allele DRB1*13:63, allele FT DRB1*13:65, allele DRB1*13:66, allele FT DRB1*13:67, allele DRB1*13:73, allele FT DRB1*13:74, allele DRB1*13:82, allele FT DRB1*13:85, allele DRB1*13:86 and allele FT DRB1*13:88). FT /FTId=VAR_062904. FT CONFLICT 104 104 V -> L (in Ref. 46; CAA04628). FT {ECO:0000305}. FT CONFLICT 121 121 Q -> H (in Ref. 25; AAC05271). FT {ECO:0000305}. FT CONFLICT 124 124 V -> G (in Ref. 11; BAA06216). FT {ECO:0000305}. SQ SEQUENCE 266 AA; 30008 MW; 17731F784445CC39 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRFLDRYF HNQEENVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEDE RAAVDTYCRH NYGVVESFTV QRRVHPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B1E_HUMAN Reviewed; 266 AA. AC Q9GIY3; A0N0W1; A2TGX3; A4ZY86; A5H000; A5HKN8; A7DZP9; A7X5B1; AC A7X5B7; A7X5E0; A7X5E6; A7X5H8; A9JPG0; B1GWE7; B2CR03; B2LVF9; AC B2NJ29; B2ZCY1; B3VTP8; B5B8U0; B5B9V5; B5LZ25; B6VEL9; B9VRA4; AC B9X248; O02876; O46793; O77969; O78210; Q0PQ39; Q155F7; Q1AP33; AC Q1JRP3; Q27PR6; Q27PR7; Q29734; Q29770; Q29772; Q29800; Q2A120; AC Q2HZE5; Q2LE76; Q2MJA6; Q2VQU1; Q307W5; Q31636; Q3LA87; Q3LA88; AC Q3LA89; Q3LA90; Q3LA91; Q3LA92; Q3T919; Q4PRC3; Q4PRC5; Q4VZY7; AC Q56FP1; Q5BM92; Q5U9W6; Q683P7; Q70GL2; Q7YNY9; Q7YQA5; Q860D8; AC Q860D9; Q860S0; Q861H5; Q861H7; Q8MH59; Q8MH60; Q8WLU3; Q95348; AC Q95HK1; Q95HL0; Q95IG2; Q9GIL5; Q9GIL6; Q9GIY0; Q9GIY1; Q9GIY2; AC Q9GJ56; Q9GJ57; Q9GJ58; Q9TPB6; Q9TPW1; Q9XRY4; Q9Y4H7; DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 12-SEP-2018, entry version 121. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-14 beta chain; DE AltName: Full=MHC class II antigen DRB1*14; DE Short=DR-14; DE Short=DR14; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*14:05). RX PubMed=12652907; DOI=10.1080/1042517021000041822; RA Kohsaka H., Nasu K., Matsushita S., Miyasaka N.; RT "Complete cDNA coding sequence of the HLA-DRB1*1405 allele."; RL DNA Seq. 13:359-361(2002). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*14:01 AND DRB1*14:04), RP AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-264 (ALLELES DRB1*14:02 AND RP DRB1*14:03). RX PubMed=11972886; DOI=10.1034/j.1399-0039.2002.590116.x; RA Corell A., Cox S.T., Soteriou B., Ramon D., Madrigal J.A., RA Marsh S.G.E.; RT "Complete cDNA sequences of the HLA-DRB1*14011, *1402, *1403 and *1404 RT alleles."; RL Tissue Antigens 59:66-69(2002). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB1*14:05). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*14:11), AND NUCLEOTIDE RP SEQUENCE [MRNA] OF 1-265 (ALLELE DRB1*14:46). RX PubMed=17174751; DOI=10.1016/j.humimm.2006.09.002; RA Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., RA de Pablo R., Garcia-Sanchez F., Vicario J.L.; RT "Group-specific amplification of cDNA from DRB1 genes. Complete coding RT sequences of partially defined alleles and identification of the new RT alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."; RL Hum. Immunol. 67:1008-1016(2006). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217 (ALLELE DRB1*14:57). RX PubMed=17026471; DOI=10.1111/j.1399-0039.2006.00669.x; RA Chen Q., Zou H., Xu X.H., Luo M., Wang J., Zuo Y.Q., Chen Y.H., RA Chen X.H., Chen X.L., Yao Z.Q., Song N., Zeng J., Mi X.Y., Sun S.X., RA Wang J.X., Zhao T.M.; RT "Characterization of HLA-B*5516, -B*1313, -B*9512, and -DRB1*1457 RT alleles identified in a southwest Chinese population."; RL Tissue Antigens 68:339-343(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-208 (ALLELE DRB1*14:54). RX PubMed=19284446; DOI=10.1111/j.1744-313X.2008.00826.x; RA Yang K.L., Chen M.J., Lee S.K., Lin C.C., Tsai M.J., Chiu H.M., RA Jiang S., Chao Y.C., Chen S.P., Lin S., Shyr M.H., Lin P.Y.; RT "New allele name of some HLA-DRB1*1401: HLA-DRB1*1454."; RL Int. J. Immunogenet. 36:119-120(2009). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-123 (ALLELE DRB1*14:19). RX PubMed=8560458; DOI=10.1111/j.1399-0039.1995.tb02506.x; RA Loeffler D., Woelpl A., Kern P., Eiermann T.H.; RT "A novel HLA-DR allele, DRB1*1419."; RL Tissue Antigens 46:343-344(1995). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB1*14:82). RA Ogrzewalla K., Tillmann G., Scheibelhut N., Lauber J., Enczmann J.; RT "A novel HLA-DRB1*14 allele identified by sequence-based typing."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-216 (ALLELES DRB1*14:06; RP DRB1*14:07; DRB1*14:10; DRB1*14:13; DRB1*14:14 AND DRB1*14:21). RC TISSUE=Peripheral blood; RX PubMed=17767557; DOI=10.1111/j.1399-0039.2007.00918.x; RA Horn P.A., Albis-Camps M., Verboom M., Bunce M., Yousaf K., RA Williams S., Blasczyk R.; RT "The nature of diversity of HLA-DRB1 exon 3."; RL Tissue Antigens 70:335-337(2007). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-124 (ALLELE DRB1*14:85). RA Maruya E., Matsushita M., Saji H., Ounuma T., Futagami T., Kojima H., RA Tujino T., Hayashi K., Kusunoki Y., Yoshida T., Maekawajiri S.; RT "HLA-DR new allele related with DRB1*1403."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:22). RX PubMed=8575830; DOI=10.1007/s002510050058; RA Adami N., Aubert V., Jeannet M., Tiercy J.M.; RT "Sequencing of a new HLA-DR14 allele (DRB1(*)1422)."; RL Immunogenetics 43:248-249(1996). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:36). RX PubMed=10321590; DOI=10.1034/j.1399-0039.1999.530421.x; RA Bodmer J., Marsh S., Albert E., Bodmer W.; RT "Nomenclature for factors of the HLA system, 1998."; RL Tissue Antigens 53:407-446(1999). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:37). RC TISSUE=Blood; RX PubMed=11380954; DOI=10.1034/j.1399-0039.2001.057004384.x; RA Wu S., Shiao Y.M., Lai C.Y., Lai S.M., Chen S.P., Sidebottom D.A., RA Hildebrand W.H., Tilanus M.G.J., Chou F.C., Tsai M.F.; RT "Polymorphism of human HLA-DRB1 antigens generated by genetic exchange RT between DR2 (DRB1*15011) and DR6 (DRB1*1405) alleles: a novel DRB1 RT allele (DRB1*1437) identified in a Paiwan tribe member of Taiwan."; RL Tissue Antigens 57:384-387(2001). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:41), AND RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-123 (ALLELE DRB1*14:42). RX PubMed=12144619; DOI=10.1034/j.1399-0039.2002.590502.x; RA Gans C.P., Tang T.F., Slack R., Ng J., Hartzman R.J., Hurley C.K.; RT "DRB1*14 diversity and DRB3 associations in four major population RT groups in the United States."; RL Tissue Antigens 59:364-369(2002). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:43). RX PubMed=15304015; DOI=10.1111/j.0001-2815.2004.00275.x; RA Chu C.C., Lee H.L., Hsieh N.K., Trejaut J., Lin M.; RT "Two novel HLA-DRB1 alleles identified using a sequence-based typing: RT HLA-DRB1*1443 and HLA-DRB1*1351*."; RL Tissue Antigens 64:308-310(2004). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*14:47 AND RP DRB1*14:48). RX PubMed=16185331; DOI=10.1111/j.1399-0039.2005.00459.x; RA Lazaro A.M., Steiner N.K., Moraes M.E., Moraes J.R., Ng J., RA Hartzman R.J., Hurley C.K.; RT "Ten novel HLA-DRB1 alleles and one novel DRB3 allele."; RL Tissue Antigens 66:327-329(2005). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:50). RC TISSUE=Peripheral blood; RX PubMed=16185333; DOI=10.1111/j.1399-0039.2005.00472a.x; RA Tijssen H.J., Zeeuw van der S.C., Joosten I.; RT "Exon 2 sequence analysis of a novel HLA-DRB1 allele, DRB1*1450."; RL Tissue Antigens 66:332-333(2005). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:49). RX PubMed=16426240; DOI=10.1111/j.1744-313X.2005.00557.x; RA Miao K.R., Xue M., Zhou X.Y., Xu R., Fei X.M., Pan Q.Q., Zhang J.W., RA Zhao X., Fan S., Kukuruga D., Xu A.L., Wang C.Y.; RT "Characterization of a novel DRB1*14 allele (DRB1*1449) in the Han- RT Chinese population."; RL Int. J. Immunogenet. 33:33-35(2006). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:56). RX PubMed=16774552; DOI=10.1111/j.1399-0039.2006.00612.x; RA Baek J.Y., Yun H.S., Hur S.S., Kwon O.J., Kwack K.; RT "Identification of a novel HLA-DRB1*14 allele, DRB1*1456, in the cord RT blood of a Korean baby."; RL Tissue Antigens 68:97-98(2006). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:60). RC TISSUE=Peripheral blood; RX PubMed=17026474; DOI=10.1111/j.1399-0039.2006.00675.x; RA Tijssen H.J., van den Dungen-Toet J.H.G., van Houwelingen K.P., RA Allebes W.A., Joosten I.; RT "Exon 2 sequence analysis of a novel HLA-DRB1 allele, DRB1*1460."; RL Tissue Antigens 68:346-347(2006). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:65). RX PubMed=17498272; DOI=10.1111/j.1399-0039.2007.00835.x; RA Abdeen H., McErlean C., Moraes M.E., Torres M., Campiotto S., RA Galvao S., Gouvea C., Middleton D.; RT "Identification of three novel alleles of HLA-DRB1 and HLA-A in the RT Brazilian population."; RL Tissue Antigens 69:607-610(2007). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:74). RX PubMed=18179646; DOI=10.1111/j.1399-0039.2007.00993.x; RA Rahal M., Kervaire B., Villard J., Tiercy J.M.; RT "DNA typing by microbead arrays and PCR-SSP: apparent false-negative RT or -positive hybridization or amplification signals disclose new HLA-B RT and -DRB1 alleles."; RL Tissue Antigens 71:238-241(2008). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:67). RC TISSUE=Blood; RX PubMed=18643964; DOI=10.1111/j.1399-0039.2008.01089.x; RA Yan L.N., Li S.Y., Dong Z., Dong L., Xie J.H., An S.P., Yuan Y.H.; RT "Sequence-based typing reveals the novel HLA-DRB1*1467 allele in a RT Chinese individual."; RL Tissue Antigens 72:409-410(2008). RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:75). RX PubMed=18937796; DOI=10.1111/j.1399-0039.2008.01116.x; RA Schuett S., Geflitter A., von Baehr V.; RT "Sequence-based typing of a novel HLA-DRB1*14 allele, DRB1*1475, in a RT Caucasian woman."; RL Tissue Antigens 72:501-502(2008). RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:61). RX PubMed=19000132; DOI=10.1111/j.1399-0039.2008.01135.x; RA Wang Z., Shan X., Zhang Z.; RT "Identification of a novel HLA-DRB allele, HLA-DRB1*1461."; RL Tissue Antigens 72:603-604(2008). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:78). RX PubMed=19140840; DOI=10.1111/j.1399-0039.2008.01175.x; RA Han S.H., Jung S.M., Park S.R., Chung S.Y., Han H.; RT "Identification of a new HLA-DRB1*14 variant, HLA-DRB1*1478, in a RT Korean individual."; RL Tissue Antigens 73:81-83(2009). RN [27] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*14:26; RP DRB1*14:27 AND DRB1*14:29). RA Kashiwase K., Tokunaga K., Akaza T., Tadokoro K., Juji T.; RT "Sequence of new allele."; RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases. RN [28] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:32). RA Blasczyk R.; RT "A new HLA-DRB1*14 variant."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [29] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:34). RA Whidborne R.S., Sayer D.C., Christiansen F.T.; RT "Novel DRB1*14 and 15 alleles in the Western Australian population."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [30] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:17). RA Gervais T.G., Latinne D.; RT "Confirmatory sequence for HLA-DRB1*1417 gene obtained by sequence RT based typing."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:18). RA Rizzo M., Steiner N.K., Nichol L., Hurley C.K.; RT "Complete exon 2 sequence for HLA-DRB1*1418."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:15). RA Kervaire B., Villard J., Tiercy J.M.; RT "An unusual HLA-DR/DQ haplotype carrying a new DR8 variant and the RT DRB3*0202 allele."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [33] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:23). RC TISSUE=Blood; RA Velickovic Z.M.; RT "Novel HLA-DRB1*11 allele."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [34] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:12). RA Oh H.B., Byun E.K., Hong S.A., Lee M.N., Kwon O.J.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [35] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:01). RA Lee T.D.; RT "Identification of a novel HLA-DRB1*14 allele."; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [36] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:53). RA Dormoy A.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [37] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:55). RC TISSUE=Leukocyte; RA Hirv K., Krauss A., Mytilineos J.; RT "Characterization of a new HLA-DRB1*14 allele."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [38] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:58). RA Karvunidis T., Jindra P., Fischer G., Koza V.; RT "Identification of a new HLA-DRB1*14 allele by sequence-based RT typing."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [39] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:59). RA Dormoy A., Weschler B., Leinsenbach R.; RT "A new DRB1*14 allele close to the DRB1*1418 allele is different for 3 RT substitutions at nucleotide positions 84, 152 and 174 leading to the RT change of 2 amino acids at positions 28 and 51."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. RN [40] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:63). RA Ye S., Liu M., Qi J.; RT "Identification a novel HLA-DRB1*14 new allele."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [41] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:30). RA Greville W.D., Dunckley H.; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [42] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:76). RC TISSUE=Blood; RA Tavoularis S., Rebeiro E., Sayer D.; RT "Identification of a novel DRB1 allele."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [43] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:77). RC TISSUE=Blood; RA Yan L.N., An S.P., Li S.Y., Xie J.H., Dong L., Dong Z., Yuan Y.H.; RT "A new allele of HLA-DRB1*14 detected with SBT."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [44] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*14:38; RP DRB1*14:39; DRB1*14:40; DRB1*14:44; DRB1*14:45 AND DRB1*14:80). RA Juji T., Shimizu M., Kashiwase K., Nakajima F., Tadokoro K., RA Tanaka H.; RT "HLA-DRB1*1401V1M, HLA-DRB1*1401V2, HLA-DRB1*1403V2, HLA-DRB1*1405V1, RT HLA-DRB1*1405V2, HLA-DRB1*1406V1."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [45] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB1*14:51; RP DRB1*14:52; DRB1*14:62; DRB1*14:64; DRB1*14:68; DRB1*14:69; RP DRB1*14:70; DRB1*14:71; DRB1*14:72; DRB1*14:73; DRB1*14:79; DRB1*14:81 RP AND DRB1*14:83). RA Lazaro A.M., Cao K., Xiao Y., Lebeck L., Hurley C.K.; RT "Novel class II allele."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [46] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:24). RA Dormoy A., Weschler B.; RT "The HLA-DRB1*14New allele has 3 nucleotide changes from the DRB1*1402 RT allele at positions 286, 298 and 299 of exon 2 where: C286->A286 RT (codon 72 (CTC->ATC)) resulting in a change of amino acid: Leu->Ile RT A298->G298 + G299->C299 (codon 76 (AGG->GCG)) resulting in a change of RT amino acid: Arg->Ala."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [47] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*14:84). RC TISSUE=Peripheral blood; RA Lee T.-D., Chien W.-C.; RT "A new DR14-related DRB1 allele, identified by sequence-based RT typing."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [48] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB1*14:35). RX PubMed=11532019; DOI=10.1046/j.1365-2370.2001.00243.x; RA Trejaut J., Kennedy A., Hobart D., Le T., Greville W.D., Ng G., RA Taverniti A., Dunckley H.; RT "PCR-RFLP typing detects new HLA-DRB1 alleles: DRB1*13022, DRB1*1336 RT and DRB1*1435."; RL Eur. J. Immunogenet. 28:441-447(2001). RN [49] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB1*14:28). RC TISSUE=Blood; RX PubMed=9243765; DOI=10.1111/j.1399-0039.1997.tb02843.x; RA Hashemi-Tavoularis S., Couture C., Buyse I.M.; RT "Identification of new DRB1*01 (DRB1*01022), DRB1*14 (DRB1*1428) and RT DRB3* (DRB3*0206) alleles."; RL Tissue Antigens 50:89-93(1997). RN [50] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB1*14:01). RC TISSUE=Peripheral blood; RX PubMed=15104685; DOI=10.1111/j.0001-2815.2004.00186.x; RA Tavoularis S., Couture C., Ribeiro-Barros E.; RT "Identification of three novel alleles: DRB3*0110, DRB1*1140, and RT DRB1*140102."; RL Tissue Antigens 63:496-500(2004). RN [51] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-123 (ALLELES DRB1*14:09 AND RP DRB1*14:25). RA Vayntrub T., Lo B.; RT "Confirmatory sequence of HLA class II DRB1*1409 and DRB1*1425."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [52] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-122 (ALLELE DRB1*14:08). RC TISSUE=Blood; RX PubMed=1644450; DOI=10.1007/BF00215663; RA Gao X., Veale A., Serjeantson S.W.; RT "HLA class II diversity in Australian aborigines: unusual HLA-DRB1 RT alleles."; RL Immunogenetics 36:333-337(1992). RN [53] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB1*14:31). RX PubMed=10599892; DOI=10.1034/j.1399-0039.1999.540510.x; RA Panigoro R., Greville W.D., Kennedy A., Trejaut J., Dunckley H.; RT "New HLA class II alleles in the Indonesian population."; RL Tissue Antigens 54:521-523(1999). RN [54] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-122 (ALLELE DRB1*14:33). RA Greville W.D., van Eijck A., Dunckley H.; RT "New HLA class II (DRB1) alleles detected by sequencing-based RT typing."; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [55] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB1*14:20). RX PubMed=8883296; DOI=10.1111/j.1399-0039.1996.tb02611.x; RA Verduyn W., Anholts J.D., Versluis L.F., Parlevliet J., Drabbels J., RA De Meester J., Tilanus M.G., Doxiadis I.I., Giphart M.J., RA Schreuder G.M.; RT "Six newly identified HLA-DRB alleles: DRB1*1121, *1419, *1420, *1421, RT DRB3*0203 and DRB5*0103."; RL Tissue Antigens 48:80-86(1996). RN [56] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-131 (ALLELE DRB1*14:24). RC TISSUE=B-cell; RA Hurley C.K.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. RN [57] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-120 (ALLELE DRB1*14:16). RA Gervais T.G., Latinne D.; RT "Confirmatory typing for exon 2 of HLA-DRB1*1416 gene, obtained by RT sequence-based typing."; RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases. RN [58] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [59] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [60] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [61] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [62] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [63] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [64] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-14 are known: CC DRB1*14:01, DRB1*14:02, DRB1*14:03, DRB1*14:04, DRB1*14:05, CC DRB1*14:06, DRB1*14:07, DRB1*14:08, DRB1*14:09, DRB1*14:10, CC DRB1*14:11, DRB1*14:12, DRB1*14:13, DRB1*14:14, DRB1*14:15, CC DRB1*14:16, DRB1*14:17, DRB1*14:18, DRB1*14:19, DRB1*14:20, CC DRB1*14:21, DRB1*14:22, DRB1*14:23, DRB1*14:24, DRB1*14:25, CC DRB1*14:26, DRB1*14:27, DRB1*14:28, DRB1*14:29, DRB1*14:30, CC DRB1*14:31, DRB1*14:32, DRB1*14:33, DRB1*14:34, DRB1*14:35, CC DRB1*14:36, DRB1*14:37, DRB1*14:38, DRB1*14:39, DRB1*14:40, CC DRB1*14:41, DRB1*14:42, DRB1*14:43, DRB1*14:44, DRB1*14:45, CC DRB1*14:46, DRB1*14:47, DRB1*14:48, DRB1*14:49, DRB1*14:50, CC DRB1*14:51, DRB1*14:52, DRB1*14:53, DRB1*14:54, DRB1*14:55, CC DRB1*14:56, DRB1*14:57, DRB1*14:58, DRB1*14:59, DRB1*14:60, CC DRB1*14:61, DRB1*14:62, DRB1*14:63, DRB1*14:64, DRB1*14:65, CC DRB1*14:67, DRB1*14:68, DRB1*14:69, DRB1*14:70, DRB1*14:71, CC DRB1*14:72, DRB1*14:73, DRB1*14:74, DRB1*14:75, DRB1*14:76, CC DRB1*14:77, DRB1*14:78, DRB1*14:79, DRB1*14:80, DRB1*14:81, CC DRB1*14:82, DRB1*14:83, DRB1*14:84 and DRB1*14:85. The sequence CC shown is that of DRB1*14:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB45249.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AB062112; BAB84521.2; -; mRNA. DR EMBL; AJ297582; CAC08822.1; -; mRNA. DR EMBL; AJ297583; CAC08823.1; -; mRNA. DR EMBL; AJ297584; CAC08824.1; -; mRNA. DR EMBL; AJ297585; CAC08825.1; -; mRNA. DR EMBL; AY663408; AAU88014.1; -; Genomic_DNA. DR EMBL; AY935719; AAX33315.1; -; mRNA. DR EMBL; AY961071; AAX63459.2; -; mRNA. DR EMBL; DQ235685; ABB52004.1; -; Genomic_DNA. DR EMBL; DQ390459; ABD60300.1; -; Genomic_DNA. DR EMBL; DQ390460; ABD60301.1; -; Genomic_DNA. DR EMBL; FJ379259; ACJ06537.1; -; Genomic_DNA. DR EMBL; Z38072; CAA86217.1; -; Genomic_DNA. DR EMBL; FM196525; CAQ86516.1; -; Genomic_DNA. DR EMBL; AM109998; CAJ33605.1; -; Genomic_DNA. DR EMBL; AM109999; CAJ33606.1; -; Genomic_DNA. DR EMBL; AM110000; CAJ33607.1; -; Genomic_DNA. DR EMBL; AM110001; CAJ33608.1; -; Genomic_DNA. DR EMBL; AM110002; CAJ33609.1; -; Genomic_DNA. DR EMBL; AM110003; CAJ33610.1; -; Genomic_DNA. DR EMBL; AB485773; BAH23562.1; -; Genomic_DNA. DR EMBL; Z50730; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ242985; CAB45249.1; ALT_SEQ; Genomic_DNA. DR EMBL; AJ251985; CAC19086.1; -; Genomic_DNA. DR EMBL; AY050186; AAL23547.1; -; Genomic_DNA. DR EMBL; AY054375; AAL15169.1; -; mRNA. DR EMBL; AF400066; AAK85431.1; -; Genomic_DNA. DR EMBL; AY267905; AAP32696.1; -; Genomic_DNA. DR EMBL; AY267906; AAP32697.1; -; Genomic_DNA. DR EMBL; AJ969417; CAI94542.1; -; Genomic_DNA. DR EMBL; AY912075; AAY17288.1; -; Genomic_DNA. DR EMBL; DQ333353; ABC59115.1; -; Genomic_DNA. DR EMBL; AM259285; CAJ90660.1; -; Genomic_DNA. DR EMBL; EF199810; ABM90423.1; -; Genomic_DNA. DR EMBL; AM774161; CAO81738.1; -; Genomic_DNA. DR EMBL; EF495154; ABP38039.1; -; Genomic_DNA. DR EMBL; AM922324; CAP58300.1; -; Genomic_DNA. DR EMBL; DQ494324; ABF50050.1; -; Genomic_DNA. DR EMBL; EU588391; ACB97664.1; -; Genomic_DNA. DR EMBL; D86502; BAA13097.1; -; Genomic_DNA. DR EMBL; D86504; BAA13099.1; -; Genomic_DNA. DR EMBL; D88310; BAA13587.1; -; Genomic_DNA. DR EMBL; AJ010982; CAA09450.1; -; Genomic_DNA. DR EMBL; AF172071; AAD51970.1; -; Genomic_DNA. DR EMBL; AJ543433; CAD65908.1; -; Genomic_DNA. DR EMBL; AY277390; AAP34694.1; -; Genomic_DNA. DR EMBL; AJ581744; CAE46451.1; -; Genomic_DNA. DR EMBL; AJ812566; CAH23708.1; -; Genomic_DNA. DR EMBL; AY770520; AAV37191.1; -; Genomic_DNA. DR EMBL; DQ021915; AAY85747.1; -; Genomic_DNA. DR EMBL; AM084908; CAJ29895.1; -; Genomic_DNA. DR EMBL; DQ327711; ABC59293.1; -; Genomic_DNA. DR EMBL; DQ358688; ABC84557.1; -; Genomic_DNA. DR EMBL; AM233907; CAJ80873.1; -; Genomic_DNA. DR EMBL; DQ643390; ABG25965.1; -; Genomic_DNA. DR EMBL; U95115; AAB58397.2; -; Genomic_DNA. DR EMBL; AM933133; CAP69806.1; -; Genomic_DNA. DR EMBL; EU545181; ACB30275.1; -; Genomic_DNA. DR EMBL; AB049830; BAB16682.1; -; Genomic_DNA. DR EMBL; AB049831; BAB16683.1; -; Genomic_DNA. DR EMBL; AB049832; BAB16684.1; -; Genomic_DNA. DR EMBL; AB087875; BAC02938.1; -; Genomic_DNA. DR EMBL; AB087876; BAC02939.1; -; Genomic_DNA. DR EMBL; AB436778; BAG32234.1; -; Genomic_DNA. DR EMBL; EF078986; ABK56696.1; -; Genomic_DNA. DR EMBL; EF536016; ABQ08747.1; -; Genomic_DNA. DR EMBL; EU029787; ABU86846.1; -; Genomic_DNA. DR EMBL; EU029788; ABU86847.1; -; Genomic_DNA. DR EMBL; EU029792; ABU86851.1; -; Genomic_DNA. DR EMBL; EU029793; ABU86852.1; -; Genomic_DNA. DR EMBL; EU029798; ABU86857.1; -; Genomic_DNA. DR EMBL; EU643616; ACD01094.1; -; Genomic_DNA. DR EMBL; EU812536; ACE88696.1; -; Genomic_DNA. DR EMBL; EU924810; ACH57405.1; -; Genomic_DNA. DR EMBL; DQ060439; AAY59541.1; -; Genomic_DNA. DR EMBL; DQ060441; AAY59543.1; -; Genomic_DNA. DR EMBL; DQ782331; ABG91054.1; -; Genomic_DNA. DR EMBL; FM179681; CAQ77159.1; -; Genomic_DNA. DR EMBL; FJ594768; ACM47962.1; -; Genomic_DNA. DR EMBL; AF177215; AAD53910.1; -; Genomic_DNA. DR EMBL; X99839; CAA68150.1; -; Genomic_DNA. DR EMBL; AJ289123; CAC19015.1; -; Genomic_DNA. DR EMBL; AY174092; AAO20089.1; -; Genomic_DNA. DR EMBL; AY174181; AAO17053.1; -; Genomic_DNA. DR EMBL; M77673; AAA73131.1; -; Genomic_DNA. DR EMBL; AF028010; AAB94612.1; -; Genomic_DNA. DR EMBL; AF112879; AAD29584.1; -; Genomic_DNA. DR EMBL; X86974; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U41489; AAA86242.1; -; Genomic_DNA. DR EMBL; AJ508388; CAD48196.1; -; Genomic_DNA. DR PIR; B33287; B33287. DR PIR; C33287; C33287. DR PIR; C60748; C60748. DR PIR; F60748; F60748. DR PIR; PH0157; PH0157. DR PIR; PH0158; PH0158. DR PIR; S03440; S03440. DR UniGene; Hs.485130; -. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q9GIY3; -. DR SMR; Q9GIY3; -. DR IntAct; Q9GIY3; 1. DR ChEMBL; CHEMBL3988561; -. DR SwissPalm; Q9GIY3; -. DR DMDM; 74761361; -. DR EPD; Q9GIY3; -. DR PeptideAtlas; Q9GIY3; -. DR PRIDE; Q9GIY3; -. DR Ensembl; ENST00000328980; ENSP00000331343; ENSG00000206306. DR Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126. DR Ensembl; ENST00000399450; ENSP00000382378; ENSG00000206240. DR Ensembl; ENST00000412634; ENSP00000408795; ENSG00000228080. DR Ensembl; ENST00000415796; ENSP00000412168; ENSG00000206306. DR Ensembl; ENST00000419393; ENSP00000403458; ENSG00000228080. DR Ensembl; ENST00000428566; ENSP00000392280; ENSG00000206240. DR UCSC; uc063uqx.1; human. DR DisGeNET; 3123; -. DR EuPathDB; HostDB:ENSG00000196126.10; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; CAB015400; -. DR HPA; CAB034021; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_Q9GIY3; -. DR HOVERGEN; HBG012730; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000196126; Expressed in 94 organ(s), highest expression level in spleen. DR ExpressionAtlas; Q9GIY3; baseline and differential. DR Genevisible; Q9GIY3; HS. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-14 beta chain. FT /FTId=PRO_5000066676. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P20039}. FT VARIANT 39 39 Y -> L (in allele DRB1*14:46; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062907. FT VARIANT 39 39 Y -> Q (in allele DRB1*14:10 and allele FT DRB1*14:57; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062906. FT VARIANT 40 40 S -> P (in allele DRB1*14:39). FT /FTId=VAR_062910. FT VARIANT 40 40 S -> R (in allele DRB1*14:46). FT /FTId=VAR_062908. FT VARIANT 40 40 S -> V (in allele DRB1*14:10 and allele FT DRB1*14:57; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062909. FT VARIANT 41 41 T -> K (in allele DRB1*14:10, allele FT DRB1*14:46 and allele DRB1*14:57). FT /FTId=VAR_062911. FT VARIANT 42 42 S -> G (in allele DRB1*14:04, allele FT DRB1*14:11, allele DRB1*14:15, allele FT DRB1*14:28, allele DRB1*14:31, allele FT DRB1*14:50, allele DRB1*14:52, allele FT DRB1*14:61, allele DRB1*14:68, allele FT DRB1*14:71, allele DRB1*14:73, allele FT DRB1*14:76 and allele DRB1*14:79). FT /FTId=VAR_062913. FT VARIANT 42 42 S -> H (in allele DRB1*14:10 and allele FT DRB1*14:57; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062912. FT VARIANT 45 45 H -> Q (in allele DRB1*14:05, allele FT DRB1*14:37, allele DRB1*14:43, allele FT DRB1*14:44, allele DRB1*14:45, allele FT DRB1*14:56 and allele DRB1*14:84). FT /FTId=VAR_062915. FT VARIANT 45 45 H -> Y (in allele DRB1*14:04, allele FT DRB1*14:11, allele DRB1*14:15, allele FT DRB1*14:28, allele DRB1*14:31, allele FT DRB1*14:50, allele DRB1*14:52, allele FT DRB1*14:68, allele DRB1*14:71, allele FT DRB1*14:73, allele DRB1*14:76 and allele FT DRB1*14:79). FT /FTId=VAR_062914. FT VARIANT 54 54 R -> Q (in allele DRB1*14:26). FT /FTId=VAR_062916. FT VARIANT 55 55 F -> Y (in allele DRB1*14:82). FT /FTId=VAR_062917. FT VARIANT 56 56 L -> M (in allele DRB1*14:83). FT /FTId=VAR_062918. FT VARIANT 57 57 D -> E (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:06, allele FT DRB1*14:12, allele DRB1*14:13, allele FT DRB1*14:18, allele DRB1*14:19, allele FT DRB1*14:20, allele DRB1*14:24, allele FT DRB1*14:27, allele DRB1*14:29, allele FT DRB1*14:40, allele DRB1*14:41, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:48, allele DRB1*14:49, allele FT DRB1*14:51, allele DRB1*14:52, allele FT DRB1*14:63, allele DRB1*14:67, allele FT DRB1*14:77, allele DRB1*14:78, allele FT DRB1*14:81, allele DRB1*14:83 and allele FT DRB1*14:85). FT /FTId=VAR_062919. FT VARIANT 59 59 Y -> H (in allele DRB1*14:70). FT /FTId=VAR_062920. FT VARIANT 61 61 H -> Y (in allele DRB1*14:25, allele FT DRB1*14:42, allele DRB1*14:53, allele FT DRB1*14:58 and allele DRB1*14:69). FT /FTId=VAR_062921. FT VARIANT 66 66 F -> N (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:06, allele FT DRB1*14:09, allele DRB1*14:12, allele FT DRB1*14:13, allele DRB1*14:17, allele FT DRB1*14:18, allele DRB1*14:19, allele FT DRB1*14:21, allele DRB1*14:24, allele FT DRB1*14:27, allele DRB1*14:29, allele FT DRB1*14:30, allele DRB1*14:33, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:48, allele DRB1*14:51, allele FT DRB1*14:52, allele DRB1*14:59, allele FT DRB1*14:63, allele DRB1*14:64, allele FT DRB1*14:67, allele DRB1*14:78, allele FT DRB1*14:80, allele DRB1*14:81, allele FT DRB1*14:83 and allele DRB1*14:85; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062923. FT VARIANT 66 66 F -> Y (in allele DRB1*14:25, allele FT DRB1*14:42, allele DRB1*14:53, allele FT DRB1*14:58 and allele DRB1*14:69). FT /FTId=VAR_062922. FT VARIANT 67 67 V -> L (in allele DRB1*14:41 and allele FT DRB1*14:77). FT /FTId=VAR_062924. FT VARIANT 74 74 G -> R (in allele DRB1*14:36 and allele FT DRB1*14:60). FT /FTId=VAR_062925. FT VARIANT 76 76 Y -> F (in allele DRB1*14:17, allele FT DRB1*14:21, allele DRB1*14:30, allele FT DRB1*14:33, allele DRB1*14:35, allele FT DRB1*14:42, allele DRB1*14:53, allele FT DRB1*14:64, allele DRB1*14:65 and allele FT DRB1*14:72). FT /FTId=VAR_062926. FT VARIANT 80 80 T -> R (in allele DRB1*14:59). FT /FTId=VAR_062927. FT VARIANT 86 86 A -> D (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:05, allele FT DRB1*14:06, allele DRB1*14:08, allele FT DRB1*14:09, allele DRB1*14:11, allele FT DRB1*14:12, allele DRB1*14:14, allele FT DRB1*14:15, allele DRB1*14:17, allele FT DRB1*14:18, allele DRB1*14:19, allele FT DRB1*14:20, allele DRB1*14:21, allele FT DRB1*14:23, allele DRB1*14:24, allele FT DRB1*14:27, allele DRB1*14:29, allele FT DRB1*14:30, allele DRB1*14:33, allele FT DRB1*14:34, allele DRB1*14:36, allele FT DRB1*14:37, allele DRB1*14:40, allele FT DRB1*14:41, allele DRB1*14:42, allele FT DRB1*14:43, allele DRB1*14:44, allele FT DRB1*14:45, allele DRB1*14:46, allele FT DRB1*14:47, allele DRB1*14:51, allele FT DRB1*14:52, allele DRB1*14:56, allele FT DRB1*14:59, allele DRB1*14:64, allele FT DRB1*14:67, allele DRB1*14:72, allele FT DRB1*14:77, allele DRB1*14:80, allele FT DRB1*14:81, allele DRB1*14:83 and allele FT DRB1*14:84). FT /FTId=VAR_062928. FT VARIANT 86 86 A -> S (in allele DRB1*14:13, allele FT DRB1*14:63, allele DRB1*14:65, allele FT DRB1*14:78 and allele DRB1*14:85). FT /FTId=VAR_062929. FT VARIANT 86 86 A -> T (in allele DRB1*14:62). FT /FTId=VAR_062930. FT VARIANT 86 86 A -> V (in allele DRB1*14:48). FT /FTId=VAR_062931. FT VARIANT 87 87 A -> E (in allele DRB1*14:11). FT /FTId=VAR_062932. FT VARIANT 89 89 H -> S (in allele DRB1*14:48 and allele FT DRB1*14:64; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062934. FT VARIANT 89 89 H -> Y (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:05, allele FT DRB1*14:06, allele DRB1*14:09, allele FT DRB1*14:11, allele DRB1*14:12, allele FT DRB1*14:13, allele DRB1*14:14, allele FT DRB1*14:15, allele DRB1*14:17, allele FT DRB1*14:18, allele DRB1*14:19, allele FT DRB1*14:20, allele DRB1*14:21, allele FT DRB1*14:23, allele DRB1*14:24, allele FT DRB1*14:27, allele DRB1*14:29, allele FT DRB1*14:30, allele DRB1*14:33, allele FT DRB1*14:36, allele DRB1*14:37, allele FT DRB1*14:40, allele DRB1*14:41, allele FT DRB1*14:42, allele DRB1*14:43, allele FT DRB1*14:44, allele DRB1*14:45, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:51, allele DRB1*14:52, allele FT DRB1*14:56, allele DRB1*14:57, allele FT DRB1*14:59, allele DRB1*14:63, allele FT DRB1*14:65, allele DRB1*14:67, allele FT DRB1*14:76, allele DRB1*14:77, allele FT DRB1*14:78, allele DRB1*14:80, allele FT DRB1*14:81, allele DRB1*14:83, allele FT DRB1*14:84 and allele DRB1*14:85). FT /FTId=VAR_062933. FT VARIANT 96 96 L -> F (in allele DRB1*14:15, allele FT DRB1*14:22, allele DRB1*14:25, allele FT DRB1*14:27, allele DRB1*14:53 and allele FT DRB1*14:73). FT /FTId=VAR_062935. FT VARIANT 96 96 L -> I (in allele DRB1*14:16, allele FT DRB1*14:24, allele DRB1*14:37, allele FT DRB1*14:45, allele DRB1*14:57, allele FT DRB1*14:63, allele DRB1*14:67 and allele FT DRB1*14:78). FT /FTId=VAR_062936. FT VARIANT 99 99 R -> D (in allele DRB1*14:03, allele FT DRB1*14:12, allele DRB1*14:15, allele FT DRB1*14:16, allele DRB1*14:22, allele FT DRB1*14:25, allele DRB1*14:27, allele FT DRB1*14:40, allele DRB1*14:53, allele FT DRB1*14:57, allele DRB1*14:63, allele FT DRB1*14:67, allele DRB1*14:69, allele FT DRB1*14:73, allele DRB1*14:74, allele FT DRB1*14:77, allele DRB1*14:78, allele FT DRB1*14:84 and allele DRB1*14:85; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062938. FT VARIANT 99 99 R -> Q (in allele DRB1*14:02, allele FT DRB1*14:06, allele DRB1*14:09, allele FT DRB1*14:13, allele DRB1*14:17, allele FT DRB1*14:19, allele DRB1*14:20, allele FT DRB1*14:21, allele DRB1*14:24, allele FT DRB1*14:29, allele DRB1*14:30, allele FT DRB1*14:33, allele DRB1*14:37, allele FT DRB1*14:41, allele DRB1*14:46, allele FT DRB1*14:47, allele DRB1*14:48, allele FT DRB1*14:49, allele DRB1*14:51, allele FT DRB1*14:52, allele DRB1*14:76, allele FT DRB1*14:79, allele DRB1*14:80 and allele FT DRB1*14:83). FT /FTId=VAR_062937. FT VARIANT 100 100 R -> A (in allele DRB1*14:24 and allele FT DRB1*14:37; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062941. FT VARIANT 100 100 R -> E (in allele DRB1*14:16 and allele FT DRB1*14:57; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062940. FT VARIANT 100 100 R -> K (in allele DRB1*14:19, allele FT DRB1*14:21, allele DRB1*14:76 and allele FT DRB1*14:79). FT /FTId=VAR_062939. FT VARIANT 102 102 A -> G (in allele DRB1*14:76 and allele FT DRB1*14:79). FT /FTId=VAR_062943. FT VARIANT 102 102 A -> S (in allele DRB1*14:56). FT /FTId=VAR_062942. FT VARIANT 103 103 E -> A (in allele DRB1*14:02, allele FT DRB1*14:06, allele DRB1*14:09, allele FT DRB1*14:13, allele DRB1*14:16, allele FT DRB1*14:17, allele DRB1*14:19, allele FT DRB1*14:20, allele DRB1*14:21, allele FT DRB1*14:22, allele DRB1*14:24, allele FT DRB1*14:25, allele DRB1*14:29, allele FT DRB1*14:30, allele DRB1*14:31, allele FT DRB1*14:32, allele DRB1*14:34, allele FT DRB1*14:37, allele DRB1*14:41, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:48, allele DRB1*14:49, allele FT DRB1*14:52, allele DRB1*14:53, allele FT DRB1*14:57, allele DRB1*14:65, allele FT DRB1*14:69, allele DRB1*14:74, allele FT DRB1*14:80, allele DRB1*14:81 and allele FT DRB1*14:83). FT /FTId=VAR_062944. FT VARIANT 103 103 E -> L (in allele DRB1*14:03, allele FT DRB1*14:12, allele DRB1*14:15, allele FT DRB1*14:27, allele DRB1*14:40, allele FT DRB1*14:55, allele DRB1*14:63, allele FT DRB1*14:67, allele DRB1*14:77, allele FT DRB1*14:78, allele DRB1*14:84 and allele FT DRB1*14:85; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062945. FT VARIANT 103 103 E -> R (in allele DRB1*14:76 and allele FT DRB1*14:79; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062946. FT VARIANT 106 106 T -> A (in allele DRB1*14:43). FT /FTId=VAR_062948. FT VARIANT 106 106 T -> N (in allele DRB1*14:38, allele FT DRB1*14:47, allele DRB1*14:50, allele FT DRB1*14:76 and allele DRB1*14:79). FT /FTId=VAR_062947. FT VARIANT 110 110 H -> Y (in allele DRB1*14:75). FT /FTId=VAR_062949. FT VARIANT 114 114 V -> A (in allele DRB1*14:28 and allele FT DRB1*14:29). FT /FTId=VAR_062950. FT VARIANT 115 115 V -> G (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:07, allele FT DRB1*14:09, allele DRB1*14:13, allele FT DRB1*14:14, allele DRB1*14:19, allele FT DRB1*14:22, allele DRB1*14:24, allele FT DRB1*14:25, allele DRB1*14:27, allele FT DRB1*14:30, allele DRB1*14:36, allele FT DRB1*14:40, allele DRB1*14:41, allele FT DRB1*14:42, allele DRB1*14:44, allele FT DRB1*14:46, allele DRB1*14:47, allele FT DRB1*14:48, allele DRB1*14:49, allele FT DRB1*14:51, allele DRB1*14:53, allele FT DRB1*14:63, allele DRB1*14:67, allele FT DRB1*14:68, allele DRB1*14:69, allele FT DRB1*14:77 and allele DRB1*14:85). FT /FTId=VAR_062951. FT VARIANT 115 115 V -> M (in allele DRB1*14:71). FT /FTId=VAR_062952. FT VARIANT 141 141 Y -> H (in allele DRB1*14:02, allele FT DRB1*14:03, allele DRB1*14:04, allele FT DRB1*14:05, allele DRB1*14:06, allele FT DRB1*14:07, allele DRB1*14:10, allele FT DRB1*14:11, allele DRB1*14:13, allele FT DRB1*14:14, allele DRB1*14:21, allele FT DRB1*14:46, allele DRB1*14:54, allele FT DRB1*14:57 and allele DRB1*14:82). FT /FTId=VAR_062953. FT CONFLICT 124 124 V -> G (in Ref. 10; BAH23562). FT {ECO:0000305}. SQ SEQUENCE 266 AA; 30139 MW; FA4BE90DFAB4FA55 CRC64; MVCLRLPGGS CMAVLTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRFLDRYF HNQEEFVRFD SDVGEYRAVT ELGRPAAEHW NSQKDLLERR RAEVDTYCRH NYGVVESFTV QRRVHPKVTV YPSKTQPLQH YNLLVCSVSG FYPGSIEVRW FRNGQEEKTG VVSTGLIHNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PRGFLS // ID 2B1F_HUMAN Reviewed; 266 AA. AC P01911; Q29790; Q29975; Q30142; Q30166; Q32MY7; Q56FN9; Q5Y7B0; AC Q5Y7B9; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 12-SEP-2018, entry version 154. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-15 beta chain; DE AltName: Full=DW2.2/DR2.2; DE AltName: Full=MHC class II antigen DRB1*15; DE Flags: Precursor; GN Name=HLA-DRB1; Synonyms=HLA-DRB2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*15:01). RC TISSUE=B-cell; RX PubMed=3259543; DOI=10.1007/BF00364432; RA Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.; RT "MHC class II sequences of an HLA-DR2 narcoleptic."; RL Immunogenetics 27:449-455(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DRB1*15:01; DRB1*15:02 AND RP DRB1*15:03). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DRB1*15:03 AND DRB1*15:04). RC TISSUE=Blood; RX PubMed=17174751; DOI=10.1016/j.humimm.2006.09.002; RA Balas A., Vilches C., Rodriguez M.A., Fernandez B., Martinez M.P., RA de Pablo R., Garcia-Sanchez F., Vicario J.L.; RT "Group-specific amplification of cDNA from DRB1 genes. Complete coding RT sequences of partially defined alleles and identification of the new RT alleles DRB1*040602, DRB1*111102, DRB1*080103, and DRB1*0113."; RL Hum. Immunol. 67:1008-1016(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB1*15:01). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRB1*15:01 AND RP DRB1*15:02). RC TISSUE=Leukocyte; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-266 (ALLELE DRB1*15:02). RC TISSUE=Lymphoblast; RX PubMed=3571980; RA Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.; RT "cDNA cloning and sequencing reveals that the electrophoretically RT constant DR beta 2 molecules, as well as the variable DR beta 1 RT molecules, from HLA-DR2 subtypes have different amino acid sequences RT including a hypervariable region for a functionally important RT epitope."; RL J. Immunol. 138:2953-2959(1987). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01). RC TISSUE=Lymphoblast; RX PubMed=2885840; DOI=10.1073/pnas.84.13.4591; RA Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.; RT "HLA-DR2 subtypes form an additional supertypic family of DR beta RT alleles."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*15:01). RC TISSUE=Lymphoblast; RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [9] RP PROTEIN SEQUENCE OF 30-228. RC TISSUE=Lymphoblast; RX PubMed=6947956; RA Kratzin H., Yang C.-Y., Gotz H., Pauly E., Kolbel S., Egert G., RA Thinnes F.P., Wernet P., Altevogt P., Hilschmann N.; RT "Primary structure of class II human histocompatibility antigens. 1st RT communication. Amino acid sequence of the N-terminal 198 residues of RT the beta chain of a HLA-Dw2,2;DR2,2-alloantigen."; RL Hoppe-Seyler's Z. Physiol. Chem. 362:1665-1669(1981). RN [10] RP PROTEIN SEQUENCE OF 30-64. RC TISSUE=B-cell; RX PubMed=6600932; DOI=10.1021/bi00270a027; RA Walker L.E., Hewick R., Hunkapiller M.W., Hood L.E., Dreyer W.J., RA Reisfeld R.A.; RT "N-terminal amino acid sequences of the alpha and beta chains of HLA- RT DR1 and HLA-DR2 antigens."; RL Biochemistry 22:185-188(1983). RN [11] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [12] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [13] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [14] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [15] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [16] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [17] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 30-227. RX PubMed=15821740; DOI=10.1038/ni1187; RA Hahn M., Nicholson M.J., Pyrdol J., Wucherpfennig K.W.; RT "Unconventional topology of self peptide-major histocompatibility RT complex binding by a human autoimmune T cell receptor."; RL Nat. Immunol. 6:490-496(2005). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-15 are known: CC DRB1*15:01, DRB1*15:02, DRB1*15:03, DRB1*15:04, DRB1*15:05, CC DRB1*15:06, DRB1*15:07, DRB1*15:08, DRB1*15:09, DRB1*15:10, CC DRB1*15:11, DRB1*15:12, DRB1*15:13, DRB1*15:14, DRB1*15:15, CC DRB1*15:16, DRB1*15:18, DRB1*15:19, DRB1*15:20, DRB1*15:21, CC DRB1*15:22, DRB1*15:23, DRB1*15:24, DRB1*15:25, DRB1*15:26, CC DRB1*15:27, DRB1*15:28, DRB1*15:29, DRB1*15:30, DRB1*15:31 and CC DRB1*15:32. The sequence shown is that of DRB1*15:01. CC -!- MISCELLANEOUS: The chain shown constituted about 70% of a pool of CC at least seven similar beta chains. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M20430; AAA59831.1; -; mRNA. DR EMBL; AY663395; AAU87979.1; -; Genomic_DNA. DR EMBL; AY663406; AAU88008.1; -; Genomic_DNA. DR EMBL; AY663411; AAU88023.1; -; Genomic_DNA. DR EMBL; AY663414; AAU88033.1; -; Genomic_DNA. DR EMBL; AY961072; AAX63460.1; -; mRNA. DR EMBL; AY961073; AAX63461.1; -; mRNA. DR EMBL; AL713966; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC033827; AAH33827.1; -; mRNA. DR EMBL; BC108922; AAI08923.1; -; mRNA. DR EMBL; M28584; AAA59681.1; -; mRNA. DR EMBL; M16957; AAA36279.1; -; mRNA. DR EMBL; M17378; AAA59801.1; -; mRNA. DR CCDS; CCDS47409.1; -. DR PIR; I68734; HLHUWB. DR RefSeq; NP_002115.2; NM_002124.3. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 1BX2; X-ray; 2.60 A; B/E=32-222. DR PDB; 1YMM; X-ray; 3.50 A; B=30-227. DR PDB; 2WBJ; X-ray; 3.00 A; B/F=30-227. DR PDBsum; 1BX2; -. DR PDBsum; 1YMM; -. DR PDBsum; 2WBJ; -. DR ProteinModelPortal; P01911; -. DR SMR; P01911; -. DR BioGrid; 109368; 39. DR IntAct; P01911; 1. DR STRING; 9606.ENSP00000353099; -. DR ChEMBL; CHEMBL3831291; -. DR iPTMnet; P01911; -. DR SwissPalm; P01911; -. DR BioMuta; ATXN1; -. DR DMDM; 166214928; -. DR EPD; P01911; -. DR PaxDb; P01911; -. DR PeptideAtlas; P01911; -. DR PRIDE; P01911; -. DR DNASU; 3123; -. DR Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126. DR GeneID; 3123; -. DR CTD; 3123; -. DR DisGeNET; 3123; -. DR EuPathDB; HostDB:ENSG00000196126.10; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; CAB015400; -. DR HPA; CAB034021; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_P01911; -. DR OpenTargets; ENSG00000196126; -. DR PharmGKB; PA35072; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P01911; -. DR PhylomeDB; P01911; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR EvolutionaryTrace; P01911; -. DR GeneWiki; HLA-DRB1; -. DR GenomeRNAi; 3123; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000196126; Expressed in 94 organ(s), highest expression level in spleen. DR CleanEx; HS_HLA-DRB1; -. DR ExpressionAtlas; P01911; baseline and differential. DR Genevisible; P01911; HS. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0002506; P:polysaccharide assembly with MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Endosome; Glycoprotein; Golgi apparatus; Immunity; Isopeptide bond; KW Lysosome; Membrane; MHC II; Polymorphism; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 29 {ECO:0000269|PubMed:6600932, FT ECO:0000269|PubMed:6947956}. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-15 beta chain. FT /FTId=PRO_0000080744. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TOPO_DOM 249 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT DISULFID 44 108 FT DISULFID 146 202 FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P20039}. FT VARIANT 5 5 K -> R (in dbSNP:rs707953). FT /FTId=VAR_050364. FT VARIANT 55 55 F -> Y (in dbSNP:rs1059569). FT /FTId=VAR_050365. FT VARIANT 59 59 Y -> H (in allele DRB1*15:03; FT dbSNP:rs11554462). FT /FTId=VAR_038162. FT VARIANT 96 96 I -> F (in allele DRB1*15:04; FT dbSNP:rs17886918). FT /FTId=VAR_038163. FT VARIANT 106 106 T -> N (in dbSNP:rs9269941). FT /FTId=VAR_050366. FT VARIANT 115 115 V -> G (in allele DRB1*15:02; FT dbSNP:rs17885482). FT /FTId=VAR_038164. FT VARIANT 164 164 G -> S (in dbSNP:rs1059633). FT /FTId=VAR_050367. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_050370. FT CONFLICT 119 119 T -> A (in Ref. 5; AAI08923). FT {ECO:0000305}. FT CONFLICT 154 154 G -> A (in Ref. 8; AAA59801). FT {ECO:0000305}. FT CONFLICT 171 171 M -> G (in Ref. 9; AA sequence). FT {ECO:0000305}. FT CONFLICT 179 180 NG -> D (in Ref. 9; AA sequence). FT {ECO:0000305}. FT STRAND 36 47 {ECO:0000244|PDB:1BX2}. FT TURN 48 51 {ECO:0000244|PDB:1BX2}. FT STRAND 52 61 {ECO:0000244|PDB:1BX2}. FT STRAND 64 70 {ECO:0000244|PDB:1BX2}. FT TURN 71 73 {ECO:0000244|PDB:1BX2}. FT STRAND 75 80 {ECO:0000244|PDB:1BX2}. FT HELIX 81 83 {ECO:0000244|PDB:1BX2}. FT HELIX 84 92 {ECO:0000244|PDB:1BX2}. FT HELIX 94 106 {ECO:0000244|PDB:1BX2}. FT HELIX 108 115 {ECO:0000244|PDB:1BX2}. FT TURN 116 121 {ECO:0000244|PDB:1BX2}. FT STRAND 127 134 {ECO:0000244|PDB:1BX2}. FT STRAND 142 154 {ECO:0000244|PDB:1BX2}. FT STRAND 157 162 {ECO:0000244|PDB:1BX2}. FT STRAND 165 167 {ECO:0000244|PDB:1BX2}. FT STRAND 169 173 {ECO:0000244|PDB:1BX2}. FT STRAND 180 182 {ECO:0000244|PDB:1BX2}. FT STRAND 184 192 {ECO:0000244|PDB:1BX2}. FT STRAND 199 205 {ECO:0000244|PDB:1BX2}. FT STRAND 209 211 {ECO:0000244|PDB:2WBJ}. FT STRAND 213 218 {ECO:0000244|PDB:1BX2}. SQ SEQUENCE 266 AA; 29966 MW; 3B5912820A4654BE CRC64; MVCLKLPGGS CMTALTVTLM VLSSPLALSG DTRPRFLWQP KRECHFFNGT ERVRFLDRYF YNQEESVRFD SDVGEFRAVT ELGRPDAEYW NSQKDILEQA RAAVDTYCRH NYGVVESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID 2B1G_HUMAN Reviewed; 266 AA. AC Q29974; A7X5J4; O98212; Q0PGR5; Q29792; Q30120; Q30159; Q30200; AC Q3HUP9; Q3KTM1; Q3LA84; Q6T865; Q95383; DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 12-SEP-2018, entry version 136. DE RecName: Full=HLA class II histocompatibility antigen, DRB1-16 beta chain; DE AltName: Full=MHC class II antigen DRB1*16; DE Short=DR-16; DE Short=DR16; DE Flags: Precursor; GN Name=HLA-DRB1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*16:01). RX PubMed=3571980; RA Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.; RT "cDNA cloning and sequencing reveals that the electrophoretically RT constant DR beta 2 molecules, as well as the variable DR beta 1 RT molecules, from HLA-DR2 subtypes have different amino acid sequences RT including a hypervariable region for a functionally important RT epitope."; RL J. Immunol. 138:2953-2959(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*16:02). RX PubMed=3129499; RA Liu C.P., Bach F.H., Wu S.K.; RT "Molecular studies of a rare DR2/LD-5a/DQw3 HLA class II haplotype. RT Multiple genetic mechanisms in the generation of polymorphic HLA class RT II genes."; RL J. Immunol. 140:3631-3639(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB1*16:03). RC TISSUE=Blood; RX PubMed=8436426; DOI=10.1007/BF00222476; RA Rosenlicht J.W., Hartung K., Deicher H., Frey J.; RT "A novel HLA-DRB1-DR2 allele associated with HLA mistyping."; RL Immunogenetics 37:479-479(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB1*16:01). RC TISSUE=Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB1*16:01). RX PubMed=2885840; DOI=10.1073/pnas.84.13.4591; RA Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.; RT "HLA-DR2 subtypes form an additional supertypic family of DR beta RT alleles."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-216 (ALLELE DRB1*16:04). RC TISSUE=Peripheral blood; RX PubMed=17767557; DOI=10.1111/j.1399-0039.2007.00918.x; RA Horn P.A., Albis-Camps M., Verboom M., Bunce M., Yousaf K., RA Williams S., Blasczyk R.; RT "The nature of diversity of HLA-DRB1 exon 3."; RL Tissue Antigens 70:335-337(2007). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:08). RX PubMed=9271639; DOI=10.1007/s002510050303; RA Reviron D., Dormoy A., Andre M., Froelich N., Roudier J., Tongio M.M., RA Mercier P.; RT "HLA-DRB1*1608: a new HLA-DRB1*16 allele with a short DRB1*03 RT sequence."; RL Immunogenetics 46:444-445(1997). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:09). RX PubMed=16101839; DOI=10.1111/j.1399-0039.2005.00443.x; RA Miao K.R., Pan Q.Q., Xue M., Zhou X.Y., Fei X.M., Tang Y.H., Xu R., RA Zhang J.W., Zhao X., Osowski L., Shi W.X., Xu A.L., Wang C.Y., RA Kukuruga D.; RT "A novel HLA allele, DRB1*1609, identified in the Chinese Han RT population*."; RL Tissue Antigens 66:248-250(2005). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:11). RX PubMed=19500310; DOI=10.1111/j.1399-0039.2009.01260.x; RA Chu C.-C., Lee H.-L., Lin M.; RT "A novel HLA-DRB1 allele, DRB*1611, is identified in two Taiwanese RT individuals."; RL Tissue Antigens 74:175-176(2009). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:05). RA Gedil M.A., Steiner N.K., Hurley C.K.; RT "Novel HLA-DRB1 allele."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:10). RA Yan L., Zhu F., He J.; RT "Identification a novel HLA-DRB1*16 allele by sequence based typing in RT Chinese."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB1*16:12). RA Lazaro A.M., Xiao Y., Hurley C.K.; RT "Novel HLA class II allele."; RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DRB1*16:01). RC TISSUE=Blood; RX PubMed=10551425; DOI=10.1034/j.1399-0039.1999.540411.x; RA Lin Y.S., Tang T.F., Ng J., Hartzman R., Hurley C.K.; RT "Two DR2-associated novel alleles arose from the silent mutation of RT codon 72: DRB1*16012, DRB5*01012."; RL Tissue Antigens 54:405-408(1999). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-120 (ALLELE DRB1*16:07). RA Brautbar C., Israel S., Safirman C., Smith A.G.; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [15] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [16] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [17] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [18] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [19] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [20] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [21] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB1-16 are known: CC DRB1*16:01; DRB1*16:02; DRB1*16:03; DRB1*16:04; DRB1*16:05; CC DRB1*16:07; DRB1*16:08; DRB1*16:09; DRB1*16:10; DRB1*16:11 and CC DRB1*16:12. The sequence shown is that of DRB1*16:02. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M28583; AAA59680.1; -; mRNA. DR EMBL; M20504; AAA59827.1; -; mRNA. DR EMBL; L02545; AAA59777.1; -; mRNA. DR EMBL; AK291987; BAF84676.1; -; mRNA. DR EMBL; M16959; AAA36281.1; -; mRNA. DR EMBL; AM110006; CAJ33613.1; -; Genomic_DNA. DR EMBL; Z72424; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY912074; AAY17287.1; -; Genomic_DNA. DR EMBL; DQ837166; ABH05946.1; -; Genomic_DNA. DR EMBL; AY428805; AAR07616.1; -; Genomic_DNA. DR EMBL; DQ192647; ABA39176.1; -; Genomic_DNA. DR EMBL; EU029801; ABU86860.1; -; Genomic_DNA. DR EMBL; U59686; AAB52230.1; -; Genomic_DNA. DR EMBL; U26659; AAD09441.1; -; Genomic_DNA. DR PIR; B27618; B27618. DR PIR; D25239; D25239. DR PIR; F27060; F27060. DR PIR; I54509; I54509. DR RefSeq; NP_002115.2; NM_002124.3. DR UniGene; Hs.485130; -. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR UniGene; Hs.736560; -. DR ProteinModelPortal; Q29974; -. DR SMR; Q29974; -. DR BioGrid; 109368; 39. DR ChEMBL; CHEMBL3988561; -. DR DMDM; 74762149; -. DR EPD; Q29974; -. DR PeptideAtlas; Q29974; -. DR PRIDE; Q29974; -. DR TopDownProteomics; Q29974; -. DR DNASU; 3123; -. DR Ensembl; ENST00000360004; ENSP00000353099; ENSG00000196126. DR GeneID; 3123; -. DR CTD; 3123; -. DR DisGeNET; 3123; -. DR EuPathDB; HostDB:ENSG00000196126.10; -. DR GeneCards; HLA-DRB1; -. DR HGNC; HGNC:4948; HLA-DRB1. DR HPA; CAB015400; -. DR HPA; CAB034021; -. DR HPA; HPA043151; -. DR MalaCards; HLA-DRB1; -. DR MIM; 142857; gene. DR neXtProt; NX_Q29974; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR TreeFam; TF336626; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR ChiTaRS; HLA-DRB1; human. DR GenomeRNAi; 3123; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000196126; Expressed in 94 organ(s), highest expression level in spleen. DR ExpressionAtlas; Q29974; baseline and differential. DR Genevisible; Q29974; HS. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; NAS:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0016045; P:detection of bacterium; ISS:UniProtKB. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISS:UniProtKB. DR GO; GO:0006955; P:immune response; ISS:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISS:UniProtKB. DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; ISS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISS:UniProtKB. DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB. DR GO; GO:0051262; P:protein tetramerization; ISS:UniProtKB. DR GO; GO:2001179; P:regulation of interleukin-10 secretion; ISS:UniProtKB. DR GO; GO:0032673; P:regulation of interleukin-4 production; ISS:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR GO; GO:0042088; P:T-helper 1 type immune response; ISS:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DRB1-16 beta chain. FT /FTId=PRO_0000391833. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 42 42 R -> K (in allele DRB1*16:12). FT /FTId=VAR_062840. FT VARIANT 43 43 E -> K (in allele DRB1*16:11). FT /FTId=VAR_062841. FT VARIANT 56 56 L -> P (in allele DRB1*16:07). FT /FTId=VAR_062842. FT VARIANT 66 66 S -> N (in allele DRB1*16:08). FT /FTId=VAR_062843. FT VARIANT 76 76 Y -> F (in allele DRB1*16:09 and allele FT DRB1*16:10). FT /FTId=VAR_062844. FT VARIANT 96 96 F -> I (in allele DRB1*16:05 and allele FT DRB1*16:07). FT /FTId=VAR_062845. FT VARIANT 96 96 F -> L (in allele DRB1*16:02, allele FT DRB1*16:10, allele DRB1*16:11 and allele FT DRB1*16:12). FT /FTId=VAR_062846. FT VARIANT 101 101 R -> A (in allele DRB1*16:03; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062847. FT VARIANT 103 103 A -> L (in allele DRB1*16:04; requires 2 FT nucleotide substitutions). FT /FTId=VAR_062848. FT VARIANT 262 262 T -> R (in dbSNP:rs9269744). FT /FTId=VAR_062849. SQ SEQUENCE 266 AA; 30030 MW; 871CC341692ECA4D CRC64; MVCLKLPGGS CMTALTVTLM VLSSPLALAG DTRPRFLWQP KRECHFFNGT ERVRFLDRYF YNQEESVRFD SDVGEYRAVT ELGRPDAEYW NSQKDFLEDR RAAVDTYCRH NYGVGESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG MVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID A0A023IKK2_RAT Unreviewed; 287 AA. AC A0A023IKK2; D3ZT06; DT 09-JUL-2014, integrated into UniProtKB/TrEMBL. DT 09-JUL-2014, sequence version 1. DT 12-SEP-2018, entry version 42. DE SubName: Full=MHC class II beta chain {ECO:0000313|EMBL:AKO62641.1}; DE SubName: Full=RT1 class II, locus Db2 {ECO:0000313|Ensembl:ENSRNOP00000042899}; DE SubName: Full=RT1-Db2 {ECO:0000313|EMBL:AGV39020.1}; GN Name=RT1-Db2 {ECO:0000313|EMBL:AKO62641.1, GN ECO:0000313|Ensembl:ENSRNOP00000042899, ECO:0000313|RGD:1595922}; GN Synonyms=Db2 {ECO:0000313|EMBL:AGV39020.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AGV39020.1}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000042899, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000042899, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000042899} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000042899}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000313|EMBL:AGV39020.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DA {ECO:0000313|EMBL:AGV39020.1}, RC DA.1F {ECO:0000313|EMBL:AGV39021.1}, and RC DA.1H {ECO:0000313|EMBL:AGV39023.1}; RX PubMed=24586191; DOI=10.1371/journal.pgen.1004151; RG EURATRANS; RA Tuncel J., Haag S., Yau A.C.Y., Norin U., Baud A., Lonnblom E., RA Maratou K., Ytterberg A.J., Ekman D., Thordardottir S., RA Johannesson M., Gillett A., Stridh P., Jagodic M., Olsson T., RA Fernandez-Teruel A., Zubarev R.A., Mott R., Aitman T.J., Flint J., RA Holmdahl R.; RT "Natural polymorphisms in Tap2 influence negative selection and RT CD4?CD8 lineage commitment in the rat."; RL PLoS Genet. 10:e1004151-e1004151(2014). RN [4] {ECO:0000313|EMBL:AKO62641.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:AKO62641.1}; RA Monzon-Casanova E.; RT "Characterisation and functional analysis of the non-polymorphic MHC RT class II molecules RT1-Db2 and H2-Eb2."; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AABR07072809; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC222923; AGV39020.1; -; mRNA. DR EMBL; KC222924; AGV39021.1; -; mRNA. DR EMBL; KC222926; AGV39023.1; -; mRNA. DR EMBL; KP012532; AKO62641.1; -; mRNA. DR RefSeq; XP_006255973.2; XM_006255911.3. DR UniGene; Rn.148699; -. DR STRING; 10116.ENSRNOP00000042899; -. DR Ensembl; ENSRNOT00000042571; ENSRNOP00000042899; ENSRNOG00000030431. DR GeneID; 24981; -. DR UCSC; RGD:1595922; rat. DR CTD; 24981; -. DR RGD; 1595922; RT1-Db2. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-RNO-202424; Downstream TCR signaling. DR Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-RNO-202433; Generation of second messenger molecules. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Reactome; R-RNO-389948; PD-1 signaling. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000030431; Expressed in 8 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 287 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015219901. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 287 AA; 32180 MW; 44DC8F3C5A80DA9C CRC64; MVCLWLPRDP CVAAVVLSLL MLSPPVALVR DPRPRFLEQL KAECHYVKGR EHVWSVTRFI YNQEEFARFD SVFGKFLAVT ELGRPIAEYL NTQKDMLDNY RASVDRCRNN YDLVDIFMSN LKAKPKVTVY PSKTQPLEYH NLLVCSVSDF YPGTIEIRWF RNGEEEKTGV VSTDLISNGD WTYQTLVMLE TVPQGGEVYT CQVEHPSLTS PVRVEWRARS TSAQNKMLSG AMGMALGLFI LAVGLFIYLR NLRAGSVSHG AGEGAESSTS RLTGSRSECH TGPALSV // ID A0A087QGJ2_APTFO Unreviewed; 222 AA. AC A0A087QGJ2; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 25-OCT-2017, entry version 16. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:KFM00346.1}; DE Flags: Fragment; GN ORFNames=AS27_10946 {ECO:0000313|EMBL:KFM00346.1}; OS Aptenodytes forsteri (Emperor penguin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; OC Aptenodytes. OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM00346.1, ECO:0000313|Proteomes:UP000053286}; RN [1] {ECO:0000313|EMBL:KFM00346.1, ECO:0000313|Proteomes:UP000053286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM00346.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL225551; KFM00346.1; -; Genomic_DNA. DR Proteomes; UP000053286; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053286}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053286}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 198 220 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 96 183 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFM00346.1}. FT NON_TER 222 222 {ECO:0000313|EMBL:KFM00346.1}. SQ SEQUENCE 222 AA; 24313 MW; BAB5792F9093AF34 CRC64; AFLVHVASSC PLAANGSALA FGFTLIFNKN PLVCYNPDAR HFIPCDWGLL HGVAGLVATF LNNDTAWVQR AEDRRQACRD LATHFWASTA LRRTPPQVRI VPVPLPNTPN AVLLTCHVWG FYPPEVTVLW LHNGDMVATG DTTKLLPNGD WTYQTQVTLM VTAKAGDTFT CFVQHASLDR SLQEDWGPGL SLGLMVKVVM AAVIMTLGLV VFAAGTFIYC RQ // ID A0A087QGJ3_APTFO Unreviewed; 243 AA. AC A0A087QGJ3; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 25-OCT-2017, entry version 14. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:KFM00347.1}; DE Flags: Fragment; GN ORFNames=AS27_10947 {ECO:0000313|EMBL:KFM00347.1}; OS Aptenodytes forsteri (Emperor penguin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae; OC Aptenodytes. OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM00347.1, ECO:0000313|Proteomes:UP000053286}; RN [1] {ECO:0000313|EMBL:KFM00347.1, ECO:0000313|Proteomes:UP000053286} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM00347.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL225551; KFM00347.1; -; Genomic_DNA. DR Proteomes; UP000053286; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053286}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053286}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 220 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 97 187 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFM00347.1}. FT NON_TER 243 243 {ECO:0000313|EMBL:KFM00347.1}. SQ SEQUENCE 243 AA; 26201 MW; DF16A51BAED0850B CRC64; GAFLVHLASS CPLAANGSVL DFDFTLIFNK NPLVCYDPDA RHFVPCDWGL LRSCATHLAT FLNNGTAWVE RAEARRRACH DLAPQFLAST VLRRTPPQAR IIPSKTGNAR APVLLTCHVW GFYPPEVTVI WLHNGDIVGP GDHPPISAVP NGDWTYQTQV TLMVAPVAGD TFTCSVQHAS LDQPLLEDWG PGLSPGLTLK VAAATMVMAL GLGFFIAGVY RYQARPLAPG YTPLPGDNYP AGN // ID A0A087X3Z1_POEFO Unreviewed; 249 AA. AC A0A087X3Z1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 28-MAR-2018, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000000494}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000000494, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000000494, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000000494}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000000494} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01012298; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AYCK01012299; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000000495; ENSPFOP00000000494; ENSPFOG00000000515. DR GeneTree; ENSGT00900000140849; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28371 MW; 8285BCE85393921F CRC64; LCSRFRQSNL LSIQYYGSSG FMTHELFRCH FNSSELQDIH YSYSYIYNKV EFIQFDSRVG SFVGLNSFGE KLAARWNNGT GWLNVSKTYR EEICQPNAEL WYRLVLDRSV EPSVTLSTVV PPTGGPSSML TCSVYGFFPK QIRVTWMRNG QEVTSDVTST TELPDGAWLY QIHSSLEFKP RSGEKISCMV EHLSLEEPLT IDWSKPMPES EKIKIAFGVL GLILGLVLSL TGFIYYKKKA GDRLSLHRS // ID A0A087X4I6_POEFO Unreviewed; 250 AA. AC A0A087X4I6; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 2. DT 28-MAR-2018, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000000689}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000000689, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000000689, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000000689}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000000689} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01028490; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000000690; ENSPFOP00000000689; ENSPFOG00000000671. DR GeneTree; ENSGT00900000140849; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0K7A; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 250 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001832274. FT TRANSMEM 216 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 250 AA; 28535 MW; 6AA97E3B7C197A7F CRC64; MDPSALGWLL VIITINSAGG FISYGTDRCV FNSTELNDIE FIRSDFYNKL EIFRFSSSLG RFVGYTEYGV KQAEYRNNNP SIIAQMKAQK ETYCLHNIDI WYQTKLTKSV APTIRLYSRT PPAGHHPSML VCRVYDFYPK TIKVRWLRDG QEVTSDVTTT DEMEDGDWYY QVHSTLEYTP RSGERISCRV EHASLKEPLV TDWADPSMPD SERNKLAIGA SGLILGLILS LAGFIYYKRK ARGRILVPTS // ID A0A087X4P8_POEFO Unreviewed; 244 AA. AC A0A087X4P8; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 28-MAR-2018, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000000751}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000000751, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000000751, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000000751}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000000751} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01028490; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AYCK01028491; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000000753; ENSPFOP00000000751; ENSPFOG00000000763. DR GeneTree; ENSGT00900000140849; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0K7A; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 15 {ECO:0000256|SAM:SignalP}. FT CHAIN 16 244 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5013334399. FT TRANSMEM 210 231 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 107 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 244 AA; 27815 MW; DBF5D2437FADCB84 CRC64; LGWLLVIITI NSAGGFEHYE LSRCDFNSTE LKDIEYIRSN FYNKLEIMRF SSSLGKFVGY TEFGVKQAEY FNSNPSIIAG LKAQKETYCL NNVGNEYQAM LTKSVAPTIR LYSRTPPAGH HPSMLVCRVY DFYPKTIKVR WLRDGQEVTS DVTTTDEMED GDWYYQVHST LEYTPRSGER ISCRVEHASL KEPLVTDWEP SMPDSERNKL AIGASGLILG LILSLAGFIY YKRKARGNSF YTTS // ID A0A087X6T9_POEFO Unreviewed; 249 AA. AC A0A087X6T9; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 28-MAR-2018, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000001492}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000001492, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000001492, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000001492}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000001492} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01008976; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000001495; ENSPFOP00000001492; ENSPFOG00000001532. DR GeneTree; ENSGT00900000140849; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0W5S; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001832418. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28158 MW; 40585E46552FD704 CRC64; MAPSPLCWLL IVIIINSADG FRNCQVNLCA FNSTELLDIQ FISSYIYNKI EYVRFDSNVG KFIGYTEFGV KNAEQWNKDP SRIAMMRAQK ETYCLNNIGV DYPNVLTKSV IPTVTLHSRT PPAGHHPSML VCSVYDFYPK TINVGWLRDG QEVTSDVTTT DEMEDGDWYY QIHSTLEYTP RPGERISCKV EHASLKEPLI TDWDPSMPKS ERNKLIIGAS GMVLGLILSL AGYIYYKTKP RSALLLPLA // ID A0A087XKT1_POEFO Unreviewed; 249 AA. AC A0A087XKT1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 2. DT 28-MAR-2018, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000006384}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000006384, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000006384, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000006384}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000006384} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01025330; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_007543619.1; XM_007543557.2. DR Ensembl; ENSPFOT00000006395; ENSPFOP00000006384; ENSPFOG00000006403. DR GeneID; 103131825; -. DR GeneTree; ENSGT00900000140849; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001833098. FT TRANSMEM 215 235 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 202 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28281 MW; B664F72E022445CD CRC64; MAPSPLCWLL IFIIVNSADG FRECEVDHCV FNSTELSDIQ FIRSSIYNKL EWLRFDSSLG RFVGYTEFGV KEAERWNNDP SYLAAMKAQR ETYCLNNVGL YYQKVLTKSV APTAKLYSRT PPAGHHPSML VCRVFDFFPK TIKVGWLRDG QEVTSDVTTT DEMEDGDWYY QVLSTLEYTP RAGERISCRV EHASLKEPLI IDWDPSMPES VKNKLVIGAS GLMMGLVLLL AGFLYNNRKL KGPILVPIS // ID A0A087YDR0_POEFO Unreviewed; 247 AA. AC A0A087YDR0; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 2. DT 28-MAR-2018, entry version 16. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000016163}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016163, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000016163, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000016163}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016163} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01021127; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000016185; ENSPFOP00000016163; ENSPFOG00000016082. DR GeneTree; ENSGT00900000140849; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0K7A; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 213 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 110 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 247 AA; 28086 MW; 85CF962B5245739C CRC64; ICETSLKIRL LFLYAPYGFE VHSVFRCLFN STELKDTQYI YSYIYNKVEF LRFDSNIGLY VGYTSFGMRQ AENLNNNPVA LSSRRAQKEV FCHHNSGVWY RNILNRSVAP SVTLSSAAPP AGGHPAMLTC SVYGFYPKQI RVTWMRDGQE VTSDVTSTAE LPDGAWLYQM HSSLEFKPRS GERISCRVEH ASLKEPLVTD WDPSMPDSER NKLAIGASGL ILGLILSLAG FIYYKRKARD RIRTRTN // ID A0A087YEM3_POEFO Unreviewed; 253 AA. AC A0A087YEM3; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 28-MAR-2018, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000016476}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016476, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000016476, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000016476}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016476} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01006469; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000016498; ENSPFOP00000016476; ENSPFOG00000016398. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G0GI5; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 253 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001834401. FT TRANSMEM 210 232 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 111 197 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 253 AA; 29018 MW; F62021232573107A CRC64; NMQATNFVFL ELLLVFSSEG AFYGYYLAHC QFNSPGSSDV VFVEQLYFNK ILLGQYNSTL GKVVAFTKKA EEFADMLNKL PRFLTHEMRL TNHCKISAQL ANEKLLTAVE PYVWLRSVKA EYSQHQQKLV CSAYDFYPKK IRVTWLKDGK KVVTSTEELP NGNWLYQIHS YLEFTPKPGE KIACMVEHAS LKEPQLYDWD LPELDSGKNM LVVDSAGLLL GLLFSVTGFL FFKKKSIERV RVSTTEEIPE NNL // ID A0A087YFZ1_POEFO Unreviewed; 279 AA. AC A0A087YFZ1; DT 29-OCT-2014, integrated into UniProtKB/TrEMBL. DT 29-OCT-2014, sequence version 1. DT 28-MAR-2018, entry version 13. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000016944}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000016944, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000016944, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000016944}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000016944} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01006477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000016966; ENSPFOP00000016944; ENSPFOG00000016876. DR GeneTree; ENSGT00900000140849; -. DR OMA; QIRVTWL; -. DR OrthoDB; EOG091G0W5S; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 279 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001834449. FT TRANSMEM 213 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 111 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 279 AA; 31409 MW; 560C8FB883BC879D CRC64; MPQAQGFSVF LVLFLTFSPG GAYYLYVMER CQFSSSDGHD AVLLDQFYYN KILEGQYNST VGKVTAYTEK GEVYAIILNN DPGFIKREIW KTNLCKRNVP LGQKLLTAVE PYVWLRSVKA EYSQHQQKLV CSAYDFYPKQ IRVTWLRDGK DVTSGVTSTD ELPNGNWLYQ IHSYLEFTPK PGEKIACMVE HASLKEPQLH DWEPESDSKW SKIAVGSAGL LLGLLFSAAG FIYYKTTSNV LPRTGGGAYN RGCMSRRNPL GCRNVEKPHT HLSTTGNSS // ID A0A091CXW4_FUKDA Unreviewed; 301 AA. AC A0A091CXW4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 20-JUN-2018, entry version 19. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|EMBL:KFO23103.1}; GN ORFNames=H920_15441 {ECO:0000313|EMBL:KFO23103.1}; OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Fukomys. OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO23103.1, ECO:0000313|Proteomes:UP000028990}; RN [1] {ECO:0000313|EMBL:KFO23103.1, ECO:0000313|Proteomes:UP000028990} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Liver {ECO:0000313|EMBL:KFO23103.1}; RA Gladyshev V.N., Fang X.; RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of RT African mole rats."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KN123813; KFO23103.1; -; Genomic_DNA. DR Ensembl; ENSFDAT00000019913; ENSFDAP00000006619; ENSFDAG00000015337. DR Proteomes; UP000028990; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028990}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028990}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 301 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001872796. FT TRANSMEM 225 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 301 AA; 33785 MW; 1B96AD7E2B637375 CRC64; MGSGWVGWVL VPLVSLTRLE SSTTEGRESP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEFVRFDSDV GVFVALTELG KPDAEQWNNR PDILETSRAS VDMVCRRNYR LGAPFTLGRR VEPLVTVYPE RTPFPQQHNL LLCSVTGFYP GDIKIQWFRN GQEERAGVVS SGLIRNGDWT FQTAVMLEMT PELGDVYSCR VEHSSLLSPV AVEWRAQSEY CWGKMLSGVA ASLLGLIFLL LGFFIHFRAW KGSVETRSDN EVNYISSSVS LDGRPFSQFF GQKEMLWGQG GEEGVADGTV S // ID A0A091DJZ0_FUKDA Unreviewed; 291 AA. AC A0A091DJZ0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 25-OCT-2017, entry version 17. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:KFO23106.1}; GN ORFNames=H920_15444 {ECO:0000313|EMBL:KFO23106.1}; OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Fukomys. OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO23106.1, ECO:0000313|Proteomes:UP000028990}; RN [1] {ECO:0000313|EMBL:KFO23106.1, ECO:0000313|Proteomes:UP000028990} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Liver {ECO:0000313|EMBL:KFO23106.1}; RA Gladyshev V.N., Fang X.; RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of RT African mole rats."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KN123813; KFO23106.1; -; Genomic_DNA. DR Proteomes; UP000028990; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028990}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028990}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 291 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001872106. FT DOMAIN 114 208 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 291 AA; 31770 MW; 3ABF8B880D45CA2F CRC64; MNSVLPLLLG LGLGCTGAGG FMAHVESTCL LDDNGTPKDF TYCISYNKDL LTCWDPEKDR MDPCEFGTLH MLAVSLSNYL NNSTRLLQRL RNGLQDCGTH TQPFWESLTH RKKPPSVQVA QTTPFNTREP VMLACYVWGF YPADVAISWL KNGQLVTPHS SVWKTAQPNG DWTYQTISHL ALTPSHGDVY TCVVEHAGTS EPTRQDWTPG LSPMQTVKVS VSAVTLGLGI IIFSIGLSSW GKAGSSSYTP LPGSTYTKGN ITIARFAPGP SEGRRVGRVR AVFSQSRGEL L // ID A0A091DQV1_FUKDA Unreviewed; 805 AA. AC A0A091DQV1; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 25-OCT-2017, entry version 17. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:KFO32838.1}; GN ORFNames=H920_05759 {ECO:0000313|EMBL:KFO32838.1}; OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Fukomys. OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO32838.1, ECO:0000313|Proteomes:UP000028990}; RN [1] {ECO:0000313|EMBL:KFO32838.1, ECO:0000313|Proteomes:UP000028990} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Liver {ECO:0000313|EMBL:KFO32838.1}; RA Gladyshev V.N., Fang X.; RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of RT African mole rats."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KN122119; KFO32838.1; -; Genomic_DNA. DR Proteomes; UP000028990; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 3. DR Gene3D; 3.10.320.10; -; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 3. DR Pfam; PF00969; MHC_II_beta; 2. DR ProDom; PD000328; MHC_II_b_N; 2. DR SMART; SM00407; IGc1; 3. DR SMART; SM00921; MHC_II_beta; 2. DR SUPFAM; SSF48726; SSF48726; 3. DR SUPFAM; SSF54452; SSF54452; 2. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00290; IG_MHC; 3. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028990}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028990}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 805 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001871870. FT TRANSMEM 200 222 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 535 556 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 744 766 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 87 202 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 433 537 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 642 746 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 805 AA; 89686 MW; 6419676C917A5AC1 CRC64; MLCLWLPGGS CMAPLLMAVT LMVLSPPLAL ARDTRPRFME SVKYECHFSN GTERVRYVER LFYNQEEFVR FDSEVGEYRS VTELGRPDAK SWNSQKETLE DRRAAVDTYC RHNYGVGESF TVQRRGHMEV RWFRNGQEQE DGVVSTGLIR NGDWTFQTLV MLETVPRSGE VYVCRVEHPS WSSPVAVEWR AQSGSARSKM LSGVGGFVLG LLFLGAGLFI YCRNQKAEVM VSEKSEVTDL TLGMLSVDTL EFNQQHAVSR APRRLLGGSS DSDTDGAESS PGFGLGQERV CFPAVGLQGR QGEPGQEQEA RVTRGRVLVF PSGGQCPPKR VALTGSLMPS ARFMEYVTSE CHFSNGTERV RFLKRYVYNQ EENLRFDSDV GEFRAVTELG RPDAESWNSQ KETLEQKRAE VDTVCRHNYG VGESFTVQRR VEPKVTVYPT KTQALQHHSL LVCSVSGFYP GHIEVRWFRN GQEQEDGVVS TGLIRNGDWT FQTLVMLETV PRSGEVYVCR VEHPSWSSPV TVEWRAQSGS ARSKMLSGVG GFVLGLLFLG AGLFIYCRNQ KAEVVVSEKS QDTLQFNQQH AVSRAPRRLL CGSSDSDTDG AESSPGFGLG QERAPESPSH PSSLALESPE SAFLSEERSV EPKVTVYPTK TQALQHHSLL VCSVSGFYPG HIEVRWFRNG QEQEDGVVST GLIRNGDWTF QTLVMLETVP RSGEVYVCRV EHPSWSSPVT VEWRAQSGSA RSKMLSGVGG FMLGLLFLGA GLFIYCRNQK GDSEVQPIGN VLETCLTDRF ALPSTACNRD ERGNR // ID A0A091E458_FUKDA Unreviewed; 337 AA. AC A0A091E458; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 20-JUN-2018, entry version 18. DE SubName: Full=H-2 class II histocompatibility antigen, A beta chain {ECO:0000313|EMBL:KFO37340.1}; GN ORFNames=H920_01256 {ECO:0000313|EMBL:KFO37340.1}; OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Fukomys. OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO37340.1, ECO:0000313|Proteomes:UP000028990}; RN [1] {ECO:0000313|EMBL:KFO37340.1, ECO:0000313|Proteomes:UP000028990} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Liver {ECO:0000313|EMBL:KFO37340.1}; RA Gladyshev V.N., Fang X.; RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of RT African mole rats."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KN120960; KFO37340.1; -; Genomic_DNA. DR Ensembl; ENSFDAT00000023072; ENSFDAP00000010162; ENSFDAG00000017990. DR Proteomes; UP000028990; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028990}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028990}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 337 AA; 38615 MW; 638ABC55B31F3F8F CRC64; MPIAQRNIVP DSKQKAKKIR TQIRKVHPDK MQMPIAEDFV YQFKCQCYFT NGTQRVRYLT RYIYNREEFV RFDSDLGEHR AVTELGRPSA KYWNSQKEIL DRTRAELDTV CRHNYELDIP VTVQRRVEPR VSISLSKTEA LNHHNLLVCS AWDFYPQQIK VQWFRNGQEE TSGVVSTPVI RNGDWTFQIL VMLEMTPRQG DVYTCRVEHP SLQSPVTVEW RAQSESAQSK MLSGIGGLVL GLIFLGLGVF IRRRNQKGTR GPPPAGNEGF SPDPVLGGRG TGVGESGVRG RCTWKNSPVC GLFPAVWMRN ERRSPVCQEA PEIFPRTWWH LSVALLP // ID A0A091E885_CORBR Unreviewed; 113 AA. AC A0A091E885; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-OCT-2016, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFO52704.1}; DE Flags: Fragment; GN ORFNames=N302_10850 {ECO:0000313|EMBL:KFO52704.1}; OS Corvus brachyrhynchos (American crow). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Corvoidea; Corvidae; OC Corvus. OX NCBI_TaxID=85066 {ECO:0000313|EMBL:KFO52704.1, ECO:0000313|Proteomes:UP000052976}; RN [1] {ECO:0000313|EMBL:KFO52704.1, ECO:0000313|Proteomes:UP000052976} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N302 {ECO:0000313|EMBL:KFO52704.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KK717795; KFO52704.1; -; Genomic_DNA. DR Proteomes; UP000052976; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000052976}; KW Reference proteome {ECO:0000313|Proteomes:UP000052976}. FT DOMAIN 20 94 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFO52704.1}. FT NON_TER 113 113 {ECO:0000313|EMBL:KFO52704.1}. SQ SEQUENCE 113 AA; 13316 MW; 60036A616BC9DE4A CRC64; GAPPDLCPAH TGVFQRRIKV ECHFINGTER VRFVQMHSYN REQYTHFDSD VGVCIRDTPD GEKQAWYWNS QLENPEYRWA LVDMHCHYNY EIVARFLVSR RVPPSPSQSL PVH // ID A0A091HI85_BUCRH Unreviewed; 98 AA. AC A0A091HI85; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-OCT-2016, entry version 9. DE SubName: Full=HLA class II histocompatibility antigen, DR beta 5 chain {ECO:0000313|EMBL:KFO94507.1}; DE Flags: Fragment; GN ORFNames=N320_05062 {ECO:0000313|EMBL:KFO94507.1}; OS Buceros rhinoceros silvestris. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros. OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO94507.1, ECO:0000313|Proteomes:UP000054064}; RN [1] {ECO:0000313|EMBL:KFO94507.1, ECO:0000313|Proteomes:UP000054064} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO94507.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL536207; KFO94507.1; -; Genomic_DNA. DR Proteomes; UP000054064; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054064}; KW Reference proteome {ECO:0000313|Proteomes:UP000054064}. FT DOMAIN 17 91 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFO94507.1}. FT NON_TER 98 98 {ECO:0000313|EMBL:KFO94507.1}. SQ SEQUENCE 98 AA; 11586 MW; 6332FD38A33EDA84 CRC64; PDLPPAHPGY FQMMDKFECH YTNGTERVRF LDRAIYNRQQ DVHFDSDVGI YVADTPMGKP TASYWNSLPD ILEDRRTAVD RFCRHNYKVS TPFITERR // ID A0A091J9V5_EGRGA Unreviewed; 243 AA. AC A0A091J9V5; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 22-NOV-2017, entry version 17. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:KFP16465.1}; DE Flags: Fragment; GN ORFNames=Z169_14344 {ECO:0000313|EMBL:KFP16465.1}; OS Egretta garzetta (Little egret). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta. OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP16465.1, ECO:0000313|Proteomes:UP000053119}; RN [1] {ECO:0000313|EMBL:KFP16465.1, ECO:0000313|Proteomes:UP000053119} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP16465.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KK501578; KFP16465.1; -; Genomic_DNA. DR Proteomes; UP000053119; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053119}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053119}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 97 187 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFP16465.1}. FT NON_TER 243 243 {ECO:0000313|EMBL:KFP16465.1}. SQ SEQUENCE 243 AA; 26485 MW; DE2A921217961EB9 CRC64; GAFLVHMASS CSLAANGSLL DFDFALVFNK NPLVCYDPDT LRFVPCDWGL LHTVATNFAT FLNNSTTWVE RVEARRQACC DLAPHFWAST VLRRMPPQAR IVPSKIGKTQ GPVRLTCHVW GFYPPEVTVI WLHNGDIVGP GDHPPISAIP NGDWTYQTQV TLTVVPMPGD TFTCSVQHAS LDQPLLEDWS PGLSPGLTLK VVAATVVMVL GLSIFSVGVY HYWAKPPAPG YTPLPGDNYP AGN // ID A0A091QP23_HALAL Unreviewed; 158 AA. AC A0A091QP23; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 25-OCT-2017, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFQ11194.1}; DE Flags: Fragment; GN ORFNames=N329_07122 {ECO:0000313|EMBL:KFQ11194.1}; OS Haliaeetus albicilla (White-tailed sea-eagle). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Falconiformes; Accipitridae; OC Accipitrinae; Haliaeetus. OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ11194.1, ECO:0000313|Proteomes:UP000054379}; RN [1] {ECO:0000313|EMBL:KFQ11194.1, ECO:0000313|Proteomes:UP000054379} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ11194.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KK665728; KFQ11194.1; -; Genomic_DNA. DR Proteomes; UP000054379; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054379}; KW Reference proteome {ECO:0000313|Proteomes:UP000054379}. FT DOMAIN 94 158 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFQ11194.1}. FT NON_TER 158 158 {ECO:0000313|EMBL:KFQ11194.1}. SQ SEQUENCE 158 AA; 18665 MW; 3DF05BD1536E9888 CRC64; TGFFQEMAKF ECHHLNGTKN IRYLEKYIYN REQRAHFDSD VGHFVADTLL GEPDAKYWNS QPDLLERKRA EVDRLCRHNY EVVTPFTVER RVEPKVRVSP MQSSSLPQTN RLVCYVTGFY PAEIEVKWFK NGQEETEHVV STDMIQNGDW TYQVLVML // ID A0A091WL04_OPIHO Unreviewed; 113 AA. AC A0A091WL04; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-OCT-2016, entry version 10. DE SubName: Full=H-2 class II histocompatibility antigen, A-D beta chain {ECO:0000313|EMBL:KFR16264.1}; DE Flags: Fragment; GN ORFNames=N306_05460 {ECO:0000313|EMBL:KFR16264.1}; OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae; OC Opisthocomus. OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR16264.1, ECO:0000313|Proteomes:UP000053605}; RN [1] {ECO:0000313|EMBL:KFR16264.1, ECO:0000313|Proteomes:UP000053605} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR16264.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KK735876; KFR16264.1; -; Genomic_DNA. DR PhylomeDB; A0A091WL04; -. DR Proteomes; UP000053605; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053605}; KW Reference proteome {ECO:0000313|Proteomes:UP000053605}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 113 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001881624. FT DOMAIN 29 103 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFR16264.1}. FT NON_TER 113 113 {ECO:0000313|EMBL:KFR16264.1}. SQ SEQUENCE 113 AA; 12735 MW; 9760178E69B8FA2A CRC64; AVLVALMVLG AHPGGGEETS GYFQEMFKGD CYFTNGTEKV RLVTRFIHNR QQFAHFDSDV GLYVADTPLG EPDAEYWNSQ PELLEQTRAQ VDTVCRNNYE ADTPFTVGRR GER // ID A0A093BNI4_CHAPE Unreviewed; 191 AA. AC A0A093BNI4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 25-OCT-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFU87751.1}; DE Flags: Fragment; GN ORFNames=M959_02433 {ECO:0000313|EMBL:KFU87751.1}; OS Chaetura pelagica (Chimney swift). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Apodiformes; Apodidae; Chaetura. OX NCBI_TaxID=8897 {ECO:0000313|EMBL:KFU87751.1, ECO:0000313|Proteomes:UP000031515}; RN [1] {ECO:0000313|EMBL:KFU87751.1, ECO:0000313|Proteomes:UP000031515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M959 {ECO:0000313|EMBL:KFU87751.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KN126229; KFU87751.1; -; Genomic_DNA. DR Proteomes; UP000031515; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031515}; KW Reference proteome {ECO:0000313|Proteomes:UP000031515}. FT DOMAIN 104 191 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFU87751.1}. FT NON_TER 191 191 {ECO:0000313|EMBL:KFU87751.1}. SQ SEQUENCE 191 AA; 22297 MW; A1FB501AC1E6A144 CRC64; GAPPDLTPPD TGVFLQMMKA ECQFLNGTER VRLVMRNIHN RQQDLHFDSD VGKYVGDTPW GQRQADYWNS QPDILEQRWT DVDTYCRYNY GMVTPFTVER RVQPEVEIFP VQSGSLPQTD RLVCAVMDFY PPEIEVKWFK DEQEETERVV STDVIQNGDW TYQVLVMLET SPERGESYRC QVEHASLQQP L // ID A0A093DGR4_CHAPE Unreviewed; 174 AA. AC A0A093DGR4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 25-OCT-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFU86786.1}; DE Flags: Fragment; GN ORFNames=M959_10922 {ECO:0000313|EMBL:KFU86786.1}; OS Chaetura pelagica (Chimney swift). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Apodiformes; Apodidae; Chaetura. OX NCBI_TaxID=8897 {ECO:0000313|EMBL:KFU86786.1, ECO:0000313|Proteomes:UP000031515}; RN [1] {ECO:0000313|EMBL:KFU86786.1, ECO:0000313|Proteomes:UP000031515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M959 {ECO:0000313|EMBL:KFU86786.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KN126148; KFU86786.1; -; Genomic_DNA. DR Proteomes; UP000031515; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031515}; KW Reference proteome {ECO:0000313|Proteomes:UP000031515}. FT DOMAIN 87 174 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFU86786.1}. FT NON_TER 174 174 {ECO:0000313|EMBL:KFU86786.1}. SQ SEQUENCE 174 AA; 20568 MW; AE1F46D8E8A3F9AA CRC64; ESECQFLNGT ERVRYVQRYL YNRQQNLHFD SDVGKFVGDT PWGQRRVADY WNSQPDFMEQ RRAAVDTFCR HNYRVASPFS VERRVQPKVR VSPMQSGSLP QTDRLVCYVS GFYPPEIEVK WFKDEQEETE RVVSTDVIQN GDWTYQVLVM LETSPERGES YRCQVEHASL QQPL // ID A0A093EQA0_9AVES Unreviewed; 243 AA. AC A0A093EQA0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 25-OCT-2017, entry version 15. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:KFV16716.1}; DE Flags: Fragment; GN ORFNames=N339_07503 {ECO:0000313|EMBL:KFV16716.1}; OS Pterocles gutturalis (yellow-throated sandgrouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Ciconiiformes; Pteroclidae; OC Pterocles. OX NCBI_TaxID=240206 {ECO:0000313|EMBL:KFV16716.1, ECO:0000313|Proteomes:UP000053149}; RN [1] {ECO:0000313|EMBL:KFV16716.1, ECO:0000313|Proteomes:UP000053149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N339 {ECO:0000313|EMBL:KFV16716.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL248992; KFV16716.1; -; Genomic_DNA. DR Proteomes; UP000053149; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053149}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053149}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 201 220 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 96 186 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV16716.1}. FT NON_TER 243 243 {ECO:0000313|EMBL:KFV16716.1}. SQ SEQUENCE 243 AA; 26333 MW; 684419958C8AC3FF CRC64; GAFLIHMASS CHLAANGSTL DFGFSIVFNK NQLVCYDPDD RLFVPCDFGL LHPYATSLAA ILNNGTAWLE RVEARQRACS DLATQFWASS AQRQTPPQAL VISSETSNAR APVLLTCHVW GFYPPEVTVI WLRNGDIAEP GEHPPISAVP NGDWTYQTQV TLMVAPVAGD TYTCSVQHAS LQQPLLEDWR PGLSPGLTLK VAAATVVMAL GLSFFITGVY RYRARPPAPG YTPLPGDNYP AGN // ID A0A093GBE9_DRYPU Unreviewed; 250 AA. AC A0A093GBE9; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 20-DEC-2017, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFV66508.1}; DE Flags: Fragment; GN ORFNames=N307_08943 {ECO:0000313|EMBL:KFV66508.1}; OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Picoides. OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV66508.1, ECO:0000313|Proteomes:UP000053875}; RN [1] {ECO:0000313|EMBL:KFV66508.1, ECO:0000313|Proteomes:UP000053875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV66508.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL215776; KFV66508.1; -; Genomic_DNA. DR Proteomes; UP000053875; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053875}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053875}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 250 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001883341. FT TRANSMEM 225 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 250 250 {ECO:0000313|EMBL:KFV66508.1}. SQ SEQUENCE 250 AA; 27798 MW; 6FF4F2EC1611CF7B CRC64; MEPGAVLAAV ALLVAPVVLG AHPAGAEKLS GVFLEMEKAE CQFLNGPERV RFVDSYIHNR EQYVHFDSDL GIFVADTPLG ERQAQHLNSL PEFLEQKRAE VDTFCRNNYK AVTSFAVERR VQPQVQIHLV QSSSLPQSTR LVCAVMDFYP AEVEVKWFRN GQEETESVVS TEVLPNGDWT YQVLVLLETS PQPGDTYLCQ VEHSSLQHPI SQRWELPSEP GRSKMLTGVG GLVLGLLCLG LGLCLHLRSK // ID A0A093IDG3_DRYPU Unreviewed; 117 AA. AC A0A093IDG3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 20-DEC-2017, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DRB1-4 beta chain {ECO:0000313|EMBL:KFV64766.1}; DE Flags: Fragment; GN ORFNames=N307_00838 {ECO:0000313|EMBL:KFV64766.1}; OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Picoides. OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV64766.1, ECO:0000313|Proteomes:UP000053875}; RN [1] {ECO:0000313|EMBL:KFV64766.1, ECO:0000313|Proteomes:UP000053875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV64766.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL215463; KFV64766.1; -; Genomic_DNA. DR Proteomes; UP000053875; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053875}; KW Reference proteome {ECO:0000313|Proteomes:UP000053875}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 117 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001887287. FT DOMAIN 36 110 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV64766.1}. FT NON_TER 117 117 {ECO:0000313|EMBL:KFV64766.1}. SQ SEQUENCE 117 AA; 13367 MW; FB01C5F7B70708B7 CRC64; GRVLGAVAML VALVVLRAQP GCGEKTTGFF QEVSEHKCQF FNGSERVRFI NRFIYNGQQY LHFDSDLGLA VADLPMGEAT AEHWNSQSDI LEYLQGSVER FCRHNYEVHK PFTVERR // ID A0A093J5P3_DRYPU Unreviewed; 112 AA. AC A0A093J5P3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 20-DEC-2017, entry version 11. DE SubName: Full=SLA class II histocompatibility antigen, DQ haplotype C beta chain {ECO:0000313|EMBL:KFV74274.1}; DE Flags: Fragment; GN ORFNames=N307_06864 {ECO:0000313|EMBL:KFV74274.1}; OS Dryobates pubescens (Downy woodpecker) (Picoides pubescens). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Piciformes; Picidae; Picoides. OX NCBI_TaxID=118200 {ECO:0000313|EMBL:KFV74274.1, ECO:0000313|Proteomes:UP000053875}; RN [1] {ECO:0000313|EMBL:KFV74274.1, ECO:0000313|Proteomes:UP000053875} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N307 {ECO:0000313|EMBL:KFV74274.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL217160; KFV74274.1; -; Genomic_DNA. DR Proteomes; UP000053875; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053875}; KW Reference proteome {ECO:0000313|Proteomes:UP000053875}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 112 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001885313. FT DOMAIN 29 103 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFV74274.1}. FT NON_TER 112 112 {ECO:0000313|EMBL:KFV74274.1}. SQ SEQUENCE 112 AA; 12724 MW; A1D59B61FB79F8FD CRC64; AMLVAVLVLG AQLARGRDIS GFLQVQHKSH CYFSNGTQRV RLLNRYIQNH QQLLHFDSDL GHFVADVPLG ELIAESWNTQ PGLLEGVWAV VETFCWNNYQ VAKSFTLERR GQ // ID A0A093KSB1_EURHL Unreviewed; 94 AA. AC A0A093KSB1; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-OCT-2016, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFW00396.1}; DE Flags: Fragment; GN ORFNames=N326_08420 {ECO:0000313|EMBL:KFW00396.1}; OS Eurypyga helias (Sunbittern). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Gruiformes; Eurypygidae; Eurypyga. OX NCBI_TaxID=54383 {ECO:0000313|EMBL:KFW00396.1, ECO:0000313|Proteomes:UP000054232}; RN [1] {ECO:0000313|EMBL:KFW00396.1, ECO:0000313|Proteomes:UP000054232} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N326 {ECO:0000313|EMBL:KFW00396.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KK559606; KFW00396.1; -; Genomic_DNA. DR Proteomes; UP000054232; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054232}; KW Reference proteome {ECO:0000313|Proteomes:UP000054232}. FT DOMAIN 10 84 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFW00396.1}. FT NON_TER 94 94 {ECO:0000313|EMBL:KFW00396.1}. SQ SEQUENCE 94 AA; 10912 MW; 519405252493E943 CRC64; TGFFQEMLTG HCHFTNGTER VRLVVRVVFN RQQYVHFDSD VGVFVADTPL GEPDARSWNS QPDVLERKRA EVDTICRHNY GAWTPFATER RGER // ID A0A093PM96_9PASS Unreviewed; 101 AA. AC A0A093PM96; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-OCT-2016, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFW77958.1}; DE Flags: Fragment; GN ORFNames=N305_05329 {ECO:0000313|EMBL:KFW77958.1}; OS Manacus vitellinus (golden-collared manakin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus. OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW77958.1, ECO:0000313|Proteomes:UP000053258}; RN [1] {ECO:0000313|EMBL:KFW77958.1, ECO:0000313|Proteomes:UP000053258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW77958.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL670058; KFW77958.1; -; Genomic_DNA. DR Proteomes; UP000053258; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053258}; KW Reference proteome {ECO:0000313|Proteomes:UP000053258}. FT DOMAIN 20 94 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFW77958.1}. FT NON_TER 101 101 {ECO:0000313|EMBL:KFW77958.1}. SQ SEQUENCE 101 AA; 11798 MW; 42D33FB7FACB6EF8 CRC64; GAPPDPCPAH TGVFQYLIIS KCHFINGTER VRFVGRLIYN REQQLHFDSD VGVYVGDTPR GEIQARHWNS DQEELESKRS TVDWFCRHNY EGFTPFTVNR R // ID A0A093Q4Q7_9PASS Unreviewed; 116 AA. AC A0A093Q4Q7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-OCT-2016, entry version 9. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:KFW83968.1}; DE Flags: Fragment; GN ORFNames=N305_03829 {ECO:0000313|EMBL:KFW83968.1}; OS Manacus vitellinus (golden-collared manakin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus. OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW83968.1, ECO:0000313|Proteomes:UP000053258}; RN [1] {ECO:0000313|EMBL:KFW83968.1, ECO:0000313|Proteomes:UP000053258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW83968.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL671865; KFW83968.1; -; Genomic_DNA. DR Proteomes; UP000053258; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053258}; KW Reference proteome {ECO:0000313|Proteomes:UP000053258}. FT DOMAIN 20 94 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFW83968.1}. FT NON_TER 116 116 {ECO:0000313|EMBL:KFW83968.1}. SQ SEQUENCE 116 AA; 13620 MW; AF6124B43E2CD6A9 CRC64; GAPPDPCPAH TGVFQRVTKR ECHFINSTER VRLLERYIYN REQLLHFDSD VGVHVEDTPH GEKFARSLNS QKEYMEYTRS AVDWYCLHNY RVVTPFTVER RVHPNPSQSL QAHPMP // ID A0A093Q9N1_9PASS Unreviewed; 84 AA. AC A0A093Q9N1; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-OCT-2016, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFW80887.1}; DE Flags: Fragment; GN ORFNames=N305_00394 {ECO:0000313|EMBL:KFW80887.1}; OS Manacus vitellinus (golden-collared manakin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus. OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW80887.1, ECO:0000313|Proteomes:UP000053258}; RN [1] {ECO:0000313|EMBL:KFW80887.1, ECO:0000313|Proteomes:UP000053258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW80887.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL671065; KFW80887.1; -; Genomic_DNA. DR Proteomes; UP000053258; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053258}; KW Reference proteome {ECO:0000313|Proteomes:UP000053258}. FT DOMAIN 1 69 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFW80887.1}. FT NON_TER 84 84 {ECO:0000313|EMBL:KFW80887.1}. SQ SEQUENCE 84 AA; 10081 MW; F9CE8AA89F1FA083 CRC64; NGTERVRYVE RHIYNREQQL HFDSDVGVYV GDTPFGESWA RYWNSNPAEL EYRRTLVDSY CRYDYKIVTP FGVERRERIP SSPS // ID A0A093QHA7_9PASS Unreviewed; 109 AA. AC A0A093QHA7; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-OCT-2016, entry version 9. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFW83457.1}; DE Flags: Fragment; GN ORFNames=N305_00385 {ECO:0000313|EMBL:KFW83457.1}; OS Manacus vitellinus (golden-collared manakin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus. OX NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW83457.1, ECO:0000313|Proteomes:UP000053258}; RN [1] {ECO:0000313|EMBL:KFW83457.1, ECO:0000313|Proteomes:UP000053258} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW83457.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL671676; KFW83457.1; -; Genomic_DNA. DR Proteomes; UP000053258; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053258}; KW Reference proteome {ECO:0000313|Proteomes:UP000053258}. FT DOMAIN 19 93 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KFW83457.1}. FT NON_TER 109 109 {ECO:0000313|EMBL:KFW83457.1}. SQ SEQUENCE 109 AA; 12668 MW; 65E5A9B890BEA9D8 CRC64; APPDPCPAHT GVFQDMFKGE CHFINGTERV KFILRYIYNR EQYMHFDSDV GVYVADTPLG EIQAKYKNSK KEELDRRQDE VDTICRNNYE VNAPFSVERR VPPSPLQSL // ID A0A094N606_ANTCR Unreviewed; 248 AA. AC A0A094N606; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 25-OCT-2017, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFZ62076.1}; DE Flags: Fragment; GN ORFNames=N321_08102 {ECO:0000313|EMBL:KFZ62076.1}; OS Antrostomus carolinensis (Chuck-will's-widow) (Caprimulgus OS carolinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Caprimulgiformes; Caprimulgidae; OC Antrostomus. OX NCBI_TaxID=279965 {ECO:0000313|EMBL:KFZ62076.1, ECO:0000313|Proteomes:UP000053620}; RN [1] {ECO:0000313|EMBL:KFZ62076.1, ECO:0000313|Proteomes:UP000053620} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N321 {ECO:0000313|EMBL:KFZ62076.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL355823; KFZ62076.1; -; Genomic_DNA. DR Proteomes; UP000053620; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053620}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000053620}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 248 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001903042. FT TRANSMEM 225 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 248 248 {ECO:0000313|EMBL:KFZ62076.1}. SQ SEQUENCE 248 AA; 28044 MW; 7B371638D4D9FA8C CRC64; MGTGRVLGTG AVLVALVVLG AHPAHGEETS CEFRPLFQAE CQFLNGTERV RFVTRSIYNR EQIVHYDSDV GDYVADTPLG EPQAKYWNSQ PDLLEQRRAE VDTYCRHNYG VGTPFTIERR VQPKVKVSPM QSSSLPQTDR LVCYVTGFYP AEIEVKWFKN GQEETERVVS TDVIQNGDWT YQVLVMLETT PQRGDTYTCQ VEHVSLQHPV TQRWELQSDG ARSKMLTGVG GFVLGLIFLA VGLFLYMR // ID A0A096M9K6_POEFO Unreviewed; 249 AA. AC A0A096M9K6; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 28-MAR-2018, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPFOP00000028097}; OS Poecilia formosa (Amazon molly) (Limia formosa). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Poecilia. OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000028097, ECO:0000313|Proteomes:UP000028760}; RN [1] {ECO:0000313|Ensembl:ENSPFOP00000028097, ECO:0000313|Proteomes:UP000028760} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=female {ECO:0000313|Ensembl:ENSPFOP00000028097}; RA Schartl M., Warren W.; RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPFOP00000028097} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AYCK01006477; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPFOT00000027775; ENSPFOP00000028097; ENSPFOG00000023257. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G0GI5; -. DR Proteomes; UP000028760; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000028760}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000028760}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 205 226 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 98 192 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28279 MW; 19BE6055BDB07EEC CRC64; LLLVFSSEDF LGAFYGYYLG RCQFNSPDSN DVVLVEQLYF NKILLGQYNS TLGKVVAFIE KAEAYADMLN KMPRFQAHQI WKINRCKTGA QLANENLPAA VEPYVWLRSV KAEYSQHQQK LVCSAYDFYP KKIRVTWLKD GKNITSGVTS TDELPNGHWL YQIHSYLEFT PKPGEKIACM VDHASLKEPK LYDLEPEPDS GKHKMVVGSA GLLLGLLFSV MGFIFFKKKS IAERVRVPTS ELNALFGIF // ID A0A096MY15_PAPAN Unreviewed; 242 AA. AC A0A096MY15; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 20-JUN-2018, entry version 23. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain-like precursor {ECO:0000313|Ensembl:ENSPANP00000004808}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000004808, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000004808} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSPANT00000009332; ENSPANP00000004808; ENSPANG00000023362. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G0K7A; -. DR Proteomes; UP000028761; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 242 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014175743. FT TRANSMEM 211 230 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 242 AA; 27555 MW; D5DB9DF6BDC5E435 CRC64; MMVLPVSGAP QTVTLTPLLM VLLTSVVQGM ATPENYVYQR RFECYAFNGT QRLLDRFIYN QEEYVRFDSD LGEFRAVTEL GPPDAEYWNR QDTLEQEQAE VDRVCRHNYE LDEAVTLKRR VQPRVNVSPS KKGPLQHHNL LVCHVTDFYP GSIQVRWFLN GQEETDGVVS TNLIRNGDWT FQILVMLEMT PQQGDVYTCQ VEHPSLDSPT LTGAGGFVLG LIICGVGIFM HRRSKKVQRG SV // ID A0A096NHD1_PAPAN Unreviewed; 224 AA. AC A0A096NHD1; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 20-JUN-2018, entry version 27. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain precursor {ECO:0000313|Ensembl:ENSPANP00000012379}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSPANP00000012379}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000012379, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000012379, ECO:0000313|Proteomes:UP000028761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., RA Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., RA Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B., RA Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B., RA Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C., RA Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D., RA Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F., RA Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G., RA Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J., RA Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J., RA Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K., RA Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L., RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L., RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M., RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N., RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O., RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., RA Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., RA Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S., RA Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T., RA Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U., RA Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W., RA Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W., RA Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N., RA Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.; RT "Whole Genome Assembly of Papio anubis."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPANP00000012379} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AHZZ02024459; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPANT00000000041; ENSPANP00000012379; ENSPANG00000009109. DR GeneTree; ENSGT00900000140849; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000028761; Chromosome 4. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014178618. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 224 AA; 26028 MW; E02CF58A9785873C CRC64; MPRKKALRIP GGLCGTTVTL MLAMLSPPVA GGRDSPEDFV YQFKGMCYFT NGTERVRLVT RYVYNREEYA RFDSDVWEYR AVTPLGRSSA EYWNSQKDVL ERTRAELDTV CKHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQRPITVEW RLPH // ID A0A096NHD5_PAPAN Unreviewed; 273 AA. AC A0A096NHD5; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 28-MAR-2018, entry version 25. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSPANP00000012383}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSPANP00000012383}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000012383, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000012383, ECO:0000313|Proteomes:UP000028761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., RA Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., RA Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B., RA Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B., RA Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C., RA Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D., RA Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F., RA Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G., RA Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J., RA Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J., RA Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K., RA Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L., RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L., RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M., RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N., RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O., RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., RA Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., RA Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S., RA Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T., RA Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U., RA Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W., RA Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W., RA Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N., RA Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.; RT "Whole Genome Assembly of Papio anubis."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPANP00000012383} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AHZZ02024476; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPANT00000006475; ENSPANP00000012383; ENSPANG00000016388. DR GeneTree; ENSGT00900000140849; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000028761; Chromosome 4. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 273 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014132805. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 273 AA; 30781 MW; 4DB9ABA161961359 CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSREA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTALLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERAGVMS TGLIGNGDWT FQTVVMLEMT PELGDVYTCL VHHSSLLSPV SVEWRVQSEY SWRKMLSGIA AFLLGLIFLL VGIVIQLRAQ KGYVRTQMSG DEVSRAVLLP QPC // ID A0A096NHE5_PAPAN Unreviewed; 263 AA. AC A0A096NHE5; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 28-MAR-2018, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPANP00000012393}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000012393, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000012393, ECO:0000313|Proteomes:UP000028761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., RA Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., RA Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B., RA Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B., RA Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C., RA Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D., RA Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F., RA Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G., RA Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J., RA Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J., RA Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K., RA Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L., RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L., RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M., RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N., RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O., RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., RA Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., RA Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S., RA Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T., RA Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U., RA Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W., RA Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W., RA Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N., RA Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.; RT "Whole Genome Assembly of Papio anubis."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPANP00000012393} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AHZZ02024485; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003897473.1; XM_003897424.3. DR Ensembl; ENSPANT00000015972; ENSPANP00000012393; ENSPANG00000019593. DR GeneID; 101016766; -. DR GeneTree; ENSGT00900000140849; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR Proteomes; UP000028761; Chromosome 4. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001922822. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 29004 MW; B43333403D86184F CRC64; MIIFLPLLLG LSLGCTRAGG FVAHVESTCL LDDDGTAKDF TYCISFNKDL LTCWDPEENK MVPCEFGVLN PVANGISHYL NQQDTLMQRL RNGLQNCTTH TQPFWGSLTH RTRPPSVQVA QTTPFNTREP VMLACYVWGF YPADVTITWM KNGNLVIPHS SGQKTAQPNG DWTYQTVSYL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGLISW RRAGSSSYTP LPGSNYPEGR HIS // ID A0A096NHF3_PAPAN Unreviewed; 258 AA. AC A0A096NHF3; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 20-JUN-2018, entry version 23. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSPANP00000012401}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSPANP00000012401}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000012401, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000012401, ECO:0000313|Proteomes:UP000028761} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., RA Aqrawi P.A., Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., RA Bandaranaike D.B., Battles P.B., Bell A.B., Beltran B.B., RA Berhane-Mersha D.B., Bess C.B., Bickham C.B., Bolden T.B., RA Carter K.C., Chau D.C., Chavez A.C., Clerc-Blankenburg K.C., RA Coyle M.C., Dao M.D., Davila M.L.D., Davy-Carroll L.D., Denson S.D., RA Dinh H.D., Fernandez S.F., Fernando P.F., Forbes L.F., Francis C.F., RA Francisco L.F., Fu Q.F., Garcia-Iii R.G., Garrett T.G., Gross S.G., RA Gubbala S.G., Hirani K.H., Hogues M.H., Hollins B.H., Jackson L.J., RA Javaid M.J., Jhangiani S.J., Johnson A.J., Johnson B.J., Jones J.J., RA Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K., Kovar C.K., RA Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L., RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L., RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M., RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N., RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O., RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., RA Perez Y.P., Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., RA Rouhana J.R., Ruiz M.R., Ruiz S.-J.R., Saada N.S., Santibanez J.S., RA Scheel M.S., Schneider B.S., Simmons D.S., Sisson I.S., Tang L.-Y.T., RA Thornton R.T., Tisius J.T., Toledanes G.T., Trejos Z.T., Usmani K.U., RA Varghese R.V., Vattathil S.V., Vee V.V., Walker D.W., RA Weissenberger G.W., White C.W., Williams A.W., Woodworth J.W., RA Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N., Nazareth L.N., RA Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.; RT "Whole Genome Assembly of Papio anubis."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPANP00000012401} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AHZZ02024502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AHZZ02024503; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AHZZ02024504; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPANT00000028720; ENSPANP00000012401; ENSPANG00000005764. DR GeneTree; ENSGT00900000140849; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G0W5S; -. DR Proteomes; UP000028761; Chromosome 4. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014154969. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29369 MW; 012E895D94225061 CRC64; MMVLQVSAAP RTVGLMALLM VLLTSVVQGR ATPENYLFQG RQECYAFNGT QRYLERYIYN REEHVRFDSD VGEFRAVTEL GRPDAEYWNS QKDKLEEMRA VVDTMCRYNY ELDEAVTLQR RVQPRVNIAP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHPSLDSP VTVEWKAQSD SARSKMLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSV // ID A0A096NSL4_PAPAN Unreviewed; 289 AA. AC A0A096NSL4; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 20-JUN-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPANP00000016035}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000016035, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000016035} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSPANT00000014467; ENSPANP00000016035; ENSPANG00000018690. DR GeneTree; ENSGT00900000140849; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000028761; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 257 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 135 223 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 289 AA; 32708 MW; 40AC13610EC013AA CRC64; DPSSVLFSSM VCLKLPGGSC MAALTVTLMV LSSPLALAGD TRPRFLEQRK AECHFFNGME RVRFVDRYIH NQEELVRFDS DVGEYRAVSE LGRPEAESWN SQKDLLEQRR AEVDTYCRHN YGGVESFTVQ RRVHPKVTVY PEKTQPLQHH NLLVCSVSGF YPGSIEVRWF RNGQEEKAGV VSTGLIQNGD WTFQTLVMLE TVPRSGEVYT CQVEHSSVTS PLTVEWRARS ESAQSKMLSG VGGFVLGLLF LGARLFIYFR NQEGEEHSGI QPTGNTFSFS FRNRFAFLE // ID A0A096NVH2_PAPAN Unreviewed; 255 AA. AC A0A096NVH2; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 20-JUN-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPANP00000017047}; OS Papio anubis (Olive baboon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Papio. OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000017047, ECO:0000313|Proteomes:UP000028761}; RN [1] {ECO:0000313|Ensembl:ENSPANP00000017047} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSPANT00000016856; ENSPANP00000017047; ENSPANG00000018690. DR GeneTree; ENSGT00900000140849; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000028761; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000028761}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000028761}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 203 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 255 AA; 29358 MW; 21BC0F1C8F8FC1BD CRC64; FSCLSFPSTR FLEQRKAECH FFNGMERVRF VDRYIHNQEE LVRFDSDVGE YRAVSELGRP EAESWNSQKD LLEQRRAEVD TYCRHNYGGV ESFTVQRRVH PKVTVYPEKT QPLQHHNLLV CSVSGFYPGS IEVRWFRNGQ EEKAGVVSTG LIQNGDWTFQ TLVMLETVPR SGEVYTCQVE HSSVTSPLTV EWRARSESAQ SKMLSGVGGF VLGLLFLGAR LFIYFRNQEG EEHSGIQPTG NTFSFSFRNR FAFLE // ID A0A099Z8H6_TINGU Unreviewed; 112 AA. AC A0A099Z8H6; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 05-OCT-2016, entry version 10. DE SubName: Full=H-2 class II histocompatibility antigen, A-Q beta chain {ECO:0000313|EMBL:KGL77090.1}; DE Flags: Fragment; GN ORFNames=N309_10601 {ECO:0000313|EMBL:KGL77090.1}; OS Tinamus guttatus (White-throated tinamou). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus. OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL77090.1, ECO:0000313|Proteomes:UP000053641}; RN [1] {ECO:0000313|EMBL:KGL77090.1, ECO:0000313|Proteomes:UP000053641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL77090.1}; RA Zhang G., Li C.; RT "Genome evolution of avian class."; RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KL889703; KGL77090.1; -; Genomic_DNA. DR Proteomes; UP000053641; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053641}; KW Reference proteome {ECO:0000313|Proteomes:UP000053641}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 112 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5001965960. FT DOMAIN 29 103 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KGL77090.1}. FT NON_TER 112 112 {ECO:0000313|EMBL:KGL77090.1}. SQ SEQUENCE 112 AA; 12685 MW; 9E61BFC36906A9AA CRC64; AVLGVLVVLG AIGSHGEETT GYFLEMGKGD CQYLNGTQRV RYLKWYIHNR QPWLHFDSDL GHYVADSPLG EPDARYFNSQ PDIMERERAE VDTVCRHNYG VATPSVVERK GE // ID A0A0D5XQ77_HUMAN Unreviewed; 269 AA. AC A0A0D5XQ77; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 18-JUL-2018, entry version 26. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000382025}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AKA20568.1}; GN Name=HLA-DQB1 {ECO:0000313|EMBL:AKA20568.1, GN ECO:0000313|Ensembl:ENSP00000382025}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AKA20568.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000382025, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|EMBL:AKA20568.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25630340; DOI=10.1111/tan.12503; RA Cervera I., Herraz M.A., Vidart J., Ortega S., Martinez-Laso J.; RT "Identification of the novel HLA-DQB1*03:03:02:04 allele in a Spanish RT individual."; RL Tissue Antigens 85:215-216(2015). RN [4] {ECO:0000313|Ensembl:ENSP00000382025} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KM519596; AKA20568.1; -; Genomic_DNA. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR PRIDE; A0A0D5XQ77; -. DR Ensembl; ENST00000399074; ENSP00000382025; ENSG00000233209. DR HGNC; HGNC:4944; HLA-DQB1. DR OrthoDB; EOG091G0SXL; -. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0D5XQ77, KW ECO:0000213|PeptideAtlas:A0A0D5XQ77}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014510352. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 233 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 269 AA; 30616 MW; 4906C4303390500A CRC64; MSWKKALRIP GGLRVATVTL MLAMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVT RYIYNREEYA RFDSDVGVYR AVTPLGPPDA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQNPIIVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IHHRSQKGPQ GPPPAGLLH // ID A0A0D9RAJ6_CHLSB Unreviewed; 266 AA. AC A0A0D9RAJ6; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 20-JUN-2018, entry version 21. DE SubName: Full=Major histocompatibility complex, class II, DR beta 1 {ECO:0000313|Ensembl:ENSCSAP00000005635}; GN Name=HLA-DRB1 {ECO:0000313|Ensembl:ENSCSAP00000005635}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005635, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005635, ECO:0000313|Proteomes:UP000029965} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005635} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC241606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC241608; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCSAT00000007457; ENSCSAP00000005635; ENSCSAG00000009383. DR GeneTree; ENSGT00900000140849; -. DR OMA; GQVDNYC; -. DR Proteomes; UP000029965; Chromosome 17. DR ExpressionAtlas; A0A0D9RAJ6; baseline. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002506; P:polysaccharide assembly with MHC class II protein complex; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002344724. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29995 MW; 9709FBA62A4CE03F CRC64; MVCLKLPGGS CMAALTMTLM VLSSPLALAG DTRSRFLEQV KSECHFFNGT ERVRFLDRYF YNQEEYVRFD SDVGEFRAVS ELGRHSAEYW NSRKDLLEDE RASVDNYCRY NYGVVESFTV QRRVQPKVTV YPAKTQPLQH HTLLVCSVNG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGLLS // ID A0A0D9RAL0_CHLSB Unreviewed; 248 AA. AC A0A0D9RAL0; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 28-MAR-2018, entry version 18. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSCSAP00000005649}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSCSAP00000005649}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005649, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005649, ECO:0000313|Proteomes:UP000029965} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005649} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC241599; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSCSAT00000007472; ENSCSAP00000005649; ENSCSAG00000009402. DR GeneTree; ENSGT00900000140849; -. DR OMA; WNNRPDI; -. DR Proteomes; UP000029965; Chromosome 17. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 203 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 191 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 248 AA; 28165 MW; DF931E64A66BA568 CRC64; MTQGIDSPED FVIQAKADCY FTNGTEKVQF VVRFIFNLEE YVRFDSDVGM FVALTKLGQP DAEQWNSRLD LLERSREAVD GVCRHNYRLS APFTVGRKVQ PEVTVYPERT ALLHQHNLLH CSVTGFYPGD IKIRWFLNGQ EERAGVMSTG LIGNGDWTFQ TVVILEMTPE LGDVYTCLVH HSSLLSPVSV EWRVQSEYSW RKILSGIAAF LLGLIFLLVG IVIQFRAQKG YVRTQMSGDE VMSLFPCL // ID A0A0D9RAN9_CHLSB Unreviewed; 263 AA. AC A0A0D9RAN9; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 28-MAR-2018, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAP00000005678}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005678, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005678, ECO:0000313|Proteomes:UP000029965} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005678} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC241457; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_007971177.1; XM_007972986.1. DR Ensembl; ENSCSAT00000007503; ENSCSAP00000005678; ENSCSAG00000009430. DR GeneID; 103221689; -. DR KEGG; csab:103221689; -. DR CTD; 101140024; -. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR Proteomes; UP000029965; Chromosome 17. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002344865. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28988 MW; 08F6DF6CE6C57BEB CRC64; MIIFLPLLLG LSLGCTRAGG FVAHVESTCL LDDDGTAKDF TYCISFNKDL LTCWDPEENK MVPCEFGVLN PVANGLSHYL NQQDTLMQRL RNGLQNCTTH TQPFWGSLTH RTRPPSVQVA QTTPFNTREP VMLACYVWGF YPADVTITWM KNGNLVIPHG SGQKTAQPNG DWTYQTLSYL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGLISW RRAGSSSYTP LPGSNYPEGR HIS // ID A0A0D9RAS6_CHLSB Unreviewed; 256 AA. AC A0A0D9RAS6; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 28-MAR-2018, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAP00000005715}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000005715, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000005715, ECO:0000313|Proteomes:UP000029965} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005715} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC242496; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_007971167.1; XM_007972976.1. DR Ensembl; ENSCSAT00000007539; ENSCSAP00000005715; ENSCSAG00000009461. DR GeneID; 103221682; -. DR KEGG; csab:103221682; -. DR CTD; 103221682; -. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; ICQVEHT; -. DR Proteomes; UP000029965; Chromosome 17. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 256 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002345232. FT TRANSMEM 225 244 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 122 226 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 256 AA; 29232 MW; 0F4B3312DA65983D CRC64; MMVLPVSGAP QTVTLMALLM VLLTSVVQGR ATPENYVYQR RYECYAFNGT QRLLDRFIYN QEEYVRFDSD LGEFRAVTEL GRPTAEYWNR DFLEQARAEV DRVCRHNYEL EEPLIRKRRV QPRVNVSPSK KGPLQHHNLL VCHVTDFYPG SIQVRWFLNG QEETAGVVST NLIRNGDWTF QILVMLEMTP QQGDVYTCQV EHPSLDSPVT VEWKAQSDSA RSKTLTGAGG FVLGLITCGV GIFMHRRSKK VQRGSA // ID A0A0D9S0C2_CHLSB Unreviewed; 252 AA. AC A0A0D9S0C2; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAP00000014311}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014311, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014311} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAT00000016396; ENSCSAP00000014311; ENSCSAG00000018300. DR GeneTree; ENSGT00900000140849; -. DR OMA; RWFRNSQ; -. DR Proteomes; UP000029965; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 214 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 252 AA; 28603 MW; 82399BC375A81128 CRC64; TVSVFSGGRP CDRILRVPTA RFLWQAKAKC HFFNGTERVR YLERHFYNQE ELVRFDSDVG EYRAVSELGR PDAEYWNSLK DYLEQARAAV DNYCRHNYGV VESFTVQRRV QPKVTVYPAK TQPLQHHNLL VCSVNGFYPG SIEVRWFRNS QEEKAGVVST GLIQNGDWTF QTLVMLETVP RSGEVYTCQV EHPSVTSPLT VEWRARSESA QSKMLSGVGG FVLGLLFLGA GLFIYFRNQK GHAGLQPTGL LS // ID A0A0D9S0C6_CHLSB Unreviewed; 236 AA. AC A0A0D9S0C6; DT 27-MAY-2015, integrated into UniProtKB/TrEMBL. DT 27-MAY-2015, sequence version 1. DT 23-MAY-2018, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCSAP00000014315}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014315, ECO:0000313|Proteomes:UP000029965}; RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014315} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCSAT00000016401; ENSCSAP00000014315; ENSCSAG00000018303. DR GeneTree; ENSGT00900000140849; -. DR OMA; RIPEAHC; -. DR Proteomes; UP000029965; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 205 224 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 102 206 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 236 AA; 27140 MW; 60A22A4510A5154E CRC64; TSPLHGLLLP AENYVYQRRY ECYAFNGTQR LLDRFIYNQE EYVRFDSDLG EFRAVTELGR PTAEYWNRDF LEQARAEVDR VCRHNYELEE PLIRKRRALV QPRVNVSPSK KGPLQHHNLL VCHVTDFYPG SIQVRWFLNG QEETAGVVST SLIRNGDWTF QILVMLEMTP QQGDVYTCQV EHPSLDSPVT VEWKTQSDST QSKTLTGAVG FVLGLIICGV GIFMHRRSKK VQQGSA // ID A0A0F8CAS2_LARCR Unreviewed; 249 AA. AC A0A0F8CAS2; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 25-OCT-2017, entry version 10. DE SubName: Full=Rano class II histocompatibility antigen, A beta chain {ECO:0000313|EMBL:KKF15359.1}; GN ORFNames=EH28_11068 {ECO:0000313|EMBL:KKF15359.1}; OS Larimichthys crocea (Large yellow croaker) (Pseudosciaena crocea). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Sciaenidae; Larimichthys. OX NCBI_TaxID=215358 {ECO:0000313|EMBL:KKF15359.1, ECO:0000313|Proteomes:UP000054355}; RN [1] {ECO:0000313|EMBL:KKF15359.1, ECO:0000313|Proteomes:UP000054355} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SSNF {ECO:0000313|EMBL:KKF15359.1}; RC TISSUE=Blood {ECO:0000313|EMBL:KKF15359.1}; RX PubMed=25835551; RA Ao J., Mu Y., Xiang L.X., Fan D., Feng M., Zhang S., Shi Q., Zhu L.Y., RA Li T., Ding Y., Nie L., Li Q., Dong W.R., Jiang L., Sun B., Zhang X., RA Li M., Zhang H.Q., Xie S., Zhu Y., Jiang X., Wang X., Mu P., Chen W., RA Yue Z., Wang Z., Wang J., Shao J.Z., Chen X.; RT "Genome Sequencing of the Perciform Fish Larimichthys crocea Provides RT Insights into Molecular and Genetic Mechanisms of Stress Adaptation."; RL PLoS Genet. 11:E1005118-E1005118(2015). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KQ042379; KKF15359.1; -; Genomic_DNA. DR Proteomes; UP000054355; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000054355}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000054355}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 214 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 115 203 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28570 MW; 4D479A922916DFA2 CRC64; MKDMDVEMRE SLTVSDCATN GSGYFMTADF RCAMYSRERT HVEYLVDWHF NEEFVMQYNS TVGKWTGFTP GGMITASLFN GDFYDVQQRK VEKQLICVDH VDMIFNVTEE SIAEPSVTLV ESTSSSKNAM LVCSAYDFYP RNIKLTWLMN GQEVTSGVTF SDVLTNGDWT YQVHSYLEYT PSIRQDRVSC MVEHASLREP KIYHRDLNQS DRRLLIGGVC FLVLGAVFLS LGLMQYRRKR GDSRFSTAL // ID A0A0G2JH31_HUMAN Unreviewed; 279 AA. AC A0A0G2JH31; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000322293}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000322293}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000322293, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000322293, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000322293} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSP00000391938} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL773543; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759848; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR788227; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000323109; ENSP00000322293; ENSG00000196610. DR Ensembl; ENST00000419519; ENSP00000406872; ENSG00000229493. DR Ensembl; ENST00000433801; ENSP00000391938; ENSG00000228813. DR Ensembl; ENST00000442043; ENSP00000394272; ENSG00000228254. DR HGNC; HGNC:4945; HLA-DQB2. DR OrthoDB; EOG091G0SXL; -. DR ChiTaRS; HLA-DQB2; human. DR GenomeRNAi; 3120; -. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A0G2JH31}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 279 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014514141. FT TRANSMEM 230 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 279 AA; 31409 MW; E562ED94C27A67AE CRC64; MSWKMALQIP GGFWAAAVTV MLVMLSTPVA EARDFPKDFL VQFKGMCYFT NGTERVRGVA RYIYNREEYG RFDSDVGEFQ AVTELGRSIE DWNNYKDFLE QERAAVDKVC RHNYEAELRT TLQRQVEPTV TISPSRTEAL NHHNLLVCSV TDFYPAQIKV QWFRNDQEET AGVVSTSLIR NGDWTFQILV MLEITPQRGD IYTCQVEHPS LQSPITVEWR AQSESAQSKM LGGVGGFVLG LIFLGLGLII RHRGQKGPRG PPPAGNISAM IQSGERAQA // ID A0A0G2JI43_HUMAN Unreviewed; 257 AA. AC A0A0G2JI43; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 20-JUN-2018, entry version 26. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000394997}; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000394997}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000394997, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000394997, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000394997} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX088556; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A0G2JI43; -. DR Ensembl; ENST00000418759; ENSP00000394997; ENSG00000234154. DR Ensembl; ENST00000439344; ENSP00000413062; ENSG00000241296. DR Ensembl; ENST00000456428; ENSP00000416157; ENSG00000242386. DR HGNC; HGNC:4935; HLA-DMB. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0G2JI43, KW ECO:0000213|PeptideAtlas:A0A0G2JI43}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 257 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014514177. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 257 AA; 28283 MW; F4A38438F6F2013D CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN SLANVLSQHL NQKDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPAEVTITWR KNGKLVMPHS SAHKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHTGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGVISW RRAGHSSDLI ISLLFIL // ID A0A0G2JII1_HUMAN Unreviewed; 228 AA. AC A0A0G2JII1; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 20-JUN-2018, entry version 23. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000398783}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000398783}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000398783, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000398783, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000398783} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSP00000395651} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX120009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR762479; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A0G2JII1; -. DR Ensembl; ENST00000411424; ENSP00000398783; ENSG00000237710. DR Ensembl; ENST00000444931; ENSP00000395651; ENSG00000226826. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0G2JII1, KW ECO:0000213|PeptideAtlas:A0A0G2JII1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 228 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014514179. FT TRANSMEM 197 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 83 182 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 228 AA; 25766 MW; 3F89A1EFBFFF77CB CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYLFQG RQECYAFNGT QRFLERYIYN REEFARFDSD VGEFRAVTEL GRPAAEYWNS QKDILEEKRA VPDRMCRHNY ELGGPMTLQR RGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID A0A0G2JIJ2_HUMAN Unreviewed; 257 AA. AC A0A0G2JIJ2; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 20-JUN-2018, entry version 25. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000399130}; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000399130}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000399130, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000399130, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000399130} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSP00000394789} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL935042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX908719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927138; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR752645; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A0G2JIJ2; -. DR Ensembl; ENST00000413617; ENSP00000394789; ENSG00000242092. DR Ensembl; ENST00000428864; ENSP00000402800; ENSG00000241674. DR Ensembl; ENST00000447454; ENSP00000396075; ENSG00000226264. DR Ensembl; ENST00000452407; ENSP00000399130; ENSG00000239329. DR HGNC; HGNC:4935; HLA-DMB. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0G2JIJ2, KW ECO:0000213|PeptideAtlas:A0A0G2JIJ2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 257 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014514147. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 257 AA; 28295 MW; E5538438EBEF0120 CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN SLANVLSQHL NQKDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPAEVTITWR KNGKLVMPHS SAHKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGVISW RRAGHSSDLI ISLLFIL // ID A0A0G2JJQ8_HUMAN Unreviewed; 266 AA. AC A0A0G2JJQ8; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 23-MAY-2018, entry version 20. DE SubName: Full=HLA class II histocompatibility antigen, DR beta 4 chain {ECO:0000313|Ensembl:ENSP00000410046}; GN Name=HLA-DRB4 {ECO:0000313|Ensembl:ENSP00000410046}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000410046, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000410046, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000410046} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX927235; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR ProteinModelPortal; A0A0G2JJQ8; -. DR PeptideAtlas; A0A0G2JJQ8; -. DR Ensembl; ENST00000411959; ENSP00000410046; ENSG00000227826. DR HGNC; HGNC:4952; HLA-DRB4. DR PhylomeDB; A0A0G2JJQ8; -. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002546614. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29971 MW; 32AE1AF1334423AF CRC64; MVCLKLPGGS CMAALTVTLT VLSSPLALAG DTQPRFLEQA KCECHFLNGT ERVWNLIRYI YNQEEYARYN SDLGEYQAVT ELGRPDAEYW NSQKDLLERR RAEVDTYCRY NYGVVESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNSQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSMM SPLTVQWSAR SESAQSKMLS GVGGFVLGLL FLGTGLFIYF RNQKGHSGLQ PTGLLS // ID A0A0G2JJV3_HUMAN Unreviewed; 228 AA. AC A0A0G2JJV3; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 12-SEP-2018, entry version 25. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000411486}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000411486}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000411486, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000411486, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000411486} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSP00000400149} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR759795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759904; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A0G2JJV3; -. DR Ensembl; ENST00000411558; ENSP00000400149; ENSG00000230763. DR Ensembl; ENST00000441981; ENSP00000411486; ENSG00000236693. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0G2JJV3, KW ECO:0000213|PeptideAtlas:A0A0G2JJV3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 228 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014514113. FT TRANSMEM 197 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 83 182 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 228 AA; 25915 MW; 9FFF8D1FB059BB21 CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYLFQG RQECYAFNGT QRFLERYIYN REEFVRFDSD VGEFRAVTEL GRPDEEYWNS QKDILEEKRA VPDRMCRHNY ELGGPMTLQR RGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHTSMDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID A0A0G2JW17_RAT Unreviewed; 261 AA. AC A0A0G2JW17; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 12-SEP-2018, entry version 18. DE SubName: Full=Rano class II histocompatibility antigen, D-1 beta chain {ECO:0000313|Ensembl:ENSRNOP00000069704}; GN Name=RT1-Db1 {ECO:0000313|Ensembl:ENSRNOP00000069704, GN ECO:0000313|RGD:1593282}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000069704, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000069704, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069704, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000069704} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069704}; RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AABR07072809; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSRNOT00000080590; ENSRNOP00000069704; ENSRNOG00000033215. DR RGD; 1593282; RT1-Db1. DR GeneTree; ENSGT00900000140849; -. DR Reactome; R-RNO-202424; Downstream TCR signaling. DR Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-RNO-202433; Generation of second messenger molecules. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Reactome; R-RNO-389948; PD-1 signaling. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000033215; Expressed in 10 organ(s), highest expression level in spleen. DR ExpressionAtlas; A0A0G2JW17; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A0G2JW17}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002546931. FT TRANSMEM 224 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 121 225 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29849 MW; E5B3E8C7E53D32B3 CRC64; MVWLARDSCV AAVILLLTVL SPPVALVRDP TPRFLEQYKS ECYFYNGTQR VRLLVRYIYN REEYTRFDSD VGEFRAVTEL GRRDTEYYNK QKEYIERERA AVDTICRHNY EISDRFLTVE PKVTVYPSKT QPLKHHNLLV CSVSDFYPGS VEVRWFRNGE EEKDGLVSTG LIPNGDWTFQ LLVMLEMVPQ GGEVYTCQVE HPSLTSPVRV EWKAQSTSAQ NKKMSGVGGI VLGLLFLGAG LFVYFRNQKG QSGLQPTGLL N // ID A0A0G2JX83_RAT Unreviewed; 197 AA. AC A0A0G2JX83; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 4. DT 12-SEP-2018, entry version 21. DE SubName: Full=Rano class II histocompatibility antigen, B-1 beta chain {ECO:0000313|Ensembl:ENSRNOP00000070172}; DE Flags: Fragment; GN Name=RT1-Bb {ECO:0000313|Ensembl:ENSRNOP00000070172, GN ECO:0000313|RGD:3469}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000070172, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000070172, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070172, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000070172} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000070172}; RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC098547; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSRNOT00000082136; ENSRNOP00000070172; ENSRNOG00000032708. DR RGD; 3469; RT1-Bb. DR GeneTree; ENSGT00900000140849; -. DR Reactome; R-RNO-202424; Downstream TCR signaling. DR Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-RNO-202433; Generation of second messenger molecules. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Reactome; R-RNO-389948; PD-1 signaling. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000032708; Expressed in 9 organ(s), highest expression level in spleen. DR ExpressionAtlas; A0A0G2JX83; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 117 197 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 197 197 {ECO:0000313|Ensembl:ENSRNOP00000070172}. SQ SEQUENCE 197 AA; 22711 MW; EDCFEFB3B500D142 CRC64; MLPHTPSSLA GSETSICKAS LSSDVSSSAF VFKGLCYYTN GTQRIRLVIR YIYNREEYVR FDSDVGEFRA LTELGRPSAE YYNKQYLERT RAELDTVCRH NYEETEVPTS LRRLEQPNVA ISLSRTEALN HHNLLVCSVT DFYPAQIKVR WFRNGQEETA GVVSTQLIRN GDWTFQILVM LEMTPQRGEV YICHVDH // ID A0A0P7TU63_9TELE Unreviewed; 132 AA. AC A0A0P7TU63; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-APR-2017, entry version 7. DE SubName: Full=MHC class II antigen beta chain-like {ECO:0000313|EMBL:KPP57116.1}; DE Flags: Fragment; GN ORFNames=Z043_125192 {ECO:0000313|EMBL:KPP57116.1}; OS Scleropages formosus (Asian bonytongue). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala; OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages. OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP57116.1, ECO:0000313|Proteomes:UP000034805}; RN [1] {ECO:0000313|EMBL:KPP57116.1, ECO:0000313|Proteomes:UP000034805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP57116.1}; RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.; RT "The genome of the Asian arowana (Scleropages formosus)."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP57116.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JARO02017560; KPP57116.1; -; Genomic_DNA. DR Proteomes; UP000034805; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034805}; KW Reference proteome {ECO:0000313|Proteomes:UP000034805}. FT DOMAIN 9 42 MHC_II_beta. {ECO:0000259|Pfam:PF00969}. FT NON_TER 1 1 {ECO:0000313|EMBL:KPP57116.1}. FT NON_TER 132 132 {ECO:0000313|EMBL:KPP57116.1}. SQ SEQUENCE 132 AA; 15671 MW; 6789107BAF8172AB CRC64; GHFEYYLREC HYSSEELKDI EFIYRFIFNK LEYARYNSTL NNLSILDIRN MGCTMRRYGT KTEKRTNSIP THNAELYFRN ILSYTVEPSV RVYSEKSGSQ RHSTMLLTPK SGETIACKVE HSSFSEPKIF KW // ID A0A0P7UAC2_9TELE Unreviewed; 177 AA. AC A0A0P7UAC2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 28-FEB-2018, entry version 8. DE SubName: Full=MHC class II beta chain-like {ECO:0000313|EMBL:KPP56627.1}; DE Flags: Fragment; GN ORFNames=Z043_125742 {ECO:0000313|EMBL:KPP56627.1}; OS Scleropages formosus (Asian bonytongue). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala; OC Osteoglossomorpha; Osteoglossiformes; Osteoglossidae; Scleropages. OX NCBI_TaxID=113540 {ECO:0000313|EMBL:KPP56627.1, ECO:0000313|Proteomes:UP000034805}; RN [1] {ECO:0000313|EMBL:KPP56627.1, ECO:0000313|Proteomes:UP000034805} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Aro1 {ECO:0000313|EMBL:KPP56627.1}; RA Tan M.H., Gan H.M., Croft L.J., Austin C.M.; RT "The genome of the Asian arowana (Scleropages formosus)."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPP56627.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JARO02019831; KPP56627.1; -; Genomic_DNA. DR Proteomes; UP000034805; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000034805}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000034805}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 143 164 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 8 82 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:KPP56627.1}. SQ SEQUENCE 177 AA; 20482 MW; C99C73CECBF6D0D3 CRC64; GFSWHTQREC RYSSEDLKDI EFIHRYIYNK LEQVRYNSTL NKFIGYTELG VKHAEKWNQD GTADQTHTNV DGYCRPNAEL YFKNILWHTE LYDGDWYHQI HSYLELTPTS GETIACQVQH SSLPKPKIYN WDPSMSDGDR NKVIIGTSGL VLGLILSLAG VIYYKKKSTG RILVPTS // ID A0A0R4IR31_DANRE Unreviewed; 250 AA. AC A0A0R4IR31; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-SEP-2018, entry version 26. DE SubName: Full=Zgc:103700 {ECO:0000313|Ensembl:ENSDARP00000154033}; GN ORFNames=zgc:103700 {ECO:0000313|Ensembl:ENSDARP00000154033, GN ECO:0000313|ZFIN:ZDB-GENE-041010-13}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000154033, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000154033, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000154033, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000154033} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000154033}; RG Ensembl; RL Submitted (APR-2018) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABZ01014762; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_009302405.1; XM_009304130.1. DR UniGene; Dr.116203; -. DR Ensembl; ENSDART00000183333; ENSDARP00000154033; ENSDARG00000116524. DR GeneID; 103911540; -. DR KEGG; dre:103911540; -. DR ZFIN; ZDB-GENE-041010-13; zgc:103700. DR GeneTree; ENSGT00900000140849; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}. SQ SEQUENCE 250 AA; 28414 MW; 797947816A3F94D5 CRC64; MYLLKLFLAI LMLAAFTGTA YGYYDYTKFE CIYSTSDYSD MVYLVSLSFN KFVDIKCNST EVKCVGFTEQ GVKFADNFNK DKAFLQNLKA SVDTFCRHNA EIIDSAVRDK AVKPKVIMKS VKQAEGRHPA MLQCSAYEFY PKKIKMYWLR DSKVITSDVT STMEMANGNW YYQIHSHLEY TPKNGEKIQC VVEHASSTQP ITKEWNPHIS ESDRNKFAIG ASGLVLGIII AIAGLIYYKK KSTGRILVPN // ID A0A0R4IRA8_DANRE Unreviewed; 277 AA. AC A0A0R4IRA8; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 12-SEP-2018, entry version 20. DE SubName: Full=Major histocompatibility complex class II integral membrane beta chain gene {ECO:0000313|Ensembl:ENSDARP00000137499}; GN Name=si:dkey-33b17.3 {ECO:0000313|Ensembl:ENSDARP00000137499}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000137499, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000137499, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000137499, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000137499} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000137499}; RG Ensembl; RL Submitted (NOV-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CT583723; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001074102.2; NM_001080633.2. DR ProteinModelPortal; A0A0R4IRA8; -. DR STRING; 7955.ENSDARP00000072268; -. DR PaxDb; A0A0R4IRA8; -. DR Ensembl; ENSDART00000159361; ENSDARP00000137499; ENSDARG00000104730. DR GeneID; 563286; -. DR ZFIN; ZDB-GENE-030616-171; si:dkey-33b17.3. DR GeneTree; ENSGT00900000140849; -. DR OMA; ICQVEHT; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 232 253 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 277 AA; 31702 MW; DE7EF380E553695F CRC64; MFSSIHFVFS VAKMSQKKLY SSLILILALF FVGESANVYY MYRVSRCIFS SSNISAMVYF DRTYFNKNLF IQFNSNLGRF EGFNEYGLKL AEFWNNGTFV DQEKDVVEFF CKYNSQIYEN SILDKAVKPK VKLSSVTRAG GRQSTVLMCS AYDFYPPHIN VFWLRNGEVM TSEVTSTMEM ADGDWYYQIH SELEYSPKPG ERISCVIEHA SSNKPMIYDW DPSLPVFERN KISIGVSALV LGIITAAAGI IYYKKKTTGR TSVVPSRLIT LPLMFGR // ID A0A0R4ISW2_DANRE Unreviewed; 253 AA. AC A0A0R4ISW2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 28-MAR-2018, entry version 16. DE SubName: Full=Si:zfos-2070c2.3 {ECO:0000313|Ensembl:ENSDARP00000140023}; GN Name=si:zfos-2070c2.3 {ECO:0000313|Ensembl:ENSDARP00000140023, GN ECO:0000313|ZFIN:ZDB-GENE-091204-413}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000140023, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000140023, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000140023, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000140023} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000140023}; RG Ensembl; RL Submitted (NOV-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CU694361; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU694380; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_009302413.1; XM_009304138.2. DR PaxDb; A0A0R4ISW2; -. DR Ensembl; ENSDART00000159276; ENSDARP00000140023; ENSDARG00000076307. DR GeneID; 100332219; -. DR KEGG; dre:100332219; -. DR ZFIN; ZDB-GENE-091204-413; si:zfos-2070c2.3. DR GeneTree; ENSGT00900000140849; -. DR OMA; GQVDNYC; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 253 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5006451649. FT TRANSMEM 220 241 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 117 206 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 253 AA; 28413 MW; AC20FDEC532E76ED CRC64; MSLIKLSCCP PILALFVLIG AENANEYYAT ELSRCIYTSH DLSDMVFIDN YYFNKHLVTQ FNSTLGKFVG FTEYGIKNAE IWNNSSLLQK EISNVDSECR FYIKTRDKAV RDKAVKPTVV LSSVTQANGR HPAMLICSAY EFYPRHIKVS WLKGGKSVTS EVTSTMEMAD GDWYYQIHSE LEYTPGPGEK ISCLVEHASS SEPMIYDWDP SLPESERNKI AVGASGLVMG FIIAAVGILY YRKKSTGMIP IPH // ID A0A0R4IVW9_DANRE Unreviewed; 245 AA. AC A0A0R4IVW9; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 24. DE SubName: Full=Si:ch73-158p21.3 {ECO:0000313|Ensembl:ENSDARP00000138504}; GN Name=si:ch73-158p21.3 {ECO:0000313|Ensembl:ENSDARP00000138504, GN ECO:0000313|ZFIN:ZDB-GENE-030131-4747}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000138504, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000138504, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000138504, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000138504} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000138504}; RG Ensembl; RL Submitted (NOV-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; FP074874; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR UniGene; Dr.132659; -. DR UniGene; Dr.79881; -. DR STRING; 7955.ENSDARP00000071675; -. DR Ensembl; ENSDART00000168831; ENSDARP00000138504; ENSDARG00000101030. DR ZFIN; ZDB-GENE-030131-4747; si:ch73-158p21.3. DR GeneTree; ENSGT00900000140849; -. DR OMA; GETISCM; -. DR PhylomeDB; A0A0R4IVW9; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 4. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 245 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015341354. SQ SEQUENCE 245 AA; 27871 MW; 2D3D23F59CC32CCF CRC64; MSPANLLLML SVFTGAADGY YFSTWSQCIY SYPDLSDMVF ILSFNFNKWM FLQFNSTVGI FVGYTEQGVK FAENFNKNEA YLQQLRAEVD IFCRHNAEIY ESAVFDKAVM PKVNLSLVQK GDSRHPYLLR CSAYDFYPQQ IKMSWLRDGR VVSDVTSSEQ MPNGDWYYQS HSELVFSPKS GETISCMVEH SSLTGPVVID WKPPVHEFEW DFQLLSAAGD ASAVLGIIIA TAGYIYYKTK TGLEI // ID A0A0U5Q247_HUMAN Unreviewed; 261 AA. AC A0A0U5Q247; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 18-JUL-2018, entry version 27. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000388763}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:CUX91142.1}; GN Name=HLA-DQB1 {ECO:0000313|EMBL:CUX91142.1, GN ECO:0000313|Ensembl:ENSP00000388763}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:CUX91142.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000388763, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000213|PDB:5KS9, ECO:0000213|PDB:5KSA, ECO:0000213|PDB:5KSB} RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 33-224, AND DISULFIDE BONDS. RX PubMed=27568928; DOI=10.1016/j.str.2016.07.010; RA Petersen J., Kooy-Winkelaar Y., Loh K.L., Tran M., van Bergen J., RA Koning F., Rossjohn J., Reid H.H.; RT "Diverse T Cell Receptor Gene Usage in HLA-DQ8-Associated Celiac RT Disease Converges into a Consensus Binding Solution."; RL Structure 24:1643-1657(2016). RN [4] {ECO:0000313|Ensembl:ENSP00000388763} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. RN [5] {ECO:0000313|EMBL:CUX91142.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28547825; DOI=.1111/tan.13057; RA Albrecht V., Zweiniger C., Surendranath V., Lang K., Schofl G., RA Dahl A., Winkler S., Lange V., Bohme I., Schmidt A.H.; RT "Dual redundant sequencing strategy: Full-length gene characterisation RT of 1056 novel and confirmatory HLA alleles."; RL HLA. 90:79-87(2017). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX248406; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; LN999749; CUX91142.1; -; Genomic_DNA. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR PDB; 5KS9; X-ray; 2.55 A; B/D=33-224. DR PDB; 5KSA; X-ray; 2.00 A; B=12-12, B=33-224. DR PDB; 5KSB; X-ray; 2.90 A; B/D=12-12, B/D=33-224. DR PDBsum; 5KS9; -. DR PDBsum; 5KSA; -. DR PDBsum; 5KSB; -. DR EPD; A0A0U5Q247; -. DR Ensembl; ENST00000414518; ENSP00000388763; ENSG00000231939. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:5KS9, ECO:0000213|PDB:5KSA, KW ECO:0000213|PDB:5KSB}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A0U5Q247, KW ECO:0000213|PeptideAtlas:A0A0U5Q247}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015049031. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 233 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT CARBOHYD 51 51 N-linked (GlcNAc...) asparagine. FT {ECO:0000213|PDB:5KS9, FT ECO:0000213|PDB:5KSB}. FT DISULFID 47 111 {ECO:0000213|PDB:5KS9, FT ECO:0000213|PDB:5KSA, FT ECO:0000213|PDB:5KSB}. FT DISULFID 149 205 {ECO:0000213|PDB:5KS9, FT ECO:0000213|PDB:5KSA, FT ECO:0000213|PDB:5KSB}. SQ SEQUENCE 261 AA; 29814 MW; ED31E2DF40FF1752 CRC64; MSWKKALRIP GGLRVATVTL MLAMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRGVT RYIYNREEYA RFDSDVGVYR AVTPLGPPAA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQNPIIVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IHHRSQKGLL H // ID A0A140T8Z1_HUMAN Unreviewed; 224 AA. AC A0A140T8Z1; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000382578}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000382578}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000382578}; RN [1] {ECO:0000313|Ensembl:ENSP00000382578, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000382578} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL935026; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EPD; A0A140T8Z1; -. DR PeptideAtlas; A0A140T8Z1; -. DR Ensembl; ENST00000399670; ENSP00000382578; ENSG00000206302. DR HGNC; HGNC:4944; HLA-DQB1. DR PhylomeDB; A0A140T8Z1; -. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T8Z1, KW ECO:0000213|PeptideAtlas:A0A140T8Z1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305425. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 224 AA; 25900 MW; 81CF8F85F6572E29 CRC64; MSWKKALRIP GGLRAATVTL MLSMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVS RSIYNREEIV RFDSDVGEFR AVTLLGLPAA EYWNSQKDIL ERKRAAVDRV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RLLH // ID A0A140T8Z3_HUMAN Unreviewed; 228 AA. AC A0A140T8Z3; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000382414}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000382414}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000382414}; RN [1] {ECO:0000313|Ensembl:ENSP00000382414, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000382414} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL845446; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T8Z3; -. DR Ensembl; ENST00000399491; ENSP00000382414; ENSG00000215048. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T8Z3, KW ECO:0000213|PeptideAtlas:A0A140T8Z3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 228 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305492. FT TRANSMEM 197 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 83 182 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 228 AA; 25819 MW; 1C838DBBAA01F724 CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYLFQG RQECYAFNGT QRFLERYIYN REELVRFDSD VGEFRAVTEL GRPEAEYWNS QKDILEEERA VPDRMCRHNY ELGGPMTLQR RGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID A0A140T8Z5_HUMAN Unreviewed; 269 AA. AC A0A140T8Z5; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 18-JUL-2018, entry version 15. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000382018}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AUV47234.1}; GN Name=HLA-DQB1 {ECO:0000313|EMBL:AUV47234.1, GN ECO:0000313|Ensembl:ENSP00000382018}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000382018}; RN [1] {ECO:0000313|Ensembl:ENSP00000382018, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000382018} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. RN [4] {ECO:0000313|EMBL:AUV47234.1} RP NUCLEOTIDE SEQUENCE. RA Wu R., Li H., Peng D., Li R., Zhang Y., Hao B., Huang E., Zheng C., RA Sun H.; RT "Massively parallel sequencing-based high-resolution HLA typing in an RT extended Chinese family."; RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:AUV47234.1} RP NUCLEOTIDE SEQUENCE. RA Marsh S.G.E.; RT "Nomenclature for factors of the HLA system, update December 2017."; RL Int. J. Immunogenet. 0:0-0(2018). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR933859; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; MG571442; AUV47234.1; -; Genomic_DNA. DR EMBL; MG571443; AUV47235.1; -; Genomic_DNA. DR PeptideAtlas; A0A140T8Z5; -. DR PRIDE; A0A140T8Z5; -. DR Ensembl; ENST00000399065; ENSP00000382018; ENSG00000231286. DR HGNC; HGNC:4944; HLA-DQB1. DR PhylomeDB; A0A140T8Z5; -. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T8Z5, KW ECO:0000213|PeptideAtlas:A0A140T8Z5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014531360. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 269 AA; 30693 MW; CECA2074265C4A21 CRC64; MSWKKALRIP GGLRAATVTL MLAMLSTPVA EGRDSPEDFV YQFKAMCYFT NGTERVRYVT RYIYNREEYA RFDSDVEVYR AVTPLGPPDA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQHG DVYTCHVEHP SLQNPITVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IHHRSQKGPQ GPPPAGLLH // ID A0A140T8Z7_HUMAN Unreviewed; 229 AA. AC A0A140T8Z7; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000385037}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000385037}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000385037}; RN [1] {ECO:0000313|Ensembl:ENSP00000385037, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000385037} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL845446; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T8Z7; -. DR PRIDE; A0A140T8Z7; -. DR Ensembl; ENST00000402095; ENSP00000385037; ENSG00000215048. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T8Z7, KW ECO:0000213|PeptideAtlas:A0A140T8Z7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000385037}. FT NON_TER 229 229 {ECO:0000313|Ensembl:ENSP00000385037}. SQ SEQUENCE 229 AA; 26137 MW; 94CCACD3F766A6F2 CRC64; KQAWRGSATR LGPQNSGRQE CYAFNGTQRF LERYIYNREE LVRFDSDVGE FRAVTELGRP EAEYWNSQKD ILEEERAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKK // ID A0A140T915_HUMAN Unreviewed; 229 AA. AC A0A140T915; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000389193}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000389193}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000389193}; RN [1] {ECO:0000313|Ensembl:ENSP00000389193, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000389193} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T915; -. DR Ensembl; ENST00000450474; ENSP00000389193; ENSG00000230708. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T915, KW ECO:0000213|PeptideAtlas:A0A140T915}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000389193}. FT NON_TER 229 229 {ECO:0000313|Ensembl:ENSP00000389193}. SQ SEQUENCE 229 AA; 26280 MW; A6A412194C0B40E8 CRC64; KQAWRGSATR LGPQNSLRQE CYAFNGTQRF LERYIYNREE FVRFDSDVGE FRAVTELGRP DEDYWNSQKD LLEEKRAVPD RVCRHNYELD EAVTLQRRVQ PKVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYICQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKK // ID A0A140T926_HUMAN Unreviewed; 175 AA. AC A0A140T926; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000389736}; DE Flags: Fragment; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000389736}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000389736}; RN [1] {ECO:0000313|Ensembl:ENSP00000389736, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000389736} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR759798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T926; -. DR PeptideAtlas; A0A140T926; -. DR Ensembl; ENST00000448590; ENSP00000389736; ENSG00000242386. DR HGNC; HGNC:4935; HLA-DMB. DR OMA; NCASHTK; -. DR PhylomeDB; A0A140T926; -. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305433. FT DOMAIN 59 137 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 175 175 {ECO:0000313|Ensembl:ENSP00000389736}. SQ SEQUENCE 175 AA; 19438 MW; 7C8B3677DE7E6717 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEE QSMITFLPLL LGLSLGCTGA GGFVAHVEST CLLDDAGTPK DFTYCISFNK DLLTCWDPEE NKMAPCEFGV LNSLANVLSQ HLNQKDTLMQ RLRNGLQNCA THTQPFWGSL TNRTRPPSVQ VAKTTPFNTR EPVMLACYVW GFYPA // ID A0A140T928_HUMAN Unreviewed; 235 AA. AC A0A140T928; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000389923}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000389923}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000389923}; RN [1] {ECO:0000313|Ensembl:ENSP00000389923, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000389923} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR759904; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T928; -. DR Ensembl; ENST00000411722; ENSP00000389923; ENSG00000236693. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T928, KW ECO:0000213|PeptideAtlas:A0A140T928}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000389923}. SQ SEQUENCE 235 AA; 27071 MW; 7761FE92FFA3C0A8 CRC64; XNYLFQGRQE CYAFNGTQRF LERYIYNREE FVRFDSDVGE FRAVTELGRP DEEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSMDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKKG EKACRFNEDL HKQGS // ID A0A140T935_HUMAN Unreviewed; 181 AA. AC A0A140T935; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 2. DT 23-MAY-2018, entry version 14. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|Ensembl:ENSP00000390574}; DE Flags: Fragment; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSP00000390574}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000390574}; RN [1] {ECO:0000313|Ensembl:ENSP00000390574, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000390574} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR788227; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T935; -. DR PeptideAtlas; A0A140T935; -. DR Ensembl; ENST00000413252; ENSP00000390574; ENSG00000243496. DR HGNC; HGNC:4937; HLA-DOB. DR ChiTaRS; HLA-DOB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T935, KW ECO:0000213|PeptideAtlas:A0A140T935}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 101 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000390574}. FT NON_TER 181 181 {ECO:0000313|Ensembl:ENSP00000390574}. SQ SEQUENCE 181 AA; 20709 MW; BCE7230176DF4211 CRC64; XNLTRLDSSM TQGTDSPEDF VIQAKADCYF TNGTEKVQFV VRFIFNLEEY VRFDSDVGMF VALTKLGQPD AEQWNSRLDL LERSRQAVDG VCRHNYRLGA PFTVGRKEVT VYPERTPLLH QHNLLHCSVT GFYPGDIKIK WFLNGQEERA GVMSTGPIRN GDWTFQTVVM LEMTPELGHV Y // ID A0A140T945_HUMAN Unreviewed; 181 AA. AC A0A140T945; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 2. DT 23-MAY-2018, entry version 14. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|Ensembl:ENSP00000391708}; DE Flags: Fragment; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSP00000391708}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000391708}; RN [1] {ECO:0000313|Ensembl:ENSP00000391708, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000391708} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR762476; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T945; -. DR Ensembl; ENST00000453971; ENSP00000391708; ENSG00000243612. DR HGNC; HGNC:4937; HLA-DOB. DR ChiTaRS; HLA-DOB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T945, KW ECO:0000213|PeptideAtlas:A0A140T945}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 101 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000391708}. FT NON_TER 181 181 {ECO:0000313|Ensembl:ENSP00000391708}. SQ SEQUENCE 181 AA; 20709 MW; BCE7230176DF4211 CRC64; XNLTRLDSSM TQGTDSPEDF VIQAKADCYF TNGTEKVQFV VRFIFNLEEY VRFDSDVGMF VALTKLGQPD AEQWNSRLDL LERSRQAVDG VCRHNYRLGA PFTVGRKEVT VYPERTPLLH QHNLLHCSVT GFYPGDIKIK WFLNGQEERA GVMSTGPIRN GDWTFQTVVM LEMTPELGHV Y // ID A0A140T958_HUMAN Unreviewed; 250 AA. AC A0A140T958; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DRB1-16 beta chain {ECO:0000313|Ensembl:ENSP00000392880}; DE Flags: Fragment; GN Name=HLA-DRB1 {ECO:0000313|Ensembl:ENSP00000392880}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000392880}; RN [1] {ECO:0000313|Ensembl:ENSP00000392880, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000392880} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR753835; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T958; -. DR Ensembl; ENST00000433975; ENSP00000392880; ENSG00000229074. DR HGNC; HGNC:4948; HLA-DRB1. DR ChiTaRS; HLA-DRB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T958, KW ECO:0000213|PeptideAtlas:A0A140T958}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 160 250 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000392880}. FT NON_TER 250 250 {ECO:0000313|Ensembl:ENSP00000392880}. SQ SEQUENCE 250 AA; 29049 MW; A6809A1ED99A8108 CRC64; XLLKLTRDFP QRHEKYQSWA GTFHLCLKKN KYPDSRSTFI KHAGSYLKRG EFLSIHTAIT CFFLQISARF LWQGKYKCHF FNGTERVQFL ERLFYNQEEF VRFDSDVGEY RAVTELGRPV AESWNSQKDI LEDRRGQVDT VCRHNYGVGE SFTVQRRVHP EVTVYPAKTQ PLQHHNLLVC SVSGFYPGSI EVRWFRNGQE EKAGVVSTGL IQNGDWTFQT LVMLETVPRS GEVYTCQVEH PSVMSPLTVE // ID A0A140T966_HUMAN Unreviewed; 229 AA. AC A0A140T966; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000393651}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000393651}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000393651}; RN [1] {ECO:0000313|Ensembl:ENSP00000393651, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000393651} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR759795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000445702; ENSP00000393651; ENSG00000230763. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T966, KW ECO:0000213|PeptideAtlas:A0A140T966}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000393651}. FT NON_TER 229 229 {ECO:0000313|Ensembl:ENSP00000393651}. SQ SEQUENCE 229 AA; 26232 MW; 90158F43185D591F CRC64; KQAWRGSATR LGPQNSGRQE CYAFNGTQRF LERYIYNREE FVRFDSDVGE FRAVTELGRP DEEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSMDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKK // ID A0A140T976_HUMAN Unreviewed; 229 AA. AC A0A140T976; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000393789}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000393789}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000393789}; RN [1] {ECO:0000313|Ensembl:ENSP00000393789, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000393789} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR762479; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T976; -. DR SMR; A0A140T976; -. DR PeptideAtlas; A0A140T976; -. DR Ensembl; ENST00000456386; ENSP00000393789; ENSG00000237710. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T976, KW ECO:0000213|PeptideAtlas:A0A140T976}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000393789}. FT NON_TER 229 229 {ECO:0000313|Ensembl:ENSP00000393789}. SQ SEQUENCE 229 AA; 26084 MW; 03DD6307AA104641 CRC64; KQAWRGSATR LGPQNSGRQE CYAFNGTQRF LERYIYNREE FARFDSDVGE FRAVTELGRP AAEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKK // ID A0A140T981_HUMAN Unreviewed; 144 AA. AC A0A140T981; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000394159}; DE Flags: Fragment; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000394159}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000394159}; RN [1] {ECO:0000313|Ensembl:ENSP00000394159, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000394159} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T981; -. DR Ensembl; ENST00000432856; ENSP00000394159; ENSG00000233209. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T981, KW ECO:0000213|PeptideAtlas:A0A140T981}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 65 144 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 144 144 {ECO:0000313|Ensembl:ENSP00000394159}. SQ SEQUENCE 144 AA; 16665 MW; 291F0DE7FAC58E1B CRC64; MSWKKALRIP GGLRVATVTP LGPPDAEYWN SQKEVLERTR AELDTVCRHN YQLELRTTLQ RRVEPTVTIS PSRTEALNHH NLLVCSVTDF YPAQIKVRWF RNDQEETTGV VSTPLIRNGD WTFQILVMLE MTPQRGDVYT CHVE // ID A0A140T999_HUMAN Unreviewed; 218 AA. AC A0A140T999; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000396323}; DE Flags: Fragment; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000396323}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000396323}; RN [1] {ECO:0000313|Ensembl:ENSP00000396323, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000396323} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL773543; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T999; -. DR Ensembl; ENST00000416131; ENSP00000396323; ENSG00000196610. DR HGNC; HGNC:4945; HLA-DQB2. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A140T999}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305362. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000396323}. SQ SEQUENCE 218 AA; 25183 MW; 6CB783677127125F CRC64; XLQIPGGFWA AAVTVMLVML STPVAEARDF PKDFLVQFKG MCYFTNGTER VRGVARYIYN REEYGRFDSD VGEFQAVTEL GRSIEDWNNY KDFLEQERAA VDKVCRHNYE AELRTTLQRQ VEPTVTISPS RTEALNHHNL LVCSVTDFYP AQIKVQWFRN DQEETAGVVS TSLIRNGDWT FQILVMLEIT PQRGDIYTCQ VEHPSLQSPI TVEWRLLH // ID A0A140T9A5_HUMAN Unreviewed; 229 AA. AC A0A140T9A5; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000396595}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000396595}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000396595}; RN [1] {ECO:0000313|Ensembl:ENSP00000396595, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000396595} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR759904; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000441678; ENSP00000396595; ENSG00000236693. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9A5, KW ECO:0000213|PeptideAtlas:A0A140T9A5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000396595}. FT NON_TER 229 229 {ECO:0000313|Ensembl:ENSP00000396595}. SQ SEQUENCE 229 AA; 26232 MW; 90158F43185D591F CRC64; KQAWRGSATR LGPQNSGRQE CYAFNGTQRF LERYIYNREE FVRFDSDVGE FRAVTELGRP DEEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSMDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKK // ID A0A140T9B0_HUMAN Unreviewed; 218 AA. AC A0A140T9B0; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000397883}; DE Flags: Fragment; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000397883}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000397883}; RN [1] {ECO:0000313|Ensembl:ENSP00000397883, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000397883} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR759848; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000447979; ENSP00000397883; ENSG00000228254. DR HGNC; HGNC:4945; HLA-DQB2. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A140T9B0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305519. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000397883}. SQ SEQUENCE 218 AA; 25183 MW; 6CB783677127125F CRC64; XLQIPGGFWA AAVTVMLVML STPVAEARDF PKDFLVQFKG MCYFTNGTER VRGVARYIYN REEYGRFDSD VGEFQAVTEL GRSIEDWNNY KDFLEQERAA VDKVCRHNYE AELRTTLQRQ VEPTVTISPS RTEALNHHNL LVCSVTDFYP AQIKVQWFRN DQEETAGVVS TSLIRNGDWT FQILVMLEIT PQRGDIYTCQ VEHPSLQSPI TVEWRLLH // ID A0A140T9C9_HUMAN Unreviewed; 175 AA. AC A0A140T9C9; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000398843}; DE Flags: Fragment; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000398843}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000398843}; RN [1] {ECO:0000313|Ensembl:ENSP00000398843, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000398843} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL935042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9C9; -. DR Ensembl; ENST00000415090; ENSP00000398843; ENSG00000241674. DR HGNC; HGNC:4935; HLA-DMB. DR OMA; NCASHTK; -. DR PhylomeDB; A0A140T9C9; -. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305582. FT DOMAIN 59 137 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 175 175 {ECO:0000313|Ensembl:ENSP00000398843}. SQ SEQUENCE 175 AA; 19438 MW; 7C8B3677DE7E6717 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEE QSMITFLPLL LGLSLGCTGA GGFVAHVEST CLLDDAGTPK DFTYCISFNK DLLTCWDPEE NKMAPCEFGV LNSLANVLSQ HLNQKDTLMQ RLRNGLQNCA THTQPFWGSL TNRTRPPSVQ VAKTTPFNTR EPVMLACYVW GFYPA // ID A0A140T9F0_HUMAN Unreviewed; 218 AA. AC A0A140T9F0; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000401270}; DE Flags: Fragment; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000401270}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000401270}; RN [1] {ECO:0000313|Ensembl:ENSP00000401270, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000401270} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR788227; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000424579; ENSP00000401270; ENSG00000228813. DR HGNC; HGNC:4945; HLA-DQB2. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A140T9F0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305530. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000401270}. SQ SEQUENCE 218 AA; 25183 MW; 6CB783677127125F CRC64; XLQIPGGFWA AAVTVMLVML STPVAEARDF PKDFLVQFKG MCYFTNGTER VRGVARYIYN REEYGRFDSD VGEFQAVTEL GRSIEDWNNY KDFLEQERAA VDKVCRHNYE AELRTTLQRQ VEPTVTISPS RTEALNHHNL LVCSVTDFYP AQIKVQWFRN DQEETAGVVS TSLIRNGDWT FQILVMLEIT PQRGDIYTCQ VEHPSLQSPI TVEWRLLH // ID A0A140T9F2_HUMAN Unreviewed; 181 AA. AC A0A140T9F2; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 2. DT 23-MAY-2018, entry version 14. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|Ensembl:ENSP00000401290}; DE Flags: Fragment; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSP00000401290}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000401290}; RN [1] {ECO:0000313|Ensembl:ENSP00000401290, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000401290} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL671681; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9F2; -. DR Ensembl; ENST00000439310; ENSP00000401290; ENSG00000241386. DR HGNC; HGNC:4937; HLA-DOB. DR ChiTaRS; HLA-DOB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9F2, KW ECO:0000213|PeptideAtlas:A0A140T9F2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 101 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000401290}. FT NON_TER 181 181 {ECO:0000313|Ensembl:ENSP00000401290}. SQ SEQUENCE 181 AA; 20709 MW; BCE7230176DF4211 CRC64; XNLTRLDSSM TQGTDSPEDF VIQAKADCYF TNGTEKVQFV VRFIFNLEEY VRFDSDVGMF VALTKLGQPD AEQWNSRLDL LERSRQAVDG VCRHNYRLGA PFTVGRKEVT VYPERTPLLH QHNLLHCSVT GFYPGDIKIK WFLNGQEERA GVMSTGPIRN GDWTFQTVVM LEMTPELGHV Y // ID A0A140T9H0_HUMAN Unreviewed; 218 AA. AC A0A140T9H0; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000403201}; DE Flags: Fragment; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000403201}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000403201}; RN [1] {ECO:0000313|Ensembl:ENSP00000403201, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000403201} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL671681; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL713890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9H0; -. DR PeptideAtlas; A0A140T9H0; -. DR Ensembl; ENST00000421468; ENSP00000403201; ENSG00000224305. DR HGNC; HGNC:4945; HLA-DQB2. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A140T9H0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305586. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000403201}. SQ SEQUENCE 218 AA; 25211 MW; 6CB551B77127115C CRC64; XLQIPGGFWA AAVTVMLVML STPVAEARDF PKDFLVQFKG MCYFTNGTER VRGVARYIYN REEYGRFDSD VGEFQAVTEL GRSIEDWNNY KDFLEQERAA VDKVCRHNYE AELRTTLQRQ VEPTVTISPS RTEALNHHNL LVCSVTDFYP AQIKVRWFRN DQEETAGVVS TSLIRNGDWT FQILVMLEIT PQRGDIYTCQ VEHPSLQSPI TVEWRLLH // ID A0A140T9H9_HUMAN Unreviewed; 144 AA. AC A0A140T9H9; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000403786}; DE Flags: Fragment; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000403786}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000403786}; RN [1] {ECO:0000313|Ensembl:ENSP00000403786, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000403786} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX927168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T9H9; -. DR Ensembl; ENST00000456954; ENSP00000403786; ENSG00000225824. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9H9, KW ECO:0000213|PeptideAtlas:A0A140T9H9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 15 {ECO:0000256|SAM:SignalP}. FT CHAIN 16 144 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5011955327. FT DOMAIN 65 144 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 144 144 {ECO:0000313|Ensembl:ENSP00000403786}. SQ SEQUENCE 144 AA; 16547 MW; D15CCC3547A4D481 CRC64; MSWKKALRIP GGLRAATVTL LGLPAAEYWN SQKDILERKR AAVDRVCRHN YQLELRTTLQ RRVEPTVTIS PSRTEALNHH NLLVCSVTDF YPAQIKVRWF RNGQEETAGV VSTPLIRNGD WTFQILVMLE MTPQRGDVYT CHVE // ID A0A140T9I2_HUMAN Unreviewed; 175 AA. AC A0A140T9I2; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000404072}; DE Flags: Fragment; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000404072}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000404072}; RN [1] {ECO:0000313|Ensembl:ENSP00000404072, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000404072} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR752645; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9I2; -. DR Ensembl; ENST00000449679; ENSP00000404072; ENSG00000226264. DR HGNC; HGNC:4935; HLA-DMB. DR OMA; NCASHTK; -. DR PhylomeDB; A0A140T9I2; -. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305440. FT DOMAIN 59 137 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 175 175 {ECO:0000313|Ensembl:ENSP00000404072}. SQ SEQUENCE 175 AA; 19438 MW; 7C8B3677DE7E6717 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEE QSMITFLPLL LGLSLGCTGA GGFVAHVEST CLLDDAGTPK DFTYCISFNK DLLTCWDPEE NKMAPCEFGV LNSLANVLSQ HLNQKDTLMQ RLRNGLQNCA THTQPFWGSL TNRTRPPSVQ VAKTTPFNTR EPVMLACYVW GFYPA // ID A0A140T9I3_HUMAN Unreviewed; 235 AA. AC A0A140T9I3; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000404116}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000404116}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000404116}; RN [1] {ECO:0000313|Ensembl:ENSP00000404116, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000404116} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX120009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9I3; -. DR PeptideAtlas; A0A140T9I3; -. DR Ensembl; ENST00000447674; ENSP00000404116; ENSG00000226826. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9I3, KW ECO:0000213|PeptideAtlas:A0A140T9I3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000404116}. SQ SEQUENCE 235 AA; 26923 MW; 2927C29A3706E143 CRC64; XNYLFQGRQE CYAFNGTQRF LERYIYNREE FARFDSDVGE FRAVTELGRP AAEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKKG EKACRFNEDL HKQGS // ID A0A140T9J1_HUMAN Unreviewed; 218 AA. AC A0A140T9J1; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000403893}; DE Flags: Fragment; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000403893}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000403893}; RN [1] {ECO:0000313|Ensembl:ENSP00000403893, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000403893} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9J1; -. DR Ensembl; ENST00000435081; ENSP00000403893; ENSG00000226165. DR HGNC; HGNC:4945; HLA-DQB2. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A140T9J1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305442. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000403893}. SQ SEQUENCE 218 AA; 25211 MW; 6CB551B77127115C CRC64; XLQIPGGFWA AAVTVMLVML STPVAEARDF PKDFLVQFKG MCYFTNGTER VRGVARYIYN REEYGRFDSD VGEFQAVTEL GRSIEDWNNY KDFLEQERAA VDKVCRHNYE AELRTTLQRQ VEPTVTISPS RTEALNHHNL LVCSVTDFYP AQIKVRWFRN DQEETAGVVS TSLIRNGDWT FQILVMLEIT PQRGDIYTCQ VEHPSLQSPI TVEWRLLH // ID A0A140T9L2_HUMAN Unreviewed; 181 AA. AC A0A140T9L2; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 2. DT 23-MAY-2018, entry version 14. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|Ensembl:ENSP00000406128}; DE Flags: Fragment; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSP00000406128}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000406128}; RN [1] {ECO:0000313|Ensembl:ENSP00000406128, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000406128} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9L2; -. DR Ensembl; ENST00000455155; ENSP00000406128; ENSG00000239457. DR HGNC; HGNC:4937; HLA-DOB. DR ChiTaRS; HLA-DOB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9L2, KW ECO:0000213|PeptideAtlas:A0A140T9L2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 101 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000406128}. FT NON_TER 181 181 {ECO:0000313|Ensembl:ENSP00000406128}. SQ SEQUENCE 181 AA; 20709 MW; BCE7230176DF4211 CRC64; XNLTRLDSSM TQGTDSPEDF VIQAKADCYF TNGTEKVQFV VRFIFNLEEY VRFDSDVGMF VALTKLGQPD AEQWNSRLDL LERSRQAVDG VCRHNYRLGA PFTVGRKEVT VYPERTPLLH QHNLLHCSVT GFYPGDIKIK WFLNGQEERA GVMSTGPIRN GDWTFQTVVM LEMTPELGHV Y // ID A0A140T9P1_HUMAN Unreviewed; 229 AA. AC A0A140T9P1; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000408940}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000408940}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000408940}; RN [1] {ECO:0000313|Ensembl:ENSP00000408940, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000408940} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX120009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9P1; -. DR SMR; A0A140T9P1; -. DR Ensembl; ENST00000418444; ENSP00000408940; ENSG00000226826. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9P1, KW ECO:0000213|PeptideAtlas:A0A140T9P1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000408940}. FT NON_TER 229 229 {ECO:0000313|Ensembl:ENSP00000408940}. SQ SEQUENCE 229 AA; 26084 MW; 03DD6307AA104641 CRC64; KQAWRGSATR LGPQNSGRQE CYAFNGTQRF LERYIYNREE FARFDSDVGE FRAVTELGRP AAEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKK // ID A0A140T9P7_HUMAN Unreviewed; 235 AA. AC A0A140T9P7; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000408879}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000408879}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000408879}; RN [1] {ECO:0000313|Ensembl:ENSP00000408879, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000408879} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL845446; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000432661; ENSP00000408879; ENSG00000215048. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9P7, KW ECO:0000213|PeptideAtlas:A0A140T9P7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000408879}. SQ SEQUENCE 235 AA; 26976 MW; 65A9284BF80514BE CRC64; XNYLFQGRQE CYAFNGTQRF LERYIYNREE LVRFDSDVGE FRAVTELGRP EAEYWNSQKD ILEEERAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKKG EKACRFNEDL HKQGS // ID A0A140T9Q1_HUMAN Unreviewed; 235 AA. AC A0A140T9Q1; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000409943}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000409943}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000409943}; RN [1] {ECO:0000313|Ensembl:ENSP00000409943, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000409943} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR759795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000455122; ENSP00000409943; ENSG00000230763. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9Q1, KW ECO:0000213|PeptideAtlas:A0A140T9Q1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000409943}. SQ SEQUENCE 235 AA; 27071 MW; 7761FE92FFA3C0A8 CRC64; XNYLFQGRQE CYAFNGTQRF LERYIYNREE FVRFDSDVGE FRAVTELGRP DEEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSMDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKKG EKACRFNEDL HKQGS // ID A0A140T9R0_HUMAN Unreviewed; 175 AA. AC A0A140T9R0; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000410329}; DE Flags: Fragment; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000410329}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000410329}; RN [1] {ECO:0000313|Ensembl:ENSP00000410329, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000410329} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX088556; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9R0; -. DR Ensembl; ENST00000449417; ENSP00000410329; ENSG00000241296. DR HGNC; HGNC:4935; HLA-DMB. DR OMA; NCASHTK; -. DR PhylomeDB; A0A140T9R0; -. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305490. FT DOMAIN 59 137 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 175 175 {ECO:0000313|Ensembl:ENSP00000410329}. SQ SEQUENCE 175 AA; 19438 MW; 7C8B3677DE7E6717 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEE QSMITFLPLL LGLSLGCTGA GGFVAHVEST CLLDDAGTPK DFTYCISFNK DLLTCWDPEE NKMAPCEFGV LNSLANVLSQ HLNQKDTLMQ RLRNGLQNCA THTQPFWGSL TNRTRPPSVQ VAKTTPFNTR EPVMLACYVW GFYPA // ID A0A140T9R2_HUMAN Unreviewed; 175 AA. AC A0A140T9R2; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000410908}; DE Flags: Fragment; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000410908}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000410908}; RN [1] {ECO:0000313|Ensembl:ENSP00000410908, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000410908} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR936913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9R2; -. DR Ensembl; ENST00000435056; ENSP00000410908; ENSG00000242092. DR HGNC; HGNC:4935; HLA-DMB. DR OMA; NCASHTK; -. DR PhylomeDB; A0A140T9R2; -. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305559. FT DOMAIN 59 137 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 175 175 {ECO:0000313|Ensembl:ENSP00000410908}. SQ SEQUENCE 175 AA; 19438 MW; 7C8B3677DE7E6717 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEE QSMITFLPLL LGLSLGCTGA GGFVAHVEST CLLDDAGTPK DFTYCISFNK DLLTCWDPEE NKMAPCEFGV LNSLANVLSQ HLNQKDTLMQ RLRNGLQNCA THTQPFWGSL TNRTRPPSVQ VAKTTPFNTR EPVMLACYVW GFYPA // ID A0A140T9R6_HUMAN Unreviewed; 224 AA. AC A0A140T9R6; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000411566}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000411566}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000411566}; RN [1] {ECO:0000313|Ensembl:ENSP00000411566, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000411566} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR933859; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T9R6; -. DR Ensembl; ENST00000424530; ENSP00000411566; ENSG00000231286. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9R6, KW ECO:0000213|PeptideAtlas:A0A140T9R6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305407. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 224 AA; 26158 MW; 30FB71AA66A52471 CRC64; MSWKKALRIP GGLRAATVTL MLAMLSTPVA EGRDSPEDFV YQFKAMCYFT NGTERVRYVT RYIYNREEYA RFDSDVEVYR AVTPLGPPDA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQHG DVYTCHVEHP SLQNPITVEW RLLH // ID A0A140T9S2_HUMAN Unreviewed; 218 AA. AC A0A140T9S2; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000411739}; DE Flags: Fragment; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000411739}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000411739}; RN [1] {ECO:0000313|Ensembl:ENSP00000411739, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000411739} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR936921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9S2; -. DR Ensembl; ENST00000418419; ENSP00000411739; ENSG00000230675. DR HGNC; HGNC:4945; HLA-DQB2. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A140T9S2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305601. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000411739}. SQ SEQUENCE 218 AA; 25211 MW; 6CB551B77127115C CRC64; XLQIPGGFWA AAVTVMLVML STPVAEARDF PKDFLVQFKG MCYFTNGTER VRGVARYIYN REEYGRFDSD VGEFQAVTEL GRSIEDWNNY KDFLEQERAA VDKVCRHNYE AELRTTLQRQ VEPTVTISPS RTEALNHHNL LVCSVTDFYP AQIKVRWFRN DQEETAGVVS TSLIRNGDWT FQILVMLEIT PQRGDIYTCQ VEHPSLQSPI TVEWRLLH // ID A0A140T9S8_HUMAN Unreviewed; 269 AA. AC A0A140T9S8; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 15. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000411427}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AMR74086.1}; GN Name=HLA-DQB1 {ECO:0000313|EMBL:AMR74086.1, GN ECO:0000313|Ensembl:ENSP00000411427}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000411427}; RN [1] {ECO:0000313|Ensembl:ENSP00000411427, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|EMBL:AMR74086.1} RP NUCLEOTIDE SEQUENCE. RA Montero G., Cervera I., Martinez-Laso J.; RT "Description of the novel HLA-DQB1*02NEW allele generated by a cross- RT linking event between HLA-DQB1*02:01:01 allele and HLA-DQB1*02:02:01 RT allele."; RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSP00000411427} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX927168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KT387605; AMR74086.1; -; Genomic_DNA. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR Ensembl; ENST00000421888; ENSP00000411427; ENSG00000225824. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9S8, KW ECO:0000213|PeptideAtlas:A0A140T9S8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014531363. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 269 AA; 30377 MW; 54BE2F95D3EF2B3F CRC64; MSWKKALRIP GGLRAATVTL MLSMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVS RSIYNREEIV RFDSDVGEFR AVTLLGLPAA EYWNSQKDIL ERKRAAVDRV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNGQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IHHRSQKGPQ GPPPAGLLH // ID A0A140T9T0_HUMAN Unreviewed; 224 AA. AC A0A140T9T0; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000412380}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000412380}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000412380}; RN [1] {ECO:0000313|Ensembl:ENSP00000412380, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000412380} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX927168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T9T0; -. DR Ensembl; ENST00000415926; ENSP00000412380; ENSG00000225824. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9T0, KW ECO:0000213|PeptideAtlas:A0A140T9T0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305416. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 224 AA; 25842 MW; 81CC8C85F5542E29 CRC64; MSWKKALRIP GGLRAATVTL MLSMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVS RSIYNREEIV RFDSDVGEFR AVTLLGLPAA EYWNSQKDIL ERKRAAVDRV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNGQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RLLH // ID A0A140T9T6_HUMAN Unreviewed; 228 AA. AC A0A140T9T6; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000412855}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000412855}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000412855}; RN [1] {ECO:0000313|Ensembl:ENSP00000412855, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000412855} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T9T6; -. DR Ensembl; ENST00000441857; ENSP00000412855; ENSG00000230708. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9T6, KW ECO:0000213|PeptideAtlas:A0A140T9T6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 228 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305477. FT TRANSMEM 197 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 83 182 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 228 AA; 25993 MW; 3E14FD90549CFEBC CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYVYQL RQECYAFNGT QRFLERYIYN REEFVRFDSD VGEFRAVTEL GRPDEDYWNS QKDLLEEKRA VPDRVCRHNY ELDEAVTLQR RGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYIC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID A0A140T9T8_HUMAN Unreviewed; 175 AA. AC A0A140T9T8; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000412415}; DE Flags: Fragment; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000412415}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000412415}; RN [1] {ECO:0000313|Ensembl:ENSP00000412415, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000412415} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9T8; -. DR Ensembl; ENST00000430099; ENSP00000412415; ENSG00000234154. DR HGNC; HGNC:4935; HLA-DMB. DR OMA; NCASHTK; -. DR PhylomeDB; A0A140T9T8; -. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305504. FT DOMAIN 59 137 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 175 175 {ECO:0000313|Ensembl:ENSP00000412415}. SQ SEQUENCE 175 AA; 19438 MW; 7C8B3677DE7E6717 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEE QSMITFLPLL LGLSLGCTGA GGFVAHVEST CLLDDAGTPK DFTYCISFNK DLLTCWDPEE NKMAPCEFGV LNSLANVLSQ HLNQKDTLMQ RLRNGLQNCA THTQPFWGSL TNRTRPPSVQ VAKTTPFNTR EPVMLACYVW GFYPA // ID A0A140T9U5_HUMAN Unreviewed; 181 AA. AC A0A140T9U5; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 2. DT 23-MAY-2018, entry version 14. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|Ensembl:ENSP00000413915}; DE Flags: Fragment; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSP00000413915}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000413915}; RN [1] {ECO:0000313|Ensembl:ENSP00000413915, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000413915} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CT009502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9U5; -. DR Ensembl; ENST00000448690; ENSP00000413915; ENSG00000241910. DR HGNC; HGNC:4937; HLA-DOB. DR ChiTaRS; HLA-DOB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9U5, KW ECO:0000213|PeptideAtlas:A0A140T9U5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 101 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000413915}. FT NON_TER 181 181 {ECO:0000313|Ensembl:ENSP00000413915}. SQ SEQUENCE 181 AA; 20709 MW; BCE7230176DF4211 CRC64; XNLTRLDSSM TQGTDSPEDF VIQAKADCYF TNGTEKVQFV VRFIFNLEEY VRFDSDVGMF VALTKLGQPD AEQWNSRLDL LERSRQAVDG VCRHNYRLGA PFTVGRKEVT VYPERTPLLH QHNLLHCSVT GFYPGDIKIK WFLNGQEERA GVMSTGPIRN GDWTFQTVVM LEMTPELGHV Y // ID A0A140T9U6_HUMAN Unreviewed; 175 AA. AC A0A140T9U6; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|Ensembl:ENSP00000414153}; DE Flags: Fragment; GN Name=HLA-DMB {ECO:0000313|Ensembl:ENSP00000414153}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000414153}; RN [1] {ECO:0000313|Ensembl:ENSP00000414153, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000414153} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX908719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927138; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9U6; -. DR STRING; 9606.ENSP00000412457; -. DR PaxDb; A0A140T9U6; -. DR Ensembl; ENST00000415927; ENSP00000414153; ENSG00000239329. DR HGNC; HGNC:4935; HLA-DMB. DR OMA; NCASHTK; -. DR PhylomeDB; A0A140T9U6; -. DR ChiTaRS; HLA-DMB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305422. FT DOMAIN 59 137 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 175 175 {ECO:0000313|Ensembl:ENSP00000414153}. SQ SEQUENCE 175 AA; 19438 MW; 7C8B3677DE7E6717 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEE QSMITFLPLL LGLSLGCTGA GGFVAHVEST CLLDDAGTPK DFTYCISFNK DLLTCWDPEE NKMAPCEFGV LNSLANVLSQ HLNQKDTLMQ RLRNGLQNCA THTQPFWGSL TNRTRPPSVQ VAKTTPFNTR EPVMLACYVW GFYPA // ID A0A140T9U9_HUMAN Unreviewed; 218 AA. AC A0A140T9U9; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000414496}; DE Flags: Fragment; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000414496}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000414496}; RN [1] {ECO:0000313|Ensembl:ENSP00000414496, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000414496} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX927160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENST00000419109; ENSP00000414496; ENSG00000229493. DR HGNC; HGNC:4945; HLA-DQB2. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A0A140T9U9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305571. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000414496}. SQ SEQUENCE 218 AA; 25183 MW; 6CB783677127125F CRC64; XLQIPGGFWA AAVTVMLVML STPVAEARDF PKDFLVQFKG MCYFTNGTER VRGVARYIYN REEYGRFDSD VGEFQAVTEL GRSIEDWNNY KDFLEQERAA VDKVCRHNYE AELRTTLQRQ VEPTVTISPS RTEALNHHNL LVCSVTDFYP AQIKVQWFRN DQEETAGVVS TSLIRNGDWT FQILVMLEIT PQRGDIYTCQ VEHPSLQSPI TVEWRLLH // ID A0A140T9Y0_HUMAN Unreviewed; 235 AA. AC A0A140T9Y0; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000416774}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000416774}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000416774}; RN [1] {ECO:0000313|Ensembl:ENSP00000416774, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000416774} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR762479; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A0A140T9Y0; -. DR Ensembl; ENST00000458614; ENSP00000416774; ENSG00000237710. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9Y0, KW ECO:0000213|PeptideAtlas:A0A140T9Y0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000416774}. SQ SEQUENCE 235 AA; 26923 MW; 2927C29A3706E143 CRC64; XNYLFQGRQE CYAFNGTQRF LERYIYNREE FARFDSDVGE FRAVTELGRP AAEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKKG EKACRFNEDL HKQGS // ID A0A140T9Y2_HUMAN Unreviewed; 235 AA. AC A0A140T9Y2; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000416855}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000416855}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000416855}; RN [1] {ECO:0000313|Ensembl:ENSP00000416855, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000416855} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T9Y2; -. DR Ensembl; ENST00000434121; ENSP00000416855; ENSG00000230708. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9Y2, KW ECO:0000213|PeptideAtlas:A0A140T9Y2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000416855}. SQ SEQUENCE 235 AA; 27093 MW; 65D0236E19B410FA CRC64; XNYVYQLRQE CYAFNGTQRF LERYIYNREE FVRFDSDVGE FRAVTELGRP DEDYWNSQKD LLEEKRAVPD RVCRHNYELD EAVTLQRRVQ PKVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYICQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKKG EKACKFNEDL HKQGS // ID A0A140T9Y4_HUMAN Unreviewed; 144 AA. AC A0A140T9Y4; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000416744}; DE Flags: Fragment; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000416744}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000416744}; RN [1] {ECO:0000313|Ensembl:ENSP00000416744, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000416744} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR933859; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T9Y4; -. DR Ensembl; ENST00000457445; ENSP00000416744; ENSG00000231286. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9Y4, KW ECO:0000213|PeptideAtlas:A0A140T9Y4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 65 144 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 144 144 {ECO:0000313|Ensembl:ENSP00000416744}. SQ SEQUENCE 144 AA; 16618 MW; 320E64F8EAC58E04 CRC64; MSWKKALRIP GGLRAATVTP LGPPDAEYWN SQKEVLERTR AELDTVCRHN YQLELRTTLQ RRVEPTVTIS PSRTEALNHH NLLVCSVTDF YPAQIKVRWF RNDQEETTGV VSTPLIRNGD WTFQILVMLE MTPQHGDVYT CHVE // ID A0A140T9Z3_HUMAN Unreviewed; 244 AA. AC A0A140T9Z3; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 12. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|Ensembl:ENSP00000431178}; DE Flags: Fragment; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSP00000431178}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000431178}; RN [1] {ECO:0000313|Ensembl:ENSP00000431178, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000431178} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T9Z3; -. DR Ensembl; ENST00000472450; ENSP00000431178; ENSG00000239457. DR HGNC; HGNC:4937; HLA-DOB. DR ChiTaRS; HLA-DOB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9Z3, KW ECO:0000213|PeptideAtlas:A0A140T9Z3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 94 184 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000431178}. SQ SEQUENCE 244 AA; 27237 MW; 29FD53C180A706D8 CRC64; VSFFSFLQNG FWVGPLGGGS ASESDPTGFL HDSRHRLSSD VGMFVALTKL GQPDAEQWNS RLDLLERSRQ AVDGVCRHNY RLGAPFTVGR KVQPEVTVYP ERTPLLHQHN LLHCSVTGFY PGDIKIKWFL NGQEERAGVM STGPIRNGDW TFQTVVMLEM TPELGHVYTC LVDHSSLLSP VSVEWRAQSE YSWRKMLSGI AAFLLGLIFL LVGIVIQLRA QKGYVRTQMS GNEVSRAVLL PQSC // ID A0A140T9Z9_HUMAN Unreviewed; 136 AA. AC A0A140T9Z9; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000433300}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000433300}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000433300}; RN [1] {ECO:0000313|Ensembl:ENSP00000433300, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000433300} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140T9Z9; -. DR Ensembl; ENST00000490862; ENSP00000433300; ENSG00000233209. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140T9Z9, KW ECO:0000213|PeptideAtlas:A0A140T9Z9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 136 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305430. FT DOMAIN 45 119 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 136 AA; 15761 MW; 5D0E1F9BBB8DE055 CRC64; MSWKKALRIP GGLRVATVTL MLAMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVT RYIYNREEYA RFDSDVGVYR AVTPLGPPDA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRGTVT GPSRSW // ID A0A140TA15_HUMAN Unreviewed; 136 AA. AC A0A140TA15; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000435701}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000435701}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000435701}; RN [1] {ECO:0000313|Ensembl:ENSP00000435701, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000435701} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR933859; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140TA15; -. DR Ensembl; ENST00000480749; ENSP00000435701; ENSG00000231286. DR HGNC; HGNC:4944; HLA-DQB1. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140TA15, KW ECO:0000213|PeptideAtlas:A0A140TA15}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 136 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305614. FT DOMAIN 45 119 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 136 AA; 15869 MW; 5952B5396F8B9237 CRC64; MSWKKALRIP GGLRAATVTL MLAMLSTPVA EGRDSPEDFV YQFKAMCYFT NGTERVRYVT RYIYNREEYA RFDSDVEVYR AVTPLGPPDA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRGTVT GPSRSW // ID A0A140TA22_HUMAN Unreviewed; 154 AA. AC A0A140TA22; DT 11-MAY-2016, integrated into UniProtKB/TrEMBL. DT 11-MAY-2016, sequence version 1. DT 23-MAY-2018, entry version 11. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|Ensembl:ENSP00000437213}; DE Flags: Fragment; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSP00000437213}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000437213}; RN [1] {ECO:0000313|Ensembl:ENSP00000437213, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000437213} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A140TA22; -. DR Ensembl; ENST00000527042; ENSP00000437213; ENSG00000239457. DR HGNC; HGNC:4937; HLA-DOB. DR ChiTaRS; HLA-DOB; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A140TA22, KW ECO:0000213|PeptideAtlas:A0A140TA22}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 154 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007305585. FT DOMAIN 39 113 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 154 154 {ECO:0000313|Ensembl:ENSP00000437213}. SQ SEQUENCE 154 AA; 17448 MW; FDB9D1BD54E61ABE CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSRQA VDGVCRHNYR LGAPFTVGRK GFYPGDIKIK WFLNGQEERA GVMSTGPIRN GDWT // ID A0A151N4Y5_ALLMI Unreviewed; 281 AA. AC A0A151N4Y5; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 28-FEB-2018, entry version 12. DE SubName: Full=Rano class II histocompatibility antigen, A beta chain-like {ECO:0000313|EMBL:KYO31858.1}; GN ORFNames=Y1Q_0003423 {ECO:0000313|EMBL:KYO31858.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO31858.1}; RN [1] {ECO:0000313|EMBL:KYO31858.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO31858.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO31858.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AKHW03004037; KYO31858.1; -; Genomic_DNA. DR RefSeq; XP_006260917.2; XM_006260855.3. DR GeneID; 102576197; -. DR KEGG; amj:102576197; -. DR KO; K06752; -. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 23 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 227 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 281 AA; 31913 MW; 7BAF872B137E5B47 CRC64; MVSAGIAGAG CTGALIVIIA LRVNKAHCTE PPEHFLLQEN HECHYVNGTQ QARYVERVIW GQQEICYYDS DVGYYVARTE EGQWIAEYRN RLEYLSFLWA SVEKFCSYSY RRFKSVAMDR KVKPKIKIYP MKTESSHTPN LLVCSVTRFY PSGIRVKWLK NGQEHTGNVV SSELLPNGDW TFQMHVKLKM VPRRGDVYAC QVDHISLQTP MTLQWEVQTY SAKSKMIAGI VSLVLGLMLI MVGLVLYLKN GEGCPWPAAA QSWDADMRSG ISTTHLLEDC S // ID A0A151P1I9_ALLMI Unreviewed; 114 AA. AC A0A151P1I9; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 05-OCT-2016, entry version 4. DE SubName: Full=SLA class II histocompatibility antigen, DQ haplotype C beta chain-like {ECO:0000313|EMBL:KYO42952.1}; GN ORFNames=Y1Q_0023120 {ECO:0000313|EMBL:KYO42952.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO42952.1}; RN [1] {ECO:0000313|EMBL:KYO42952.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO42952.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO42952.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AKHW03001299; KYO42952.1; -; Genomic_DNA. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}. FT DOMAIN 18 92 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 114 AA; 13489 MW; 47BED0F8FF2E4DCC CRC64; MFLLVFQAAL FPNQKDKHEC LYTNSTQRVR YVNRYVWNQQ DYVHFDSDVG VFVADTELGE PTATCWNSQK EELEYRRGLV DRFCRHNYGM FERGHVISRS VVSTVYPDGA KIIW // ID A0A151P1Q2_ALLMI Unreviewed; 296 AA. AC A0A151P1Q2; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 25-OCT-2017, entry version 7. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain-like {ECO:0000313|EMBL:KYO42953.1}; GN ORFNames=Y1Q_0023121 {ECO:0000313|EMBL:KYO42953.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO42953.1}; RN [1] {ECO:0000313|EMBL:KYO42953.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO42953.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO42953.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AKHW03001299; KYO42953.1; -; Genomic_DNA. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 296 AA; 33770 MW; 3B5014353499F6F2 CRC64; MGTSESLGAG SCWAGALLVK LLFLRTHMAH CMRYPEHFMV QGKQECHYTN GSRRVRYLDR EIWNQEQFIH FDSDEGRWVA DTELGEPYAR YWNSQKDVLE YRQGSVNTFC RHDYQAITPY SVARTVKPKV KVSPTKSGAK VHLDTLVCFV TGFYPGGIEV KWLKNRQEQT AGVVSTELMQ NGDWTFQILV MLEMTPRSGD VYTCQVEHSS LMGSLTVAWE AKSDSARRKM LTGIGGFMMG LIFLALGLLV YLRNKKGQPV PQPIAQPGWE LEHGTFSVRK RRSLHLPHRH YSGLFS // ID A0A151P6D8_ALLMI Unreviewed; 83 AA. AC A0A151P6D8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 05-OCT-2016, entry version 4. DE SubName: Full=HLA class II histocompatibility antigen, DR beta 5 chain-like {ECO:0000313|EMBL:KYO44628.1}; GN ORFNames=Y1Q_0002454 {ECO:0000313|EMBL:KYO44628.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO44628.1}; RN [1] {ECO:0000313|EMBL:KYO44628.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO44628.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO44628.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AKHW03000699; KYO44628.1; -; Genomic_DNA. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}. FT DOMAIN 12 82 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 83 AA; 9961 MW; CB40E068557CC2A7 CRC64; MGTDHFLYQD KQECYYTKGT QRARFLYRHI WNQQQDVHFD SDVGVFVADT ELGEPATKHW NSQKDVLEYN RRSVDRFCQN SNP // ID A0A151PDW8_ALLMI Unreviewed; 118 AA. AC A0A151PDW8; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 05-OCT-2016, entry version 4. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYO47170.1}; GN ORFNames=Y1Q_0015396 {ECO:0000313|EMBL:KYO47170.1}; OS Alligator mississippiensis (American alligator). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae; OC Alligator. OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO47170.1}; RN [1] {ECO:0000313|EMBL:KYO47170.1, ECO:0000313|Proteomes:UP000050525} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO47170.1}; RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415; RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., RA Gongora J., Dalzell P., Moran C., Bed'hom B., Abzhanov A., RA Burgess S.C., Cooksey A.M., Castoe T.A., Crawford N.G., Densmore L.D., RA Drew J.C., Edwards S.V., Faircloth B.C., Fujita M.K., Greenwold M.J., RA Hoffmann F.G., Howard J.M., Iguchi T., Janes D.E., Khan S.Y., RA Kohno S., de Koning A.J., Lance S.L., McCarthy F.M., McCormack J.E., RA Merchant M.E., Peterson D.G., Pollock D.D., Pourmand N., Raney B.J., RA Roessler K.A., Sanford J.R., Sawyer R.H., Schmidt C.J., Triplett E.W., RA Tuberville T.D., Venegas-Anaya M., Howard J.T., Jarvis E.D., RA Guillette L.J.Jr., Glenn T.C., Green R.E., Ray D.A.; RT "Sequencing three crocodilian genomes to illuminate the evolution of RT archosaurs and amniotes."; RL Genome Biol. 13:415-415(2012). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KYO47170.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AKHW03000478; KYO47170.1; -; Genomic_DNA. DR Proteomes; UP000050525; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000050525}; KW Reference proteome {ECO:0000313|Proteomes:UP000050525}. FT DOMAIN 6 80 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 118 AA; 13608 MW; 1E385EC8205A7564 CRC64; MIMSKADCVY TNGTQQLKCL YSCIWDRQQD VHFDSNVGMH VADTVWAEPD AKHWNSQKEE PQHAWSEMDS FCRHNYGVYE NFINTHKGEF CRYDYGLAEQ SHVIGRSGES PESGAIVQ // ID A0A182DWE9_HUMAN Unreviewed; 258 AA. AC A0A182DWE9; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 12-SEP-2018, entry version 22. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000372582}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:SIT60377.1}; GN Name=HLA-DPB1 {ECO:0000313|EMBL:SIT60377.1, GN ECO:0000313|Ensembl:ENSP00000372582}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000372582, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000372582, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000372582} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2016) to UniProtKB. RN [3] {ECO:0000313|EMBL:SIT60377.1} RP NUCLEOTIDE SEQUENCE. RA Song W.-J., Kurnit D.M.; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:SIT60377.1} RP NUCLEOTIDE SEQUENCE. RA Lang K., Schoefl G., Schmidt A., Lange V.; RT "Complementing the HLA-DPB1 Database: Full-Length Gene RT Characterization of all Common and Well-Documented Alleles."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:SJK83243.1} RP NUCLEOTIDE SEQUENCE. RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; LT707878; SIT60377.1; -; Genomic_DNA. DR EMBL; LT707879; SIT60378.1; -; Genomic_DNA. DR EMBL; LT707880; SIT60379.1; -; Genomic_DNA. DR EMBL; LT707881; SIT60380.1; -; Genomic_DNA. DR EMBL; LT707882; SIT60381.1; -; Genomic_DNA. DR EMBL; LT707883; SIT60382.1; -; Genomic_DNA. DR EMBL; LT718928; SJK83243.1; -; Genomic_DNA. DR EMBL; LT718929; SJK83244.1; -; Genomic_DNA. DR EMBL; LT718930; SJK83245.1; -; Genomic_DNA. DR EMBL; LT718931; SJK83246.1; -; Genomic_DNA. DR EMBL; LT718963; SJK83278.1; -; Genomic_DNA. DR Ensembl; ENST00000383102; ENSP00000372582; ENSG00000230708. DR HGNC; HGNC:4940; HLA-DPB1. DR PhylomeDB; A0A182DWE9; -. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A182DWE9, KW ECO:0000213|PeptideAtlas:A0A182DWE9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015052676. FT TRANSMEM 227 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29357 MW; 8BAB349E25A0FFA2 CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYVYQL RQECYAFNGT QRFLERYIYN REEFVRFDSD VGEFRAVTEL GRPDEDYWNS QKDLLEEKRA VPDRVCRHNY ELDEAVTLQR RVQPKVNVSP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYIC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID A0A182DWF4_HUMAN Unreviewed; 228 AA. AC A0A182DWF4; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 23-MAY-2018, entry version 10. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000388249}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000388249}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000388249, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000388249, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000388249} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR847849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A182DWF4; -. DR Ensembl; ENST00000447783; ENSP00000388249; ENSG00000229295. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A182DWF4, KW ECO:0000213|PeptideAtlas:A0A182DWF4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 228 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008116502. FT TRANSMEM 197 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 83 182 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 228 AA; 25897 MW; 924988887EA2D751 CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYLFQG RQECYAFNGT QRFLERYIYN REEFVRFDSD VGEFRAVTEL GRPDEEYWNS QKDILEEERA VPDRMCRHNY ELGGPMTLQR RGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID A0A182DWF5_HUMAN Unreviewed; 235 AA. AC A0A182DWF5; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 23-MAY-2018, entry version 10. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000389618}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000389618}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000389618, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000389618, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000389618} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR847849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A182DWF5; -. DR Ensembl; ENST00000445925; ENSP00000389618; ENSG00000229295. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A182DWF5, KW ECO:0000213|PeptideAtlas:A0A182DWF5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000389618}. SQ SEQUENCE 235 AA; 27054 MW; 7C704955E413D77E CRC64; XNYLFQGRQE CYAFNGTQRF LERYIYNREE FVRFDSDVGE FRAVTELGRP DEEYWNSQKD ILEEERAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKKG EKACRFNEDL HKQGS // ID A0A182DWG2_HUMAN Unreviewed; 229 AA. AC A0A182DWG2; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 23-MAY-2018, entry version 10. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000399852}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000399852}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000399852, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000399852, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000399852} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR847849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A182DWG2; -. DR Ensembl; ENST00000415438; ENSP00000399852; ENSG00000229295. DR HGNC; HGNC:4940; HLA-DPB1. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A182DWG2, KW ECO:0000213|PeptideAtlas:A0A182DWG2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000399852}. FT NON_TER 229 229 {ECO:0000313|Ensembl:ENSP00000399852}. SQ SEQUENCE 229 AA; 26215 MW; 84C70321729CE65A CRC64; KQAWRGSATR LGPQNSGRQE CYAFNGTQRF LERYIYNREE FVRFDSDVGE FRAVTELGRP DEEYWNSQKD ILEEERAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKK // ID A0A182DWH4_HUMAN Unreviewed; 266 AA. AC A0A182DWH4; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 07-SEP-2016, sequence version 1. DT 23-MAY-2018, entry version 10. DE SubName: Full=HLA class II histocompatibility antigen, DR beta 3 chain {ECO:0000313|Ensembl:ENSP00000416022}; GN Name=HLA-DRB3 {ECO:0000313|Ensembl:ENSP00000416022}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000416022, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000416022, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000416022} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR788283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; A0A182DWH4; -. DR Ensembl; ENST00000426847; ENSP00000416022; ENSG00000230463. DR HGNC; HGNC:4951; HLA-DRB3. DR PhylomeDB; A0A182DWH4; -. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A0A182DWH4, KW ECO:0000213|PeptideAtlas:A0A182DWH4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29941 MW; F08F1C26E99D184A CRC64; MVCLKLPGGS SLAALTVTLM VLSSRLAFAG DTRPRFLELL KSECHFFNGT ERVRFLERHF HNQEEYARFD SDVGEYRAVR ELGRPDAEYW NSQKDLLEQK RGQVDNYCRH NYGVGESFTV QRRVHPQVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWSAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID A2AAZ0_HUMAN Unreviewed; 224 AA. AC A2AAZ0; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 12-SEP-2018, entry version 86. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000382029}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000382029}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000382029, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000382029, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000382029} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; A2AAZ0; -. DR SMR; A2AAZ0; -. DR MaxQB; A2AAZ0; -. DR PeptideAtlas; A2AAZ0; -. DR PRIDE; A2AAZ0; -. DR Ensembl; ENST00000399079; ENSP00000382029; ENSG00000179344. DR UCSC; uc011dqd.3; human. DR EuPathDB; HostDB:ENSG00000179344.16; -. DR HGNC; HGNC:4944; HLA-DQB1. DR OpenTargets; ENSG00000179344; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000179344; Expressed in 206 organ(s), highest expression level in right lung. DR ExpressionAtlas; A2AAZ0; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:A2AAZ0, KW ECO:0000213|PeptideAtlas:A2AAZ0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5002642641. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 224 AA; 25962 MW; DEF952049C8E61DB CRC64; MSWKKALRIP GDLRVATVTL MLAMLSSLLA EGRDSPEDFV FQFKGMCYFT NGTERVRLVT RYIYNREEYA RFDSDVGVYR AVTPQGRPDA EYWNSQKEVL EGTRAELDTV CRHNYEVAFR GILQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RLLH // ID A2ADX3_HUMAN Unreviewed; 275 AA. AC A2ADX3; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 12-SEP-2018, entry version 113. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000410512}; DE SubName: Full=cDNA FLJ40688 fis, clone THYMU2024185, highly similar to HLA class II histocompatibility antigen, DX beta chain {ECO:0000313|EMBL:BAG53563.1}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000410512}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000410512, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000410512, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|EMBL:BAG53563.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Thymus {ECO:0000313|EMBL:BAG53563.1}; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] {ECO:0000313|Ensembl:ENSP00000410512} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [4] {ECO:0000313|Ensembl:ENSP00000387578} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL671681; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL672104; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL713890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK098007; BAG53563.1; -; mRNA. DR RefSeq; XP_005249108.1; XM_005249051.4. DR UniGene; Hs.731563; -. DR PRIDE; A2ADX3; -. DR Ensembl; ENST00000415137; ENSP00000387578; ENSG00000224305. DR Ensembl; ENST00000435145; ENSP00000410512; ENSG00000232629. DR Ensembl; ENST00000442806; ENSP00000394759; ENSG00000226165. DR Ensembl; ENST00000455520; ENSP00000409159; ENSG00000230675. DR GeneID; 3120; -. DR UCSC; uc003obz.3; human. DR CTD; 3120; -. DR EuPathDB; HostDB:ENSG00000232629.8; -. DR HGNC; HGNC:4945; HLA-DQB2. DR OpenTargets; ENSG00000232629; -. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR ChiTaRS; HLA-DQB2; human. DR GenomeRNAi; 3120; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000232629; Expressed in 120 organ(s), highest expression level in skin of abdomen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A2ADX3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 275 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014565236. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 275 AA; 30948 MW; 6E1A385D96839EE0 CRC64; MALQIPGGFW AAAVTVMLVM LSTPVAEARD FPKDFLVQFK GMCYFTNGTE RVRGVARYIY NREEYGRFDS DVGEFQAVTE LGRSIEDWNN YKDFLEQERA AVDKVCRHNY EAELRTTLQR QVEPTVTISP SRTEALNHHN LLVCSVTDFY PAQIKVRWFR NDQEETAGVV STSLIRNGDW TFQILVMLEI TPQRGDIYTC QVEHPSLQSP ITVEWRAQSE SAQSKMLSGI GGFVLGLIFL GLGLIIRHRG QKGPRGPPPA GNISAMIQSG ERAQA // ID A2VDX2_BOVIN Unreviewed; 261 AA. AC A2VDX2; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 12-SEP-2018, entry version 102. DE SubName: Full=Major histocompatibility complex, class II, DQ beta {ECO:0000313|EMBL:AAI33450.1}; GN Name=BOLA-DQB {ECO:0000313|EMBL:AAI33450.1, GN ECO:0000313|Ensembl:ENSBTAP00000043594}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI33450.1}; RN [1] {ECO:0000313|EMBL:AAI33450.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hereford {ECO:0000313|EMBL:AAI33450.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:AAI33450.1}; RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y., RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C., RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J., RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J., RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., RA Siddiqui A., Holt R., Jones S.J., Marra M.A.; RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000043594, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000043594, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [3] {ECO:0000313|Ensembl:ENSBTAP00000043594} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000043594}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; DAAA02055283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC133449; AAI33450.1; -; mRNA. DR RefSeq; NP_001012694.2; NM_001012676.3. DR UniGene; Bt.102153; -. DR STRING; 9913.ENSBTAP00000043594; -. DR Ensembl; ENSBTAT00000046279; ENSBTAP00000043594; ENSBTAG00000021077. DR GeneID; 282495; -. DR KEGG; bta:282495; -. DR CTD; 282495; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-BTA-202424; Downstream TCR signaling. DR Reactome; R-BTA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-BTA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-BTA-202433; Generation of second messenger molecules. DR Reactome; R-BTA-2132295; MHC class II antigen presentation. DR Reactome; R-BTA-389948; PD-1 signaling. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000021077; Expressed in 8 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014083552. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29618 MW; B6D583735672D8A7 CRC64; MSGMVALWIP RGLWTAAVMV TLAVLSTPGA EGRDSPQDTV VHFMCQCYFT NGTERVRYVT RYIYNQEETA YYDSDVGEYR AVTQLGRTLA EYWNSQKDIL EQTRAELDTV CRHNYQLEVI TSLQRQVEPT VTISLSRTEA LNHHNLLVCS VTDFYPGQIK VRWFQNGKEE TAGIVSTPLI RNGDWTFQIL VMLEMTPKRG DVYTCRVEHP SLQSPISVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI VRRRSQKGLM H // ID A4Q982_MACMU Unreviewed; 266 AA. AC A4Q982; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 12-SEP-2018, entry version 90. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:CAM84164.1}; GN Name=drb {ECO:0000313|EMBL:CAM84164.1}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|EMBL:CAM84164.1}; RN [1] {ECO:0000313|EMBL:CAM84164.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2Y {ECO:0000313|EMBL:CAM84164.1}; RA Groot, De N., Doxiadis G.G.M., Bontrop R.E.; RT "Mhc-cDRB analyses of the rhesus macaque."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAM84164.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=2Y {ECO:0000313|EMBL:CAM84164.1}; RA Groot N.D.; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AM690327; CAM84164.1; -; mRNA. DR RefSeq; NP_001305273.1; NM_001318344.1. DR UniGene; Mmu.10374; -. DR ProteinModelPortal; A4Q982; -. DR STRING; 9544.ENSMMUP00000002057; -. DR GeneID; 705588; -. DR KEGG; mcc:705588; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Bgee; ENSMMUG00000008227; Expressed in 13 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5009946436. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29690 MW; 5DB136107721F42B CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLAVAG DTRPRFLEQA KAECHFFNGT ERVRFLERHF YNQEELVRFD SDVGEYRAVT ELGRPTAESW NSRKDVLERA RTAADTYCRH NYRGGESFTV QRRVQPKVTV YPAKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKAG VVSTGLIHNG DWTFQTLVML ETVPQSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHAGLQ PTGLLS // ID A5D9J8_PIG Unreviewed; 277 AA. AC A5D9J8; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 12-SEP-2018, entry version 94. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|EMBL:CAN13320.1}; GN Name=SLA-DOB {ECO:0000313|EMBL:CAN13320.1}; GN ORFNames=SBAB-554F3.4-001 {ECO:0000313|EMBL:CAN13320.1}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:CAN13320.1}; RN [1] {ECO:0000313|EMBL:CAN13320.1} RP NUCLEOTIDE SEQUENCE. RA Sehra H.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX323833; CAN13320.1; -; Genomic_DNA. DR RefSeq; XP_003128376.1; XM_003128328.4. DR UniGene; Ssc.28057; -. DR STRING; 9823.ENSSSCP00000001586; -. DR PaxDb; A5D9J8; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Bgee; ENSSSCG00000001465; Expressed in 5 organ(s), highest expression level in liver. DR ExpressionAtlas; A5D9J8; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. SQ SEQUENCE 277 AA; 31286 MW; 04DDECC2EA249620 CRC64; MIYTTSFSFS PSRMGSSWVP WVVALLVMVI RLDSSMTQGR DPPEDFVIQA KADCYFTNGT QRVQFVVRFI FNLEEFVRFD SDLGKFVALT ELGQPDAELW NSRPDILESS RASVDVLCRR NYWLGAPLTV ERKVQPEVTV HPERTPSLQL RNLLLCSVTG FYPGAIEIRW FRNGQEQREG VLATGLVRNG DWTFQTVVML EMTPELGDVY TCLVDHPSLL SPVSVEWRAQ SDCSWTKLLI GVAAFLGGLT FLLVGIIIHV RARKGRVETQ LSGDEPH // ID A5D9L3_PIG Unreviewed; 272 AA. AC A5D9L3; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 12-SEP-2018, entry version 96. DE SubName: Full=MHC class II, DM beta precursor {ECO:0000313|Ensembl:ENSSSCP00000001591}; DE SubName: Full=Major histocompatibility complex, class II, DM beta {ECO:0000313|EMBL:CAN13292.1}; GN Name=SLA-DMB {ECO:0000313|EMBL:CAN13292.1, GN ECO:0000313|Ensembl:ENSSSCP00000001591}; GN ORFNames=SBAB-1044B7.2-001 {ECO:0000313|EMBL:CAN13292.1}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:CAN13292.1}; RN [1] {ECO:0000313|EMBL:CAN13292.1} RP NUCLEOTIDE SEQUENCE. RA Beasley H.; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSSCP00000001591, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000001591}; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSSSCP00000001591} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEMK02000055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX324144; CAN13292.1; -; Genomic_DNA. DR RefSeq; NP_001107179.1; NM_001113707.1. DR UniGene; Ssc.50352; -. DR STRING; 9823.ENSSSCP00000001591; -. DR PRIDE; A5D9L3; -. DR Ensembl; ENSSSCT00000001633; ENSSSCP00000001591; ENSSSCG00000001469. DR GeneID; 100135050; -. DR KEGG; ssc:100135050; -. DR CTD; 100135050; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000231198; -. DR HOVERGEN; HBG007327; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Reactome; R-SSC-2132295; MHC class II antigen presentation. DR Proteomes; UP000008227; Chromosome 7. DR Bgee; ENSSSCG00000001469; Expressed in 5 organ(s), highest expression level in lung. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:A5D9L3}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 272 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015086484. FT DOMAIN 123 229 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 272 AA; 29847 MW; 725C53E6A3CAC6F9 CRC64; MPCISPEQSM SALLQLLLGL SLGCTGAGGF VAHVESTCLL DDEGTPQDFT YCISFNKDLL TCWDPQETRM VPCEFGALNA LATYFSVYLN QQEKLLQRLS NGLQNCATHT QPFWKSLTHR TQPPSVQVAK TTPFNTRESV MLACYVWGFY PADVIITWRK NGQPVLPHGK AHMITQPNGD WTYQTVSHLA TTPSYGDTYT CVVEHIGVPE PILQDWTSGL SPVQTVKISV SVATLGLGLI IFSLGLLSCQ RSVAPGYIFL PGTTYPEGQH IS // ID A5HUL8_CHICK Unreviewed; 258 AA. AC A5HUL8; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 12-SEP-2018, entry version 99. DE SubName: Full=MHC class II M beta chain 2 {ECO:0000313|EMBL:BAF63002.1}; GN Name=DMB2 {ECO:0000313|EMBL:BAF63002.1, GN ECO:0000313|Ensembl:ENSGALP00000053589}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|EMBL:BAF63002.1}; RN [1] {ECO:0000313|Ensembl:ENSGALP00000053589, ECO:0000313|Proteomes:UP000000539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000053589, RC ECO:0000313|Proteomes:UP000000539}; RX PubMed=15592404; DOI=10.1038/nature03154; RG International Chicken Genome Sequencing Consortium; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., RA Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., RA Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., RA Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C., RA Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., RA Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., RA Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., RA Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., RA Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., RA Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., RA van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., RA Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., RA Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., RA Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., RA Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., RA Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., RA Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., RA Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., RA King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., RA Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., RA Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., RA Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., RA Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., RA Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., RA Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., RA Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., RA Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., RA Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., RA Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., RA Mardis E.R., Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide RT unique perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [2] {ECO:0000313|EMBL:BAF63002.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17513765; DOI=10.4049/jimmunol.178.11.7162; RA Shiina T., Briles W.E., Goto R.M., Hosomichi K., Yanagiya K., RA Shimizu S., Inoko H., Miller M.M.; RT "Extended gene map reveals tripartite motif, C-type lectin, and Ig RT superfamily type genes within a subregion of the chicken MHC-B RT affecting infectious disease."; RL J. Immunol. 178:7162-7172(2007). RN [3] {ECO:0000313|EMBL:BAG69451.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cornell-N {ECO:0000313|EMBL:BAG69451.1}; RX PubMed=18714011; RA Hosomichi K., Miller M.M., Goto R.M., Wang Y., Suzuki S., Kulski J.K., RA Nishibori M., Inoko H., Hanzawa K., Shiina T.; RT "Contribution of mutation, recombination, and gene conversion to RT chicken MHC-B haplotype diversity."; RL J. Immunol. 181:3393-3399(2008). RN [4] {ECO:0000313|Ensembl:ENSGALP00000053589} RP IDENTIFICATION. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000053589}; RG Ensembl; RL Submitted (OCT-2016) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AADN04000555; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB268588; BAF63002.1; -; Genomic_DNA. DR EMBL; AB426152; BAG69451.1; -; Genomic_DNA. DR RefSeq; NP_001128638.1; NM_001135166.1. DR UniGene; Gga.11537; -. DR Ensembl; ENSGALT00000076652; ENSGALP00000053589; ENSGALG00000038393. DR GeneID; 417051; -. DR KEGG; gga:417051; -. DR CTD; 417051; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000231198; -. DR HOVERGEN; HBG007327; -. DR KO; K06752; -. DR Proteomes; UP000000539; Chromosome 16. DR Bgee; ENSGALG00000000166; Expressed in 10 organ(s), highest expression level in heart. DR ExpressionAtlas; A5HUL8; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000539}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000539}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014296981. FT TRANSMEM 213 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 111 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 27887 MW; 578A3261926EC77D CRC64; MLVLLGLLLG VRGAGAFMVH VANSCPLAAN GSLRGFDLTV AFNKNPLVCY DPDGHLFNAC DWGLLHGVAG QIAIALNNDS TWVQRAEARR RACSKLAAQF WAQTALRRTQ PQVRIVPAQT GNPSVPIRLT CHVWGFYPPE VTIIWLHNGD IVGPGDHSPM FAIPNGNWTY QTQVALSVAP EVGDTYTCSV QHASLEEPLL EDWRPGLTLE VTLMVAVATV VMVLGLSLLF IGVYCWRAQP PAPGYAPLPG HNYPSGSI // ID B4DJG1_HUMAN Unreviewed; 136 AA. AC B4DJG1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 18-JUL-2018, entry version 74. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000435178}; DE SubName: Full=cDNA FLJ53582, highly similar to HLA class II histocompatibility antigen, DQ(1)beta chain {ECO:0000313|EMBL:BAG58823.1}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000435178}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG58823.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000435178, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|EMBL:BAG58823.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Thalamus {ECO:0000313|EMBL:BAG58823.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., RA Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., RA Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., RA Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSP00000435178} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX927168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK296060; BAG58823.1; -; mRNA. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR EPD; B4DJG1; -. DR MaxQB; B4DJG1; -. DR PRIDE; B4DJG1; -. DR Ensembl; ENST00000473366; ENSP00000435178; ENSG00000225824. DR UCSC; uc063wye.1; human. DR HGNC; HGNC:4944; HLA-DQB1. DR HOVERGEN; HBG012730; -. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Proteomics identification {ECO:0000213|MaxQB:B4DJG1, KW ECO:0000213|PeptideAtlas:B4DJG1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 136 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014567680. FT DOMAIN 45 119 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 136 AA; 15679 MW; BA1C9E4CFB258A89 CRC64; MSWKKALRIP GGLRAATVTL MLSMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVS RSIYNREEIV RFDSDVGEFR AVTLLGLPAA EYWNSQKDIL ERKRAAVDRV CRHNYQLELR TTLQRRGMVT GPSRSW // ID DMB_HUMAN Reviewed; 263 AA. AC P28068; O77936; Q13012; Q29751; Q58ZE2; Q5SNZ8; Q5STC4; Q9XRX2; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1992, sequence version 1. DT 12-SEP-2018, entry version 179. DE RecName: Full=HLA class II histocompatibility antigen, DM beta chain; DE AltName: Full=MHC class II antigen DMB; DE AltName: Full=Really interesting new gene 7 protein; DE Flags: Precursor; GN Name=HLA-DMB; Synonyms=DMB, RING7; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DMB*01:01). RX PubMed=1922365; DOI=10.1038/353571a0; RA Kelly A.P., Monaco J.J., Cho S., Trowsdale J.; RT "A new human HLA class II-related locus, DM."; RL Nature 353:571-573(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DMB*01:01). RX PubMed=8034636; RA Radley E., Alderton R.P., Kelly A., Trowsdale J., Beck S.; RT "Genomic organization of HLA-DMA and HLA-DMB. Comparison of the gene RT organization of all six class II families in the human major RT histocompatibility complex."; RL J. Biol. Chem. 269:18834-18838(1994). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DMB*01:01). RX PubMed=8568858; DOI=10.1006/jmbi.1996.0001; RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., RA Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., RA Radley E., Thorpe K.L., Trowsdale J.; RT "Evolutionary dynamics of non-coding sequences within the class II RT region of the human MHC."; RL J. Mol. Biol. 255:1-13(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DMB*01:07). RX PubMed=15787724; DOI=10.1111/j.1399-0039.2005.00385.x; RA Gu H., Moon S.-M., Kim J.-J., Ryu H.-J., Kwack K., Kimm K., Lee J.-K., RA Oh B.; RT "Identification of a novel HLA-DMB allele (DMB*0107) in the Korean RT population."; RL Tissue Antigens 65:393-394(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-197. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DMB*01:01). RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 114-207 (ALLELES DMB*01:02 AND RP DMB*01:03). RX PubMed=8225438; DOI=10.1007/BF00171797; RA Sanderson F., Powis S.H., Kelly A.P., Trowsdale J.; RT "Limited polymorphism in HLA-DM does not involve the peptide binding RT groove."; RL Immunogenetics 39:56-58(1994). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 121-200 (ALLELE DMB*01:04). RX PubMed=8406617; DOI=10.1007/BF00184526; RA Carrington M., Yeager M., Mann D.; RT "Characterization of HLA-DMB polymorphism."; RL Immunogenetics 38:446-449(1993). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-207 (ALLELE DMB*01:05). RC TISSUE=Blood; RX PubMed=9157091; DOI=10.1016/0198-8859(95)00171-9; RA Kim T.-G., Carrington M., Choi H.B., Kim H.Y., Han H.; RT "Three HLA-DMB variants in Korean patients with autoimmune diseases."; RL Hum. Immunol. 46:58-60(1996). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 19-112 AND 152-207 (ALLELE RP DMB*01:06). RX PubMed=10885572; DOI=10.1034/j.1399-0039.2000.550514.x; RA McTernan C.L., Mijovic C.H., Cockram C.S., Barnett A.H.; RT "The nucleotide sequence of a new DMB allele, DMB*0106."; RL Tissue Antigens 55:470-472(2000). RN [12] RP FUNCTION. RX PubMed=8849454; DOI=10.1126/science.274.5287.618; RA Weber D.A., Evavold B.D., Jensen P.E.; RT "Enhanced dissociation of HLA-DR-bound peptides in the presence of RT HLA-DM."; RL Science 274:618-620(1996). RN [13] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-248 AND LEU-251. RX PubMed=8757605; RA Copier J., Kleijmeer M.J., Ponnambalam S., Oorschot V., Potter P., RA Trowsdale J., Kelly A.; RT "Targeting signal and subcellular compartments involved in the RT intracellular trafficking of HLA-DMB."; RL J. Immunol. 157:1017-1027(1996). RN [14] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-218 IN COMPLEX WITH DMA, RP FUNCTION, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=9768757; DOI=10.1016/S1074-7613(00)80620-2; RA Mosyak L., Zaller D.M., Wiley D.C.; RT "The structure of HLA-DM, the peptide exchange catalyst that loads RT antigen onto class II MHC molecules during antigen presentation."; RL Immunity 9:377-383(1998). RN [16] RP X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 19-218 IN COMPLEX WITH DMA, RP FUNCTION, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=16547258; DOI=10.4049/jimmunol.176.7.4208; RA Nicholson M.J., Moradi B., Seth N.P., Xing X., Cuny G.D., Stein R.L., RA Wucherpfennig K.W.; RT "Small molecules that enhance the catalytic efficiency of HLA-DM."; RL J. Immunol. 176:4208-4220(2006). CC -!- FUNCTION: Plays a critical role in catalyzing the release of class CC II-associated invariant chain peptide (CLIP) from newly CC synthesized MHC class II molecules and freeing the peptide binding CC site for acquisition of antigenic peptides. In B-cells, the CC interaction between HLA-DM and MHC class II molecules is regulated CC by HLA-DO. {ECO:0000269|PubMed:16547258, CC ECO:0000269|PubMed:8849454, ECO:0000269|PubMed:9768757}. CC -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain CC (DMB). {ECO:0000269|PubMed:16547258, ECO:0000269|PubMed:9768757}. CC -!- INTERACTION: CC Q6ICR9:HLA-DMA; NbExp=5; IntAct=EBI-2877138, EBI-16027071; CC -!- SUBCELLULAR LOCATION: Late endosome membrane CC {ECO:0000269|PubMed:8757605}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:8757605}. Lysosome membrane CC {ECO:0000269|PubMed:8757605}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:8757605}. Note=Localizes to late endocytic CC compartment. Associates with lysosome membranes. CC -!- DOMAIN: The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic CC residue) motif mediates the targeting to the lysosomal CC compartments. CC -!- POLYMORPHISM: The following alleles of DMB are known: DMB*01:01, CC DMB*01:02, DMB*01:03, DMB*01:04 (DMB3.4), DMB*01:05, DMB*01:06, CC and DMB*01:07. The sequence shown is that of DMB*01:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; Z23139; CAA80670.1; -; mRNA. DR EMBL; U15085; AAB60387.1; -; mRNA. DR EMBL; X76776; CAA54171.1; -; Genomic_DNA. DR EMBL; X87344; CAA60782.1; -; Genomic_DNA. DR EMBL; AY645722; AAV97947.1; -; mRNA. DR EMBL; AL662845; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL645941; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL935042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX088556; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927138; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR752645; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03657.1; -; Genomic_DNA. DR EMBL; BC027175; AAH27175.1; -; mRNA. DR EMBL; Z24750; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z24751; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U00700; AAA03296.1; -; Genomic_DNA. DR EMBL; U16762; AAC50514.1; -; Genomic_DNA. DR EMBL; AF134890; AAD30279.1; -; Genomic_DNA. DR EMBL; AF072680; AAC26112.1; -; Genomic_DNA. DR CCDS; CCDS4760.1; -. DR PIR; I37533; I37533. DR RefSeq; NP_002109.2; NM_002118.4. DR UniGene; Hs.351279; -. DR PDB; 1HDM; X-ray; 2.50 A; B=19-218. DR PDB; 2BC4; X-ray; 2.27 A; B/D=19-218. DR PDB; 4FQX; X-ray; 2.60 A; D=19-211. DR PDB; 4GBX; X-ray; 3.00 A; D=19-211. DR PDB; 4I0P; X-ray; 3.20 A; B/F=21-211. DR PDBsum; 1HDM; -. DR PDBsum; 2BC4; -. DR PDBsum; 4FQX; -. DR PDBsum; 4GBX; -. DR PDBsum; 4I0P; -. DR ProteinModelPortal; P28068; -. DR SMR; P28068; -. DR BioGrid; 109354; 11. DR DIP; DIP-6185N; -. DR IntAct; P28068; 10. DR MINT; P28068; -. DR STRING; 9606.ENSP00000398890; -. DR iPTMnet; P28068; -. DR PhosphoSitePlus; P28068; -. DR BioMuta; HLA-DMB; -. DR DMDM; 133160; -. DR PaxDb; P28068; -. DR PeptideAtlas; P28068; -. DR PRIDE; P28068; -. DR ProteomicsDB; 54443; -. DR DNASU; 3109; -. DR Ensembl; ENST00000383231; ENSP00000372718; ENSG00000241674. DR Ensembl; ENST00000395312; ENSP00000378723; ENSG00000242092. DR Ensembl; ENST00000412948; ENSP00000413471; ENSG00000241296. DR Ensembl; ENST00000418107; ENSP00000398890; ENSG00000242574. DR Ensembl; ENST00000424822; ENSP00000414817; ENSG00000234154. DR Ensembl; ENST00000428420; ENSP00000393646; ENSG00000239329. DR Ensembl; ENST00000440078; ENSP00000411321; ENSG00000226264. DR Ensembl; ENST00000450897; ENSP00000408453; ENSG00000242386. DR GeneID; 3109; -. DR KEGG; hsa:3109; -. DR UCSC; uc003ocl.2; human. DR CTD; 3109; -. DR DisGeNET; 3109; -. DR EuPathDB; HostDB:ENSG00000242574.8; -. DR GeneCards; HLA-DMB; -. DR H-InvDB; HIX0166396; -. DR H-InvDB; HIX0207613; -. DR H-InvDB; HIX0207705; -. DR H-InvDB; HIX0207762; -. DR HGNC; HGNC:4935; HLA-DMB. DR HPA; HPA012298; -. DR MIM; 142856; gene. DR neXtProt; NX_P28068; -. DR PharmGKB; PA35059; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR HOVERGEN; HBG007327; -. DR InParanoid; P28068; -. DR KO; K06752; -. DR OrthoDB; EOG091G0G84; -. DR PhylomeDB; P28068; -. DR TreeFam; TF335727; -. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR SIGNOR; P28068; -. DR ChiTaRS; HLA-DMB; human. DR EvolutionaryTrace; P28068; -. DR GeneWiki; HLA-DMB; -. DR GenomeRNAi; 3109; -. DR PRO; PR:P28068; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000242574; Expressed in 226 organ(s), highest expression level in leukocyte. DR CleanEx; HS_HLA-DMB; -. DR ExpressionAtlas; P28068; baseline and differential. DR Genevisible; P28068; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:UniProtKB. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002399; P:MHC class II protein complex assembly; IMP:UniProtKB. DR GO; GO:0002503; P:peptide antigen assembly with MHC class II protein complex; IDA:UniProtKB. DR GO; GO:2001190; P:positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Endosome; KW Glycoprotein; Immunity; Immunoglobulin domain; Lysosome; Membrane; KW MHC II; Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 263 HLA class II histocompatibility antigen, FT DM beta chain. FT /FTId=PRO_0000018960. FT TOPO_DOM 19 218 Lumenal. {ECO:0000255}. FT TRANSMEM 219 239 Helical. {ECO:0000255}. FT TOPO_DOM 240 263 Cytoplasmic. {ECO:0000255}. FT DOMAIN 114 208 Ig-like C1-type. FT REGION 19 112 Beta-1. FT REGION 113 207 Beta-2. FT REGION 208 218 Connecting peptide. {ECO:0000255}. FT MOTIF 248 251 YXXZ motif. FT CARBOHYD 110 110 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:16335952}. FT DISULFID 29 97 FT DISULFID 135 192 FT VARIANT 28 28 T -> A (in allele DMB*01:07; FT dbSNP:rs17583782). FT /FTId=VAR_050360. FT VARIANT 45 45 S -> F (in allele DMB*01:06; FT dbSNP:rs41560814). FT /FTId=VAR_016752. FT VARIANT 49 49 D -> V (in allele DMB*01:07; FT dbSNP:rs17617333). FT /FTId=VAR_050361. FT VARIANT 71 71 S -> N (in allele DMB*01:07; FT dbSNP:rs17617321). FT /FTId=VAR_050362. FT VARIANT 162 162 A -> E (in allele DMB*01:02 and allele FT DMB*01:06; dbSNP:rs2071555). FT /FTId=VAR_016753. FT VARIANT 162 162 A -> V (in allele DMB*01:04 and allele FT DMB*01:05; dbSNP:rs2071555). FT /FTId=VAR_016754. FT VARIANT 197 197 I -> T (in allele DMB*01:03, allele FT DMB*01:04 and allele DMB*01:06; FT dbSNP:rs1042337). FT {ECO:0000269|PubMed:14574404}. FT /FTId=VAR_016755. FT MUTAGEN 248 248 Y->A: Abolishes targeting to endosomes FT and results in relocalization to the cell FT membrane. {ECO:0000269|PubMed:8757605}. FT MUTAGEN 251 251 L->A: Abolishes targeting to endosomes FT and results in relocalization to the cell FT membrane. {ECO:0000269|PubMed:8757605}. FT STRAND 22 32 {ECO:0000244|PDB:2BC4}. FT STRAND 33 35 {ECO:0000244|PDB:4FQX}. FT STRAND 37 46 {ECO:0000244|PDB:2BC4}. FT STRAND 49 55 {ECO:0000244|PDB:2BC4}. FT TURN 56 59 {ECO:0000244|PDB:2BC4}. FT STRAND 60 63 {ECO:0000244|PDB:2BC4}. FT STRAND 67 69 {ECO:0000244|PDB:4I0P}. FT HELIX 70 81 {ECO:0000244|PDB:2BC4}. FT HELIX 84 91 {ECO:0000244|PDB:2BC4}. FT HELIX 93 109 {ECO:0000244|PDB:2BC4}. FT STRAND 116 121 {ECO:0000244|PDB:2BC4}. FT STRAND 128 143 {ECO:0000244|PDB:2BC4}. FT STRAND 146 151 {ECO:0000244|PDB:2BC4}. FT STRAND 154 156 {ECO:0000244|PDB:2BC4}. FT STRAND 170 172 {ECO:0000244|PDB:2BC4}. FT STRAND 174 182 {ECO:0000244|PDB:2BC4}. FT STRAND 190 195 {ECO:0000244|PDB:2BC4}. FT STRAND 199 201 {ECO:0000244|PDB:2BC4}. FT STRAND 203 207 {ECO:0000244|PDB:2BC4}. FT HELIX 212 214 {ECO:0000244|PDB:2BC4}. SQ SEQUENCE 263 AA; 28943 MW; 9B50F6CC22B3A4BA CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN SLANVLSQHL NQKDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPAEVTITWR KNGKLVMPHS SAHKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGVISW RRAGHSSYTP LPGSNYSEGW HIS // ID DMB_MOUSE Reviewed; 261 AA. AC P35737; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 28-FEB-2018, entry version 127. DE RecName: Full=Class II histocompatibility antigen, M beta 1 chain; DE AltName: Full=H2-M beta 1 chain; DE Flags: Precursor; GN Name=H2-DMb1; Synonyms=H-2Mb1, Mb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=BALB/cJ; RX PubMed=1922366; DOI=10.1038/353573a0; RA Cho S., Attaya M., Monaco J.J.; RT "New class II-like genes in the murine MHC."; RL Nature 353:573-576(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/cJ; RX PubMed=8575819; DOI=10.1007/BF00587301; RA Peleraux A., Karlsson L., Chambers J., Peterson P.A.; RT "Genomic organization of a mouse MHC class II region including the H2- RT M and Lmp2 loci."; RL Immunogenetics 43:204-214(1996). RN [3] RP SUBCELLULAR LOCATION. RX PubMed=7584146; DOI=10.1016/1074-7613(95)90127-2; RA Lindstedt R., Liljedahl M., Peleraux A., Peterson P.A., Karlsson L.; RT "The MHC class II molecule H2-M is targeted to an endosomal RT compartment by a tyrosine-based targeting motif."; RL Immunity 3:561-572(1995). CC -!- FUNCTION: Plays a critical role in catalyzing the release of class CC II HLA-associated invariant chain-derived peptides (CLIP) from CC newly synthesized class II HLA molecules and freeing the peptide CC binding site for acquisition of antigenic peptides. CC -!- SUBUNIT: Heterodimer of an alpha chain (DMA) and a beta chain CC (DMB). CC -!- SUBCELLULAR LOCATION: Late endosome membrane CC {ECO:0000269|PubMed:7584146}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:7584146}. Lysosome membrane CC {ECO:0000269|PubMed:7584146}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:7584146}. Note=Localizes to late endocytic CC compartment. Associates with lysosome membranes. CC -!- DOMAIN: The YXXZ (Tyr-Xaa-Xaa-Zaa, where Zaa is a hydrophobic CC residue) motif mediates the targeting to the lysosomal CC compartments. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X62743; CAA44605.1; -; mRNA. DR EMBL; U35323; AAA98931.1; -; Genomic_DNA. DR CCDS; CCDS37581.1; -. DR PIR; S17889; S17889. DR UniGene; Mm.460938; -. DR ProteinModelPortal; P35737; -. DR SMR; P35737; -. DR STRING; 10090.ENSMUSP00000109870; -. DR iPTMnet; P35737; -. DR PhosphoSitePlus; P35737; -. DR PaxDb; P35737; -. DR PRIDE; P35737; -. DR MGI; MGI:95922; H2-DMb1. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR HOGENOM; HOG000231198; -. DR HOVERGEN; HBG007327; -. DR InParanoid; P35737; -. DR PhylomeDB; P35737; -. DR ChiTaRS; Mb; mouse. DR PRO; PR:P35737; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-DMB1; -. DR CleanEx; MM_MB; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042613; C:MHC class II protein complex; ISO:MGI. DR GO; GO:0023026; F:MHC class II protein complex binding; ISO:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:MGI. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Endosome; Glycoprotein; Immunity; KW Lysosome; Membrane; MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 261 Class II histocompatibility antigen, M FT beta 1 chain. FT /FTId=PRO_0000018961. FT TOPO_DOM 19 218 Lumenal. {ECO:0000255}. FT TRANSMEM 219 239 Helical. {ECO:0000255}. FT TOPO_DOM 240 261 Cytoplasmic. {ECO:0000255}. FT DOMAIN 114 204 Ig-like C1-type. FT REGION 19 112 Beta-1. FT REGION 113 207 Beta-2. FT REGION 208 218 Connecting peptide. {ECO:0000255}. FT MOTIF 248 251 YXXZ motif. FT CARBOHYD 75 75 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 29 97 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 135 192 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 261 AA; 28899 MW; 4986A222912286D9 CRC64; MAALWLLLLV LSLHCMGAGG FVAHVESTCV LDDAGTPQDF TYCVSFNKDL LACWDPIVGK IVPCEFGVLY PLAENFSRIL NKEESLLQRL QNGLPDCASH TQPFWNALTH RTRPPSVRVA QTTPFNTREP VMLACYVWGF YPADVTITWM KNGQLVPSHS NKEKTAQPNG DWTYQTVSYL ALTPSYGDVY TCVVQHSGTS EPIRGDWTPG LSPIQTVKVS VSAATLGLGF IIFCVGFFRW RKSHSSSYTP LSGSTYPEGR H // ID DOB_HUMAN Reviewed; 273 AA. AC P13765; B0V0Y0; Q29746; Q29825; Q6FHC2; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 12-SEP-2018, entry version 173. DE RecName: Full=HLA class II histocompatibility antigen, DO beta chain; DE AltName: Full=MHC class II antigen DOB; DE Flags: Precursor; GN Name=HLA-DOB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DOB*01:01). RX PubMed=2998758; RA Tonnelle C., Demars R., Long E.O.; RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of RT expression."; RL EMBO J. 4:2839-2847(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DOB*01:01). RX PubMed=2499532; DOI=10.1007/BF00375872; RA Jonsson A.-K., Rask L.; RT "Human class II DNA and DOB genes display low sequence variability."; RL Immunogenetics 29:411-413(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DOB*01:01). RX PubMed=1453454; DOI=10.1016/0022-2836(92)90832-5; RA Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., RA Trowsdale J.; RT "DNA sequence analysis of 66 kb of the human MHC class II region RT encoding a cluster of genes for antigen processing."; RL J. Mol. Biol. 228:433-441(1992). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-210. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-210. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DOB*01:01). RC TISSUE=B-cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DOB*01:02). RX PubMed=3036827; RA Servenius B., Rask L., Peterson P.A.; RT "Class II genes of the human major histocompatibility complex. The DO RT beta gene is a divergent member of the class II beta gene family."; RL J. Biol. Chem. 262:8759-8766(1987). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DOB*01:03). RX PubMed=8568858; DOI=10.1006/jmbi.1996.0001; RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., RA Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., RA Radley E., Thorpe K.L., Trowsdale J.; RT "Evolutionary dynamics of non-coding sequences within the class II RT region of the human MHC."; RL J. Mol. Biol. 255:1-13(1996). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 32-273 (ALLELE DOB*01:04). RX PubMed=12445321; DOI=10.1034/j.1399-0039.2002.590608.x; RA Naruse T.K., Kawata H., Inoko H., Isshiki G., Yamano K., Hino M., RA Tatsumi N.; RT "The HLA-DOB gene displays limited polymorphism with only one amino RT acid substitution."; RL Tissue Antigens 59:512-519(2002). RN [10] RP REVIEW. RX PubMed=10837054; DOI=10.1146/annurev.immunol.18.1.113; RA Alfonso C., Karlsson L.; RT "Nonclassical MHC class II molecules."; RL Annu. Rev. Immunol. 18:113-142(2000). CC -!- FUNCTION: Important modulator in the HLA class II restricted CC antigen presentation pathway by interaction with the HLA-DM CC molecule in B-cells. Modifies peptide exchange activity of HLA-DM. CC -!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain CC (DOB). Forms a heterotetrameric complex with an HLA-DM molecule CC during intracellular transport in endosomal/lysosomal compartments CC in B-cells. CC -!- SUBCELLULAR LOCATION: Endosome membrane; Single-pass type I CC membrane protein. Lysosome membrane; Single-pass type I membrane CC protein. Note=Complexes with HLA-DM molecule during intracellular CC transport and in endosomal/lysosomal compartments. CC Heterotetramerization is necessary to exit the ER. CC -!- POLYMORPHISM: The following alleles of DOB are known: DOB*01:01, CC DOB*01:02, DOB*01:03 and DOB*01:04. The sequence shown is that of CC DOB*01:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X03066; CAA26870.1; -; mRNA. DR EMBL; M26040; AAA59718.1; -; mRNA. DR EMBL; X66401; CAA47028.1; -; Genomic_DNA. DR EMBL; CR541832; CAG46631.1; -; mRNA. DR EMBL; CR788227; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC006097; AAH06097.1; -; mRNA. DR EMBL; L29472; AAA59717.1; -; Genomic_DNA. DR EMBL; X87344; CAA60789.1; -; Genomic_DNA. DR EMBL; AB035252; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS4754.1; -. DR PIR; S27335; A24669. DR RefSeq; NP_002111.1; NM_002120.3. DR UniGene; Hs.1802; -. DR PDB; 4I0P; X-ray; 3.20 A; D/H=30-218. DR PDBsum; 4I0P; -. DR ProteinModelPortal; P13765; -. DR SMR; P13765; -. DR BioGrid; 109357; 3. DR DIP; DIP-60117N; -. DR IntAct; P13765; 3. DR STRING; 9606.ENSP00000390020; -. DR iPTMnet; P13765; -. DR PhosphoSitePlus; P13765; -. DR BioMuta; HLA-DOB; -. DR DMDM; 122261; -. DR PaxDb; P13765; -. DR PeptideAtlas; P13765; -. DR PRIDE; P13765; -. DR ProteomicsDB; 52985; -. DR DNASU; 3112; -. DR Ensembl; ENST00000426644; ENSP00000395780; ENSG00000243612. DR Ensembl; ENST00000438763; ENSP00000390020; ENSG00000241106. DR Ensembl; ENST00000447178; ENSP00000405108; ENSG00000241386. DR Ensembl; ENST00000454286; ENSP00000397268; ENSG00000243496. DR Ensembl; ENST00000454969; ENSP00000410390; ENSG00000241910. DR Ensembl; ENST00000456406; ENSP00000394783; ENSG00000239457. DR GeneID; 3112; -. DR KEGG; hsa:3112; -. DR UCSC; uc011gkh.2; human. DR CTD; 3112; -. DR DisGeNET; 3112; -. DR EuPathDB; HostDB:ENSG00000241106.6; -. DR GeneCards; HLA-DOB; -. DR H-InvDB; HIX0207728; -. DR H-InvDB; HIX0207758; -. DR HGNC; HGNC:4937; HLA-DOB. DR HPA; HPA013846; -. DR MIM; 142920; gene. DR MIM; 600629; gene. DR neXtProt; NX_P13765; -. DR OpenTargets; ENSG00000241106; -. DR PharmGKB; PA35061; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P13765; -. DR KO; K06752; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG09370LQE; -. DR PhylomeDB; P13765; -. DR TreeFam; TF336626; -. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR SIGNOR; P13765; -. DR ChiTaRS; HLA-DOB; human. DR GeneWiki; HLA-DOB; -. DR GenomeRNAi; 3112; -. DR PRO; PR:P13765; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000241106; Expressed in 84 organ(s), highest expression level in small intestine Peyer's patch. DR CleanEx; HS_HLA-DOB; -. DR ExpressionAtlas; P13765; baseline and differential. DR Genevisible; P13765; HS. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0023026; F:MHC class II protein complex binding; IDA:UniProtKB. DR GO; GO:0032395; F:MHC class II receptor activity; TAS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IDA:UniProtKB. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Endosome; KW Glycoprotein; Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 26 FT CHAIN 27 273 HLA class II histocompatibility antigen, FT DO beta chain. FT /FTId=PRO_0000018963. FT TOPO_DOM 27 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 273 Cytoplasmic. {ECO:0000255}. FT DOMAIN 123 213 Ig-like C1-type. FT REGION 27 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 45 45 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 41 105 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 143 199 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 18 18 R -> Q (in allele DOB*01:02; FT dbSNP:rs2071554). FT /FTId=VAR_016743. FT VARIANT 210 210 V -> I (in dbSNP:rs11575907). FT {ECO:0000269|PubMed:14574404, FT ECO:0000269|Ref.4}. FT /FTId=VAR_050363. FT VARIANT 234 234 L -> F (in allele DOB*01:04; FT dbSNP:rs2070121). FT /FTId=VAR_016745. FT VARIANT 244 244 V -> I (in allele DOB*01:03; FT dbSNP:rs2621330). FT /FTId=VAR_016744. FT STRAND 34 44 {ECO:0000244|PDB:4I0P}. FT TURN 45 48 {ECO:0000244|PDB:4I0P}. FT STRAND 49 58 {ECO:0000244|PDB:4I0P}. FT STRAND 61 67 {ECO:0000244|PDB:4I0P}. FT TURN 68 70 {ECO:0000244|PDB:4I0P}. FT STRAND 72 75 {ECO:0000244|PDB:4I0P}. FT HELIX 78 80 {ECO:0000244|PDB:4I0P}. FT HELIX 81 89 {ECO:0000244|PDB:4I0P}. FT HELIX 91 103 {ECO:0000244|PDB:4I0P}. FT HELIX 105 112 {ECO:0000244|PDB:4I0P}. FT HELIX 113 115 {ECO:0000244|PDB:4I0P}. FT TURN 116 118 {ECO:0000244|PDB:4I0P}. FT STRAND 124 131 {ECO:0000244|PDB:4I0P}. FT STRAND 139 151 {ECO:0000244|PDB:4I0P}. FT STRAND 154 159 {ECO:0000244|PDB:4I0P}. FT STRAND 166 169 {ECO:0000244|PDB:4I0P}. FT STRAND 177 179 {ECO:0000244|PDB:4I0P}. FT STRAND 181 189 {ECO:0000244|PDB:4I0P}. FT STRAND 197 202 {ECO:0000244|PDB:4I0P}. FT STRAND 210 214 {ECO:0000244|PDB:4I0P}. SQ SEQUENCE 273 AA; 30822 MW; C06A1360DCC4AD26 CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSRQA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIKWFLN GQEERAGVMS TGPIRNGDWT FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWRKMLSGIA AFLLGLIFLL VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QSC // ID DOB_PANTR Reviewed; 273 AA. AC P18467; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 23-MAY-2018, entry version 106. DE RecName: Full=Patr class II histocompatibility antigen, DO beta chain; DE AltName: Full=ChLa class II histocompatibility antigen, DO beta chain; DE AltName: Full=MHC class II antigen DOB; DE Flags: Precursor; GN Name=Patr-DOB; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2744808; DOI=10.1007/BF02421475; RA Kasahara M., Klein D., Klein J.; RT "Nucleotide sequence of a chimpanzee DOB cDNA clone."; RL Immunogenetics 30:66-68(1989). CC -!- FUNCTION: Important modulator in the HLA class II restricted CC antigen presentation pathway by interaction with the HLA-DM CC molecule in B-cells. Modifies peptide exchange activity of HLA-DM. CC -!- SUBUNIT: Heterodimer of an alpha chain (DOA) and a beta chain CC (DOB). Forms a heterotetrameric complex with an HLA-DM molecule CC during intracellular transport in endosomal/lysosomal compartments CC in B-cells. CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Single-pass CC type I membrane protein {ECO:0000250}. Lysosome membrane CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. CC Note=Complexes with HLA-DM molecule during intracellular transport CC and in endosomal/lysosomal compartments. Heterotetramerization is CC necessary to exit the ER. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M24358; AAA35409.1; -; mRNA. DR PIR; A45879; A45879. DR RefSeq; NP_001123943.1; NM_001130471.1. DR UniGene; Ptr.6214; -. DR ProteinModelPortal; P18467; -. DR SMR; P18467; -. DR STRING; 9598.ENSPTRP00000030772; -. DR PaxDb; P18467; -. DR PRIDE; P18467; -. DR GeneID; 471977; -. DR KEGG; ptr:471977; -. DR CTD; 471977; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR InParanoid; P18467; -. DR KO; K06752; -. DR Proteomes; UP000002277; Unplaced. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Endosome; Glycoprotein; Immunity; KW Lysosome; Membrane; MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 26 FT CHAIN 27 273 Patr class II histocompatibility antigen, FT DO beta chain. FT /FTId=PRO_0000018964. FT TOPO_DOM 27 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 273 Cytoplasmic. {ECO:0000255}. FT DOMAIN 123 213 Ig-like C1-type. FT REGION 27 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 45 45 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 41 105 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 143 199 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 273 AA; 30922 MW; 8AC0A1F56A06D30D CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSRQA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERARVMS TGPIRNGDWT FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWKKMLSGIA AFLLGLIFLL VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QSC // ID DPB1_HUMAN Reviewed; 258 AA. AC P04440; A0PFJ7; A5I886; A8YPB3; B5U8B4; B7VF80; B7VF87; B8ZX68; AC B8ZYT0; B9W5S8; B9W6F7; B9W6F9; C0MPP5; C0MPQ2; C0MPQ3; C0MPQ5; AC C0MPQ6; C0MPQ7; C4R9J5; C5IZL1; O00259; O19698; O19700; O19702; AC O19749; O46884; O77952; O98215; O98216; O98217; O98218; O98219; AC O98222; O98223; P01916; P04232; P13763; P79493; P79608; Q0P0L4; AC Q0ZFN3; Q14279; Q27S71; Q29682; Q29684; Q29698; Q29714; Q29775; AC Q29776; Q29778; Q29779; Q29781; Q29827; Q29828; Q29879; Q29880; AC Q29898; Q29977; Q2MGW3; Q30015; Q30031; Q30032; Q30033; Q30034; AC Q30050; Q30051; Q30052; Q30053; Q30054; Q30055; Q30174; Q4GY31; AC Q4JHD8; Q5ENE0; Q5ENE1; Q5ENW3; Q5EP46; Q5EP47; Q5EP49; Q5EP51; AC Q5EP52; Q5EP53; Q5EP56; Q5I4H8; Q5I4H9; Q5ISH4; Q5ISH5; Q5SQ73; AC Q5STP2; Q5YLA6; Q6IVX1; Q6LBX2; Q6LBX3; Q6LBX4; Q6LBX5; Q6LBX6; AC Q6LBX7; Q6PWX6; Q6TAS4; Q714U1; Q714U2; Q7YQ10; Q860Z7; Q8HWL7; AC Q8HWT5; Q8SNC4; Q95HC1; Q95IT7; Q95IT8; Q9BD13; Q9GIM2; Q9GIM4; AC Q9GIX6; Q9GJ41; Q9MY67; Q9TNT7; Q9TQE2; Q9XS11; Q9XS12; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 12-SEP-2018, entry version 170. DE RecName: Full=HLA class II histocompatibility antigen, DP beta 1 chain; DE AltName: Full=HLA class II histocompatibility antigen, DP(W4) beta chain; DE AltName: Full=MHC class II antigen DPB1; DE Flags: Precursor; GN Name=HLA-DPB1; Synonyms=HLA-DP1B; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DPB1*02:01), AND NUCLEOTIDE RP SEQUENCE [GENOMIC DNA] (ALLELES DPB1*03:01 AND DPB1*04:01). RX PubMed=6098459; RA Kappes D.J., Arnot D., Okada K., Strominger J.L.; RT "Structure and polymorphism of the HLA class II SB light chain RT genes."; RL EMBO J. 3:2985-2993(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DPB1*02:01). RX PubMed=2998758; RA Tonnelle C., Demars R., Long E.O.; RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of RT expression."; RL EMBO J. 4:2839-2847(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DPB1*04:01). RX PubMed=2987832; DOI=10.1093/nar/13.5.1607; RA Kelly A., Trowsdale J.; RT "Complete nucleotide sequence of a functional HLA-DP beta gene and the RT region between the DP beta 1 and DP alpha 1 genes: comparison of the RT 5' ends of HLA class II genes."; RL Nucleic Acids Res. 13:1607-1621(1985). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DPB1*04:01). RX PubMed=3036829; RA Gustafsson K., Widmark E., Jonsson A.-K., Servenius B., Sachs D.H., RA Larhammar D., Rask L., Peterson P.A.; RT "Class II genes of the human major histocompatibility complex. RT Evolution of the DP region as deduced from nucleotide sequences of the RT four genes."; RL J. Biol. Chem. 262:8778-8786(1987). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DPB1*04:01). RX PubMed=2838415; DOI=10.1016/0888-7543(88)90103-6; RA Compagnone-Post P., Turco E., Robinson C., Trucco M.; RT "The beta-chains of DP4 molecules from different haplotypes are RT encoded by the same gene."; RL Genomics 2:8-13(1988). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DPB1*01:01). RX PubMed=1529429; DOI=10.1111/j.1399-0039.1992.tb01938.x; RA Korioth F., Hartung K., Deicher H., Frey J.; RT "A new HLA-DPB1 allele from a patient with systemic lupus RT erythematosus."; RL Tissue Antigens 39:216-219(1992). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DPB1*01:01; DPB1*02:02; RP DPB1*04:01; DPB1*04:02; DPB1*05:01; DPB1*05:02; DPB1*06:02; RP DPB1*08:02; DPB1*09:01; DPB1*09:02; DPB1*13:01; DPB1*15:01 AND RP DPB1*19:01). RX PubMed=16189666; DOI=10.1007/s00251-005-0043-8; RA Reinders J., Rozemuller E.H., van Gent R., Arts-Hilkes Y.H., RA van den Tweel J.G., Tilanus M.G.J.; RT "Extended HLA-DPB1 polymorphism: an RNA approach for HLA-DPB1 RT typing."; RL Immunogenetics 57:790-794(2005). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DPB1*02:02; DPB1*05:01 AND RP DPB1*13:01). RA Lee E., Kim E., Kwack K.; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DPB1*04:01). RC TISSUE=Spleen; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DPB1*01:01). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DPB1*02:02; RP DPB1*03:01; DPB1*04:01 AND DPB1*04:02). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DPB1*04:01). RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DPB1*01:01 AND RP DPB1*04:01). RC TISSUE=B-cell, and Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-258 (ALLELE DPB1*04:01). RX PubMed=2714855; DOI=10.1007/BF00352845; RA Lee J.S., Sartoris S., Briata P., Choi E., Cullen C., Lepaslier D., RA Yunis I.; RT "Sequence polymorphism of HLA-DP beta chains."; RL Immunogenetics 29:346-349(1989). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-114 (ALLELE DPB1*75:01). RA Louie L., Ginther C., Francisco A.M., van der Zwan A.W., RA Katongole-Mbidde E., Tilanus M.G.J., Klitz W.; RT "HLA and mtDNA variation among the Baganda in Uganda."; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-122 (ALLELE DPB1*56:01). RX PubMed=7638863; DOI=10.1111/j.1399-0039.1995.tb02450.x; RA Rani R., Fernandez-Vina M.A., Zhang S., Stastny P.; RT "HLA-DPB1 alleles in a population from north India and description of RT a new variant (DPB1*5601)."; RL Tissue Antigens 45:264-269(1995). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-121 (ALLELE DPB1*39:01). RX PubMed=1481203; DOI=10.1111/j.1399-0039.1992.tb02055.x; RA Hessner M.J., Baxter-Lowe L.A.; RT "Characterization of novel HLA-DPB1 alleles by oligotyping and RT nucleotide sequencing."; RL Tissue Antigens 40:261-263(1992). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-121 (ALLELE DPB1*67:01). RX PubMed=8896187; DOI=10.1111/j.1399-0039.1996.tb02637.x; RA Meyer C.G., May J., Simon C., Bohm B.O., Loeliger C.C.; RT "DPB1*TF, a novel HLA class II DPB1 allele (DPB1*6701) identified in a RT Turkish family."; RL Tissue Antigens 48:231-232(1996). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-121 (DPB1*77:01 AND RP DPB1*78:01). RX PubMed=9756410; DOI=10.1111/j.1399-0039.1998.tb02285.x; RA Voorter C., Richeldi L., Gervais T., van den Berg-Loonen E.; RT "Identification of two new DPB1 alleles, DPB1*7701 and *7801, by RT sequence-based typing."; RL Tissue Antigens 52:190-192(1998). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-121 (ALLELE DPB1*79:01). RX PubMed=9756411; DOI=10.1111/j.1399-0039.1998.tb02286.x; RA Voorter C., Chatelain B., Sintnicolaas K., Tilanus M.G.J., Hidajat M., RA van den Berg-Loonen E.; RT "Identification of a new DPB1 allele (DPB1*7901) by sequence-based RT typing."; RL Tissue Antigens 52:193-195(1998). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-121 (ALLELE DPB1*04:03). RX PubMed=16147881; DOI=10.1080/10425170500061442; RA Weston A., Ensey J.S., Frye B.L.; RT "DNA-sequence determination of exon 2 of a novel HLA-DPB1 allele, HLA- RT DPB1*0403."; RL DNA Seq. 16:235-236(2005). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-121 (ALLELE DPB1*98:01). RC TISSUE=Blood; RA Cox S.T., Wallis-Jones S.; RT "Two new HLA DP alleles."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-121 (ALLELE DPB1*20:02), AND RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*14:02). RA Cox S.T.; RT "Sequence of DPB1*0301 allele, and sequence of HLA-DPB1*66new."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-121 (ALLELE DPB1*21:02). RA Casanova A.A.; RT "Sequence of DPB1*0101 variant."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-119 (ALLELES DPB1*30:01; RP DPB1*32:01; DPB1*33:01; DPB1*34:01 AND DPB1*35:01), AND NUCLEOTIDE RP SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*27:01). RX PubMed=1440570; DOI=10.1111/j.1399-0039.1992.tb02109.x; RA Moonsamy P.V., Suraj V.C., Bugawan T.L., Saiki R.K., Stoneking M., RA Roudier J., Magzoub M.M., Hill A.V., Begovich A.B.; RT "Genetic diversity within the HLA class II region: ten new DPB1 RT alleles and their population distribution."; RL Tissue Antigens 40:153-157(1992). RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-119 (ALLELE DPB1*58:01). RX PubMed=7806296; DOI=10.1007/BF00182337; RA Versluis L.F., van der Zwan A.W., Tilanus M.G.J., Daly L.N., RA Degli-Eposti M.A., Dawkins R.L.; RT "Identification of the novel HLA-DPB1*5801 allele detected by RT sequenced based typing."; RL Immunogenetics 41:173-173(1995). RN [27] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-119 (ALLELES DPB1*60:01 AND RP DPB1*62:01). RX PubMed=8773318; DOI=10.1111/j.1399-0039.1996.tb02556.x; RA Zimmerman P.A., Steiner L.L., Titanji V.P., Nde P.N., Bradley J.E., RA Pogonka T., Begovich A.B.; RT "Three new DPB1 alleles identified in a Bantu-speaking population from RT central Cameroon."; RL Tissue Antigens 47:293-299(1996). RN [28] RP NUCLEOTIDE SEQUENCE [MRNA] OF 35-258, AND VARIANTS LEU-94; VAL-105; RP ASP-113; GLU-114; ALA-115; VAL-116; LYS-125 AND ILE-199. RX PubMed=6330724; DOI=10.1073/pnas.81.13.3934; RA Gorski J., Rollini P., Long E., Mach B.; RT "Molecular organization of the HLA-SB region of the human major RT histocompatibility complex and evidence for two SB beta-chain genes."; RL Proc. Natl. Acad. Sci. U.S.A. 81:3934-3938(1984). RN [29] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-215 (ALLELE DPB1*24:02). RX PubMed=19775376; DOI=10.1111/j.1399-0039.2009.01325.x; RA Witter K., Kirchner E., Borelli C., Messer G., Albert T., Zahn R., RA Kauke T.; RT "In a study for acne vulgaris, sequence-based HLA typing showed a RT novel DPB1 allele, DPB1*2402."; RL Tissue Antigens 74:354-356(2009). RN [30] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-215 (ALLELES DPB1*06:01; RP DPB1*16:01; DPB1*17:01; DPB1*18:01; DPB1*20:01; DPB1*23:01; RP DPB1*26:01; DPB1*26:02; DPB1*28:01; DPB1*45:01; DPB1*55:01; DPB1*85:01 RP AND DPB1*88:01). RA Witter K., Tran H., Sabine S.; RT "Confirmation of several HLA-DPB1 alleles including exon 3."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*04:01). RX PubMed=2460556; RA Bugawan T.L., Horn G.T., Long C.M., Mickelson E., Hansen J.A., RA Ferrara G.B., Angelini G., Erlich H.A.; RT "Analysis of HLA-DP allelic sequence polymorphism using the in vitro RT enzymatic DNA amplification of DP-alpha and DP-beta loci."; RL J. Immunol. 141:4024-4030(1988). RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*04:01), AND RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-121 (ALLELE DPB1*08:01). RX PubMed=2242906; DOI=10.1007/BF00187094; RA Bugawan T.L., Begovich A.B., Erlich H.A.; RT "Rapid HLA-DPB typing using enzymatically amplified DNA and RT nonradioactive sequence-specific oligonucleotide probes."; RL Immunogenetics 32:231-241(1990). RN [33] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*46:01). RC TISSUE=Leukocyte; RX PubMed=8344726; DOI=10.1007/BF00210483; RA Buyse I., Emonds M.P., Bouillon R., Marynen P., Cassiman J.J.; RT "Novel class II HLA-DRB4 and DPB1 alleles found in the Belgian RT population."; RL Immunogenetics 38:380-380(1993). RN [34] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*41:01). RX PubMed=7901923; DOI=10.1111/j.1399-0039.1993.tb02016.x; RA Mizuki N., Ohno S., Sugimura K., Seki T., Ishioka M., Inoko H., RA Geng L.; RT "Identification of a new HLA-DPB1 allele detected by PCR-RFLP and its RT nucleotide sequence determination by direct sequencing after PCR RT amplification."; RL Tissue Antigens 41:259-262(1993). RN [35] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*47:01). RC TISSUE=Blood; RX PubMed=7912859; DOI=10.1111/j.1399-0039.1994.tb02297.x; RA Koshizaka T., Taguchi M., Onishi H., Kobayashi S., Inoko H.; RT "A new HLA-DPB1 allele, DPB1*SUT (DPB1*4701)."; RL Tissue Antigens 43:50-53(1994). RN [36] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*51:01). RC TISSUE=Blood; RX PubMed=7839356; DOI=10.1111/j.1399-0039.1994.tb02382.x; RA Kaneshige T., Kinoshita T., Hashimoto M., Matsumoto Y., Moribe T., RA Ichikawa Y., Fukunishi T., Uchida K.; RT "Direct sequencing of a novel DPB1 allele (DPB1*5101) of the RT heterozygote from the membrane of reverse dot blot analysis."; RL Tissue Antigens 44:204-207(1994). RN [37] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*66:01). RC TISSUE=Blood; RX PubMed=8781129; DOI=10.1007/BF02602788; RA Schnittger L., May J., Kretschmer C., Kremsner P.G., Meyer C.G.; RT "DPB1*BR: an Mhc class II DPB1 allele (DPB1*6601) of negroid origin."; RL Immunogenetics 44:405-406(1996). RN [38] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*65:01). RX PubMed=8824162; DOI=10.1007/BF02602812; RA Versluis L.F., Philippe M., Van der Zwan A., Thonnard J., Tongio M.M., RA Tilanus M.G.J.; RT "Identification of a new HLA-DPB1*6501 allele in a Caucasian RT individual."; RL Immunogenetics 44:483-484(1996). RN [39] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELES DPB1*82:01 AND RP DPB1*83:01). RX PubMed=11169249; DOI=10.1034/j.1399-0039.2000.560613.x; RA Voorter C., Tilanus M.G.J., van den Berg-Loonen E.; RT "Two new HLA DPB1 alleles identified by sequence-based typing: RT DPB1*8201 and DPB1*8301."; RL Tissue Antigens 56:560-562(2000). RN [40] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*86:01). RX PubMed=11556983; DOI=10.1034/j.1399-0039.2001.057006536.x; RA Bengtsson M.; RT "DPB1*8601, a previously unrecognized DPB1 variant in the Caucasoid RT population."; RL Tissue Antigens 57:536-539(2001). RN [41] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*87:01). RX PubMed=11782281; DOI=10.1034/j.1399-0039.2001.580410.x; RA Grams S.E., Wu J., Noreen H.J., Mangaccat J., Cognato M.A., RA Johnson S., Segall M., Williams T.M., Begovich A.B.; RT "Three new DP alleles identified in a study of 800 unrelated bone RT marrow donor-recipient pairs."; RL Tissue Antigens 58:272-275(2001). RN [42] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*90:01). RX PubMed=12135440; DOI=10.1034/j.1399-0039.2002.590419.x; RA Bengtsson M., Danielsson F., Jansson I.E., Johansson U.; RT "Identification of a new HLA-DPB1 allele,HLA-DPB1*9001."; RL Tissue Antigens 59:344-346(2002). RN [43] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*93:01). RX PubMed=12694578; DOI=10.1046/j.0001-2815.2002.00143.x; RA Liu Z.-H., Fan X., Lin J., Fu Y., Liu X., Xu A.; RT "Identification of a novel DPB1 allele, DPB1*9301, by sequence-based RT typing in a Lahu ethnic minority of China."; RL Tissue Antigens 61:261-262(2003). RN [44] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELES DPB1*94:01 AND RP DPB1*95:01). RX PubMed=12890000; DOI=10.1034/j.1399-0039.2003.00066.x; RA Luo M., Ramdahin S., Iqbal S., Pan Y., Jacobson K., Narayansingh M.J., RA Schroeder M., Brunham R.C., Embree J., Plummer F.A.; RT "High resolution sequence-based DPB1 typing identified two novel DPB1 RT alleles, DPB1*9401 and DPB1*9501, from a Kenyan population."; RL Tissue Antigens 62:182-184(2003). RN [45] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (DPB1*96:01). RX PubMed=12890001; DOI=10.1034/j.1399-0039.2003.00081.x; RA Witter K., Gervais T., Dunn P.P., Voorter C., Muramoto J., RA Albert E.D.; RT "Sequence-based typing identifies a novel HLA-DPB1 allele, RT DPB1*9601."; RL Tissue Antigens 62:185-187(2003). RN [46] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*01:02). RX PubMed=15361132; DOI=10.1111/j.1399-0039.2004.00276.x; RA Lv F., Lin J., Liu Z.-H., Gao J., Fu Y., Xu A.; RT "Identification of a novel HLA-DPB1 allele--DPB1*0102."; RL Tissue Antigens 64:512-514(2004). RN [47] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*17:02). RC TISSUE=Blood; RX PubMed=16866899; DOI=10.1111/j.1399-0039.2006.00630.x; RA Li M., Nie J., Xu Y., Xu A., Yu X.; RT "Identification of a novel HLA-DPB1 allele, DPB1*1702."; RL Tissue Antigens 68:187-188(2006). RN [48] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELES DPB1*21:01; RP DPB1*22:01; DPB1*24:01; DPB1*25:01; DPB1*29:01 AND DPB1*31:01). RA Kimura A.; RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases. RN [49] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*89:01). RA Dormoy A., Routoulp M., Froelich N., Tongio M.M.; RT "A new HLA-DPB1* allele identical to the DPB1*0101 allele except for RT the polymorphic positions 226 and 228 where G and A are found RT respectively in place of A and G."; RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases. RN [50] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELES DPB1*91:01 AND RP DPB1*92:01). RA Varney M.D., Rossi V.; RT "A novel DPB1 allele."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [51] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*10:01). RA Luo M., Mao X., Shehzad I., Jacobson K., Kwan L., Shroeder M., RA Plummer F.A.; RT "Sequence-based DPB typing fills the missing exon 2 sequences of RT multiple HLA-DPB1 alleles."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [52] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*99:01). RA Edelshtein D., Sidebottom D., Chen D.-F., Baxter-Lowe L.A.; RT "A novel DPB1 allele identified by sequence-based typing and Confirmed RT by SSP."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [53] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*02:03). RA Wu J., Williams T.M., Cognato M.A.; RT "Novel human HLA-DPB1 allele identified in potential bone marrow RT donors."; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [54] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELES DPB1*10:02 AND RP DPB1*11:02). RA Garbarino L., Chiesa A., Pastori F., Sacchi N., Cusano R., Bottero F., RA Bossi R.; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [55] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*13:02). RA Moonsamy P.V., Bonella P.L., Sali P.J., Bentley L.G., Post J.L., RA Goodwin G., Erlich H.E.; RT "The identification of a new DPB1 allele in a type 1 diabetes genetics RT consortium family."; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [56] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*16:02). RA Kashiwase K., Ichihara T., Shimizu M., Satake M.; RT "HLA-DPB1*8601V1."; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [57] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*18:02). RA Cordovado S.K., Hancock L.N., Mueller P.W.; RT "Identification of a novel DPB1 allele by sequence-based typing in the RT GoKinD population."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. RN [58] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*19:02). RA Monos D.S.; RT "A New HLA-DPB1 allele."; RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases. RN [59] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*11:01). RC TISSUE=Peripheral blood; RA Vilches C.; RT "Complete exon 2 sequence of the HLA-DPB1*110101 allele."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [60] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*22:02). RC TISSUE=Peripheral blood; RA McWhinnie A.J.M., Wallis-Jones S., Little A.M.; RT "Exon 2 sequence of a new HLA-DPB1 allele DPB1*XX exhibiting single RT nucleotide difference G337A from HLA-DPB1*1401."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [61] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DPB1*25:02). RA Lazaro A.M., Xiao Y., Nehlsen-Cannarella S.L., Fagoaga O.R., RA Hurley C.K.; RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases. RN [62] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELES DPB1*40:01; RP DPB1*48:01; DPB1*49:01; DPB1*50:01; DPB1*51:01; DPB1*52:01 AND RP DPB1*53:01). RX PubMed=8085260; DOI=10.1111/j.1399-0039.1994.tb02333.x; RA Moonsamy P.V., Aldrich C.L., Petersdorf E.W., Hill A.V., RA Begovich A.B.; RT "Seven new DPB1 alleles and their population distribution."; RL Tissue Antigens 43:249-252(1994). RN [63] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELES DPB1*59:01; RP DPB1*68:01; DPB1*70:01; DPB1*71:01; DPB1*72:01 AND DPB1*73:01). RX PubMed=9174146; DOI=10.1111/j.1399-0039.1997.tb02788.x; RA Noreen H.J., Steiner L.L., Davidson M., Johnson S., Segall M., RA Begovich A.B.; RT "Six new DPB1 alleles identified in a study of 1,302 unrelated bone RT marrow donor-recipient pairs."; RL Tissue Antigens 49:512-516(1997). RN [64] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DPB1*80:01), AND RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-117 (ALLELE DPB1*81:01). RX PubMed=10090623; DOI=10.1034/j.1399-0039.1999.530213.x; RA Steiner L.L., Wu J., Noreen H.J., Moehlenkamp C., Cavalli A.S., RA Davidson M., Johnson S., Winden T., Segall M., Begovich A.B., RA Williams T.M.; RT "Four new DP alleles identified in a study of 500 unrelated bone RT marrow donor-recipient pairs."; RL Tissue Antigens 53:201-206(1999). RN [65] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DPB1*97:01). RX PubMed=15140044; DOI=10.1111/j.0001-2815.2004.00198.x; RA Lapi S., Curcio M., Fornaciari S., Mariotti M.L., Isola P., Bonci F., RA Pistello M., Scatena F.; RT "Identification of a novel HLA-DPB1 allele, DPB1*9701, by sequence- RT based typing."; RL Tissue Antigens 63:606-608(2004). RN [66] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DPB1*63:01). RA Begovich A.B., Steiner L.L.; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [67] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DPB1*76:01). RA Rozemuller E.H.; RT "A new HLA-DPB1 allele: a variant of DPB1*1401."; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [68] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DPB1*44:01). RX PubMed=7744621; DOI=10.1016/0198-8859(94)00100-5; RA Versluis L.F., Tilanus M.G.J., Verduyn W., Abdulkadir J., RA Giphart M.J.; RT "Novel HLA-DPB1 alleles detected in the Ethiopian population."; RL Hum. Immunol. 42:181-183(1995). RN [69] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-118 (ALLELE DPB1*59:01). RX PubMed=8851734; DOI=10.1111/j.1399-0039.1996.tb02533.x; RA Noble J.A., Cavalli A.S., Erlich H.A.; RT "DPB1*5901a: a novel HLA-DPB1 allele from a Caucasian family with RT insulin-dependent diabetes mellitus."; RL Tissue Antigens 47:159-162(1996). RN [70] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-118 (ALLELE DPB1*03:02). RX PubMed=15982263; DOI=10.1111/j.1399-0039.2005.00429.x; RA Sheldon M.H., Azzaro M.P., Sayer D., Bunce M., Sortino G.; RT "Identification of a new allele in a Sicilian individual: HLA- RT DPB1*0302."; RL Tissue Antigens 66:64-66(2005). RN [71] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-117 (ALLELE DPB1*69:01). RA Varney M.D., Tait B.D.; RT "Identification of a novel DPB allele."; RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases. RN [72] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-114 (ALLELE DPB1*44:01). RC TISSUE=Blood; RA Easteal S., Croft L.; RT "A new HLA-DPB1 alleles from Santa Cruz Island, Solomon Islands."; RL Submitted (MAR-1993) to the EMBL/GenBank/DDBJ databases. RN [73] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-121 (ALLELE DPB1*37:01). RX PubMed=1412421; DOI=10.1111/j.1399-0039.1992.tb01966.x; RA Meyer C.G., Schnittger L., Begovich A.B., Erlich H.A., Horstmann R.D.; RT "DPB1*WA4 - an additional HLA class II allele identified in west RT Africa."; RL Tissue Antigens 40:98-99(1992). RN [74] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-119 (ALLELE DPB1*38:01). RX PubMed=1358867; DOI=10.1016/0198-8859(92)90113-2; RA Mitsunaga S., Kuwata S., Tokunaga K., Uchikawa C., Takahashi K., RA Akaza T., Mitomi Y., Juji T.; RT "Family study on HLA-DPB1 polymorphism: linkage analysis with HLA- RT DR/DQ and two 'new' alleles."; RL Hum. Immunol. 34:203-211(1992). RN [75] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-119 (ALLELE DPB1*36:01). RX PubMed=7817379; DOI=10.1111/j.1399-0039.1994.tb02370.x; RA Ogawa K., Itho H., Nakajyo S., Kobayashi K., Sekiguchi S., RA Koshizaka T., Taguchi M., Onishi H., Kobayashi S., Inoko H.; RT "A novel HLA-DPB1 allele, DPB1*3601 (DPB1*KT)."; RL Tissue Antigens 44:134-136(1994). RN [76] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-119 (ALLELE DPB1*74:01). RX PubMed=9694359; DOI=10.1111/j.1399-0039.1998.tb03009.x; RA Steiner L.L., Cavalli A., Zimmerman P.A., Boatin B.A., Titanji V.P., RA Bradley J.E., Lucius R., Nutman T.B., Begovich A.B.; RT "Three new DP alleles identified in sub-Saharan Africa: DPB1*7401, RT DPA1*02013, and DPA1*0302."; RL Tissue Antigens 51:653-657(1998). RN [77] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-115 (ALLELE DPB1*57:01). RC TISSUE=Lymphocyte; RX PubMed=8525482; DOI=10.1111/j.1399-0039.1995.tb03122.x; RA Mersch G., Mytilineos J., De Canck I., Deufel A., Mijs W., Scherer S., RA Jannes G., Opelz G., Rossau R.; RT "Characterization of a new DPB1 allele (DPB1*5701) isolated from a RT Caucasian individual."; RL Tissue Antigens 46:208-212(1995). RN [78] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-121 (ALLELE DPB1*84:01). RX PubMed=10958363; DOI=10.1034/j.1399-0039.2000.560114.x; RA McTernan C.L., Mijovic C.H., Cockram C.S., Barnett A.H.; RT "The nucleotide sequence of two new DP alleles, DPA1*02015 and RT DPB1*8401, identified in a Chinese subject."; RL Tissue Antigens 56:95-98(2000). RN [79] RP NUCLEOTIDE SEQUENCE [MRNA] OF 78-258 (ALLELE DPB1*02:01). RX PubMed=6310612; DOI=10.1073/pnas.80.19.6036; RA Roux-Dosseto M., Auffray C., Lillie J.W., Boss J.M., Cohen D., RA Demars R., Mawas C., Seidman J.G., Strominger J.L.; RT "Genetic mapping of a human class II antigen beta-chain cDNA clone to RT the SB region of the HLA complex."; RL Proc. Natl. Acad. Sci. U.S.A. 80:6036-6040(1983). RN [80] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [81] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [82] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [83] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [84] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [85] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Note=The MHC class II complex transits through CC a number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- POLYMORPHISM: The following alleles of HLA-DPB1 are known: CC DPB1*01:01, DPB1*01:02, DPB1*02:01, DPB1*02:02, DPB1*02:03, CC DPB1*03:01, DPB1*03:02, DPB1*04:01, DPB1*04:02, DPB1*04:03, CC DPB1*05:01, DPB1*05:02, DPB1*06:01, DPB1*06:02, DPB1*08:01, CC DPB1*08:02, DPB1*09:01, DPB1*09:02, DPB1*10:01, DPB1*10:02, CC DPB1*11:01, DPB1*11:02, DPB1*13:01, DPB1*13:02, DPB1*14:01, CC DPB1*14:02, DPB1*15:01, DPB1*15:02, DPB1*16:01, DPB1*16:02, CC DPB1*17:01, DPB1*17:02, DPB1*18:01, DPB1*18:02, DPB1*19:01, CC DPB1*19:02, DPB1*20:01, DPB1*20:02, DPB1*21:01, DPB1*21:02, CC DPB1*22:01, DPB1*22:02, DPB1*23:01, DPB1*24:01, DPB1*24:02, CC DPB1*25:01, DPB1*25:02, DPB1*26:01, DPB1*26:02, DPB1*27:01, CC DPB1*28:01, DPB1*29:01, DPB1*30:01, DPB1*31:01, DPB1*32:01, CC DPB1*33:01, DPB1*34:01, DPB1*35:01, DPB1*36:01, DPB1*37:01, CC DPB1*38:01, DPB1*39:01, DPB1*40:01, DPB1*41:01, DPB1*44:01, CC DPB1*45:01, DPB1*46:01, DPB1*47:01, DPB1*48:01, DPB1*49:01, CC DPB1*50:01, DPB1*51:01, DPB1*52:01, DPB1*53:01, DPB1*54:01, CC DPB1*55:01, DPB1*56:01, DPB1*57:01, DPB1*58:01, DPB1*59:01, CC DPB1*60:01, DPB1*62:01, DPB1*63:01, DPB1*65:01, DPB1*66:01, CC DPB1*67:01, DPB1*68:01, DPB1*69:01, DPB1*70:01, DPB1*71:01, CC DPB1*72:01, DPB1*73:01, DPB1*74:01, DPB1*75:01, DPB1*76:01, CC DPB1*77:01, DPB1*78:01, DPB1*79:01, DPB1*80:01, DPB1*81:01, CC DPB1*82:01, DPB1*83:01, DPB1*84:01, DPB1*85:01, DPB1*86:01, CC DPB1*87:01, DPB1*88:01, DPB1*89:01, DPB1*90:01, DPB1*91:01, CC DPB1*92:01, DPB1*93:01, DPB1*94:01, DPB1*95:01, DPB1*96:01, CC DPB1*97:01, DPB1*98:01 and DPB1*99:01. The sequence shown is that CC of DPB1*04:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAQ12564.1; Type=Frameshift; Positions=39; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X01426; CAA25672.1; -; mRNA. DR EMBL; X02964; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X03023; CAE82008.1; -; Genomic_DNA. DR EMBL; X03024; CAE82007.1; -; Genomic_DNA. DR EMBL; X03022; CAA26823.1; -; Genomic_DNA. DR EMBL; X03025; CAE82037.1; -; Genomic_DNA. DR EMBL; X03026; CAE82042.1; -; Genomic_DNA. DR EMBL; X03028; CAE82073.1; -; Genomic_DNA. DR EMBL; X03027; CAE82043.1; -; Genomic_DNA. DR EMBL; X03067; CAA26871.1; -; mRNA. DR EMBL; X02228; CAA26147.1; -; Genomic_DNA. DR EMBL; J03041; AAA35993.1; -; mRNA. DR EMBL; M83664; AAA59837.1; -; mRNA. DR EMBL; AY804132; AAW78737.1; -; mRNA. DR EMBL; AY804133; AAW78738.1; -; mRNA. DR EMBL; AY804135; AAW78740.1; -; mRNA. DR EMBL; AY804136; AAW78741.1; -; mRNA. DR EMBL; AY804137; AAW78742.1; -; mRNA. DR EMBL; AY804138; AAW78743.1; -; mRNA. DR EMBL; AY804139; AAW78744.1; -; mRNA. DR EMBL; AY804141; AAW78746.1; -; mRNA. DR EMBL; AY804142; AAW78747.1; -; mRNA. DR EMBL; AY804143; AAW78748.1; -; mRNA. DR EMBL; AY831401; AAW80919.1; -; mRNA. DR EMBL; AY831402; AAW80920.1; -; mRNA. DR EMBL; AY831403; AAW80921.1; -; mRNA. DR EMBL; AY831404; AAW80922.1; -; mRNA. DR EMBL; AY656678; AAV71025.1; -; mRNA. DR EMBL; AY656679; AAV71026.1; -; mRNA. DR EMBL; AY656680; AAV71027.1; -; mRNA. DR EMBL; AK313305; BAG36110.1; -; mRNA. DR EMBL; BT019780; AAV38583.1; -; mRNA. DR EMBL; AL645931; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL662824; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL805913; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL845446; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX120009; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759904; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR762479; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03674.1; -; Genomic_DNA. DR EMBL; BC007963; AAH07963.1; -; mRNA. DR EMBL; BC013184; AAH13184.1; -; mRNA. DR EMBL; M28202; AAA53197.1; -; mRNA. DR EMBL; Y09327; CAA70507.1; -; Genomic_DNA. DR EMBL; L31816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M97686; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X96985; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Y13900; CAA74199.1; -; Genomic_DNA. DR EMBL; Y14230; CAA74608.1; -; Genomic_DNA. DR EMBL; Y16095; CAA76060.1; -; Genomic_DNA. DR EMBL; AY823995; AAW79272.1; -; Genomic_DNA. DR EMBL; AJ563603; CAD91639.1; -; Genomic_DNA. DR EMBL; AM039828; CAJ01690.1; -; Genomic_DNA. DR EMBL; AM408787; CAL64063.1; -; Genomic_DNA. DR EMBL; AM698036; CAM91695.1; -; Genomic_DNA. DR EMBL; M84619; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M84620; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M84622; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M84623; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M84624; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M84626; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X82123; CAA57635.1; -; Genomic_DNA. DR EMBL; U22311; AAB60413.1; -; Genomic_DNA. DR EMBL; U22313; AAB17108.1; -; Genomic_DNA. DR EMBL; K01615; AAA36313.1; -; mRNA. DR EMBL; FM883600; CAT04585.2; -; Genomic_DNA. DR EMBL; FM882212; CAT03206.1; -; Genomic_DNA. DR EMBL; FM956650; CAX11690.1; -; Genomic_DNA. DR EMBL; FM991729; CAX20314.1; -; Genomic_DNA. DR EMBL; FM992080; CAX21583.2; -; Genomic_DNA. DR EMBL; FM992366; CAX30407.1; -; Genomic_DNA. DR EMBL; FM992364; CAX30405.1; -; Genomic_DNA. DR EMBL; FN252853; CAX53275.1; -; Genomic_DNA. DR EMBL; FN256250; CAX53717.1; -; Genomic_DNA. DR EMBL; FN256251; CAX53721.1; -; Genomic_DNA. DR EMBL; FN256254; CAX53718.1; -; Genomic_DNA. DR EMBL; FN256253; CAX53726.1; -; Genomic_DNA. DR EMBL; FN256255; CAX53722.1; -; Genomic_DNA. DR EMBL; FN393829; CAY85528.1; -; Genomic_DNA. DR EMBL; M23675; AAA59740.1; -; Genomic_DNA. DR EMBL; M62326; AAA59719.1; -; Genomic_DNA. DR EMBL; M62331; AAA59724.1; -; Genomic_DNA. DR EMBL; L07768; AAA59690.1; -; Genomic_DNA. DR EMBL; D13174; BAA02465.1; -; Genomic_DNA. DR EMBL; D10834; BAA01614.1; -; Genomic_DNA. DR EMBL; D28809; BAA05970.1; -; Genomic_DNA. DR EMBL; X96986; CAA65710.2; -; Genomic_DNA. DR EMBL; X91886; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Y18498; CAC12860.1; -; Genomic_DNA. DR EMBL; AJ238005; CAC12865.1; -; Genomic_DNA. DR EMBL; AJ271373; CAB70605.2; -; Genomic_DNA. DR EMBL; AF288354; AAG30143.1; -; Genomic_DNA. DR EMBL; AJ292074; CAC27995.1; -; Genomic_DNA. DR EMBL; AF536241; AAN33050.1; -; Genomic_DNA. DR EMBL; AF549409; AAQ12563.1; -; Genomic_DNA. DR EMBL; AF549410; AAQ12564.1; ALT_FRAME; Genomic_DNA. DR EMBL; AJ514871; CAD55852.1; -; Genomic_DNA. DR EMBL; AY374100; AAR21105.1; -; Genomic_DNA. DR EMBL; DQ206450; ABB17974.1; -; Genomic_DNA. DR EMBL; M83914; AAA36264.1; -; Genomic_DNA. DR EMBL; M83915; AAA36259.1; -; Genomic_DNA. DR EMBL; M83916; AAA36260.1; -; Genomic_DNA. DR EMBL; M83917; AAA36261.1; -; Genomic_DNA. DR EMBL; M83918; AAA36262.1; -; Genomic_DNA. DR EMBL; M83919; AAA36263.1; -; Genomic_DNA. DR EMBL; AJ297820; CAC14048.1; -; Genomic_DNA. DR EMBL; AY029777; AAK40344.1; -; Genomic_DNA. DR EMBL; AF489518; AAL92172.1; -; Genomic_DNA. DR EMBL; AF492640; AAO84765.1; -; Genomic_DNA. DR EMBL; AY425707; AAR29060.1; -; Genomic_DNA. DR EMBL; AY572830; AAS77869.1; -; Genomic_DNA. DR EMBL; AY855160; AAW33682.1; -; Genomic_DNA. DR EMBL; AY855161; AAW33683.1; -; Genomic_DNA. DR EMBL; DQ089022; AAY98352.1; -; Genomic_DNA. DR EMBL; AB247517; BAE78492.1; -; Genomic_DNA. DR EMBL; DQ386161; ABD36812.1; -; Genomic_DNA. DR EMBL; DQ485789; ABF47047.1; -; Genomic_DNA. DR EMBL; AM887530; CAP08783.1; -; Genomic_DNA. DR EMBL; FM211032; CAR66500.1; -; Genomic_DNA. DR EMBL; FJ976693; ACS12738.1; -; Genomic_DNA. DR EMBL; L17310; AAA53479.1; -; Genomic_DNA. DR EMBL; L17311; AAA53480.1; -; Genomic_DNA. DR EMBL; L17313; AAA53481.1; -; Genomic_DNA. DR EMBL; L17314; AAA53482.1; -; Genomic_DNA. DR EMBL; L22076; AAA53476.1; -; Genomic_DNA. DR EMBL; L22077; AAA53477.1; -; Genomic_DNA. DR EMBL; L23400; AAA58441.1; -; Genomic_DNA. DR EMBL; U59437; AAD09481.1; -; Genomic_DNA. DR EMBL; U59438; AAD09482.1; -; Genomic_DNA. DR EMBL; U59439; AAD09483.1; -; Genomic_DNA. DR EMBL; U59440; AAD09484.1; -; Genomic_DNA. DR EMBL; U59441; AAD09485.1; -; Genomic_DNA. DR EMBL; U59442; AAD09486.1; -; Genomic_DNA. DR EMBL; AF074845; AAD39682.1; -; Genomic_DNA. DR EMBL; AF074846; AAD39683.1; -; Genomic_DNA. DR EMBL; AY033075; AAK51161.1; -; Genomic_DNA. DR EMBL; U34033; AAA81335.1; -; Genomic_DNA. DR EMBL; Z92523; CAB06822.1; -; Genomic_DNA. DR EMBL; X78042; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U29534; AAB52511.1; -; Genomic_DNA. DR EMBL; AY618897; AAT40308.1; -; Genomic_DNA. DR EMBL; X97406; CAA66059.1; -; Genomic_DNA. DR EMBL; L01466; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M87046; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; D10478; BAA01281.1; -; Genomic_DNA. DR EMBL; D10882; BAA01704.1; -; Genomic_DNA. DR EMBL; U94839; AAC64232.1; -; Genomic_DNA. DR EMBL; X80752; CAA56728.1; -; Genomic_DNA. DR EMBL; AF077015; AAC26835.1; -; Genomic_DNA. DR EMBL; K00409; AAA36312.1; -; mRNA. DR CCDS; CCDS4765.1; -. DR PIR; A02228; HLHUS1. DR PIR; A02229; HLHUPB. DR PIR; D30536; D30536. DR PIR; D30537; D30537. DR PIR; E30536; E30536. DR PIR; I37298; I37298. DR PIR; I37541; S49382. DR PIR; I38195; HLHUS2. DR PIR; I38197; I38197. DR PIR; I59621; I59621. DR PIR; I59637; I59637. DR PIR; I59641; I59641. DR PIR; I81234; I81234. DR PIR; I81235; I81235. DR PIR; I81236; I81236. DR PIR; I81237; I81237. DR PIR; I81238; I81238. DR RefSeq; NP_002112.3; NM_002121.5. DR UniGene; Hs.485130; -. DR PDB; 3LQZ; X-ray; 3.25 A; B=33-218. DR PDB; 4P4K; X-ray; 2.80 A; B/F=32-218. DR PDB; 4P4R; X-ray; 3.00 A; B/D=32-218. DR PDB; 4P57; X-ray; 2.60 A; B/D=33-218. DR PDB; 4P5K; X-ray; 2.59 A; B/E=33-218. DR PDB; 4P5M; X-ray; 1.70 A; B/D/F/H=33-218. DR PDBsum; 3LQZ; -. DR PDBsum; 4P4K; -. DR PDBsum; 4P4R; -. DR PDBsum; 4P57; -. DR PDBsum; 4P5K; -. DR PDBsum; 4P5M; -. DR ProteinModelPortal; P04440; -. DR SMR; P04440; -. DR BioGrid; 109360; 40. DR IntAct; P04440; 10. DR MINT; P04440; -. DR STRING; 9606.ENSP00000408146; -. DR iPTMnet; P04440; -. DR PhosphoSitePlus; P04440; -. DR SwissPalm; P04440; -. DR BioMuta; HLA-DPB1; -. DR DMDM; 122263; -. DR MaxQB; P04440; -. DR PaxDb; P04440; -. DR PeptideAtlas; P04440; -. DR PRIDE; P04440; -. DR ProteomicsDB; 51715; -. DR DNASU; 3115; -. DR Ensembl; ENST00000399500; ENSP00000382422; ENSG00000215048. DR Ensembl; ENST00000411749; ENSP00000414196; ENSG00000236693. DR Ensembl; ENST00000418931; ENSP00000408146; ENSG00000223865. DR Ensembl; ENST00000425130; ENSP00000396095; ENSG00000230763. DR Ensembl; ENST00000433800; ENSP00000407674; ENSG00000226826. DR Ensembl; ENST00000454006; ENSP00000389288; ENSG00000237710. DR GeneID; 3115; -. DR KEGG; hsa:3115; -. DR UCSC; uc003ocu.3; human. DR CTD; 3115; -. DR DisGeNET; 3115; -. DR EuPathDB; HostDB:ENSG00000223865.10; -. DR GeneCards; HLA-DPB1; -. DR HGNC; HGNC:4940; HLA-DPB1. DR HPA; HPA011078; -. DR HPA; HPA058509; -. DR MalaCards; HLA-DPB1; -. DR MIM; 142858; gene. DR neXtProt; NX_P04440; -. DR OpenTargets; ENSG00000223865; -. DR Orphanet; 133; Chronic berylliosis. DR Orphanet; 900; Granulomatosis with polyangiitis. DR PharmGKB; PA35064; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P04440; -. DR KO; K06752; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR PhylomeDB; P04440; -. DR TreeFam; TF336626; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SIGNOR; P04440; -. DR ChiTaRS; HLA-DPB1; human. DR EvolutionaryTrace; P04440; -. DR GeneWiki; HLA-DPB1; -. DR GenomeRNAi; 3115; -. DR PRO; PR:P04440; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000223865; Expressed in 112 organ(s), highest expression level in lung. DR CleanEx; HS_HLA-DPB1; -. DR ExpressionAtlas; P04440; baseline and differential. DR Genevisible; P04440; HS. DR GO; GO:0009986; C:cell surface; IMP:UniProtKB. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; IDA:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IMP:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB. DR GO; GO:0050870; P:positive regulation of T cell activation; IMP:UniProtKB. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:UniProtKB. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 29 FT CHAIN 30 258 HLA class II histocompatibility antigen, FT DP beta 1 chain. FT /FTId=PRO_0000018984. FT TOPO_DOM 30 225 Extracellular. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TOPO_DOM 247 258 Cytoplasmic. {ECO:0000255}. FT DOMAIN 124 212 Ig-like C1-type. FT REGION 30 121 Beta-1. FT REGION 122 215 Beta-2. FT REGION 216 225 Connecting peptide. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 144 200 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VARIANT 16 16 T -> M (in allele DPB1*09:02; FT dbSNP:rs41558014). FT /FTId=VAR_060627. FT VARIANT 24 24 T -> I (in dbSNP:rs11551416). FT /FTId=VAR_060628. FT VARIANT 30 30 R -> P (in allele DPB1*75:01). FT /FTId=VAR_060629. FT VARIANT 31 31 A -> L (in allele DPB1*75:01; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060630. FT VARIANT 32 32 T -> P (in allele DPB1*75:01). FT /FTId=VAR_060631. FT VARIANT 33 33 P -> A (in allele DPB1*75:01). FT /FTId=VAR_060632. FT VARIANT 37 37 L -> V (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*05:02, allele FT DPB1*06:01, allele DPB1*09:01, allele FT DPB1*09:02, allele DPB1*10:01, allele FT DPB1*11:01, allele DPB1*11:02, allele FT DPB1*13:01, allele DPB1*13:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*15:01, allele DPB1*16:02, allele FT DPB1*17:01, allele DPB1*17:02, allele FT DPB1*18:01, allele DPB1*20:02, allele FT DPB1*21:01, allele DPB1*21:02, allele FT DPB1*20:01, allele DPB1*22:02, allele FT DPB1*25:01, allele DPB1*25:02, allele FT DPB1*26:01, allele DPB1*27:01, allele FT DPB1*29:01, allele DPB1*30:01, allele FT DPB1*35:01, allele DPB1*36:01, allele FT DPB1*37:01, allele DPB1*44:01, allele FT DPB1*45:01, allele DPB1*50:01, allele FT DPB1*52:01, allele DPB1*54:01, allele FT DPB1*55:01, allele DPB1*56:01, allele FT DPB1*58:01, allele DPB1*66:01, allele FT DPB1*67:01, allele DPB1*69:01, allele FT DPB1*70:01, allele DPB1*74:01, allele FT DPB1*76:01, allele DPB1*78:01, allele FT DPB1*79:01, allele DPB1*85:01, allele FT DPB1*86:01, allele DPB1*87:01, allele FT DPB1*88:01, allele DPB1*89:01, allele FT DPB1*90:01, allele DPB1*91:01, allele FT DPB1*92:01, allele DPB1*93:01 and allele FT DPB1*98:01; dbSNP:rs1126504). FT /FTId=VAR_060633. FT VARIANT 38 38 F -> D (in allele DPB1*70:01; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060635. FT VARIANT 38 38 F -> H (in allele DPB1*09:01, allele FT DPB1*10:01, allele DPB1*14:01, allele FT DPB1*16:02, allele DPB1*17:01, allele FT DPB1*22:02, allele DPB1*30:01, allele FT DPB1*35:01, allele DPB1*45:01, allele FT DPB1*54:01, allele DPB1*55:01, allele FT DPB1*58:01, allele DPB1*66:01, allele FT DPB1*67:01, allele DPB1*76:01, allele FT DPB1*86:01, allele DPB1*91:01 and allele FT DPB1*98:01; requires 2 nucleotide FT substitutions). FT /FTId=VAR_060634. FT VARIANT 38 38 F -> L (in dbSNP:rs12722013). FT /FTId=VAR_060636. FT VARIANT 38 38 F -> Y (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*05:02, allele FT DPB1*06:01, allele DPB1*09:02, allele FT DPB1*11:01, allele DPB1*11:02, allele FT DPB1*13:01, allele DPB1*13:02, allele FT DPB1*14:02, allele DPB1*15:01, allele FT DPB1*17:02, allele DPB1*18:01, allele FT DPB1*20:02, allele DPB1*21:01, allele FT DPB1*21:02, allele DPB1*20:01, allele FT DPB1*25:01, allele DPB1*25:02, allele FT DPB1*26:01, allele DPB1*27:01, allele FT DPB1*29:01, allele DPB1*36:01, allele FT DPB1*37:01, allele DPB1*44:01, allele FT DPB1*50:01, allele DPB1*52:01, allele FT DPB1*56:01, allele DPB1*69:01, allele FT DPB1*74:01, allele DPB1*78:01, allele FT DPB1*79:01, allele DPB1*85:01, allele FT DPB1*87:01, allele DPB1*88:01, allele FT DPB1*89:01, allele DPB1*90:01, allele FT DPB1*92:01 and allele DPB1*93:01; FT dbSNP:rs1126509). FT /FTId=VAR_033433. FT VARIANT 40 40 G -> L (in allele DPB1*03:01, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*09:01, allele DPB1*09:02, allele FT DPB1*10:01, allele DPB1*11:01, allele FT DPB1*11:02, allele DPB1*13:01, allele FT DPB1*13:02, allele DPB1*14:01, allele FT DPB1*14:02, allele DPB1*16:02, allele FT DPB1*17:01, allele DPB1*17:02, allele FT DPB1*20:02, allele DPB1*21:01, allele FT DPB1*20:01, allele DPB1*22:02, allele FT DPB1*25:01, allele DPB1*26:01, allele FT DPB1*27:01, allele DPB1*29:01, allele FT DPB1*30:01, allele DPB1*35:01, allele FT DPB1*36:01, allele DPB1*37:01, allele FT DPB1*44:01, allele DPB1*45:01, allele FT DPB1*52:01, allele DPB1*54:01, allele FT DPB1*55:01, allele DPB1*56:01, allele FT DPB1*58:01, allele DPB1*66:01, allele FT DPB1*67:01, allele DPB1*69:01, allele FT DPB1*70:01, allele DPB1*74:01, allele FT DPB1*76:01, allele DPB1*78:01, allele FT DPB1*79:01, allele DPB1*85:01, allele FT DPB1*86:01, allele DPB1*87:01, allele FT DPB1*88:01, allele DPB1*91:01, allele FT DPB1*92:01, allele DPB1*93:01 and allele FT DPB1*98:01; requires 2 nucleotide FT substitutions; dbSNP:rs386699869). FT /FTId=VAR_060637. FT VARIANT 40 40 G -> V (in dbSNP:rs1126513). FT /FTId=VAR_033434. FT VARIANT 41 41 R -> L (in allele DPB1*77:01; FT dbSNP:rs41540313). FT /FTId=VAR_060638. FT VARIANT 44 44 C -> G (in allele DPB1*26:02). FT /FTId=VAR_060639. FT VARIANT 46 46 A -> P (in allele DPB1*38:01; FT dbSNP:rs41555313). FT /FTId=VAR_060640. FT VARIANT 46 46 A -> T (in allele DPB1*18:02; FT dbSNP:rs41555313). FT /FTId=VAR_060641. FT VARIANT 57 57 Y -> D (in allele DPB1*99:01; FT dbSNP:rs41553416). FT /FTId=VAR_060642. FT VARIANT 61 61 R -> P (in allele DPB1*14:02 and allele FT DPB1*21:02; dbSNP:rs41561114). FT /FTId=VAR_060643. FT VARIANT 62 62 E -> Q (ind allele DPB1*11:01, allele FT DPB1*15:01 and allele DPB1*74:01; FT dbSNP:rs12722018). FT /FTId=VAR_033435. FT VARIANT 64 64 F -> L (in allele DPB1*02:02, allele FT DPB1*02:03, allele DPB1*05:01, allele FT DPB1*15:02, allele DPB1*17:02, allele FT DPB1*19:02, allele DPB1*21:01, allele FT DPB1*21:01, allele DPB1*22:01, allele FT DPB1*34:01, allele DPB1*36:01, allele FT DPB1*38:01, allele DPB1*44:01, allele FT DPB1*48:01, allele DPB1*58:01, allele FT DPB1*62:01, allele DPB1*63:01, allele FT DPB1*95:01 and allele DPB1*97:01; FT dbSNP:rs9277348). FT /FTId=VAR_060644. FT VARIANT 64 64 F -> Y (in allele DPB1*01:01, allele FT DPB1*01:02, allele DPB1*09:02, allele FT DPB1*11:01, allele DPB1*13:01, allele FT DPB1*15:01, allele DPB1*20:02, allele FT DPB1*21:02, allele DPB1*25:02, allele FT DPB1*26:01, allele DPB1*27:01, allele FT DPB1*39:01, allele DPB1*40:01, allele FT DPB1*49:01, allele DPB1*53:01, allele FT DPB1*65:01, allele DPB1*74:01, allele FT DPB1*85:01, allele DPB1*89:01 and allele FT DPB1*96:01; dbSNP:rs1042117). FT /FTId=VAR_033436. FT VARIANT 65 65 A -> V (in allele DPB1*01:02, allele FT DPB1*02:01, allele DPB1*02:02, allele FT DPB1*02:03, allele DPB1*03:01, allele FT DPB1*04:02, allele DPB1*04:03, allele FT DPB1*05:01, allele DPB1*05:02, allele FT DPB1*06:01, allele DPB1*06:02, allele FT DPB1*08:01, allele DPB1*08:02, allele FT DPB1*09:01, allele DPB1*10:01, allele FT DPB1*10:02, allele DPB1*11:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*15:02, allele DPB1*16:01, allele FT DPB1*16:02, allele DPB1*17:01, allele FT DPB1*17:02, allele DPB1*18:01, allele FT DPB1*18:02, allele DPB1*19:01, allele FT DPB1*19:02, allele DPB1*21:01, allele FT DPB1*20:01, allele DPB1*22:01, allele FT DPB1*22:02, allele DPB1*23:01, allele FT DPB1*25:01, allele DPB1*26:02, allele FT DPB1*29:01, allele DPB1*30:01, allele FT DPB1*32:01, allele DPB1*34:01, allele FT DPB1*35:01, allele DPB1*36:01, allele FT DPB1*37:01, allele DPB1*38:01, allele FT DPB1*41:01, allele DPB1*44:01, allele FT DPB1*45:01, allele DPB1*46:01, allele FT DPB1*47:01, allele DPB1*48:01, allele FT DPB1*50:01, allele DPB1*52:01, allele FT DPB1*54:01, allele DPB1*55:01, allele FT DPB1*57:01, allele DPB1*58:01, allele FT DPB1*59:01, allele DPB1*60:01, allele FT DPB1*62:01, allele DPB1*63:01, allele FT DPB1*67:01, allele DPB1*68:01, allele FT DPB1*69:01, allele DPB1*70:01, allele FT DPB1*71:01, allele DPB1*73:01, allele FT DPB1*75:01, allele DPB1*77:01, allele FT DPB1*78:01, allele DPB1*79:01, allele FT DPB1*80:01, allele DPB1*82:01, allele FT DPB1*83:01, allele DPB1*84:01, allele FT DPB1*86:01, allele DPB1*87:01, allele FT DPB1*88:01, allele DPB1*91:01, allele FT DPB1*93:01, allele DPB1*94:01, allele FT DPB1*95:01, allele DPB1*97:01 and allele FT DPB1*98:01; dbSNP:rs1042121). FT /FTId=VAR_033437. FT VARIANT 68 68 D -> Y (in allele DPB1*24:02; FT dbSNP:rs77062860). FT /FTId=VAR_060645. FT VARIANT 72 72 G -> W (in allele DPB1*97:01; FT dbSNP:rs41552915). FT /FTId=VAR_060646. FT VARIANT 84 84 A -> D (in allele DPB1*02:01, allele FT DPB1*03:01, allele DPB1*04:02, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*06:02, allele DPB1*08:01, allele FT DPB1*09:01, allele DPB1*10:01, allele FT DPB1*10:02, allele DPB1*11:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*16:01, allele DPB1*16:02, allele FT DPB1*17:01, allele DPB1*18:01, allele FT DPB1*18:01, allele DPB1*18:02, allele FT DPB1*19:02, allele DPB1*20:01, allele FT DPB1*22:02, allele DPB1*25:01, allele FT DPB1*25:02, allele DPB1*26:02, allele FT DPB1*28:01, allele DPB1*29:01, allele FT DPB1*32:01, allele DPB1*35:01, allele FT DPB1*37:01, allele DPB1*41:01, allele FT DPB1*44:01, allele DPB1*45:01, allele FT DPB1*46:01, allele DPB1*48:01, allele FT DPB1*49:01, allele DPB1*50:01, allele FT DPB1*51:01, allele DPB1*53:01, allele FT DPB1*57:01, allele DPB1*59:01, allele FT DPB1*60:01, allele DPB1*68:01, allele FT DPB1*69:01, allele DPB1*70:01, allele FT DPB1*73:01, allele DPB1*75:01, allele FT DPB1*76:01, allele DPB1*77:01, allele FT DPB1*78:01, allele DPB1*79:01, allele FT DPB1*80:01, allele DPB1*81:01, allele FT DPB1*82:01, allele DPB1*83:01, allele FT DPB1*86:01, allele DPB1*88:01, allele FT DPB1*91:01, allele DPB1*92:01, allele FT DPB1*93:01, allele DPB1*94:01 and allele FT DPB1*98:01; dbSNP:rs707958). FT /FTId=VAR_054662. FT VARIANT 84 84 A -> E (in allele DPB1*01:02, allele FT DPB1*02:02, allele DPB1*02:03, allele FT DPB1*05:01, allele DPB1*08:02, allele FT DPB1*17:02, allele DPB1*19:01, allele FT DPB1*21:01, allele DPB1*22:01, allele FT DPB1*24:01, allele DPB1*30:01, allele FT DPB1*36:01, allele DPB1*38:01, allele FT DPB1*47:01, allele DPB1*54:01, allele FT DPB1*84:01 and allele DPB1*97:01; FT dbSNP:rs386699870). FT /FTId=VAR_060647. FT VARIANT 84 84 A -> V (in dbSNP:rs707958). FT /FTId=VAR_059511. FT VARIANT 85 85 A -> E (in allele DPB1*02:01, allele FT DPB1*03:01, allele DPB1*04:02, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*06:02, allele DPB1*08:01, allele FT DPB1*09:01, allele DPB1*10:01, allele FT DPB1*10:02, allele DPB1*11:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*16:01, allele DPB1*16:02, allele FT DPB1*17:01, allele DPB1*18:01, allele FT DPB1*18:02, allele DPB1*19:02, allele FT DPB1*20:01, allele DPB1*22:02, allele FT DPB1*25:01, allele DPB1*25:02, allele FT DPB1*26:02, allele DPB1*28:01, allele FT DPB1*29:01, allele DPB1*32:01, allele FT DPB1*35:01, allele DPB1*37:01, allele FT DPB1*41:01, allele DPB1*44:01, allele FT DPB1*45:01, allele DPB1*46:01, allele FT DPB1*48:01, allele DPB1*49:01, allele FT DPB1*50:01, allele DPB1*51:01, allele FT DPB1*53:01, allele DPB1*57:01, allele FT DPB1*59:01, allele DPB1*60:01, allele FT DPB1*68:01, allele DPB1*69:01, allele FT DPB1*70:01, allele DPB1*73:01, allele FT DPB1*75:01, allele DPB1*76:01, allele FT DPB1*77:01, allele DPB1*78:01, allele FT DPB1*79:01, allele DPB1*80:01, allele FT DPB1*81:01, allele DPB1*82:01, allele FT DPB1*83:01, allele DPB1*84:01, allele FT DPB1*86:01, allele DPB1*88:01, allele FT DPB1*91:01, allele DPB1*92:01, allele FT DPB1*93:01, allele DPB1*94:01 and allele FT DPB1*98:01; dbSNP:rs1042131). FT /FTId=VAR_033438. FT VARIANT 86 86 E -> D (in allele DPB1*03:01, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*09:01, allele DPB1*10:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*17:01, allele DPB1*20:01, allele FT DPB1*22:02, allele DPB1*29:01, allele FT DPB1*35:01, allele DPB1*44:01, allele FT DPB1*46:01, allele DPB1*50:01, allele FT DPB1*57:01, allele DPB1*69:01, allele FT DPB1*70:01, allele DPB1*76:01, allele FT DPB1*78:01, allele DPB1*80:01, allele FT DPB1*86:01, allele DPB1*88:01, allele FT DPB1*91:01, allele DPB1*92:01 and allele FT DPB1*98:01; dbSNP:rs1042133). FT /FTId=VAR_033439. FT VARIANT 86 86 E -> V (in allele DPB1*32:01; FT dbSNP:rs41545212). FT /FTId=VAR_060648. FT VARIANT 89 89 N -> H (in allele DPB1*02:03; FT dbSNP:rs41550319). FT /FTId=VAR_060649. FT VARIANT 93 93 D -> H (in allele DPB1*96:01; FT dbSNP:rs41560812). FT /FTId=VAR_060650. FT VARIANT 94 94 I -> F (allele DPB1*41:01 and allele FT DPB1*83:01; dbSNP:rs1042136). FT /FTId=VAR_059512. FT VARIANT 94 94 I -> L (in allele DPB1*03:01, allele FT DPB1*03:02, allele DPB1*05:02, allele FT DPB1*06:01, allele DPB1*10:02, allele FT DPB1*11:01, allele DPB1*14:01, allele FT DPB1*14:02, allele DPB1*15:01, allele FT DPB1*17:02, allele DPB1*20:01, allele FT DPB1*22:02, allele DPB1*25:01, allele FT DPB1*28:01, allele DPB1*29:01, allele FT DPB1*31:01, allele DPB1*34:01, allele FT DPB1*44:01, allele DPB1*45:01, allele FT DPB1*50:01, allele DPB1*52:01, allele FT DPB1*56:01, allele DPB1*57:01, allele FT DPB1*59:01, allele DPB1*67:01, allele FT DPB1*69:01, allele DPB1*70:01, allele FT DPB1*72:01, allele DPB1*73:01, allele FT DPB1*74:01, allele DPB1*76:01, allele FT DPB1*78:01, allele DPB1*87:01, allele FT DPB1*91:01, allele DPB1*92:01 and allele FT DPB1*95:01; dbSNP:rs1042136). FT {ECO:0000269|PubMed:6330724}. FT /FTId=VAR_059513. FT VARIANT 94 94 I -> N (in allele DPB1*60:01; FT dbSNP:rs41547212). FT /FTId=VAR_060651. FT VARIANT 98 98 K -> E (in allele DPB1*02:01, allele FT DPB1*02:02, allele DPB1*02:03, allele FT DPB1*04:03, allele DPB1*06:01, allele FT DPB1*08:01, allele DPB1*08:02, allele FT DPB1*09:01, allele DPB1*09:02, allele FT DPB1*10:01, allele DPB1*11:02, allele FT DPB1*13:01, allele DPB1*13:02, allele FT DPB1*16:01, allele DPB1*16:02, allele FT DPB1*17:01, allele DPB1*18:02, allele FT DPB1*19:01, allele DPB1*20:02, allele FT DPB1*21:01, allele DPB1*22:01, allele FT DPB1*26:02, allele DPB1*29:01, allele FT DPB1*30:01, allele DPB1*32:01, allele FT DPB1*33:01, allele DPB1*37:01, allele FT DPB1*41:01, allele DPB1*44:01, allele FT DPB1*46:01, allele DPB1*47:01, allele FT DPB1*48:01, allele DPB1*54:01, allele FT DPB1*55:01, allele DPB1*58:01, allele FT DPB1*71:01, allele DPB1*81:01, allele FT DPB1*86:01, allele DPB1*88:01, allele FT DPB1*93:01 and allele DPB1*95:01; FT dbSNP:rs1042140). FT /FTId=VAR_033440. FT VARIANT 98 98 K -> R (in allele DPB1*11:01, allele FT DPB1*15:01, allele DPB1*69:01 and allele FT DPB1*74:01; dbSNP:rs12722027). FT /FTId=VAR_033441. FT VARIANT 99 99 R -> W (in allele DPB1*94:01; FT dbSNP:rs41554314). FT /FTId=VAR_060652. FT VARIANT 101 101 V -> L (in allele DPB1*31:01 and allele FT DPB1*34:01; dbSNP:rs41546618). FT /FTId=VAR_060653. FT VARIANT 102 102 P -> L (in allele DPB1*78:01; FT dbSNP:rs41551920). FT /FTId=VAR_060654. FT VARIANT 105 105 M -> I (in allele DPB1*08:02, allele FT DPB1*09:02, allele DPB1*13:01, allele FT DPB1*13:02 and allele DPB1*19:01; FT dbSNP:rs1042153). FT /FTId=VAR_033443. FT VARIANT 105 105 M -> V (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*05:02, allele FT DPB1*08:01, allele DPB1*09:01, allele FT DPB1*10:01, allele DPB1*14:01, allele FT DPB1*14:02, allele DPB1*17:02, allele FT DPB1*21:02, allele DPB1*22:02, allele FT DPB1*25:01, allele DPB1*25:02, allele FT DPB1*26:01, allele DPB1*29:01, allele FT DPB1*35:01, allele DPB1*37:01, allele FT DPB1*44:01, allele DPB1*45:01, allele FT DPB1*50:01, allele DPB1*52:01, allele FT DPB1*54:01, allele DPB1*56:01, allele FT DPB1*57:01, allele DPB1*65:01, allele FT DPB1*67:01, allele DPB1*68:01, allele FT DPB1*70:01, allele DPB1*73:01, allele FT DPB1*75:01, allele DPB1*76:01, allele FT DPB1*78:01, allele DPB1*79:01, allele FT DPB1*84:01, allele DPB1*88:01, allele FT DPB1*90:01 and allele DPB1*92:01; FT dbSNP:rs1042151). FT {ECO:0000269|PubMed:6330724}. FT /FTId=VAR_033442. FT VARIANT 113 113 G -> D (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*03:02, allele FT DPB1*04:03, allele DPB1*05:01, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*08:01, allele DPB1*08:02, allele FT DPB1*09:01, allele DPB1*09:02, allele FT DPB1*10:01, allele DPB1*11:01, allele FT DPB1*11:01, allele DPB1*13:01, allele FT DPB1*13:02, allele DPB1*13:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*16:01, allele DPB1*17:01, allele FT DPB1*17:02, allele DPB1*19:01, allele FT DPB1*21:01, allele DPB1*21:01, allele FT DPB1*21:02, allele DPB1*21:02, allele FT DPB1*20:01, allele DPB1*22:01, allele FT DPB1*25:01, allele DPB1*25:02, allele FT DPB1*26:01, allele DPB1*27:01, allele FT DPB1*29:01, allele DPB1*30:01, allele FT DPB1*31:01, allele DPB1*35:01, allele FT DPB1*36:01, allele DPB1*37:01, allele FT DPB1*38:01, allele DPB1*44:01, allele FT DPB1*45:01, allele DPB1*50:01, allele FT DPB1*52:01, allele DPB1*54:01, allele FT DPB1*55:01, allele DPB1*56:01, allele FT DPB1*57:01, allele DPB1*58:01, allele FT DPB1*63:01, allele DPB1*65:01, allele FT DPB1*67:01, allele DPB1*68:01, allele FT DPB1*69:01, allele DPB1*70:01, allele FT DPB1*76:01, allele DPB1*78:01, allele FT DPB1*79:01, allele DPB1*84:01, allele FT DPB1*85:01, allele DPB1*87:01, allele FT DPB1*88:01, allele DPB1*89:01, allele FT DPB1*90:01, allele DPB1*91:01, allele FT DPB1*92:01, allele DPB1*93:01, allele FT DPB1*97:01 and allele DPB1*98:01; FT dbSNP:rs1042169). FT {ECO:0000269|PubMed:6330724}. FT /FTId=VAR_060657. FT VARIANT 113 113 G -> N (in allele DPB1*22:02; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060655. FT VARIANT 113 113 G -> V (in allele DPB1*15:01, allele FT DPB1*18:01, allele DPB1*28:01, allele FT DPB1*34:01, allele DPB1*40:01, allele FT DPB1*53:01, allele DPB1*62:01 and allele FT DPB1*74:01; dbSNP:rs1042169). FT /FTId=VAR_060656. FT VARIANT 114 114 G -> E (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*03:02, allele FT DPB1*04:03, allele DPB1*05:01, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*08:01, allele DPB1*08:02, allele FT DPB1*09:01, allele DPB1*09:02, allele FT DPB1*10:01, allele DPB1*11:01, allele FT DPB1*13:01, allele DPB1*13:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*16:01, allele DPB1*17:01, allele FT DPB1*17:02, allele DPB1*19:01, allele FT DPB1*21:01, allele DPB1*21:02, allele FT DPB1*20:01, allele DPB1*22:01, allele FT DPB1*22:02, allele DPB1*25:01, allele FT DPB1*25:02, allele DPB1*26:01, allele FT DPB1*27:01, allele DPB1*29:01, allele FT DPB1*30:01, allele DPB1*31:01, allele FT DPB1*35:01, allele DPB1*36:01, allele FT DPB1*37:01, allele DPB1*38:01, allele FT DPB1*44:01, allele DPB1*45:01, allele FT DPB1*50:01, allele DPB1*52:01, allele FT DPB1*54:01, allele DPB1*55:01, allele FT DPB1*56:01, allele DPB1*57:01, allele FT DPB1*58:01, allele DPB1*63:01, allele FT DPB1*65:01, allele DPB1*67:01, allele FT DPB1*68:01, allele DPB1*69:01, allele FT DPB1*70:01, allele DPB1*76:01, allele FT DPB1*78:01, allele DPB1*79:01, allele FT DPB1*84:01, allele DPB1*85:01, allele FT DPB1*87:01, allele DPB1*88:01, allele FT DPB1*89:01, allele DPB1*90:01, allele FT DPB1*91:01, allele DPB1*92:01, allele FT DPB1*93:01, allele DPB1*97:01 and allele FT DPB1*98:01; dbSNP:rs9277354). FT {ECO:0000269|PubMed:6330724}. FT /FTId=VAR_033444. FT VARIANT 115 115 P -> A (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*03:02, allele FT DPB1*04:03, allele DPB1*05:01, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*08:01, allele DPB1*08:02, allele FT DPB1*09:01, allele DPB1*09:02, allele FT DPB1*10:01, allele DPB1*11:01, allele FT DPB1*13:01, allele DPB1*13:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*16:01, allele DPB1*17:01, allele FT DPB1*17:02, allele DPB1*19:01, allele FT DPB1*21:01, allele DPB1*21:02, allele FT DPB1*20:01, allele DPB1*22:01, allele FT DPB1*22:02, allele DPB1*25:01, allele FT DPB1*25:02, allele DPB1*26:01, allele FT DPB1*27:01, allele DPB1*29:01, allele FT DPB1*30:01, allele DPB1*31:01, allele FT DPB1*35:01, allele DPB1*36:01, allele FT DPB1*37:01, allele DPB1*38:01, allele FT DPB1*44:01, allele DPB1*45:01, allele FT DPB1*50:01, allele DPB1*52:01, allele FT DPB1*54:01, allele DPB1*55:01, allele FT DPB1*56:01, allele DPB1*57:01, allele FT DPB1*58:01, allele DPB1*63:01, allele FT DPB1*65:01, allele DPB1*67:01, allele FT DPB1*68:01, allele DPB1*69:01, allele FT DPB1*70:01, allele DPB1*76:01, allele FT DPB1*78:01, allele DPB1*79:01, allele FT DPB1*84:01, allele DPB1*85:01, allele FT DPB1*87:01, allele DPB1*88:01, allele FT DPB1*89:01, allele DPB1*90:01, allele FT DPB1*91:01, allele DPB1*92:01, allele FT DPB1*93:01, allele DPB1*97:01 and allele FT DPB1*98:01; dbSNP:rs9277355). FT {ECO:0000269|PubMed:6330724}. FT /FTId=VAR_033445. FT VARIANT 116 116 M -> V (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*03:02, allele FT DPB1*04:03, allele DPB1*05:01, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*08:01, allele DPB1*08:02, allele FT DPB1*09:01, allele DPB1*09:02, allele FT DPB1*10:01, allele DPB1*11:01, allele FT DPB1*13:01, allele DPB1*13:02, allele FT DPB1*14:01, allele DPB1*14:02, allele FT DPB1*16:01, allele DPB1*17:01, allele FT DPB1*17:02, allele DPB1*19:01, allele FT DPB1*21:01, allele DPB1*21:02, allele FT DPB1*20:01, allele DPB1*22:01, allele FT DPB1*22:02, allele DPB1*25:01, allele FT DPB1*25:02, allele DPB1*26:01, allele FT DPB1*27:01, allele DPB1*29:01, allele FT DPB1*30:01, allele DPB1*31:01, allele FT DPB1*35:01, allele DPB1*36:01, allele FT DPB1*37:01, allele DPB1*38:01, allele FT DPB1*44:01, allele DPB1*45:01, allele FT DPB1*50:01, allele DPB1*52:01, allele FT DPB1*54:01, allele DPB1*55:01, allele FT DPB1*56:01, allele DPB1*58:01, allele FT DPB1*63:01, allele DPB1*65:01, allele FT DPB1*67:01, allele DPB1*68:01, allele FT DPB1*69:01, allele DPB1*70:01, allele FT DPB1*76:01, allele DPB1*78:01, allele FT DPB1*79:01, allele DPB1*84:01, allele FT DPB1*85:01, allele DPB1*87:01, allele FT DPB1*88:01, allele DPB1*89:01, allele FT DPB1*90:01, allele DPB1*91:01, allele FT DPB1*92:01, allele DPB1*93:01, allele FT DPB1*97:01 and allele DPB1*98:01; FT dbSNP:rs9277356). FT {ECO:0000269|PubMed:6330724}. FT /FTId=VAR_033446. FT VARIANT 120 120 R -> H (in allele DPB1*82:01 and allele FT DPB1*85:01; dbSNP:rs41541915). FT /FTId=VAR_060658. FT VARIANT 125 125 R -> K (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*05:01, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*09:01, allele DPB1*09:02, allele FT DPB1*13:01, allele DPB1*14:01, allele FT DPB1*15:01, allele DPB1*18:01, allele FT DPB1*19:01, allele DPB1*20:01, allele FT DPB1*26:01, allele DPB1*45:01 and allele FT DPB1*85:01; dbSNP:rs1126537). FT {ECO:0000269|PubMed:6330724}. FT /FTId=VAR_060659. FT VARIANT 199 199 T -> I (in allele DPB1*01:01, allele FT DPB1*03:01, allele DPB1*05:01, allele FT DPB1*05:02, allele DPB1*06:01, allele FT DPB1*09:01, allele DPB1*09:02, allele FT DPB1*13:01, allele DPB1*14:01, allele FT DPB1*15:01, allele DPB1*18:01, allele FT DPB1*19:01, allele DPB1*20:01, allele FT DPB1*26:01, allele DPB1*45:01 and allele FT DPB1*85:01; dbSNP:rs1042335). FT {ECO:0000269|PubMed:6330724}. FT /FTId=VAR_060660. FT VARIANT 207 207 L -> M (in allele DPB1*04:02; FT dbSNP:rs14362). FT /FTId=VAR_033447. FT VARIANT 223 223 R -> Q (in allele DPB1*01:01; FT dbSNP:rs9276). FT /FTId=VAR_050393. FT VARIANT 234 234 V -> M (in allele DPB1*05:01 and allele FT DPB1*19:01; dbSNP:rs11551421). FT /FTId=VAR_050394. FT VARIANT 244 244 I -> T (in allele DPB1*15:01; FT dbSNP:rs3097675). FT /FTId=VAR_033448. FT STRAND 37 47 {ECO:0000244|PDB:4P5M}. FT STRAND 50 59 {ECO:0000244|PDB:4P5M}. FT STRAND 62 68 {ECO:0000244|PDB:4P5M}. FT TURN 69 71 {ECO:0000244|PDB:4P5M}. FT STRAND 73 78 {ECO:0000244|PDB:4P5M}. FT HELIX 79 81 {ECO:0000244|PDB:4P5M}. FT HELIX 82 89 {ECO:0000244|PDB:4P5M}. FT HELIX 92 99 {ECO:0000244|PDB:4P5M}. FT TURN 100 104 {ECO:0000244|PDB:4P5M}. FT HELIX 105 112 {ECO:0000244|PDB:4P5M}. FT HELIX 114 118 {ECO:0000244|PDB:4P5M}. FT STRAND 125 130 {ECO:0000244|PDB:4P5M}. FT HELIX 134 137 {ECO:0000244|PDB:4P5M}. FT STRAND 141 152 {ECO:0000244|PDB:4P5M}. FT STRAND 155 160 {ECO:0000244|PDB:4P5M}. FT STRAND 163 165 {ECO:0000244|PDB:4P5M}. FT STRAND 167 171 {ECO:0000244|PDB:4P5M}. FT STRAND 178 180 {ECO:0000244|PDB:4P5M}. FT STRAND 182 189 {ECO:0000244|PDB:4P5M}. FT STRAND 197 203 {ECO:0000244|PDB:4P5M}. FT STRAND 211 216 {ECO:0000244|PDB:4P5M}. SQ SEQUENCE 258 AA; 29159 MW; E74777D438DE9C41 CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYLFQG RQECYAFNGT QRFLERYIYN REEFARFDSD VGEFRAVTEL GRPAAEYWNS QKDILEEKRA VPDRMCRHNY ELGGPMTLQR RVQPRVNVSP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID DQB1_HUMAN Reviewed; 261 AA. AC P01920; A1KR27; A2RPH3; A4Q9R4; A4USG2; A4USG5; A6N8I7; A9YQA0; AC B0S7Y7; B1A0K6; B1GXI3; B3VLT3; B5BLN7; B7VU69; C0MQ34; C0MQ35; AC C8ZL52; C8ZLJ8; C8ZLJ9; C9DRQ3; O19708; O19713; O19724; O62861; AC O78046; O78221; O78223; O98034; O98201; P01917; P01918; P01919; AC P03992; P05537; P79482; P79526; P79544; P79551; Q08GC8; Q09035; AC Q0E4V9; Q1M312; Q29731; Q29877; Q29884; Q29915; Q29966; Q2P9N3; AC Q2QK85; Q30061; Q30075; Q30076; Q30080; Q30081; Q30082; Q30083; AC Q30084; Q30089; Q30095; Q31633; Q38I47; Q45UE3; Q4QZB5; Q53I44; AC Q564J6; Q5G841; Q5ISH1; Q5ISH3; Q5W1E1; Q5Y7G8; Q643R4; Q6B9X1; AC Q70VH8; Q7YP69; Q8HWH0; Q8MH58; Q8SNB4; Q8SND1; Q8SP70; Q8WMA3; AC Q9BD17; Q9MYH2; Q9TPA9; Q9XRY6; Q9XRY7; Q9XRZ2; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 02-MAR-2010, sequence version 2. DT 12-SEP-2018, entry version 177. DE RecName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain; DE AltName: Full=MHC class II antigen DQB1; DE Flags: Precursor; GN Name=HLA-DQB1; Synonyms=HLA-DQB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQB1*02:01), AND NUCLEOTIDE RP SEQUENCE [MRNA] OF 33-261 (CLONE PII-BETA-2) (ALLELE DQB1*05:01). RX PubMed=6415003; DOI=10.1016/0198-8859(83)90087-3; RA Larhammar D., Andersson G., Andersson M., Bill P., Boehme J., RA Claesson L., Denaro M., Emmoth E., Gustafsson K., Hammarling U., RA Heldin E., Hyldig-Nielsen J.-J., Lind P., Schenning L., Servenius B., RA Widmark E., Rask L., Peterson P.A.; RT "Molecular analysis of human class II transplantation antigens and RT their genes."; RL Hum. Immunol. 8:95-103(1983). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQB1*02:01). RX PubMed=6954511; DOI=10.1073/pnas.79.12.3687; RA Larhammar D., Schenning L., Gustafsson K., Wiman K., Claesson L., RA Rask L., Peterson P.A.; RT "Complete amino acid sequence of an HLA-DR antigen-like beta chain as RT predicted from the nucleotide sequence: similarities with RT immunoglobulins and HLA-A, -B, and -C antigens."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3687-3691(1982). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQB1*03:02). RX PubMed=6316358; DOI=10.1073/pnas.80.23.7313; RA Larhammar D., Hyldig-Nielsen J.-J., Servenius B., Andersson G., RA Rask L., Peterson P.A.; RT "Exon-intron organization and complete nucleotide sequence of a human RT major histocompatibility antigen DC beta gene."; RL Proc. Natl. Acad. Sci. U.S.A. 80:7313-7317(1983). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQB1*02:01). RX PubMed=6206493; DOI=10.1073/pnas.81.16.5199; RA Boss J.M., Strominger J.L.; RT "Cloning and sequence analysis of the human major histocompatibility RT complex gene DC-3 beta."; RL Proc. Natl. Acad. Sci. U.S.A. 81:5199-5203(1984). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQB1*05:01). RX PubMed=2998758; RA Tonnelle C., Demars R., Long E.O.; RT "DO beta: a new beta chain gene in HLA-D with a distinct regulation of RT expression."; RL EMBO J. 4:2839-2847(1985). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQB1*05:01). RX PubMed=2888727; DOI=10.1007/BF00346523; RA Turco E., Care A., Compagnone-Post P., Robinson C., Cascino I., RA Trucco M.; RT "Allelic forms of the alpha- and beta-chain genes encoding DQw1- RT positive heterodimers."; RL Immunogenetics 26:282-290(1987). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQB1*03:02). RX PubMed=3036828; RA Jonsson A.-K., Hyldig-Nielsen J.-J., Servenius B., Larhammar D., RA Andersson G., Joergensen F., Peterson P.A., Rask L.; RT "Class II genes of the human major histocompatibility complex. RT Comparisons of the DQ and DX alpha and beta genes."; RL J. Biol. Chem. 262:8767-8777(1987). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-15; SER-28; GLY-45; RP LEU-58; GLY-77; GLY-102 AND ARG-199. RX PubMed=3584986; RA Schiffenbauer J., Didier D.K., Klearman M., Rice K., Shuman S., RA Tieber V.L., Kittlesen D.J., Schwartz B.D.; RT "Complete sequence of the HLA DQ alpha and DQ beta cDNA from a RT DR5/DQw3 cell line."; RL J. Immunol. 139:228-233(1987). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQB1*06:02). RX PubMed=3259543; DOI=10.1007/BF00364432; RA Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.; RT "MHC class II sequences of an HLA-DR2 narcoleptic."; RL Immunogenetics 27:449-455(1988). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQB1*03:03). RX PubMed=2050393; DOI=10.1007/BF00216702; RA Giorda R., Turco E., Trucco M.; RT "Full length beta chain cDNAs of DQw9 and DQw8 molecules encode RT proteins that differ only at amino acid 57."; RL Immunogenetics 33:404-408(1991). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DQB1*06:12). RX PubMed=8988543; DOI=10.1111/j.1399-0039.1996.tb02674.x; RA Vilches C., Garcia-Pacheco J.M., de Pablo R., Puente S., Kreisler M.; RT "Complete coding region of the new HLA-DQB1*0612 allele, obtained by RT RT-PCR."; RL Tissue Antigens 48:589-592(1996). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DQB1*02:01). RX PubMed=9271631; DOI=10.1007/s002510050295; RA Ellis M.C., Hetisimer A.H., Ruddy D.A., Hansen S.L., Kronmal G.S., RA McClelland E., Quintana L., Drayna D.T., Aldrich M.S., Mignot E.; RT "HLA class II haplotype and sequence analysis support a role for DQ in RT narcolepsy."; RL Immunogenetics 46:410-417(1997). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELES DQB1*03:01 AND DQB1*03:03). RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELES DQB1*03:01; DQB1*04:01 AND RP DQB1*05:02). RA Kim E., Lee E., Kwack K.; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DQB1*02:02; RP DQB1*03:01 AND DQB1*03:03). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [16] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DQB1*03:02). RC TISSUE=B-cell; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [17] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-126 (ALLELE DQB1*06:02). RX PubMed=2925231; DOI=10.1007/BF00373644; RA Hiraiwa A., Seyfried C.E., Nepom G.T., Milner E.C.; RT "Sequence analysis of HLA class II domains: characterization of the RT DQw3 family of DQB genes."; RL Immunogenetics 29:186-190(1989). RN [18] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-261 (ALLELE DQB1*03:01), AND RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-261 (ALLELE DQB1*03:09). RA White J.M., Baxter-Lowe L.A.; RT "Nucleotide Deletions in a DQB1*0301 variant."; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-126 (ALLELE DQB1*06:02). RX PubMed=2494138; DOI=10.1016/0198-8859(89)90058-X; RA Uryu N., Maeda M., Nagata Y., Matsuki K., Juji T., Honda Y., Kawai J., RA Ando A., Tsuji K., Inoko H.; RT "No difference in the nucleotide sequence of the DQ beta beta 1 domain RT between narcoleptic and healthy individuals with DR2,Dw2."; RL Hum. Immunol. 24:175-181(1989). RN [20] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-261 (ALLELE DQB1*04:02). RX PubMed=2777341; DOI=10.1007/BF02421214; RA Jonsson A.-K., Andersson L., Rask L.; RT "Complete sequences of DQA1 and DQB1 cDNA clones corresponding to the RT DQw4 specificity."; RL Immunogenetics 30:232-234(1989). RN [21] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-261 (ALLELES DQB1*03:03; DQB1*05:01; RP DQB1*05:03; DQB1*06:01; DQB1*06:02; DQB1*06:03 AND DQB1*06:04), AND RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-126 (ALLELE DQB1*03:01). RX PubMed=8929711; DOI=10.1111/j.1399-0039.1996.tb02512.x; RA Yasunaga S., Kimura A., Hamaguchi K., Ronningen K.S., Sasazuki T.; RT "Different contribution of HLA-DR and -DQ genes in susceptibility and RT resistance to insulin-dependent diabetes mellitus (IDDM)."; RL Tissue Antigens 47:37-48(1996). RN [22] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-261 (ALLELE DQB1*03:10). RX PubMed=11098940; DOI=10.1034/j.1399-0039.2000.560412.x; RA Balas A., Santos S., Aviles M.J., Garcia-Sanchez F., Lillo R., RA Vicario J.L.; RT "Identification by sequencing based typing and complete coding region RT analysis of three new HLA class II alleles: DRB3*0210, DRB3*0211 and RT DQB1*0310."; RL Tissue Antigens 56:380-384(2000). RN [23] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-261 (ALLELE DQB1*06:09). RA Yasunaga S.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-231 (ALLELES DQB1*03:04 AND RP DQB1*03:05). RX PubMed=7928445; DOI=10.1016/0198-8859(94)90060-4; RA Cucca F., Frau F., Lampis R., Floris M., Argiolas L., Macis D., RA Cao A., De Virgiliis S., Congia M.; RT "HLA-DQB1*0305 and -DQB1*0304 alleles among Sardinians. Evolutionary RT and practical implications for oligotyping."; RL Hum. Immunol. 40:143-149(1994). RN [25] RP PROTEIN SEQUENCE OF 33-181 AND 200-230 (ALLELE DQB1*06:02). RX PubMed=6576979; RA Goetz H., Kratzin H., Thinnes F.P., Yang C.-Y., Kruse T., Pauly E., RA Koelbel S., Egert G., Wernet P., Hilschmann N.; RT "Primary structure of human class II histocompatibility antigens 3rd RT communication. Amino acid sequence comparison between DR and DC RT subclass antigens derived from a lymphoblastoid B cell line homozygous RT at the HLA loci (HLA-A3,3; B7,7; Dw2,2; DR2,2: MT1,1; Dc1,1: MB1,1)."; RL Hoppe-Seyler's Z. Physiol. Chem. 364:749-755(1983). RN [26] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-140 (ALLELE DQB1*06:05). RX PubMed=2212675; RA Lee K.W., Johnson A.H., Hurley C.K.; RT "Two divergent routes of evolution gave rise to the DRw13 RT haplotypes."; RL J. Immunol. 145:3119-3125(1990). RN [27] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-126 (ALLELE DQB1*02:01). RX PubMed=3020127; RA Karr R.W., Gregersen P.K., Obata F., Goldberg D., Maccari J., RA Alber C., Silver J.; RT "Analysis of DR-beta and DQ-beta chain cDNA clones from a DR7 RT haplotype."; RL J. Immunol. 137:2886-2890(1986). RN [28] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-126 (ALLELE DQB1*06:22). RX PubMed=17868257; DOI=10.1111/j.1399-0039.2007.00927.x; RA Chang Y., Fan T.X., Santana Z., Day N.K.; RT "Identification of a novel allele HLA-DQB1*0622."; RL Tissue Antigens 70:442-444(2007). RN [29] RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-122 (ALLELE DQB1*06:02). RX PubMed=2886427; DOI=10.1007/BF00345460; RA Lee B.S., Bell J.I., Rust N.A., McDevitt H.O.; RT "Structural and functional variability among DQ beta alleles of DR2 RT subtypes."; RL Immunogenetics 26:85-91(1987). RN [30] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-107 (ALLELE DQB1*03:07). RX PubMed=9174147; DOI=10.1111/j.1399-0039.1997.tb02789.x; RA Thye T., Muntau B., Stelma F.F., Horstmann R.D.; RT "A novel allele, DQB1*0307, in a West African family."; RL Tissue Antigens 49:517-518(1997). RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-126 (ALLELE DQB1*06:18). RX PubMed=11782280; DOI=10.1034/j.1399-0039.2001.580409.x; RA Casamitjana N., Gil J., Campos E., Santos M., Nogues N., Ribera A., RA Palou E.; RT "Identification of a novel HLA-DQB1*06 allele, DQB1*0618."; RL Tissue Antigens 58:269-271(2001). RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-126 (ALLELE DQB1*06:19). RA Bowman S., Diviney M., Dunckley H., Holdsworth R., Varney M.; RT "A new DQB1*0602 variant found in Australian Caucasian."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [33] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-121 (ALLELE DQB1*06:13). RX PubMed=9458130; DOI=10.1111/j.1399-0039.1997.tb02935.x; RA Hsu S.H., Robbins F.M., Modelo R.B., Brunner J., Flomenberg N.; RT "Identification of a new DQB1*0613 allele in a family."; RL Tissue Antigens 50:685-687(1997). RN [34] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-257 (ALLELE DQB1*06:36). RC TISSUE=Peripheral blood; RA Skrablin P.S., Richter R., Seidl C., Seifried E.; RT "New HLA-DQB1*06 allele found in a voluntary blood stem cell donor."; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [35] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELE DQB1*03:19). RX PubMed=17559588; DOI=10.1111/j.1399-0039.2007.00848.x; RA Witter K., Mautner J., Albert T., Zahn R., Kauke T.; RT "HLA-DQB1*0319, a novel HLA-DQB1 allele, shows strong haplotype RT association to HLA-DRB1*1102."; RL Tissue Antigens 70:73-75(2007). RN [36] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELE DQB1*06:34). RX PubMed=18331527; DOI=10.1111/j.1399-0039.2008.01021.x; RA Witter K., Albert T., Zahn R., Kauke T.; RT "HLA-DQB1*0634, a novel DQB1 allele found by high-resolution HLA RT typing of a sibling pair for potential bone marrow transplantation."; RL Tissue Antigens 71:486-488(2008). RN [37] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELE DQB1*03:21), AND RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELES DQB1*02:05 AND RP DQB1*03:20). RX PubMed=18588576; DOI=10.1111/j.1399-0039.2008.01070.x; RA Lazaro A.M., Xiao Y., Masaberg C., Lebeck L., Ng J., Hurley C.K., RA Posch P.E.; RT "Novel alleles at the HLA-DRB1 and -DQB1 loci."; RL Tissue Antigens 72:72-74(2008). RN [38] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELE DQB1*03:22). RC TISSUE=Peripheral blood; RX PubMed=19254265; DOI=10.1111/j.1399-0039.2008.01201.x; RA Witter K., Lochmann E., Vecchiato C., Albert T., Zahn R., Kauke T.; RT "Sequence-based HLA high-resolution retyping of a bone marrow RT donor/recipient pair reveals the novel HLA allele DQB1*0322."; RL Tissue Antigens 73:283-285(2009). RN [39] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELE DQB1*03:23). RC TISSUE=Peripheral blood; RX PubMed=19493242; DOI=10.1111/j.1399-0039.2009.01231.x; RA Wienzek S., Verboom M., Blasczyk R., Bein G., Horn P.A.; RT "DQB1*0323 is the result of a gene conversion event between a DQB1*06 RT and a DQB1*030303 allele."; RL Tissue Antigens 73:624-625(2009). RN [40] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELE DQB1*02:04). RA Gragg H., Cordovado S.K., Hendrix M.M., Mueller P.W.; RT "Identification of a novel HLA-DQB1*02 allele."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [41] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELE DQB1*03:25). RA Thompson E.M., Mehdizadeh Kashi Z., Martin R.K.; RT "Homo sapiens novel MHC class II HLA-DQB1 gene HLA-DQB1*03 novel RT allele, exons 2 and 3."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [42] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELE DQB1*03:24). RA Michaud C., Giannoli C., Favre Victoire I., Dubois V.; RT "A new HLA-DQB allele, identified by routine sequencing."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [43] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-220 (ALLELES DQB1*06:38 AND RP DQB1*06:39). RC TISSUE=Blood; RA Anholts J.D.H.; RT "New alleles found during routine SBT HLA typing."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [44] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:10). RX PubMed=8896183; DOI=10.1111/j.1399-0039.1996.tb02633.x; RA Mersch G., Semana G., De Canck I., Jannes G., Rombout A., Sterker G., RA Rossau R.; RT "Characterization of a new DQB1 allele (DQB1*0610) which differs from RT DQB1*0602 at the highly polymorphic 57-codon."; RL Tissue Antigens 48:217-220(1996). RN [45] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:06). RC TISSUE=Blood; RX PubMed=8988541; DOI=10.1111/j.1399-0039.1996.tb02672.x; RA Saito S., Ota S., Hashizume K., Yamada E., Kaneshige T., Hashimoto M., RA Oguchi H., Ishii E., Fukushima H.; RT "A new HLA-DQB1*0306 allele sharing motifs from DQB1*03032 and DQB1*04 RT sequences."; RL Tissue Antigens 48:580-585(1996). RN [46] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:11), AND RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-120 (ALLELE DQB1*06:20). RX PubMed=15361133; DOI=10.1111/j.1399-0039.2004.00307.x; RA Hogbin J.P., Greville W., Chapman G., Kennedy A., Velickovic Z.M., RA Dunckley H.; RT "Identification of two novel HLA class II alleles, DQB1*0311 and RT DQB1*0620."; RL Tissue Antigens 64:515-517(2004). RN [47] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:16). RA Chen D.-F., DeOliveira A., Peplinski S., Herczyk W., Reinsmoen N.L.; RT "A novel DQB1*03 allele revealed by rSSOP and identified by SBT."; RL Hum. Immunol. 66:30-30(2005). RN [48] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:14). RX PubMed=15853909; DOI=10.1111/j.1399-0039.2005.00397.x; RA Gu H., Kimm K., Lee J.K., Oh B.; RT "Identification of a novel HLA-DQB1 allele, DQB1*0314, by sequence- RT based typing in the Korean population."; RL Tissue Antigens 65:503-504(2005). RN [49] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:28). RX PubMed=17212715; DOI=10.1111/j.1399-0039.2006.00733.x; RA Witter K., Albert T., Zahn R., Kauke T.; RT "A novel HLA-DQB1*06 allele, DQB1*0628, found through routine RT sequence-based HLA typing and confirmation of DQB1*060302."; RL Tissue Antigens 69:102-103(2007). RN [50] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:32). RC TISSUE=Blood; RX PubMed=17999653; DOI=10.1111/j.1399-0039.2007.00967.x; RA Emmerich F., Schonemann C., Diederich G., Horn P.A., Salama A.; RT "Identification of a novel HLA-DQB1 allele, HLA-DQB1*0632."; RL Tissue Antigens 71:94-95(2008). RN [51] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*05:05). RX PubMed=19392794; DOI=10.1111/j.1399-0039.2009.01248.x; RA Giannoli C., Paturel L., Favre-Victoire I., Bera O., Dubois V.; RT "Two new HLA-DQB alleles routinely identified by sequence-based RT typing: DQB1*030103 and DQB1*0505."; RL Tissue Antigens 73:622-623(2009). RN [52] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*02:03). RA Olerup O.H.; RT "A novel DQB1*02 allele."; RL Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases. RN [53] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:05). RA Rugg J., Blanton M., Whitacre L., Balakrishnan K., Lebeer K., RA Van Reybroeck G., Mersch G.; RT "Detection of a new DQB1 allele."; RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases. RN [54] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:15). RA Shah A., Ross J., Chenery P., Holman R., Madrigal A., Little A.M.; RT "Two novel DQB1*06 alleles, identified by reverse line blot assay."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [55] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:05). RC TISSUE=Peripheral blood; RA Moine A.; RT "A new variant form of the HLA DQB1*0305 allele."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [56] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:12). RA Schwarz K., Zenz C.; RT "Homo sapiens HLA-DQB1*0312 allele, exon 2."; RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases. RN [57] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:13). RA Wu J., Bassinger S., Williams T.M.; RT "Novel human HLA-DQB1 allele identified in potential bone marrow RT donors."; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. RN [58] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:21). RA De Canck I.; RT "Identification of a new HLA-DQB1*06 allele by INNO-LiPA."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [59] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:17). RA Bassinger S., Wu J., Zhang Q., Brinkema C., Smith A.G., Williams T.M.; RT "Novel DQB1*06 alleles."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [60] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:23). RA Hirv K., Krauss A., Mytilineos J.; RT "Characterization of a new HLA-DQB1 allele by direct sequencing."; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. RN [61] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:15). RC TISSUE=Peripheral blood; RA Velickovic Z.M.; RT "Novel HLA-DQB1*03 allele."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [62] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:24). RA Schranz P., Seelig R., Seelig H.P.; RT "A new HLA-DQB1 allele."; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [63] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:25). RA Watabe K., Hashimoto M.; RT "Homo sapiens HLA-DQ gene for MHC class2 antigen, partial cds, allele: RT HLA-DQB1*060401V."; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [64] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:17). RA Chu C.-C.; RT "A novel DQB1 allele found in Taiwan."; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [65] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:18). RA Hendrix M.M., Cordovado S.K., Mueller P.W.; RT "High resolution genotyping of HLA-DQB1 exon 2 and 3."; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [66] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:29). RA Horn P.A., Blasczyk R.; RT "A novel HLA-DRQ1*06 allele."; RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases. RN [67] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:31). RA Nieberle I., Hirschmann D., Woelpl A.; RT "Identification of several new class I and II alleles in routine HLA- RT testing."; RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases. RN [68] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:33). RA Yu M., Hall J.E., Hartman K.J., Caparelli E., Czech J., Smyth E., RA Jennings L.; RT "A novel HLA-DQB1*06 allele identified by PCR-SBT in a caucasian NMDP RT donor."; RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases. RN [69] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*04:03). RA Vigh A., Hirv K., Mytilineos J.; RT "Characterization of a new HLA-Cw*07 allele."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [70] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*06:37). RA Fuerst D., Mytilineos J.; RT "A new variant of HLA-DQB1*06."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [71] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-126 (ALLELE DQB1*03:26). RA Yang K., Chen M.; RT "Novel DQB1*03 found in CAP test sample."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [72] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-122 (ALLELE DQB1*06:16). RX PubMed=10323344; DOI=10.1034/j.1399-0039.1999.530410.x; RA Luo M., Blanchard J., Maclean I., Brunham R.; RT "Identification of a novel DQB1 allele DBQ1*0616."; RL Tissue Antigens 53:381-382(1999). RN [73] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-115 (ALLELE DQB1*06:30). RA Rizzo M., Hurley C.K.; RT "Novel HLA-DQB1 allele."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [74] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-126 (ALLELE DQB1*06:14). RC TISSUE=Blood; RX PubMed=9802612; DOI=10.1111/j.1399-0039.1998.tb03047.x; RA Hashemi-tavoularis S., Ouellet S., Sengar D.P.S., Buyse I.M.; RT "A novel DRB3 allele (DRB3*0208), a new allelic variant of DRB1*1502 RT (DRB1*15023) and two new DQB1 (DQB1*03012 and DQB1*0614) alleles."; RL Tissue Antigens 52:294-299(1998). RN [75] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-125 (ALLELE DQB1*06:11). RX PubMed=8896171; DOI=10.1111/j.1399-0039.1996.tb02621.x; RA Williams T.M., Bassinger S., Moehlenkamp C., Wu J., Montoya G.D., RA Griffith B.B., McAuley J.D., Goldman S., Maurer D.H., Troup G.M.; RT "Strategy for distinguishing a new DQB1 allele (DQB1*0611) from the RT closely related DQB1*0602 allele via sequence specific PCR or direct RT DNA sequencing."; RL Tissue Antigens 48:143-147(1996). RN [76] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-125 (ALLELE DQB1*06:27). RX PubMed=16441489; DOI=10.1111/j.1399-0039.2006.00515.x; RA Brixner V., Mosebach M., Schmidt M., Hermann S., Seifried E., RA Martin H., Seidl C.; RT "HLA-DRB1*0826 and HLA-DQB1*0627, two novel class II alleles RT identified in blood stem cell donors of Caucasian origin."; RL Tissue Antigens 67:160-162(2006). RN [77] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-122 (ALLELES DQB1*06:07 AND RP DQB1*06:08). RA Dinauer D.M., Hessner M.J.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [78] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-114 (ALLELE DQB1*05:04). RX PubMed=1440562; DOI=10.1111/j.1399-0039.1992.tb01958.x; RA Fenske T.S., Baxter-Lowe L.A.; RT "Two novel HLA-DQB1*06 alleles reveal additional heterogeneity of HLA- RT DQw1."; RL Tissue Antigens 40:49-52(1992). RN [79] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-109 (ALLELE DQB1*02:01). RX PubMed=2308943; DOI=10.1073/pnas.87.5.1835; RA Gyllensten U.B., Lashkari D., Erlich H.A.; RT "Allelic diversification at the class II DQB locus of the mammalian RT major histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 87:1835-1839(1990). RN [80] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 53-109 (ALLELES DQB1*02:01 AND RP DQB1*06:02). RX PubMed=2010218; DOI=10.1007/BF01719235; RA Bugawan T.L., Erlich H.A.; RT "Rapid typing of HLA-DQB1 DNA polymorphism using nonradioactive RT oligonucleotide probes and amplified DNA."; RL Immunogenetics 33:163-170(1991). RN [81] RP NUCLEOTIDE SEQUENCE [MRNA] OF 135-217 (ALLELE DQB1*02:01). RX PubMed=6952552; DOI=10.1111/j.1365-3083.1981.tb00603.x; RA Larhammar D., Wiman K., Schenning L., Claesson L., Gustafsson K., RA Peterson P.A., Rask L.; RT "Evolutionary relationship between HLA-DR antigen beta-chains, HLA-A, RT B, C antigen subunits and immunoglobulin chains."; RL Scand. J. Immunol. 14:617-622(1981). RN [82] RP POLYMORPHISM. RX PubMed=18565458; DOI=10.1016/S1474-4422(08)70140-6; RA Bourgin P., Zeitzer J.M., Mignot E.; RT "CSF hypocretin-1 assessment in sleep and neurological disorders."; RL Lancet Neurol. 7:649-662(2008). RN [83] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [84] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [85] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [86] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [87] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [88] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [89] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 35-224 OF HLA-DQA1/HLA-DQB1 RP HETERODIMER IN COMPLEX WITH INS PEPTIDE, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=11376336; DOI=10.1038/88694; RA Lee K.H., Wucherpfennig K.W., Wiley D.C.; RT "Structure of a human insulin peptide-HLA-DQ8 complex and RT susceptibility to type 1 diabetes."; RL Nat. Immunol. 2:501-507(2001). RN [90] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 35-231 OF HLA-DQA1/HLA-DQB1 RP HETERODIMER (HLA-DQ0602) IN COMPLEX WITH HCRT PEPTIDE, POLYMORPHISM, RP SUBUNIT, AND DISULFIDE BONDS. RX PubMed=14769912; DOI=10.1073/pnas.0308458100; RA Siebold C., Hansen B.E., Wyer J.R., Harlos K., Esnouf R.E., RA Svejgaard A., Bell J.I., Strominger J.L., Jones E.Y., Fugger L.; RT "Crystal structure of HLA-DQ0602 that protects against type 1 diabetes RT and confers strong susceptibility to narcolepsy."; RL Proc. Natl. Acad. Sci. U.S.A. 101:1999-2004(2004). RN [91] RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF 33-230 OF HLA-DQA1/HLA-DQB1 RP HETERODIMER (DQ2) IN COMPLEX WITH TRITICUM AESTIVUM ALPHA/BETA-GLIADIN RP PEPTIDE, SUBUNIT, AND POLYMORPHISM. RX PubMed=15020763; DOI=10.1073/pnas.0306885101; RA Kim C.Y., Quarsten H., Bergseng E., Khosla C., Sollid L.M.; RT "Structural basis for HLA-DQ2-mediated presentation of gluten epitopes RT in celiac disease."; RL Proc. Natl. Acad. Sci. U.S.A. 101:4175-4179(2004). RN [92] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-224 OF HLA-DQA1/HLA-DQB1 RP HETERODIMER IN COMPLEX WITH TRITICUM AESTIVUM ALPHA/BETA-GLIADIN RP PEPTIDE, POLYMORPHISM, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=17629515; DOI=10.1016/j.immuni.2007.05.015; RA Henderson K.N., Tye-Din J.A., Reid H.H., Chen Z., Borg N.A., RA Beissbarth T., Tatham A., Mannering S.I., Purcell A.W., Dudek N.L., RA van Heel D.A., McCluskey J., Rossjohn J., Anderson R.P.; RT "A structural and immunological basis for the role of human leukocyte RT antigen DQ8 in celiac disease."; RL Immunity 27:23-34(2007). RN [93] RP VARIANT [LARGE SCALE ANALYSIS] ALA-172, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC {ECO:0000269|PubMed:11376336, ECO:0000269|PubMed:14769912, CC ECO:0000269|PubMed:15020763, ECO:0000269|PubMed:17629515}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Note=The MHC class II complex transits through CC a number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- POLYMORPHISM: The following alleles of HLA-DQB1 are known: CC DQB1*02:01, DQB1*02:02, DQB1*02:03, DQB1*02:04, DQB1*02:05, CC DQB1*03:01, DQB1*03:02, DQB1*03:03, DQB1*03:04, DQB1*03:05, CC DQB1*03:06, DQB1*03:07, DQB1*03:08, DQB1*03:09, DQB1*03:10, CC DQB1*03:11, DQB1*03:12, DQB1*03:13, DQB1*03:14, DQB1*03:15, CC DQB1*03:16, DQB1*03:17, DQB1*03:18, DQB1*03:19, DQB1*03:20, CC DQB1*03:21, DQB1*03:22, DQB1*03:23, DQB1*03:24, DQB1*03:25, CC DQB1*03:26, DQB1*04:01, DQB1*04:02, DQB1*04:03, DQB1*05:01, CC DQB1*05:02, DQB1*05:03, DQB1*05:04, DQB1*05:05, DQB1*06:01, CC DQB1*06:02, DQB1*06:03, DQB1*06:04, DQB1*06:05, DQB1*06:06, CC DQB1*06:07, DQB1*06:08, DQB1*06:09, DQB1*06:10, DQB1*06:11, CC DQB1*06:12, DQB1*06:13, DQB1*06:14, DQB1*06:15, DQB1*06:16, CC DQB1*06:17, DQB1*06:18, DQB1*06:19, DQB1*06:20, DQB1*06:21, CC DQB1*06:22, DQB1*06:23, DQB1*06:24, DQB1*06:25, DQB1*06:27, CC DQB1*06:28, DQB1*06:29, DQB1*06:30, DQB1*06:31, DQB1*06:32, CC DQB1*06:33, DQB1*06:34, DQB1*06:35, DQB1*06:36, DQB1*06:37, CC DQB1*06:38, and DQB1*06:39. The sequence shown is that of CC DQB1*03:01. CC -!- POLYMORPHISM: DQ2 (heterodimer of DQA1*05:01/DQB1*02:01) is CC associated with more than 90% of celiac disease patients. A CC minority displays DQ8 (heterodimer of DQA1*03/DQB1*03:02). CC -!- POLYMORPHISM: DQ0602 (heterodimer of DQA1*01:02/DQB1*06:02) CC confers dominant protection against type 1 diabetes (T1D) and CC strong susceptibility to narcolepsy. DQB1*06:02 has been found to CC be present in most of the narcolepsy patients. As well 98% of the CC patients with an HCRT deficiency are positive for DQB1*06:02. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC64403.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAJ57391.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and CC polymorphism database; CC URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=HLA-DQB1"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; K01499; AAA98746.1; -; Genomic_DNA. DR EMBL; K02405; AAA75521.1; -; Genomic_DNA. DR EMBL; X03068; CAA26872.1; -; mRNA. DR EMBL; M17564; AAA59765.1; -; mRNA. DR EMBL; M29613; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M29616; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M16996; AAA59770.1; -; mRNA. DR EMBL; M20432; AAA59769.1; -; mRNA. DR EMBL; M60028; AAA59755.1; -; mRNA. DR EMBL; X96420; CAA65280.1; -; mRNA. DR EMBL; U92032; AAB91991.1; -; Genomic_DNA. DR EMBL; AY663393; AAU87973.1; -; Genomic_DNA. DR EMBL; AY663394; AAU87977.1; -; Genomic_DNA. DR EMBL; AY663397; AAU87986.1; -; Genomic_DNA. DR EMBL; AY663409; AAU88017.1; -; Genomic_DNA. DR EMBL; AY663404; AAU88002.1; -; Genomic_DNA. DR EMBL; AY663410; AAU88020.1; -; Genomic_DNA. DR EMBL; AY663412; AAU88027.1; -; Genomic_DNA. DR EMBL; AY656681; AAV71028.1; -; mRNA. DR EMBL; AY656682; AAV71029.1; -; mRNA. DR EMBL; AY656683; AAV71030.1; -; mRNA. DR EMBL; BX927168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR933859; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC012106; AAH12106.1; -; mRNA. DR EMBL; M25327; AAA59677.1; -; mRNA. DR EMBL; U66400; AAB51698.1; -; mRNA. DR EMBL; U83582; AAB41231.1; -; mRNA. DR EMBL; AH002887; AAA59762.1; -; Genomic_DNA. DR EMBL; M26042; AAA36270.1; -; mRNA. DR EMBL; M33907; AAA52672.1; -; mRNA. DR EMBL; L34096; AAC41964.1; -; mRNA. DR EMBL; L34098; AAC41966.1; -; mRNA. DR EMBL; L34101; AAC41969.1; -; mRNA. DR EMBL; L34103; AAC41971.1; -; mRNA. DR EMBL; L34104; AAC41972.1; -; mRNA. DR EMBL; L34105; AAC41973.1; -; mRNA. DR EMBL; L34106; AAC41974.1; -; mRNA. DR EMBL; L34107; AAC41975.1; -; mRNA. DR EMBL; AF195245; AAF28315.1; -; mRNA. DR EMBL; L42626; AAA85335.1; -; mRNA. DR EMBL; X76553; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X76554; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M59800; AAA64235.1; -; mRNA. DR EMBL; M14189; AAA36268.1; -; mRNA. DR EMBL; AY672649; AAT77952.1; -; Genomic_DNA. DR EMBL; M17207; AAA59697.1; -; mRNA. DR EMBL; Z49215; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY026349; AAK01944.1; -; Genomic_DNA. DR EMBL; AF091305; AAC64403.2; ALT_SEQ; Genomic_DNA. DR EMBL; U77344; AAB19215.1; -; Genomic_DNA. DR EMBL; FN256435; CAX62164.1; -; Genomic_DNA. DR EMBL; FN256435; CAX62165.1; -; Genomic_DNA. DR EMBL; AM400970; CAL47037.1; -; Genomic_DNA. DR EMBL; AM421131; CAM07104.1; -; Genomic_DNA. DR EMBL; EF484936; ABO87661.1; -; Genomic_DNA. DR EMBL; EF484939; ABO87664.1; -; Genomic_DNA. DR EMBL; EU275158; ABY26531.1; -; Genomic_DNA. DR EMBL; AM944346; CAQ16179.1; -; Genomic_DNA. DR EMBL; FM200854; CAR31119.1; -; Genomic_DNA. DR EMBL; AH013029; AAP93137.1; -; Genomic_DNA. DR EMBL; EU770203; ACF16333.1; -; Genomic_DNA. DR EMBL; FM955320; CAW24712.1; -; Genomic_DNA. DR EMBL; FN552709; CBF35736.1; -; Genomic_DNA. DR EMBL; FN552710; CBF35739.1; -; Genomic_DNA. DR EMBL; X86327; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; D78569; BAA11413.1; -; Genomic_DNA. DR EMBL; AF439338; AAL35222.1; -; Genomic_DNA. DR EMBL; AF384556; AAM53072.1; -; Genomic_DNA. DR EMBL; DQ026226; AAY89656.1; -; Genomic_DNA. DR EMBL; AY762968; AAV97949.1; -; Genomic_DNA. DR EMBL; AM181332; CAJ57391.1; ALT_SEQ; Genomic_DNA. DR EMBL; AM691798; CAM88661.1; -; Genomic_DNA. DR EMBL; AM259942; CAJ90956.1; -; Genomic_DNA. DR EMBL; U39090; AAB02681.1; -; Genomic_DNA. DR EMBL; AJ003005; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ012156; CAA09929.1; -; Genomic_DNA. DR EMBL; AJ290396; CAC27418.1; -; Genomic_DNA. DR EMBL; AF469118; AAL77085.1; -; Genomic_DNA. DR EMBL; AF479569; AAM09472.1; -; Genomic_DNA. DR EMBL; AJ535315; CAD59445.2; -; Genomic_DNA. DR EMBL; AF181983; AAD54423.2; -; Genomic_DNA. DR EMBL; AY733062; AAU33811.1; -; Genomic_DNA. DR EMBL; AJ854065; CAH69441.1; -; Genomic_DNA. DR EMBL; AJ964903; CAI79639.1; -; Genomic_DNA. DR EMBL; AB211231; BAD95610.1; -; Genomic_DNA. DR EMBL; DQ114427; AAZ20753.1; -; Genomic_DNA. DR EMBL; DQ227421; ABB05231.1; -; Genomic_DNA. DR EMBL; AM403489; CAL48285.1; -; Genomic_DNA. DR EMBL; AM490069; CAM32717.1; -; Genomic_DNA. DR EMBL; EF622510; ABR24117.1; -; Genomic_DNA. DR EMBL; EU410617; ABZ89500.1; -; Genomic_DNA. DR EMBL; GQ422610; ACV66342.1; -; Genomic_DNA. DR EMBL; FN550110; CBE66554.1; -; Genomic_DNA. DR EMBL; AF087939; AAD39697.1; -; Genomic_DNA. DR EMBL; AY094140; AAM14401.1; -; Genomic_DNA. DR EMBL; AJ001257; CAA04631.1; -; Genomic_DNA. DR EMBL; U39086; AAA93181.1; -; Genomic_DNA. DR EMBL; AJ965439; CAI84643.1; -; Genomic_DNA. DR EMBL; AF112463; AAD23990.1; -; Genomic_DNA. DR EMBL; AF112464; AAD23991.1; -; Genomic_DNA. DR EMBL; M94773; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M65042; AAA36241.1; -; Genomic_DNA. DR EMBL; M25025; AAA59793.1; -; mRNA. DR PIR; A02234; HLHU1C. DR PIR; A35055; A35055. DR PIR; A94003; HLHUDB. DR PIR; B32527; B32527. DR PIR; B37044; B37044. DR PIR; C24669; HLHU2C. DR PIR; F30575; F30575. DR PIR; I54480; I54480. DR PIR; I68732; I68732. DR PIR; I72482; I72482. DR PIR; S46648; S46648. DR RefSeq; NP_001230891.1; NM_001243962.1. DR RefSeq; NP_002114.3; NM_002123.4. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR PDB; 1JK8; X-ray; 2.40 A; B=35-224. DR PDB; 1NBN; Model; -; B=35-224. DR PDB; 1S9V; X-ray; 2.22 A; B/E=33-230. DR PDB; 1UVQ; X-ray; 1.80 A; B=35-230. DR PDB; 2NNA; X-ray; 2.10 A; B=33-224. DR PDB; 4GG6; X-ray; 3.20 A; B/D=33-224. DR PDB; 4OZF; X-ray; 2.70 A; B=33-224. DR PDB; 4OZG; X-ray; 3.00 A; B/D=33-224. DR PDB; 4OZH; X-ray; 2.80 A; B/D=33-224. DR PDB; 4OZI; X-ray; 3.20 A; B/D=33-224. DR PDBsum; 1JK8; -. DR PDBsum; 1NBN; -. DR PDBsum; 1S9V; -. DR PDBsum; 1UVQ; -. DR PDBsum; 2NNA; -. DR PDBsum; 4GG6; -. DR PDBsum; 4OZF; -. DR PDBsum; 4OZG; -. DR PDBsum; 4OZH; -. DR PDBsum; 4OZI; -. DR ProteinModelPortal; P01920; -. DR SMR; P01920; -. DR BioGrid; 109364; 11. DR IntAct; P01920; 3. DR MINT; P01920; -. DR DrugBank; DB00071; Insulin Pork. DR iPTMnet; P01920; -. DR PhosphoSitePlus; P01920; -. DR BioMuta; HLA-DQB1; -. DR DMDM; 290457643; -. DR PeptideAtlas; P01920; -. DR PRIDE; P01920; -. DR ProteomicsDB; 51513; -. DR DNASU; 3119; -. DR Ensembl; ENST00000399088; ENSP00000382038; ENSG00000231286. DR Ensembl; ENST00000413089; ENSP00000396539; ENSG00000231286. DR Ensembl; ENST00000416192; ENSP00000410107; ENSG00000233209. DR Ensembl; ENST00000419914; ENSP00000402865; ENSG00000225824. DR Ensembl; ENST00000422950; ENSP00000414079; ENSG00000233209. DR Ensembl; ENST00000424806; ENSP00000410330; ENSG00000225824. DR GeneID; 3119; -. DR KEGG; hsa:3119; -. DR UCSC; uc011hep.3; human. DR CTD; 3119; -. DR DisGeNET; 3119; -. DR GeneCards; HLA-DQB1; -. DR GeneReviews; HLA-DQB1; -. DR HGNC; HGNC:4944; HLA-DQB1. DR HPA; HPA013667; -. DR MalaCards; HLA-DQB1; -. DR MIM; 604305; gene. DR neXtProt; NX_P01920; -. DR Orphanet; 703; Bullous pemphigoid. DR Orphanet; 555; Celiac disease. DR Orphanet; 243377; Diabetes mellitus type 1. DR Orphanet; 930; Idiopathic achalasia. DR Orphanet; 802; Multiple sclerosis. DR Orphanet; 83465; Narcolepsy without cataplexy. DR Orphanet; 2073; Narcolepsy-cataplexy. DR PharmGKB; PA35068; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P01920; -. DR KO; K06752; -. DR PhylomeDB; P01920; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SIGNOR; P01920; -. DR ChiTaRS; HLA-DQB1; human. DR EvolutionaryTrace; P01920; -. DR GeneWiki; HLA-DQB1; -. DR GenomeRNAi; 3119; -. DR PRO; PR:P01920; -. DR Proteomes; UP000005640; Chromosome 6. DR CleanEx; HS_HLA-DQB1; -. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; IDA:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Endosome; Glycoprotein; Golgi apparatus; Immunity; Lysosome; Membrane; KW MHC II; Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 32 {ECO:0000269|PubMed:6576979}. FT CHAIN 33 261 HLA class II histocompatibility antigen, FT DQ beta 1 chain. FT /FTId=PRO_0000018989. FT TOPO_DOM 33 230 Extracellular. {ECO:0000255}. FT TRANSMEM 231 251 Helical. {ECO:0000255}. FT TOPO_DOM 252 261 Cytoplasmic. {ECO:0000255}. FT DOMAIN 129 217 Ig-like C1-type. FT REGION 33 126 Beta-1. FT REGION 127 220 Beta-2. FT REGION 221 230 Connecting peptide. FT CARBOHYD 51 51 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 47 111 FT DISULFID 149 205 FT VARIANT 6 6 A -> S (in allele DQB1*05:01 and allele FT DQB1*05:02; dbSNP:rs1049056). FT /FTId=VAR_056570. FT VARIANT 12 12 G -> D (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*06:02 and allele FT DQB1*06:12; dbSNP:rs1049057). FT /FTId=VAR_062679. FT VARIANT 15 15 A -> V (in allele DQB1*03:02, allele FT DQB1*03:03, allele DQB1*04:01, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*06:02 and allele DQB1*06:12; FT dbSNP:rs3189152). FT {ECO:0000269|PubMed:3584986}. FT /FTId=VAR_062680. FT VARIANT 23 23 A -> S (in allele DQB1*02:01 and allele FT DQB1*02:02; dbSNP:rs3891176). FT /FTId=VAR_062681. FT VARIANT 24 24 M -> I (in allele DQB1*05:01 and allele FT DQB1*05:02; dbSNP:rs1049059). FT /FTId=VAR_062682. FT VARIANT 27 27 T -> A (in allele DQB1*04:01; FT dbSNP:rs1049060). FT /FTId=VAR_062683. FT VARIANT 27 27 T -> S (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*06:02 and allele FT DQB1*06:12; dbSNP:rs1049060). FT /FTId=VAR_062684. FT VARIANT 28 28 P -> L (in allele DQB1*06:02 and allele FT DQB1*06:12; dbSNP:rs1049062). FT /FTId=VAR_062685. FT VARIANT 28 28 P -> S (in allele DQB1*05:01 and allele FT DQB1*05:02; dbSNP:rs1049061). FT {ECO:0000269|PubMed:3584986}. FT /FTId=VAR_062686. FT VARIANT 29 29 V -> L (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*06:02 and allele FT DQB1*06:12; dbSNP:rs1130366). FT /FTId=VAR_062687. FT VARIANT 35 35 S -> P (in allele DQB1*06:01; FT dbSNP:rs12722106). FT /FTId=VAR_062688. FT VARIANT 41 41 Y -> F (in allele DQB1*04:01, allele FT DQB1*04:02, allele DQB1*04:03, allele FT DQB1*06:02, allele DQB1*06:10, allele FT DQB1*06:13, allele DQB1*06:14, allele FT DQB1*06:15, allele DQB1*06:16, allele FT DQB1*06:19, allele DQB1*06:20, allele FT DQB1*06:22, allele DQB1*06:23, allele FT DQB1*06:24, allele DQB1*06:29, allele FT DQB1*06:33 and allele DQB1*06:37; FT dbSNP:rs9274407). FT /FTId=VAR_062689. FT VARIANT 41 41 Y -> L (in allele DQB1*06:01 and allele FT DQB1*06:35; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062690. FT VARIANT 43 43 F -> L (in allele DQB1*06:33; FT dbSNP:rs56173496). FT /FTId=VAR_062691. FT VARIANT 45 45 A -> G (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*02:05, allele FT DQB1*03:02, allele DQB1*03:03, allele FT DQB1*03:05, allele DQB1*03:06, allele FT DQB1*03:07, allele DQB1*03:08, allele FT DQB1*03:11, allele DQB1*03:15, allele FT DQB1*03:17, allele DQB1*03:18, allele FT DQB1*03:20, allele DQB1*03:23, allele FT DQB1*03:25, allele DQB1*03:26, allele FT DQB1*04:01, allele DQB1*04:02, allele FT DQB1*04:03, allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:04, allele DQB1*05:05, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:07, allele DQB1*06:08, allele FT DQB1*06:09, allele DQB1*06:10, allele FT DQB1*06:11, allele DQB1*06:12, allele FT DQB1*06:13, allele DQB1*06:14, allele FT DQB1*06:15, allele DQB1*06:16, allele FT DQB1*06:17, allele DQB1*06:18, allele FT DQB1*06:19, allele DQB1*06:20, allele FT DQB1*06:21, allele DQB1*06:22, allele FT DQB1*06:23, allele DQB1*06:24, allele FT DQB1*06:25, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:29, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:34, allele DQB1*06:36, allele FT DQB1*06:37, allele DQB1*06:38 and allele FT DQB1*06:39; dbSNP:rs1130375). FT {ECO:0000269|PubMed:3584986}. FT /FTId=VAR_061472. FT VARIANT 46 46 M -> L (in allele DQB1*03:11, allele FT DQB1*03:26, allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:04, allele DQB1*05:05, allele FT DQB1*06:05, allele DQB1*06:20 and allele FT DQB1*06:31; dbSNP:rs1130368). FT /FTId=VAR_061473. FT VARIANT 55 55 R -> L (in allele DQB1*04:01; FT dbSNP:rs41540813). FT /FTId=VAR_062692. FT VARIANT 58 58 Y -> G (in allele DQB1*03:05, allele FT DQB1*03:17, allele DQB1*04:01, allele FT DQB1*04:02, allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:04, allele DQB1*05:05 and allele FT DQB1*06:23; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062693. FT VARIANT 58 58 Y -> L (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*02:05, allele FT DQB1*03:02, allele DQB1*03:03, allele FT DQB1*03:06, allele DQB1*03:07, allele FT DQB1*03:08, allele DQB1*03:11, allele FT DQB1*03:12, allele DQB1*03:15, allele FT DQB1*03:18, allele DQB1*03:20, allele FT DQB1*03:23, allele DQB1*03:25, allele FT DQB1*03:26, allele DQB1*04:03, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:06, allele DQB1*06:07, allele FT DQB1*06:08, allele DQB1*06:09, allele FT DQB1*06:10, allele DQB1*06:11, allele FT DQB1*06:12, allele DQB1*06:13, allele FT DQB1*06:14, allele DQB1*06:15, allele FT DQB1*06:16, allele DQB1*06:17, allele FT DQB1*06:18, allele DQB1*06:19, allele FT DQB1*06:20, allele DQB1*06:21, allele FT DQB1*06:22, allele DQB1*06:24, allele FT DQB1*06:25, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:29, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:34, allele DQB1*06:36, allele FT DQB1*06:37, allele DQB1*06:38 and allele FT DQB1*06:39; requires 2 nucleotide FT substitutions; dbSNP:rs766817072). FT {ECO:0000269|PubMed:3584986}. FT /FTId=VAR_062694. FT VARIANT 59 59 V -> L (in allele DQB1*03:18; FT dbSNP:rs41563539). FT /FTId=VAR_062695. FT VARIANT 60 60 T -> S (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04 and allele DQB1*02:05; FT dbSNP:rs9274405). FT /FTId=VAR_062696. FT VARIANT 62 62 Y -> H (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:05, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:07, allele FT DQB1*06:08, allele DQB1*06:14, allele FT DQB1*06:17, allele DQB1*06:21, allele FT DQB1*06:25, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:30, allele FT DQB1*06:31, allele DQB1*06:32, allele FT DQB1*06:34, allele DQB1*06:36, allele FT DQB1*06:38 and allele DQB1*06:39; FT dbSNP:rs281862065). FT /FTId=VAR_062697. FT VARIANT 62 62 Y -> S (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04 and allele DQB1*02:05). FT /FTId=VAR_062698. FT VARIANT 69 69 Y -> D (in allele DQB1*06:01 and allele FT DQB1*06:35; dbSNP:rs281874782). FT /FTId=VAR_062699. FT VARIANT 69 69 Y -> I (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04 and allele DQB1*02:05; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062700. FT VARIANT 70 70 A -> T (in allele DQB1*03:20; FT dbSNP:rs45519640). FT /FTId=VAR_062701. FT VARIANT 70 70 A -> V (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*02:05, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*05:03, allele DQB1*05:04, allele FT DQB1*06:01, allele DQB1*06:28 and allele FT DQB1*06:35; dbSNP:rs1063318). FT /FTId=VAR_062702. FT VARIANT 77 77 E -> G (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*02:05, allele FT DQB1*03:02, allele DQB1*03:03, allele FT DQB1*03:05, allele DQB1*03:06, allele FT DQB1*03:07, allele DQB1*03:08, allele FT DQB1*03:10, allele DQB1*03:11, allele FT DQB1*03:12, allele DQB1*03:14, allele FT DQB1*03:15, allele DQB1*03:17, allele FT DQB1*03:18, allele DQB1*03:20, allele FT DQB1*03:23, allele DQB1*03:25, allele FT DQB1*03:26, allele DQB1*04:01, allele FT DQB1*04:02, allele DQB1*04:03, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*05:03, allele DQB1*05:04, allele FT DQB1*05:05, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:06, allele DQB1*06:07, allele FT DQB1*06:08, allele DQB1*06:09, allele FT DQB1*06:10, allele DQB1*06:11, allele FT DQB1*06:12, allele DQB1*06:13, allele FT DQB1*06:14, allele DQB1*06:15, allele FT DQB1*06:16, allele DQB1*06:17, allele FT DQB1*06:18, allele DQB1*06:19, allele FT DQB1*06:20, allele DQB1*06:21, allele FT DQB1*06:22, allele DQB1*06:23, allele FT DQB1*06:24, allele DQB1*06:25, allele FT DQB1*06:27, allele DQB1*06:28, allele FT DQB1*06:29, allele DQB1*06:30, allele FT DQB1*06:31, allele DQB1*06:32, allele FT DQB1*06:33, allele DQB1*06:34, allele FT DQB1*06:36, allele DQB1*06:37, allele FT DQB1*06:38 and allele DQB1*06:39; FT dbSNP:rs1049083). FT {ECO:0000269|PubMed:3584986}. FT /FTId=VAR_062703. FT VARIANT 78 78 V -> E (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04 and allele DQB1*02:05; FT dbSNP:rs9274398). FT /FTId=VAR_062704. FT VARIANT 79 79 Y -> F (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04 and allele DQB1*02:05; FT dbSNP:rs9274397). FT /FTId=VAR_062705. FT VARIANT 81 81 A -> V (in allele DQB1*03:07; FT dbSNP:rs41558214). FT /FTId=VAR_062706. FT VARIANT 84 84 P -> L (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04 and allele DQB1*02:05; FT dbSNP:rs9274395). FT /FTId=VAR_062707. FT VARIANT 85 85 L -> Q (in allele DQB1*03:23, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*05:03, allele DQB1*05:04, allele FT DQB1*05:05, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:06, allele DQB1*06:07, allele FT DQB1*06:08, allele DQB1*06:09, allele FT DQB1*06:10, allele DQB1*06:11, allele FT DQB1*06:12, allele DQB1*06:13, allele FT DQB1*06:14, allele DQB1*06:15, allele FT DQB1*06:16, allele DQB1*06:17, allele FT DQB1*06:18, allele DQB1*06:20, allele FT DQB1*06:22, allele DQB1*06:21, allele FT DQB1*06:23, allele DQB1*06:24, allele FT DQB1*06:25, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:29, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:34, allele DQB1*06:36, allele FT DQB1*06:37, allele DQB1*06:38 and allele FT DQB1*06:39; dbSNP:rs1140313). FT /FTId=VAR_062708. FT VARIANT 87 87 P -> L (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04 and allele DQB1*02:05; FT dbSNP:rs1130380). FT /FTId=VAR_062709. FT VARIANT 87 87 P -> Q (in allele DQB1*03:16; FT dbSNP:rs1130380). FT /FTId=VAR_062710. FT VARIANT 87 87 P -> R (in allele DQB1*03:23, allele FT DQB1*03:25, allele DQB1*04:01, allele FT DQB1*04:02, allele DQB1*04:03, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*05:03, allele DQB1*05:04, allele FT DQB1*05:05, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:06, allele DQB1*06:07, allele FT DQB1*06:08, allele DQB1*06:09, allele FT DQB1*06:10, allele DQB1*06:11, allele FT DQB1*06:12, allele DQB1*06:13, allele FT DQB1*06:14, allele DQB1*06:15, allele FT DQB1*06:16, allele DQB1*06:17, allele FT DQB1*06:18, allele DQB1*06:19, allele FT DQB1*06:20, allele DQB1*06:21, allele FT DQB1*06:22, allele DQB1*06:23, allele FT DQB1*06:24, allele DQB1*06:25, allele FT DQB1*06:27, allele DQB1*06:28, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:34, allele DQB1*06:35, allele FT DQB1*06:36, allele DQB1*06:37, allele FT DQB1*06:38 and allele DQB1*06:39; FT dbSNP:rs1130380). FT /FTId=VAR_062711. FT VARIANT 88 88 P -> L (in allele DQB1*03:25, allele FT DQB1*04:01, allele DQB1*04:02 and allele FT DQB1*04:03; dbSNP:rs1130381). FT /FTId=VAR_062712. FT VARIANT 89 89 D -> A (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:04, allele FT DQB1*02:05, allele DQB1*03:02, allele FT DQB1*03:04, allele DQB1*03:05, allele FT DQB1*03:07, allele DQB1*03:08, allele FT DQB1*03:11, allele DQB1*03:14, allele FT DQB1*03:18 and allele DQB1*06:29; FT dbSNP:rs1071637). FT /FTId=VAR_062713. FT VARIANT 89 89 D -> S (in allele DQB1*05:02, allele FT DQB1*05:04, allele DQB1*05:05, allele FT DQB1*06:10 and allele DQB1*06:25; FT requires 2 nucleotide substitutions). FT /FTId=VAR_062714. FT VARIANT 89 89 D -> V (in allele DQB1*05:01, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:06, allele DQB1*06:08, allele FT DQB1*06:09, allele DQB1*06:12, allele FT DQB1*06:13, allele DQB1*06:17, allele FT DQB1*06:18, allele DQB1*06:21, allele FT DQB1*06:22, allele DQB1*06:27, allele FT DQB1*06:34, allele DQB1*06:36, allele FT DQB1*06:38 and allele DQB1*06:39; FT dbSNP:rs1071637). FT /FTId=VAR_062715. FT VARIANT 92 92 Y -> N (in allele DQB1*06:16; FT dbSNP:rs41562414). FT /FTId=VAR_062716. FT VARIANT 94 94 N -> K (in allele DQB1*06:37; FT dbSNP:rs1130382). FT /FTId=VAR_062717. FT VARIANT 95 95 S -> R (in allele DQB1*03:15; FT dbSNP:rs41556215). FT /FTId=VAR_062718. FT VARIANT 98 98 E -> D (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*02:05, allele FT DQB1*03:06, allele DQB1*03:25, allele FT DQB1*04:01, allele DQB1*04:02, allele FT DQB1*04:03, allele DQB1*05:04, allele FT DQB1*06:01 and allele DQB1*06:35; FT dbSNP:rs9274390). FT /FTId=VAR_062719. FT VARIANT 99 99 V -> D (in allele DQB1*03:13; FT dbSNP:rs41563814). FT /FTId=VAR_062720. FT VARIANT 99 99 V -> I (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*02:05, allele FT DQB1*03:06, allele DQB1*03:25, allele FT DQB1*04:01, allele DQB1*04:02, allele FT DQB1*04:03, allele DQB1*05:04, allele FT DQB1*06:01 and allele DQB1*06:35; FT dbSNP:rs9274390). FT /FTId=VAR_062721. FT VARIANT 102 102 R -> E (in allele DQB1*03:06, allele FT DQB1*03:25, allele DQB1*04:01, allele FT DQB1*04:02, allele DQB1*04:03 and allele FT DQB1*05:04; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062722. FT VARIANT 102 102 R -> G (in allele DQB1*03:08, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*05:03, allele DQB1*05:05, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:08, allele DQB1*06:10, allele FT DQB1*06:11, allele DQB1*06:12, allele FT DQB1*06:13, allele DQB1*06:14, allele FT DQB1*06:16, allele DQB1*06:17, allele FT DQB1*06:19, allele DQB1*06:20, allele FT DQB1*06:21, allele DQB1*06:23, allele FT DQB1*06:24, allele DQB1*06:28, allele FT DQB1*06:29, allele DQB1*06:30, allele FT DQB1*06:31 and allele DQB1*06:33; FT dbSNP:rs1130386). FT {ECO:0000269|PubMed:3584986}. FT /FTId=VAR_062723. FT VARIANT 103 103 T -> A (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:05, allele DQB1*06:17, allele FT DQB1*06:24 and allele DQB1*06:30; FT dbSNP:rs1130390). FT /FTId=VAR_062724. FT VARIANT 103 103 T -> D (in allele DQB1*03:06, allele FT DQB1*03:25, allele DQB1*04:01, allele FT DQB1*04:02, allele DQB1*04:03 and allele FT DQB1*05:04; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062725. FT VARIANT 103 103 T -> K (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04 and allele DQB1*02:05). FT /FTId=VAR_062726. FT VARIANT 106 106 E -> A (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*02:05 and allele FT DQB1*06:06; dbSNP:rs1130387). FT /FTId=VAR_062727. FT VARIANT 106 106 E -> S (in allele DQB1*03:06, allele FT DQB1*03:25, allele DQB1*04:01, allele FT DQB1*04:02, allele DQB1*04:03, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*05:03, allele DQB1*05:04 and allele FT DQB1*05:05; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062728. FT VARIANT 107 107 L -> V (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*02:05, allele FT DQB1*03:06, allele DQB1*03:25, allele FT DQB1*04:01, allele DQB1*04:02, allele FT DQB1*04:03, allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:04, allele DQB1*05:05 and allele FT DQB1*06:06; dbSNP:rs9274384). FT /FTId=VAR_062729. FT VARIANT 109 109 T -> R (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:03, allele FT DQB1*02:04, allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:04, allele DQB1*05:05 and allele FT DQB1*06:06; dbSNP:rs1130392). FT /FTId=VAR_062730. FT VARIANT 116 116 Q -> E (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:05, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:07, allele DQB1*06:08, allele FT DQB1*06:09, allele DQB1*06:10, allele FT DQB1*06:11, allele DQB1*06:12, allele FT DQB1*06:13, allele DQB1*06:14, allele FT DQB1*06:15, allele DQB1*06:16, allele FT DQB1*06:17, allele DQB1*06:18, allele FT DQB1*06:19, allele DQB1*06:20, allele FT DQB1*06:21, allele DQB1*06:22, allele FT DQB1*06:23, allele DQB1*06:24, allele FT DQB1*06:25, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:29, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:34, allele DQB1*06:35, allele FT DQB1*06:36, allele DQB1*06:37, allele FT DQB1*06:38, allele DQB1*06:39; FT dbSNP:rs1140316). FT /FTId=VAR_062731. FT VARIANT 117 117 L -> V (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:05, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:07, allele DQB1*06:08, allele FT DQB1*06:09, allele DQB1*06:10, allele FT DQB1*06:11, allele DQB1*06:12, allele FT DQB1*06:13, allele DQB1*06:14, allele FT DQB1*06:15, allele DQB1*06:16, allele FT DQB1*06:17, allele DQB1*06:18, allele FT DQB1*06:19, allele DQB1*06:20, allele FT DQB1*06:21, allele DQB1*06:22, allele FT DQB1*06:23, allele DQB1*06:24, allele FT DQB1*06:25, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:29, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:34, allele DQB1*06:35, allele FT DQB1*06:36, allele DQB1*06:37, allele FT DQB1*06:38 and allele DQB1*06:39; FT dbSNP:rs1140317). FT /FTId=VAR_062732. FT VARIANT 118 118 E -> A (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:05, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:08, allele DQB1*06:10, allele FT DQB1*06:11, allele DQB1*06:13, allele FT DQB1*06:14, allele DQB1*06:16, allele FT DQB1*06:18, allele DQB1*06:19, allele FT DQB1*06:20, allele DQB1*06:23, allele FT DQB1*06:24, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:29, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:35 and allele DQB1*06:37; FT dbSNP:rs9274380). FT /FTId=VAR_062733. FT VARIANT 118 118 E -> G (in allele DQB1*06:04, allele FT DQB1*06:05, allele DQB1*06:07, allele FT DQB1*06:09, allele DQB1*06:12, allele FT DQB1*06:15, allele DQB1*06:17, allele FT DQB1*06:21, allele DQB1*06:22, allele FT DQB1*06:25, allele DQB1*06:34, allele FT DQB1*06:36, allele DQB1*06:38 and allele FT DQB1*06:39; dbSNP:rs9274380). FT /FTId=VAR_062734. FT VARIANT 119 119 L -> F (in allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:08, allele DQB1*06:10, allele FT DQB1*06:11, allele DQB1*06:13, allele FT DQB1*06:14, allele DQB1*06:16, allele FT DQB1*06:18, allele DQB1*06:19, allele FT DQB1*06:20, allele DQB1*06:23, allele FT DQB1*06:24, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:29, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:35 and allele DQB1*06:37; FT dbSNP:rs9274379). FT /FTId=VAR_062735. FT VARIANT 119 119 L -> Y (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:05, allele DQB1*06:04, allele FT DQB1*06:05, allele DQB1*06:07, allele FT DQB1*06:09, allele DQB1*06:12, allele FT DQB1*06:15, allele DQB1*06:17, allele FT DQB1*06:21, allele DQB1*06:22, allele FT DQB1*06:25, allele DQB1*06:34, allele FT DQB1*06:36, allele DQB1*06:38 and allele FT DQB1*06:39; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062736. FT VARIANT 121 121 T -> G (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:05, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:07, allele DQB1*06:08, allele FT DQB1*06:09, allele DQB1*06:10, allele FT DQB1*06:11, allele DQB1*06:12, allele FT DQB1*06:13, allele DQB1*06:14, allele FT DQB1*06:15, allele DQB1*06:16, allele FT DQB1*06:17, allele DQB1*06:18, allele FT DQB1*06:19, allele DQB1*06:21, allele FT DQB1*06:22, allele DQB1*06:23, allele FT DQB1*06:24, allele DQB1*06:25, allele FT DQB1*06:27, allele DQB1*06:28, allele FT DQB1*06:29, allele DQB1*06:30, allele FT DQB1*06:31, allele DQB1*06:32, allele FT DQB1*06:33, allele DQB1*06:34, allele FT DQB1*06:35, allele DQB1*06:36, allele FT DQB1*06:37, allele DQB1*06:38 and allele FT DQB1*06:39; requires 2 nucleotide FT substitutions). FT /FTId=VAR_062737. FT VARIANT 122 122 T -> I (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*05:05, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:05, allele FT DQB1*06:07, allele DQB1*06:08, allele FT DQB1*06:09, allele DQB1*06:10, allele FT DQB1*06:11, allele DQB1*06:12, allele FT DQB1*06:14, allele DQB1*06:15, allele FT DQB1*06:16, allele DQB1*06:17, allele FT DQB1*06:18, allele DQB1*06:19, allele FT DQB1*06:21, allele DQB1*06:22, allele FT DQB1*06:23, allele DQB1*06:24, allele FT DQB1*06:25, allele DQB1*06:27, allele FT DQB1*06:28, allele DQB1*06:29, allele FT DQB1*06:30, allele DQB1*06:31, allele FT DQB1*06:32, allele DQB1*06:33, allele FT DQB1*06:34, allele DQB1*06:35, allele FT DQB1*06:36, allele DQB1*06:37, allele FT DQB1*06:38 and allele DQB1*06:39; FT dbSNP:rs1140320). FT /FTId=VAR_062738. FT VARIANT 148 148 V -> I (in allele DQB1*05:01, allele FT DQB1*05:02 and allele DQB1*05:03; FT dbSNP:rs1049100). FT /FTId=VAR_056571. FT VARIANT 157 157 A -> G (in allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:09, allele FT DQB1*06:12, allele DQB1*06:34, allele FT DQB1*06:36, allele DQB1*06:38 and allele FT DQB1*06:39; dbSNP:rs1063322). FT /FTId=VAR_062739. FT VARIANT 157 157 A -> S (in allele DQB1*05:01, allele FT DQB1*05:02 and allele DQB1*05:03). FT /FTId=VAR_062740. FT VARIANT 158 158 Q -> H (in allele DQB1*05:02; FT dbSNP:rs41542812). FT /FTId=VAR_062741. FT VARIANT 162 162 R -> Q (in allele DQB1*03:22, allele FT DQB1*06:04, allele DQB1*06:09, allele FT DQB1*06:12, allele DQB1*06:34, allele FT DQB1*06:36 and allele DQB1*06:38; FT dbSNP:rs41544112). FT /FTId=VAR_062742. FT VARIANT 165 165 R -> Q (in allele DQB1*06:38; FT dbSNP:rs9273989). FT /FTId=VAR_062744. FT VARIANT 165 165 R -> W (in allele DQB1*03:21; FT dbSNP:rs63626961). FT /FTId=VAR_062743. FT VARIANT 167 167 D -> G (in allele DQB1*02:02; FT dbSNP:rs2647032). FT /FTId=VAR_062745. FT VARIANT 168 168 Q -> E (in allele DQB1*02:04; FT dbSNP:rs9273981). FT /FTId=VAR_062746. FT VARIANT 172 172 T -> A (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:04, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*05:03, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:09, allele FT DQB1*06:12, allele DQB1*06:34, allele FT DQB1*06:36, allele DQB1*06:38 and allele FT DQB1*06:39; dbSNP:rs1063323). FT {ECO:0000244|PubMed:21269460}. FT /FTId=VAR_062747. FT VARIANT 194 194 E -> D (in dbSNP:rs9273952). FT /FTId=VAR_056572. FT VARIANT 197 197 P -> L (in dbSNP:rs9273948). FT /FTId=VAR_059522. FT VARIANT 199 199 H -> R (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:04, allele FT DQB1*03:02, allele DQB1*03:03, allele FT DQB1*03:05, allele DQB1*03:23, allele FT DQB1*03:25, allele DQB1*04:01, allele FT DQB1*04:02, allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:09, allele FT DQB1*06:12, allele DQB1*06:34, allele FT DQB1*06:36, allele DQB1*06:38 and allele FT DQB1*06:39; dbSNP:rs701564). FT {ECO:0000269|PubMed:3584986}. FT /FTId=VAR_062748. FT VARIANT 200 201 GD -> A (in allele DQB1*03:09). FT /FTId=VAR_062749. FT VARIANT 202 202 V -> I (in allele DQB1*03:24; FT dbSNP:rs80255621). FT /FTId=VAR_062750. FT VARIANT 214 214 N -> S (in allele DQB1*02:01, allele FT DQB1*02:02, allele DQB1*02:04, allele FT DQB1*05:01, allele DQB1*05:02, allele FT DQB1*05:03, allele DQB1*06:01, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:09, allele FT DQB1*06:12, allele DQB1*06:34, allele FT DQB1*06:36, allele DQB1*06:38 and allele FT DQB1*06:39; dbSNP:rs1130398). FT /FTId=VAR_062751. FT VARIANT 217 217 T -> I (in allele DQB1*03:02, allele FT DQB1*03:03, allele DQB1*03:05, allele FT DQB1*03:19, allele DQB1*03:25, allele FT DQB1*04:01 and allele DQB1*04:02; FT dbSNP:rs1130399). FT /FTId=VAR_062752. FT VARIANT 218 218 V -> A (in allele DQB1*06:36; FT dbSNP:rs281864132). FT /FTId=VAR_062753. FT VARIANT 229 229 S -> N (in allele DQB1*06:01; FT dbSNP:rs1130429). FT /FTId=VAR_062754. FT VARIANT 235 235 I -> V (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*06:02, allele DQB1*06:03, allele FT DQB1*06:04, allele DQB1*06:09, allele FT DQB1*06:12 and allele DQB1*06:36; FT dbSNP:rs1049163). FT /FTId=VAR_062755. FT VARIANT 252 252 H -> R (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*06:01, allele DQB1*06:02, allele FT DQB1*06:03, allele DQB1*06:04, allele FT DQB1*06:09, allele DQB1*06:12 and allele FT DQB1*06:36; dbSNP:rs1140342). FT /FTId=VAR_062756. FT VARIANT 253 253 H -> Q (in allele DQB1*05:01, allele FT DQB1*05:02, allele DQB1*05:03, allele FT DQB1*06:01, allele DQB1*06:02, allele FT DQB1*06:03, allele DQB1*06:04, allele FT DQB1*06:09, allele DQB1*06:12 and allele FT DQB1*06:36; dbSNP:rs1140343). FT /FTId=VAR_062757. FT VARIANT 256 256 Q -> R (in allele DQB1*05:01, allele FT DQB1*05:02 and allele DQB1*05:03; FT dbSNP:rs1130432). FT /FTId=VAR_061474. FT CONFLICT 111 111 C -> S (in Ref. 71; AAD39697). FT {ECO:0000305}. FT CONFLICT 113 113 H -> Q (in Ref. 22; AAF28315). FT {ECO:0000305}. FT CONFLICT 173 173 G -> A (in Ref. 24; X76553/X76554). FT {ECO:0000305}. FT CONFLICT 214 214 N -> T (in Ref. 8; AAA59770). FT {ECO:0000305}. FT STRAND 40 50 {ECO:0000244|PDB:1UVQ}. FT TURN 51 54 {ECO:0000244|PDB:1UVQ}. FT STRAND 55 64 {ECO:0000244|PDB:1UVQ}. FT STRAND 67 73 {ECO:0000244|PDB:1UVQ}. FT TURN 74 76 {ECO:0000244|PDB:1UVQ}. FT STRAND 78 83 {ECO:0000244|PDB:1UVQ}. FT HELIX 84 86 {ECO:0000244|PDB:1UVQ}. FT HELIX 87 94 {ECO:0000244|PDB:1UVQ}. FT HELIX 97 109 {ECO:0000244|PDB:1UVQ}. FT HELIX 111 117 {ECO:0000244|PDB:1UVQ}. FT HELIX 119 122 {ECO:0000244|PDB:1UVQ}. FT STRAND 130 135 {ECO:0000244|PDB:1UVQ}. FT STRAND 141 144 {ECO:0000244|PDB:1JK8}. FT STRAND 146 157 {ECO:0000244|PDB:1UVQ}. FT STRAND 160 165 {ECO:0000244|PDB:1UVQ}. FT STRAND 168 170 {ECO:0000244|PDB:1UVQ}. FT STRAND 174 176 {ECO:0000244|PDB:1UVQ}. FT STRAND 183 185 {ECO:0000244|PDB:1UVQ}. FT STRAND 187 194 {ECO:0000244|PDB:1UVQ}. FT STRAND 203 208 {ECO:0000244|PDB:1UVQ}. FT STRAND 216 220 {ECO:0000244|PDB:1UVQ}. SQ SEQUENCE 261 AA; 29991 MW; 79B1E571A628CF96 CRC64; MSWKKALRIP GGLRAATVTL MLAMLSTPVA EGRDSPEDFV YQFKAMCYFT NGTERVRYVT RYIYNREEYA RFDSDVEVYR AVTPLGPPDA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQHG DVYTCHVEHP SLQNPITVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IHHRSQKGLL H // ID DQB2_HUMAN Reviewed; 268 AA. AC P05538; A6NIA5; Q29826; Q29870; Q29871; Q29872; Q29873; Q5SR06; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 2. DT 12-SEP-2018, entry version 163. DE RecName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain; DE AltName: Full=HLA class II histocompatibility antigen, DX beta chain; DE AltName: Full=MHC class II antigen DQB2; DE Flags: Precursor; GN Name=HLA-DQB2; Synonyms=HLA-DXB; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3036828; RA Jonsson A.-K., Hyldig-Nielsen J.-J., Servenius B., Larhammar D., RA Andersson G., Joergensen F., Peterson P.A., Rask L.; RT "Class II genes of the human major histocompatibility complex. RT Comparisons of the DQ and DX alpha and beta genes."; RL J. Biol. Chem. 262:8767-8777(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8568858; DOI=10.1006/jmbi.1996.0001; RA Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., RA Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., RA Radley E., Thorpe K.L., Trowsdale J.; RT "Evolutionary dynamics of non-coding sequences within the class II RT region of the human MHC."; RL J. Mol. Biol. 255:1-13(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP GLN-161. RC TISSUE=Squamous cell carcinoma; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-125. RX PubMed=3858830; DOI=10.1073/pnas.82.10.3410; RA Okada K., Boss J.M., Prentice H., Spies T., Mengler R., Auffray C., RA Lillie J.W., Grossberger D., Strominger J.L.; RT "Gene organization of DC and DX subregions of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 82:3410-3414(1985). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-125. RX PubMed=2564844; DOI=10.1007/BF00717908; RA Berdoz J., Tiercy J.-M., Rollini P., Mach B., Gorski J.; RT "Remarkable sequence conservation of the HLA-DQB2 locus (DX beta) RT within the highly polymorphic DQ subregion of the human MHC."; RL Immunogenetics 29:241-248(1989). RN [7] RP LACK OF EXPRESSION. RX PubMed=9036956; RA Rudy G.B., Lew A.M.; RT "The nonpolymorphic MHC class II isotype, HLA-DQA2, is expressed on RT the surface of B lymphoblastoid cells."; RL J. Immunol. 158:2116-2125(1997). RN [8] RP LACK OF EXPRESSION. RX PubMed=11334674; DOI=10.1016/S0198-8859(01)00236-1; RA Indovina P., Megiorni F., Fontemaggi G., Coni P., Mora B., RA Mazzilli M.C.; RT "Absence of in vivo DNA-protein interactions in the DQA2 and DQB2 RT promoter regions."; RL Hum. Immunol. 62:504-508(2001). RN [9] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [10] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [11] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [12] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [13] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [14] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [15] RP FUNCTION, INTERACTION WITH CD74; HLA-DMA; HLA-DQA1 AND HLA-DQA2, RP VARIANTS GLN-161; GLY-232 AND VAL-234, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=22407913; DOI=10.4049/jimmunol.1103048; RA Lenormand C., Bausinger H., Gross F., Signorino-Gelo F., Koch S., RA Peressin M., Fricker D., Cazenave J.P., Bieber T., Hanau D., RA de la Salle H., Tourne S.; RT "HLA-DQA2 and HLA-DQB2 genes are specifically expressed in human RT Langerhans cells and encode a new HLA class II molecule."; RL J. Immunol. 188:3903-3911(2012). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. {ECO:0000269|PubMed:22407913}. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. Dimer formation with HLA-DQA2, but not CC with HLA-DQA1, is required for efficient exit from the endoplasmic CC reticulum (ER). In the ER, forms a heterononamer; 3 MHC class II CC molecules bind to a CD74 homotrimer (also known as invariant chain CC or HLA class II histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. Association with CC HLA-DMA also occurs in skin Langerhans cells, in post-Golgi CC compartments. {ECO:0000269|PubMed:22407913}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22407913}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:22407913}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:22407913}. Endosome membrane CC {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:22407913}. Lysosome membrane CC {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:22407913}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P05538-1; Sequence=Displayed; CC Name=2; CC IsoId=P05538-2; Sequence=VSP_045914, VSP_045915; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Restricted to skin Langerhans cells (at CC protein level). {ECO:0000269|PubMed:22407913}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA60790.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M29614; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M29615; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X87344; CAA60790.1; ALT_INIT; Genomic_DNA. DR EMBL; AL671681; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL672104; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL713890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC031995; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; M11136; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M24920; AAA52667.1; -; Genomic_DNA. DR EMBL; M24921; AAA52668.1; -; Genomic_DNA. DR EMBL; M24922; AAA52669.1; -; Genomic_DNA. DR EMBL; M24923; AAA52670.1; -; Genomic_DNA. DR CCDS; CCDS56419.1; -. [P05538-2] DR PIR; D29312; D29312. DR PIR; G35058; G35058. DR RefSeq; NP_001185787.1; NM_001198858.1. [P05538-2] DR UniGene; Hs.731563; -. DR ProteinModelPortal; P05538; -. DR SMR; P05538; -. DR BioGrid; 109365; 9. DR iPTMnet; P05538; -. DR PhosphoSitePlus; P05538; -. DR BioMuta; HLA-DQB2; -. DR DMDM; 122271; -. DR PeptideAtlas; P05538; -. DR PRIDE; P05538; -. DR ProteomicsDB; 51844; -. DR Ensembl; ENST00000399661; ENSP00000382569; ENSG00000196610. DR Ensembl; ENST00000411527; ENSP00000390431; ENSG00000232629. [P05538-2] DR Ensembl; ENST00000426733; ENSP00000393969; ENSG00000226165. [P05538-2] DR Ensembl; ENST00000430849; ENSP00000389067; ENSG00000228813. DR Ensembl; ENST00000432486; ENSP00000410132; ENSG00000228254. DR Ensembl; ENST00000438757; ENSP00000408884; ENSG00000224305. [P05538-2] DR Ensembl; ENST00000456529; ENSP00000399594; ENSG00000230675. [P05538-2] DR Ensembl; ENST00000457432; ENSP00000396502; ENSG00000229493. DR GeneID; 3120; -. DR KEGG; hsa:3120; -. DR UCSC; uc003oby.5; human. [P05538-1] DR CTD; 3120; -. DR DisGeNET; 3120; -. DR EuPathDB; HostDB:ENSG00000232629.8; -. DR GeneCards; HLA-DQB2; -. DR H-InvDB; HIX0165918; -. DR H-InvDB; HIX0166089; -. DR H-InvDB; HIX0166694; -. DR H-InvDB; HIX0167203; -. DR HGNC; HGNC:4945; HLA-DQB2. DR MIM; 615161; gene. DR neXtProt; NX_P05538; -. DR OpenTargets; ENSG00000232629; -. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR InParanoid; P05538; -. DR PhylomeDB; P05538; -. DR TreeFam; TF336626; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SIGNOR; P05538; -. DR ChiTaRS; HLA-DQB2; human. DR GeneWiki; HLA-DQB2; -. DR GenomeRNAi; 3120; -. DR PRO; PR:P05538; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000232629; Expressed in 120 organ(s), highest expression level in skin of abdomen. DR ExpressionAtlas; P05538; baseline and differential. DR Genevisible; P05538; HS. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome. DR GO; GO:0042613; C:MHC class II protein complex; NAS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0006955; P:immune response; NAS:UniProtKB. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Complete proteome; KW Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein; KW Golgi apparatus; Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1 32 FT CHAIN 33 268 HLA class II histocompatibility antigen, FT DQ beta 2 chain. FT /FTId=PRO_0000018992. FT TOPO_DOM 33 229 Extracellular. {ECO:0000255}. FT TRANSMEM 230 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 268 Cytoplasmic. {ECO:0000255}. FT DOMAIN 128 216 Ig-like C1-type. FT REGION 33 126 Beta-1. FT REGION 127 229 Beta-2. FT CARBOHYD 51 51 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 47 110 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 148 204 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT VAR_SEQ 1 4 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045914. FT VAR_SEQ 221 257 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_045915. FT VARIANT 161 161 R -> Q (in dbSNP:rs1049110). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:22407913}. FT /FTId=VAR_069445. FT VARIANT 232 232 S -> G. {ECO:0000269|PubMed:22407913}. FT /FTId=VAR_069446. FT VARIANT 234 234 I -> V. {ECO:0000269|PubMed:22407913}. FT /FTId=VAR_069447. FT CONFLICT 106 106 V -> L (in Ref. 6; AAA52667/AAA52668/ FT AAA52669/AAA52670). {ECO:0000305}. FT CONFLICT 266 268 LLH -> HLL (in Ref. 2; CAA60790). FT {ECO:0000305}. SQ SEQUENCE 268 AA; 30387 MW; 2746ED6CC5D44AF2 CRC64; MSWKMALQIP GGFWAAAVTV MLVMLSTPVA EARDFPKDFL VQFKGMCYFT NGTERVRGVA RYIYNREEYG RFDSDVGEFQ AVTELGRSIE DWNNYKDFLE QERAAVDKVC RHNYEAELRT TLQRQVEPTV TISPSRTEAL NHHNLLVCSV TDFYPAQIKV RWFRNDQEET AGVVSTSLIR NGDWTFQILV MLEITPQRGD IYTCQVEHPS LQSPITVEWR AQSESAQSKM LSGIGGFVLG LIFLGLGLII RHRGQKGPRG PPPAGLLH // ID DRB3_HUMAN Reviewed; 266 AA. AC P79483; A0ZXY9; A7MA46; B5AU12; B5AU13; B5AU14; B8YAC6; C6H115; AC C6H116; O02875; O19590; O46701; O46794; O78049; O78162; P01913; AC P79663; Q29721; Q29809; Q2PPD0; Q30144; Q507L8; Q5SP44; Q5STE0; AC Q6YJU6; Q70M87; Q7YQ62; Q860I9; Q8SP69; Q8WLT7; Q8WLT8; Q95359; AC Q95HM8; Q95IE5; Q96H16; Q9BCP3; Q9BD18; Q9MYA4; Q9MYH3; Q9MYH4; AC Q9TP01; Q9TP02; Q9TPB5; Q9TQ21; Q9UIN3; Q9UIN5; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 20-JUN-2018, entry version 148. DE RecName: Full=HLA class II histocompatibility antigen, DR beta 3 chain; DE AltName: Full=MHC class II antigen DRB3; DE Flags: Precursor; GN Name=HLA-DRB3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*02:01). RX PubMed=11894954; RA Long E.O., Wake C.T., Gorski J., Mach B.; RT "Complete sequence of an HLA-DR beta chain deduced from a cDNA clone RT and identification of multiple non-allelic DR beta chain genes."; RL EMBO J. 2:389-394(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE DRB3*01:01). RX PubMed=3459965; DOI=10.1038/322067a0; RA Gorski J., Mach B.; RT "Polymorphism of human Ia antigens: gene conversion between two DR RT beta loci results in a new HLA-D/DR specificity."; RL Nature 322:67-70(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*01:01). RC TISSUE=Blood; RX PubMed=9234492; DOI=10.1111/j.1399-0039.1997.tb02818.x; RA Martinez-Quiles N., Martin-Villa J.M., Martinez-Laso J., RA Perez-Blas M., Ferre-Lopez S., Moreno-Pelayo M.A., Alvarez-Tejado M., RA Arnaiz-Villena A.; RT "Description of two new HLA-DRB alleles (DRB1*0310 and DRB3*01012) RT found in a Spanish infant."; RL Tissue Antigens 49:658-661(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*01:01), AND NUCLEOTIDE RP SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DRB3*01:04). RC TISSUE=Blood; RX PubMed=10902611; DOI=10.1034/j.1399-0039.2000.550606.x; RA Coquillard G.J., Tang T.F., Steiner N., Perlee L., Ng J., RA Hartzman R.J., Hurley C.K.; RT "DRB3 alleles with variations in the annealing sites of commonly used RT amplification primers."; RL Tissue Antigens 55:558-563(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*01:01). RA Kim K.H., Kang J.H., Maeng C.Y., Han H., Park J.H., Hahm K.S., RA Kim K.L.; RT "Cloning and nucleotide sequence analysis of HLA-DRB3*01012 from EBV- RT transformed Korean B-cell line by sequence based typing."; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*03:01). RA Spierings E., Zegveld S.T., Goulmy E.; RT "HLA-DRB3*03011 sequence complete mRNA."; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB3*02:01). RA Mach B.F., Long E.O., Wake C.T.; RT "DNA sequences coding for the DR beta-chain locus of the human RT lymphocyte antigen complex and polypeptides, diagnostic typing RT processes and products related thereto."; RL Patent number EP0103960, 28-MAR-1984. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELES DRB3*01:01 AND RP DRB3*02:02). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELES DRB3*01:01 AND RP DRB3*02:02). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB3*02:01). RX PubMed=6414998; DOI=10.1016/0198-8859(83)90089-7; RA Long E.O., Gorski J., Rollini P., Wake C.T., Strubin M., RA Rabourdin-Combe C., Mach B.; RT "Molecular analysis of the genes for human class II antigens of the RT major histocompatibility complex."; RL Hum. Immunol. 8:113-121(1983). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELE DRB3*02:01). RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELES DRB3*02:10 AND RP DRB3*02:11). RX PubMed=11098940; DOI=10.1034/j.1399-0039.2000.560412.x; RA Balas A., Santos S., Aviles M.J., Garcia-Sanchez F., Lillo R., RA Vicario J.L.; RT "Identification by sequencing based typing and complete coding region RT analysis of three new HLA class II alleles: DRB3*0210, DRB3*0211 and RT DQB1*0310."; RL Tissue Antigens 56:380-384(2000). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB3*02:24). RA Westerink N., Bacelar M., Arts-Hilkes Y., Mulder W., Rozemuller E.H.; RT "A new HLA-DRB3*02 allele identified by sequencing based typing."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-124 (ALLELE DRB3*02:18). RX PubMed=15140047; DOI=10.1111/j.0001-2815.2004.00196.x; RA Balas A., Aviles M.J., Lillo R., Alonso-Nieto M., Zarapuz L., RA Garcia-Villaescusa R., Garcia-Sanchez F., Vicario J.L.; RT "Sequencing of two new HLA class II alleles: DRB3*0218 and RT DQB1*030202."; RL Tissue Antigens 63:614-616(2004). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:09). RX PubMed=10958362; DOI=10.1034/j.1399-0039.2000.560113.x; RA Morabito A., Pera C., Longo A., Delfino L., Ferrara G.B.; RT "Identification of a new DRB3*02 allelic variant (DRB3*0209) by high- RT resolution sequence-based typing."; RL Tissue Antigens 56:90-94(2000). RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*01:05). RX PubMed=11972885; DOI=10.1034/j.1399-0039.2002.590115.x; RA Tang T.F., Lin Y.-S., Robbins F.M., Li L., Sintasath D., RA Coquillard G., Huang A., Heine U., Ng J., Hartzman R.J., Hurley C.K.; RT "Description of fourteen new DRB alleles found in a stem cell donor RT registry."; RL Tissue Antigens 59:63-65(2002). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:19). RX PubMed=15496209; DOI=10.1111/j.1399-0039.2004.00296.x; RA Dubois V., Favre-Victoire I., Gebuhrer L.; RT "Three new DRB alleles routinely identified by sequence-based typing: RT DRB1*010103, DRB1*0326 and DRB3*0219."; RL Tissue Antigens 64:621-623(2004). RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:23). RC TISSUE=Peripheral blood; RX PubMed=18764810; DOI=10.1111/j.1399-0039.2008.01124.x; RA Danzer M., Polin H., Hofer K., Proll J., Gabriel C.; RT "Characterisation of two novel HLA alleles, HLA-Cw*0429 and HLA- RT DRB3*0223."; RL Tissue Antigens 72:498-499(2008). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB3*01:01; RP DRB3*01:12 AND DRB3*01:13). RX PubMed=19000136; DOI=10.1111/j.1399-0039.2008.01158.x; RA Lee K.W., Jung Y.A.; RT "Description of three novel HLA-DRB3 alleles: DRB3*010105, DRB3*0112 RT and DRB3*0113."; RL Tissue Antigens 73:83-84(2009). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:04). RA Keller E.; RT "New DRB3*02 variant."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB3*02:12 AND RP DRB3*02:13). RA Greville W.D., Ng G., Kennedy A., Dunckley H.; RT "An HLA-DRB3 allele detected by SBT."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:14). RA Moine A.; RT "A new HLA DRB3* allele very similar to DRB3*02021 and DRB3*0212 RT alleles."; RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases. RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:15). RA Varney M.; RT "A novel DRB3 allele."; RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases. RN [24] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:16). RA Avergas C.U., Iglehart B.A., Leffell M.S.; RT "Identification of a novel DRB3*0216 allele."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [25] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:17). RA Hogbin J.-P., Chapman G., Greville W.D.; RT "Novel HLA-DRB3 allele revealed by sequencing based typing."; RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases. RN [26] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*01:11). RA Perasaari J., Egle Jansson I., Partanen J., Bengtsson M.; RT "Description of a new DRB3* allele."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [27] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:20). RA Colombini I., Malagoli A., Carella G.; RT "New HLA-DRB3*02 allele."; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [28] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:21). RA Garino E., Berrino M., Bertinetto F., Brancatello F., Caropreso P., RA Chidichimo R., Frisaldi E., Mazzola G., Panniello M., Tondat F., RA Locatelli F., Amoroso A.; RT "New HLA-DRB3*02 allelic variant identified by high resolution RT sequence-based typing."; RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases. RN [29] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELES DRB3*02:22). RA Dormoy A., Froelich N.; RT "The DRB3 new allele is identical to the current HLA-DRB3*020201 RT allele except a point substitution at codon 74 where a G is found in RT place of A."; RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases. RN [30] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*02:25). RC TISSUE=Peripheral blood; RA Dormoy A., Derin R., Jollet I., Weschler B., Leisenbach R.; RT "The new DRB3 allele is identical to the DRB3*020201 allele except a RT mutation at position 266 leading to the change of the amino acid 65 RT (Tyr (TAC) -> Ser(TCC)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [31] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB3*01:14). RA Garritsen H.S.P., Fae I., Legath N., Hannig H., Fischer G.F.; RT "Identification of a novel HLA-DRB3*01 allele containing a DRB1 RT sequence motive by micro-TGGE and confirmed by cloning and direct RT sequencing."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [32] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB3*02:02). RA Greville W.D., Ng G., Kennedy A., Dunckley H.; RT "New HLA class II (DRB3) allele detected by sequencing-based typing."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [33] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB3*01:08). RC TISSUE=Bone marrow; RA Loeliger C.; RT "Description of a new HLA-DRB3 allele in a Spanish bone marrow RT donor."; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [34] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-122 (ALLELE DRB3*01:09). RA Li L., Hurley C.K.; RT "Novel HLA*DRB3 allele."; RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases. RN [35] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-121 (ALLELE DRB3*02:05). RX PubMed=9162096; DOI=10.1007/s002510050248; RA Robbins F., Hurley C.K., Tang T., Yao H., Lin Y.S., Wade J., RA Goeken N., Hartzman R.J.; RT "Diversity associated with the second expressed HLA-DRB locus in the RT human population."; RL Immunogenetics 46:104-110(1997). RN [36] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-117 (ALLELE DRB3*01:03). RA Olerup O.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. RN [37] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB3*02:06). RX PubMed=9243765; DOI=10.1111/j.1399-0039.1997.tb02843.x; RA Hashemi-Tavoularis S., Couture C., Buyse I.M.; RT "Identification of new DRB1*01 (DRB1*01022), DRB1*14 (DRB1*1428) and RT DRB3* (DRB3*0206) alleles."; RL Tissue Antigens 50:89-93(1997). RN [38] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELES DRB3*02:08 AND RP DRB3*03:02). RC TISSUE=Blood; RX PubMed=9802612; DOI=10.1111/j.1399-0039.1998.tb03047.x; RA Hashemi-tavoularis S., Ouellet S., Sengar D.P.S., Buyse I.M.; RT "A novel DRB3 allele (DRB3*0208), a new allelic variant of DRB1*1502 RT (DRB1*15023) and two new DQB1 (DQB1*03012 and DQB1*0614) alleles."; RL Tissue Antigens 52:294-299(1998). RN [39] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELES DRB3*01:06 AND RP DRB3*01:07). RC TISSUE=Peripheral blood; RX PubMed=11380956; DOI=10.1034/j.1399-0039.2001.570420.x; RA Tavoularis S., Ouellet S., Stephens S.; RT "Identification of three new DRB3* (DRB3*0106, DRB3*0107 and RT DRB3*02022) alleles."; RL Tissue Antigens 57:390-393(2001). RN [40] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB3*01:10). RC TISSUE=Peripheral blood; RX PubMed=15104685; DOI=10.1111/j.0001-2815.2004.00186.x; RA Tavoularis S., Couture C., Ribeiro-Barros E.; RT "Identification of three novel alleles: DRB3*0110, DRB1*1140, and RT DRB1*140102."; RL Tissue Antigens 63:496-500(2004). RN [41] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB3*03:03). RX PubMed=10599892; DOI=10.1034/j.1399-0039.1999.540510.x; RA Panigoro R., Greville W.D., Kennedy A., Trejaut J., Dunckley H.; RT "New HLA class II alleles in the Indonesian population."; RL Tissue Antigens 54:521-523(1999). RN [42] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-117 (ALLELE DRB3*01:02). RX PubMed=9234494; DOI=10.1111/j.1399-0039.1997.tb02820.x; RA Guttridge M.G., Hudson L., Williams H., Dunn P., Duy S., Darke C.; RT "Identification and nucleotide sequence of two novel DRB3 alleles, RT DRB3*0102 and DRB3*010133."; RL Tissue Antigens 49:665-667(1997). RN [43] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB3*02:07). RX PubMed=9389331; DOI=10.1111/j.1399-0039.1997.tb02912.x; RA Voorter C.E., Hentges F., van den Berg-Loonen E.M.; RT "Identification of a new DRB3*02 allele (DRB3*0207) by sequence-based RT typing."; RL Tissue Antigens 50:552-554(1997). RN [44] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB3*02:03). RA Anholts J.D.H., Verduijn W., Schreuder G.M.T.; RT "Five new DRB1 alleles found during routine DRB oligotyping."; RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases. RN [45] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 43-120 (ALLELE DRB3*02:02). RA Eberle M., Asu U., Taylor M., Hunter J.B., Fuller T.C., Maurer D.; RT "Identification of a putative DR8 founder haplotype containing a novel RT DRB1*0801 allele."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [46] RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-217 (ALLELE DRB3*01:01/DRB3*01:02). RX PubMed=2471740; RA Gorski J.; RT "HLA-DR beta-chain polymorphism. Second domain polymorphism reflects RT evolutionary relatedness of alleles and may explain public serologic RT epitopes."; RL J. Immunol. 143:329-333(1989). RN [47] RP IDENTIFICATION OF THE ALLOANTIGEN HPA-1A BY MASS SPECTROMETRY, AND RP ASSOCIATION TO ALLELE HLA-DRB3*01:01. RX PubMed=19494351; DOI=10.1182/blood-2009-04-211839; RA Anani Sarab G., Moss M., Barker R.N., Urbaniak S.J.; RT "Naturally processed peptides spanning the HPA-1a polymorphism are RT efficiently generated and displayed from platelet glycoprotein by HLA- RT DRB3*0101-positive antigen-presenting cells."; RL Blood 114:1954-1957(2009). RN [48] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [49] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [50] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [51] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [52] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [53] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [54] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [55] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB3 RP HETERODIMER IN COMPLEX WITH ITGB3 PEPTIDE (ALLOANTIGEN HPA-1A), RP SUBUNIT, AND DISULFIDE BOND. RX PubMed=17583734; DOI=10.1016/j.jmb.2007.05.025; RA Parry C.S., Gorski J., Stern L.J.; RT "Crystallographic structure of the human leukocyte antigen DRA, RT DRB3*0101: models of a directional alloimmune response and RT autoimmunity."; RL J. Mol. Biol. 371:435-446(2007). RN [56] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB3 RP HETERODIMER IN COMPLEX WITH EEF1A2 PEPTIDE, GLYCOSYLATION AT ASN-48, RP AND DISULFIDE BOND. RX PubMed=18697946; DOI=10.1073/pnas.0805810105; RA Dai S., Crawford F., Marrack P., Kappler J.W.; RT "The structure of HLA-DR52c: comparison to other HLA-DRB3 alleles."; RL Proc. Natl. Acad. Sci. U.S.A. 105:11893-11897(2008). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC {ECO:0000269|PubMed:17583734, ECO:0000269|PubMed:18697946}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173}. CC Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Lysosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173}. Note=The MHC class II complex CC transits through a number of intracellular compartments in the CC endocytic pathway until it reaches the cell membrane for antigen CC presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB3 are known: DRB3*01:01, CC DRB3*01:02, DRB3*01:03, DRB3*01:04, DRB3*01:05, DRB3*01:06, CC DRB3*01:07, DRB3*01:08, DRB3*01:09, DRB3*01:10, DRB3*01:11, CC DRB3*01:12, DRB3*01:13, DRB3*01:14, DRB3*02:01, DRB3*02:02, CC DRB3*02:03, DRB3*02:04, DRB3*02:05, DRB3*02:06, DRB3*02:07, CC DRB3*02:08, DRB3*02:09, DRB3*02:10, DRB3*02:11, DRB3*02:12, CC DRB3*02:13, DRB3*02:14, DRB3*02:15, DRB3*02:16, DRB3*02:17, CC DRB3*02:18, DRB3*02:19, DRB3*02:20, DRB3*02:21, DRB3*02:22, CC DRB3*02:23, DRB3*02:24, DRB3*02:25, DRB3*03:01, DRB3*03:02 and CC DRB3*03:03. The sequence shown is that of DRB3*01:01. Allele CC DRB3*01:01 belongs to an ancestral haplotype and is associated CC with autoimmune diseases that are linked to antigen presentation. CC It is found in more than 95% of the homozygous HPA-1B mothers that CC produce anti-HPA-1A antibodies, this leads to neonatal alloimmune CC thrombocytopenia (NAIT). CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- CAUTION: HLA-DRB3, HLA-DRB4 and HLA-DRB5 may represent a unique CC gene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; V00522; CAA23781.1; -; mRNA. DR EMBL; X04055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; X04058; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U66825; AAD43828.1; -; mRNA. DR EMBL; AF026467; AAC05599.1; -; Genomic_DNA. DR EMBL; AF199236; AAF13065.2; -; mRNA. DR EMBL; U95819; AAD00819.1; -; mRNA. DR EMBL; AY138123; AAN15205.1; -; mRNA. DR EMBL; A06800; CAA00596.1; -; mRNA. DR EMBL; AL662842; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL929581; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR788283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z84814; CAB06607.1; -; Genomic_DNA. DR EMBL; BC008987; AAH08987.1; -; mRNA. DR EMBL; BC106057; AAI06058.1; -; mRNA. DR EMBL; M17380; AAA59804.1; -; mRNA. DR EMBL; AF192258; AAF26358.1; -; mRNA. DR EMBL; AF192259; AAF26359.1; -; mRNA. DR EMBL; FJ515276; ACL50609.1; -; Genomic_DNA. DR EMBL; AY291205; AAP43643.1; -; Genomic_DNA. DR EMBL; AF148518; AAF67837.1; -; Genomic_DNA. DR EMBL; AF081677; AAC32202.1; -; Genomic_DNA. DR EMBL; AY271986; AAP23230.1; -; Genomic_DNA. DR EMBL; AM747470; CAO00528.1; -; Genomic_DNA. DR EMBL; EU873151; ACF33221.1; -; Genomic_DNA. DR EMBL; EU873152; ACF33222.1; -; Genomic_DNA. DR EMBL; EU873153; ACF33223.1; -; Genomic_DNA. DR EMBL; X91639; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF208484; AAF23165.1; -; Genomic_DNA. DR EMBL; AF208485; AAF23166.1; -; Genomic_DNA. DR EMBL; AJ290395; CAC27417.1; -; Genomic_DNA. DR EMBL; AF427138; AAL26538.1; -; Genomic_DNA. DR EMBL; AF455114; AAL57866.1; -; Genomic_DNA. DR EMBL; AF461431; AAL66370.1; -; Genomic_DNA. DR EMBL; AJ564210; CAD91915.2; -; Genomic_DNA. DR EMBL; AY958608; AAY28717.1; -; Genomic_DNA. DR EMBL; DQ311653; ABC33924.1; -; Genomic_DNA. DR EMBL; AM413002; CAL85628.1; -; Genomic_DNA. DR EMBL; FN424163; CAZ66795.1; -; Genomic_DNA. DR EMBL; FN424162; CAZ66766.1; -; Genomic_DNA. DR EMBL; AF177216; AAD53911.1; -; Genomic_DNA. DR EMBL; AF361865; AAK38297.1; -; Genomic_DNA. DR EMBL; AY042679; AAK94514.1; -; Genomic_DNA. DR EMBL; U36826; AAB63531.1; -; Genomic_DNA. DR EMBL; U94590; AAB53324.1; -; Genomic_DNA. DR EMBL; X95760; CAA65066.1; -; Genomic_DNA. DR EMBL; Y13715; CAA74043.1; -; Genomic_DNA. DR EMBL; AJ001255; CAA04629.1; -; Genomic_DNA. DR EMBL; AJ242860; CAB62390.1; -; Genomic_DNA. DR EMBL; AJ242862; CAB62392.1; -; Genomic_DNA. DR EMBL; AJ315477; CAC86562.1; -; Genomic_DNA. DR EMBL; AF028012; AAB94614.1; -; Genomic_DNA. DR EMBL; Y08063; CAA69301.1; -; Genomic_DNA. DR EMBL; Y10180; CAA71253.1; -; Genomic_DNA. DR EMBL; X86977; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF152845; AAD45286.1; -; Genomic_DNA. DR PIR; B60748; B60748. DR PIR; E28043; E28043. DR PIR; I37469; HLHU5D. DR PIR; PT0164; PT0164. DR PIR; PT0165; PT0165. DR PIR; PT0166; PT0166. DR PIR; S03442; S03442. DR RefSeq; NP_072049.2; NM_022555.3. DR UniGene; Hs.696211; -. DR PDB; 2Q6W; X-ray; 2.25 A; B/E=30-219. DR PDB; 3C5J; X-ray; 1.80 A; B=30-219. DR PDB; 4H1L; X-ray; 3.30 A; B/E=33-219. DR PDBsum; 2Q6W; -. DR PDBsum; 3C5J; -. DR PDBsum; 4H1L; -. DR ProteinModelPortal; P79483; -. DR SMR; P79483; -. DR BioGrid; 109370; 14. DR IntAct; P79483; 3. DR BindingDB; P79483; -. DR ChEMBL; CHEMBL3460; -. DR iPTMnet; P79483; -. DR PhosphoSitePlus; P79483; -. DR SwissPalm; P79483; -. DR DMDM; 34395491; -. DR MaxQB; P79483; -. DR PeptideAtlas; P79483; -. DR PRIDE; P79483; -. DR ProteomicsDB; 57661; -. DR TopDownProteomics; P79483; -. DR DNASU; 3125; -. DR Ensembl; ENST00000307137; ENSP00000302517; ENSG00000196101. DR Ensembl; ENST00000383126; ENSP00000372607; ENSG00000231679. DR GeneID; 3125; -. DR KEGG; hsa:3125; -. DR UCSC; uc011fni.2; human. DR CTD; 3125; -. DR DisGeNET; 3125; -. DR GeneCards; HLA-DRB3; -. DR HGNC; HGNC:4951; HLA-DRB3. DR HPA; HPA043151; -. DR MIM; 612735; gene. DR neXtProt; NX_P79483; -. DR PharmGKB; PA35074; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P79483; -. DR KO; K06752; -. DR PhylomeDB; P79483; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SIGNOR; P79483; -. DR EvolutionaryTrace; P79483; -. DR GeneWiki; HLA-DRB3_(gene); -. DR GenomeRNAi; 3125; -. DR PRO; PR:P79483; -. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0032395; F:MHC class II receptor activity; NAS:UniProtKB. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DR beta 3 chain. FT /FTId=PRO_0000018956. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18697946}. FT DISULFID 44 108 FT DISULFID 146 202 FT VARIANT 37 37 L -> S (in allele DRB3*01:04). FT /FTId=VAR_060739. FT VARIANT 38 38 E -> Q (in allele DRB3*02:12; FT dbSNP:rs1071747). FT /FTId=VAR_060740. FT VARIANT 39 39 L -> Y (in allele DRB3*01:14; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060741. FT VARIANT 40 40 R -> C (in allele DRB3*01:02). FT /FTId=VAR_016686. FT VARIANT 40 40 R -> L (in allele DRB3*02:01, allele FT DRB3*02:02, allele DRB3*02:03, allele FT DRB3*02:04, allele DRB3*02:05, allele FT DRB3*02:06, allele DRB3*02:07, allele FT DRB3*02:08, allele DRB3*02:09, allele FT DRB3*02:10, allele DRB3*02:11, allele FT DRB3*02:12, allele DRB3*02:13, allele FT DRB3*02:14, allele DRB3*02:15, allele FT DRB3*02:16, allele DRB3*02:17, allele FT DRB3*02:18, allele DRB3*02:19, allele FT DRB3*02:20, allele DRB3*02:21, allele FT DRB3*02:22, allele DRB3*02:23, allele FT DRB3*02:24, allele DRB3*02:25, allele FT DRB3*03:01, allele DRB3*03:02 and allele FT DRB3*03:03; dbSNP:rs1071748). FT /FTId=VAR_060742. FT VARIANT 40 40 R -> S (in allele DRB3*01:14; FT dbSNP:rs1136752). FT /FTId=VAR_060743. FT VARIANT 41 41 K -> T (in allele DRB3*01:14; FT dbSNP:rs200581589). FT /FTId=VAR_060744. FT VARIANT 55 55 Y -> F (in allele DRB3*01:09, allele FT DRB3*02:01, allele DRB3*02:02, allele FT DRB3*02:03, allele DRB3*02:04, allele FT DRB3*02:05, allele DRB3*02:06, allele FT DRB3*02:07, allele DRB3*02:08, allele FT DRB3*02:09, allele DRB3*02:10, allele FT DRB3*02:11, allele DRB3*02:12, allele FT DRB3*02:14, allele DRB3*02:15, allele FT DRB3*02:16, allele DRB3*02:17, allele FT DRB3*02:18, allele DRB3*02:19, allele FT DRB3*02:20, allele DRB3*02:21, allele FT DRB3*02:22, allele DRB3*02:23, allele FT DRB3*02:24, allele DRB3*02:25, allele FT DRB3*03:01, allele DRB3*03:02 and allele FT DRB3*03:03; dbSNP:rs147440497). FT /FTId=VAR_060746. FT VARIANT 55 55 Y -> L (in allele DRB3*02:13; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060745. FT VARIANT 57 57 D -> E (in allele DRB3*01:03, allele FT DRB3*01:09, allele DRB3*02:01, allele FT DRB3*02:02, allele DRB3*02:03, allele FT DRB3*02:04, allele DRB3*02:05, allele FT DRB3*02:06, allele DRB3*02:07, allele FT DRB3*02:08, allele DRB3*02:09, allele FT DRB3*02:10, allele DRB3*02:11, allele FT DRB3*02:12, allele DRB3*02:13, allele FT DRB3*02:14, allele DRB3*02:15, allele FT DRB3*02:16, allele DRB3*02:17, allele FT DRB3*02:18, allele DRB3*02:19, allele FT DRB3*02:20, allele DRB3*02:21, allele FT DRB3*02:22, allele DRB3*02:23, allele FT DRB3*02:24, allele DRB3*02:25, allele FT DRB3*03:01, allele DRB3*03:02 and allele FT DRB3*03:03; dbSNP:rs202185589). FT /FTId=VAR_060747. FT VARIANT 57 57 D -> N (in allele DRB3*01:05; FT dbSNP:rs142793258). FT /FTId=VAR_060748. FT VARIANT 58 58 R -> I (in allele DRB3*01:11). FT /FTId=VAR_060749. FT VARIANT 59 59 Y -> H (in allele DRB3*01:09, allele FT DRB3*02:01, allele DRB3*02:02, allele FT DRB3*02:03, allele DRB3*02:04, allele FT DRB3*02:06, allele DRB3*02:07, allele FT DRB3*02:08, allele DRB3*02:09, allele FT DRB3*02:10, allele DRB3*02:11, allele FT DRB3*02:12, allele DRB3*02:13, allele FT DRB3*02:14, allele DRB3*02:15, allele FT DRB3*02:16, allele DRB3*02:17, allele FT DRB3*02:18, allele DRB3*02:19, allele FT DRB3*02:20, allele DRB3*02:21, allele FT DRB3*02:22, allele DRB3*02:23, allele FT DRB3*02:24, allele DRB3*02:25 and allele FT DRB3*03:02; dbSNP:rs138849995). FT /FTId=VAR_060750. FT VARIANT 66 66 F -> L (in allele DRB3*01:13; FT dbSNP:rs707956). FT /FTId=VAR_060752. FT VARIANT 66 66 F -> N (in allele DRB3*01:08, allele FT DRB3*02:06 and allele DRB3*02:20; FT requires 2 nucleotide substitutions). FT /FTId=VAR_060753. FT VARIANT 66 66 F -> S (in allele DRB3*02:03; FT dbSNP:rs200042906). FT /FTId=VAR_060751. FT VARIANT 66 66 F -> Y (in allele DRB3*01:07, allele FT DRB3*01:09, allele DRB3*02:01, allele FT DRB3*02:02, allele DRB3*02:04, allele FT DRB3*02:05, allele DRB3*02:07, allele FT DRB3*02:08, allele DRB3*02:09, allele FT DRB3*02:10, allele DRB3*02:11, allele FT DRB3*02:12, allele DRB3*02:13, allele FT DRB3*02:14, allele DRB3*02:15, allele FT DRB3*02:16, allele DRB3*02:17, allele FT DRB3*02:18, allele DRB3*02:19, allele FT DRB3*02:21, allele DRB3*02:22, allele FT DRB3*02:23, allele DRB3*02:24 and allele FT DRB3*02:25; dbSNP:rs200042906). FT /FTId=VAR_060754. FT VARIANT 67 67 L -> A (in allele DRB3*01:07, allele FT DRB3*01:09, allele DRB3*02:01, allele FT DRB3*02:02, allele DRB3*02:04, allele FT DRB3*02:05, allele DRB3*02:06, allele FT DRB3*02:07, allele DRB3*02:08, allele FT DRB3*02:09, allele DRB3*02:10, allele FT DRB3*02:11, allele DRB3*02:12, allele FT DRB3*02:13, allele DRB3*02:14, allele FT DRB3*02:15, allele DRB3*02:16, allele FT DRB3*02:17, allele DRB3*02:18, allele FT DRB3*02:19, allele DRB3*02:21, allele FT DRB3*02:22, allele DRB3*02:23, allele FT DRB3*02:24 and allele DRB3*02:25; FT requires 2 nucleotide substitutions). FT /FTId=VAR_060755. FT VARIANT 67 67 L -> V (in allele DRB3*01:06, allele FT DRB3*01:08, allele DRB3*02:03, allele FT DRB3*02:20, allele DRB3*03:01, allele FT DRB3*03:02 and allele DRB3*03:03; FT dbSNP:rs1059580). FT /FTId=VAR_060756. FT VARIANT 68 68 R -> S (in allele DRB3*01:10; FT dbSNP:rs774894415). FT /FTId=VAR_060757. FT VARIANT 80 80 T -> R (in allele DRB3*01:07, allele FT DRB3*02:01, allele DRB3*02:02, allele FT DRB3*02:03, allele DRB3*02:04, allele FT DRB3*02:05, allele DRB3*02:06, allele FT DRB3*02:07, allele DRB3*02:08, allele FT DRB3*02:11, allele DRB3*02:12, allele FT DRB3*02:13, allele DRB3*02:14, allele FT DRB3*02:15, allele DRB3*02:16, allele FT DRB3*02:17, allele DRB3*02:18, allele FT DRB3*02:19, allele DRB3*02:20, allele FT DRB3*02:21, allele DRB3*02:22, allele FT DRB3*02:23, allele DRB3*02:24 and allele FT DRB3*02:25; dbSNP:rs79606458). FT /FTId=VAR_060758. FT VARIANT 84 84 R -> L (in allele DRB3*02:23). FT /FTId=VAR_060759. FT VARIANT 86 86 V -> A (in allele DRB3*02:16; FT dbSNP:rs144532965). FT /FTId=VAR_060760. FT VARIANT 86 86 V -> D (in allele DRB3*01:07, allele FT DRB3*02:01, allele DRB3*02:02, allele FT DRB3*02:03, allele DRB3*02:04, allele FT DRB3*02:05, allele DRB3*02:06, allele FT DRB3*02:10, allele DRB3*02:11, allele FT DRB3*02:12, allele DRB3*02:13, allele FT DRB3*02:14, allele DRB3*02:15, allele FT DRB3*02:17, allele DRB3*02:18, allele FT DRB3*02:19, allele DRB3*02:20, allele FT DRB3*02:22, allele DRB3*02:23, allele FT DRB3*02:24 and allele DRB3*02:25; FT dbSNP:rs144532965). FT /FTId=VAR_060762. FT VARIANT 86 86 V -> S (in allele DRB3*02:08; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060761. FT VARIANT 87 87 A -> E (in allele DRB3*02:18). FT /FTId=VAR_060763. FT VARIANT 89 89 S -> H (in allele DRB3*02:16; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060764. FT VARIANT 89 89 S -> Y (in allele DRB3*01:07, allele FT DRB3*02:01, allele DRB3*02:02, allele FT DRB3*02:03, allele DRB3*02:04, allele FT DRB3*02:05, allele DRB3*02:06, allele FT DRB3*02:07, allele DRB3*02:08, allele FT DRB3*02:10, allele DRB3*02:11, allele FT DRB3*02:12, allele DRB3*02:13, allele FT DRB3*02:14, allele DRB3*02:15, allele FT DRB3*02:17, allele DRB3*02:18, allele FT DRB3*02:20, allele DRB3*02:22, allele FT DRB3*02:23 and allele DRB3*02:24; FT dbSNP:rs41541218). FT /FTId=VAR_060765. FT VARIANT 96 96 L -> F (in allele DRB3*02:17; FT dbSNP:rs696318). FT /FTId=VAR_060766. FT VARIANT 96 96 L -> I (in allele DRB3*02:11; FT dbSNP:rs696318). FT /FTId=VAR_060767. FT VARIANT 102 102 G -> A (in dbSNP:rs17878857). FT /FTId=VAR_033396. FT VARIANT 103 103 R -> Q (in allele DRB3*01:07, allele FT DRB3*02:01, allele DRB3*02:02, allele FT DRB3*02:03, allele DRB3*02:05, allele FT DRB3*02:06, allele DRB3*02:07, allele FT DRB3*02:08, allele DRB3*02:09, allele FT DRB3*02:10, allele DRB3*02:11, allele FT DRB3*02:12, allele DRB3*02:13, allele FT DRB3*02:14, allele DRB3*02:15, allele FT DRB3*02:16, allele DRB3*02:17, allele FT DRB3*02:18, allele DRB3*02:20, allele FT DRB3*02:21, allele DRB3*02:23, allele FT DRB3*02:24, allele DRB3*02:25, allele FT DRB3*03:01 and allele DRB3*03:02; FT dbSNP:rs1059598). FT /FTId=VAR_060768. FT VARIANT 106 106 N -> T (in allele DRB3*02:15; FT dbSNP:rs115817940). FT /FTId=VAR_060769. FT VARIANT 113 113 G -> R (in allele DRB3*01:12). FT /FTId=VAR_060770. FT VARIANT 114 114 V -> A (in dbSNP:rs1136778). FT /FTId=VAR_033397. FT VARIANT 115 115 G -> A (in allele DRB3*02:14). FT /FTId=VAR_060771. FT VARIANT 115 115 G -> V (in allele DRB3*02:01, allele FT DRB3*02:04, allele DRB3*02:24, allele FT DRB3*03:01 and allele DRB3*03:02; FT dbSNP:rs41556512). FT /FTId=VAR_060772. FT VARIANT 169 169 A -> T (in allele DRB3*03:01; FT dbSNP:rs75709987). FT /FTId=VAR_060773. FT VARIANT 178 178 Q -> H (in allele DRB3*03:01; FT dbSNP:rs139485758). FT /FTId=VAR_060774. FT VARIANT 193 193 V -> F (in allele DRB3*02:01). FT /FTId=VAR_060775. FT VARIANT 212 212 A -> P (in allele DRB3*02:01, allele FT DRB3*02:02, allele DRB3*02:10, allele FT DRB3*02:11, allele DRB3*02:24 and allele FT DRB3*03:01; dbSNP:rs142204283). FT /FTId=VAR_060776. FT VARIANT 218 218 R -> S (in allele DRB3*02:01, allele FT DRB3*02:02, allele DRB3*02:10 and allele FT DRB3*02:11; dbSNP:rs147669022). FT /FTId=VAR_060777. FT STRAND 36 47 {ECO:0000244|PDB:2Q6W}. FT TURN 48 51 {ECO:0000244|PDB:4H1L}. FT STRAND 52 61 {ECO:0000244|PDB:2Q6W}. FT STRAND 64 70 {ECO:0000244|PDB:2Q6W}. FT TURN 71 73 {ECO:0000244|PDB:2Q6W}. FT STRAND 75 80 {ECO:0000244|PDB:2Q6W}. FT HELIX 81 83 {ECO:0000244|PDB:2Q6W}. FT HELIX 84 91 {ECO:0000244|PDB:2Q6W}. FT TURN 94 96 {ECO:0000244|PDB:2Q6W}. FT HELIX 100 102 {ECO:0000244|PDB:2Q6W}. FT HELIX 103 106 {ECO:0000244|PDB:2Q6W}. FT HELIX 108 115 {ECO:0000244|PDB:2Q6W}. FT TURN 116 121 {ECO:0000244|PDB:2Q6W}. FT STRAND 127 134 {ECO:0000244|PDB:2Q6W}. FT STRAND 142 154 {ECO:0000244|PDB:2Q6W}. FT STRAND 157 162 {ECO:0000244|PDB:2Q6W}. FT STRAND 165 167 {ECO:0000244|PDB:2Q6W}. FT STRAND 171 173 {ECO:0000244|PDB:2Q6W}. FT STRAND 180 182 {ECO:0000244|PDB:2Q6W}. FT STRAND 184 192 {ECO:0000244|PDB:2Q6W}. FT STRAND 200 205 {ECO:0000244|PDB:2Q6W}. FT STRAND 213 217 {ECO:0000244|PDB:2Q6W}. SQ SEQUENCE 266 AA; 29962 MW; 2FC3AE68D3B10EAD CRC64; MVCLKLPGGS SLAALTVTLM VLSSRLAFAG DTRPRFLELR KSECHFFNGT ERVRYLDRYF HNQEEFLRFD SDVGEYRAVT ELGRPVAESW NSQKDLLEQK RGRVDNYCRH NYGVGESFTV QRRVHPQVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SALTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID DRB4_HUMAN Reviewed; 266 AA. AC P13762; B0S863; O78042; P79664; Q29889; Q30163; Q6TLK6; Q860N4; AC Q861F3; Q8WLT9; Q9BS54; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2009, sequence version 2. DT 18-JUL-2018, entry version 141. DE RecName: Full=HLA class II histocompatibility antigen, DR beta 4 chain; DE AltName: Full=MHC class II antigen DRB4; DE Flags: Precursor; GN Name=HLA-DRB4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB4*01:01). RX PubMed=3110774; DOI=10.1073/pnas.84.14.4929; RA Young J.A.T., Wilkinson D., Bodmer W.F., Trowsdale J.; RT "Sequence and evolution of HLA-DR7- and -DRw53-associated beta-chain RT genes."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4929-4933(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB4*01:03). RX PubMed=11972878; DOI=10.1034/j.1399-0039.2002.590108.x; RA De Pablo R., Solis R., Balas A., Vilches C.; RT "Specific amplification of the HLA-DRB4 gene from c-DNA. Complete RT coding sequence of the HLA alleles DRB4*0103101 and DRB4*01033."; RL Tissue Antigens 59:44-46(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB4*01:03). RA Song C.-H., Lee J.-K., Koh I., Lee J.-Y., Lim Y.-H., Kang J., RA Cha Y.-Y., Yun H.-S., Lee E.-J., Kwack K.; RT "Human leukocyte antigen DRB4*01030101 allele."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB4*01:03). RA Wallace L.T., Rudersdorf R., Watkins D.I.; RT "The MHC class II alleles of Homo sapiens."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB4*01:03). RC TISSUE=Synovium; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB4*01:03). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB4*01:03). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-266 (ALLELE DRB4*01:03). RX PubMed=3467350; DOI=10.1073/pnas.84.1.209; RA Curtsinger J.M., Hilden J.M., Cairns J.S., Bach F.H.; RT "Evolutionary and genetic implications of sequence variation in two RT nonallelic HLA-DR beta-chain cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 84:209-213(1987). RN [9] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-266 (ALLELE DRB4*01:03). RX PubMed=3036826; RA Andersson G., Larhammar D., Widmark E., Servenius B., Peterson P.A., RA Rask L.; RT "Class II genes of the human major histocompatibility complex. RT Organization and evolutionary relationship of the DR beta genes."; RL J. Biol. Chem. 262:8748-8758(1987). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB4*01:02). RA Greville W.D.; RT "HLA-DRB4 exon 2 and exon 3 variation."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-214 (ALLELE DRB4*01:06). RA Chapman G., Hogbin J.-P., Greville W.D.; RT "Novel HLA-DRB4 allele identified by sequencing based typing."; RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB4*01:04). RA Kashiwase K.; RT "HLA-DRB4*01V1(DRB4*0104) DNA Sequence."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-116 (ALLELE DRB4*01:05). RX PubMed=9234493; DOI=10.1111/j.1399-0039.1997.tb02819.x; RA Voorter C., Emonds M.P., van den Berg-Loonen E.; RT "Identification of a new DRB4 allele (DRB4*0105) by sequence-based RT typing."; RL Tissue Antigens 49:662-664(1997). RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-120 (ALLELE DRB4*01:07). RA Mele L., Binello S., Balza G., Mazzola G., Garino E.; RT "DRB4* genomic sequence: a new allele."; RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases. RN [15] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [16] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [17] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [18] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [19] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [20] RP UBIQUITINATION AT LYS-254 BY MARCH1 AND MARCH8, MUTAGENESIS OF RP LYS-254; LEU-264 AND LEU-265, AND SUBCELLULAR LOCATION. RX PubMed=19117940; DOI=10.1074/jbc.M805736200; RA Lapaque N., Jahnke M., Trowsdale J., Kelly A.P.; RT "The HLA-DRalpha chain is modified by polyubiquitination."; RL J. Biol. Chem. 284:7007-7016(2009). RN [21] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [22] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane CC protein. Endoplasmic reticulum membrane; Single-pass type I CC membrane protein. Golgi apparatus, trans-Golgi network membrane; CC Single-pass type I membrane protein. Endosome membrane; Single- CC pass type I membrane protein. Lysosome membrane; Single-pass type CC I membrane protein. Late endosome membrane; Single-pass type I CC membrane protein. Note=The MHC class II complex transits through a CC number of intracellular compartments in the endocytic pathway CC until it reaches the cell membrane for antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC sorting into the endosome system and down-regulation of MHC class CC II. When associated with ubiquitination of the alpha subunit of CC HLA-DR: HLA-DRA 'Lys-244', the down-regulation of MHC class II may CC be highly effective. {ECO:0000269|PubMed:18305173, CC ECO:0000269|PubMed:19117940}. CC -!- POLYMORPHISM: The following alleles of DRB4 are known: DRB4*01:01, CC DRB4*01:02, DRB4*01:03, DRB4*01:04, DRB4*01:05, DRB4*01:06 and CC DRB4*01:07. The sequence shown is that of DRB4*01:03. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC -!- CAUTION: HLA-DRB3, HLA-DRB4 and HLA-DRB5 may represent a unique CC gene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M16942; AAA36296.1; -; mRNA. DR EMBL; AF361548; AAM00252.1; -; mRNA. DR EMBL; AF361549; AAM00253.1; -; mRNA. DR EMBL; DQ284431; ABC66198.1; -; mRNA. DR EMBL; GQ891550; ACX50637.1; -; mRNA. DR EMBL; AK292151; BAF84840.1; -; mRNA. DR EMBL; BX571807; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX120007; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927235; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR788250; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005312; AAH05312.1; -; mRNA. DR EMBL; M15178; AAA35995.1; -; mRNA. DR EMBL; M20555; AAA59830.1; -; Genomic_DNA. DR EMBL; AH012539; AAO43051.1; -; Genomic_DNA. DR EMBL; AH011268; AAL48256.1; -; Genomic_DNA. DR EMBL; AB107960; BAC75547.1; -; Genomic_DNA. DR EMBL; Y09313; CAA70497.1; -; Genomic_DNA. DR EMBL; AY394720; AAQ96922.1; -; Genomic_DNA. DR PIR; B28031; B28031. DR PIR; I59092; I59092. DR PIR; PT0168; PT0168. DR RefSeq; NP_068818.4; NM_021983.4. DR RefSeq; XP_016885779.1; XM_017030290.1. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR ProteinModelPortal; P13762; -. DR SMR; P13762; -. DR BioGrid; 109371; 10. DR IntAct; P13762; 1. DR ChEMBL; CHEMBL3988561; -. DR iPTMnet; P13762; -. DR DMDM; 281371554; -. DR PeptideAtlas; P13762; -. DR PRIDE; P13762; -. DR ProteomicsDB; 52984; -. DR DNASU; 3126; -. DR Ensembl; ENST00000411565; ENSP00000410857; ENSG00000227357. DR GeneID; 3126; -. DR KEGG; hsa:3126; -. DR CTD; 3126; -. DR DisGeNET; 3126; -. DR GeneCards; HLA-DRB4; -. DR H-InvDB; HIX0033495; -. DR HGNC; HGNC:4952; HLA-DRB4. DR neXtProt; NX_P13762; -. DR OpenTargets; ENSG00000227357; -. DR PharmGKB; PA35075; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P13762; -. DR KO; K06752; -. DR OrthoDB; EOG091G0SXL; -. DR PhylomeDB; P13762; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SIGNOR; P13762; -. DR GeneWiki; HLA-DRB4; -. DR GenomeRNAi; 3126; -. DR PRO; PR:P13762; -. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Immunity; Isopeptide bond; Lysosome; Membrane; MHC II; Polymorphism; KW Reference proteome; Signal; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT SIGNAL 1 29 FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DR beta 4 chain. FT /FTId=PRO_0000018991. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 216 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CROSSLNK 254 254 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000269|PubMed:19117940}. FT VARIANT 105 105 D -> G (in allele DRB4*01:02). FT /FTId=VAR_060778. FT VARIANT 106 106 T -> N (in allele DRB4*01:04). FT /FTId=VAR_060779. FT VARIANT 110 110 Y -> H (in allele DRB4*01:05). FT /FTId=VAR_060780. FT VARIANT 113 113 G -> R (in allele DRB4*01:07). FT /FTId=VAR_060781. FT VARIANT 141 141 H -> Y (in allele DRB4*01:06). FT /FTId=VAR_060782. FT VARIANT 164 164 G -> S (in allele DRB4*01:01 and allele FT DRB4*01:06). FT /FTId=VAR_060783. FT MUTAGEN 254 254 K->R: Almost no change in down-regulation FT of MHC class II. No ubiquitination and FT complete loss of down-regulation of MHC FT class II; when associated with 'R-244' of FT HLA-DRA. {ECO:0000269|PubMed:19117940}. FT MUTAGEN 264 264 L->A: Almost no change in down-regulation FT of MHC class II; when associated with A- FT 265. {ECO:0000269|PubMed:19117940}. FT MUTAGEN 265 265 L->A: Almost no change in down-regulation FT of MHC class II; when associated with A- FT 264. {ECO:0000269|PubMed:19117940}. SQ SEQUENCE 266 AA; 29941 MW; 96FF5FE572403FAE CRC64; MVCLKLPGGS CMAALTVTLT VLSSPLALAG DTQPRFLEQA KCECHFLNGT ERVWNLIRYI YNQEEYARYN SDLGEYQAVT ELGRPDAEYW NSQKDLLERR RAEVDTYCRY NYGVVESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSMM SPLTVQWSAR SESAQSKMLS GVGGFVLGLL FLGTGLFIYF RNQKGHSGLQ PTGLLS // ID DRB5_HUMAN Reviewed; 266 AA. AC Q30154; B2RBV6; C7C4X3; O00157; O00283; O46700; Q29703; Q29787; AC Q29788; Q30126; Q30150; Q30199; Q6SJR2; Q7M2H9; Q8HWS7; Q8WLR5; AC Q9MY54; Q9XRX6; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 12-SEP-2018, entry version 163. DE RecName: Full=HLA class II histocompatibility antigen, DR beta 5 chain; DE AltName: Full=DR beta-5; DE AltName: Full=DR2-beta-2; DE AltName: Full=Dw2; DE AltName: Full=MHC class II antigen DRB5; DE Flags: Precursor; GN Name=HLA-DRB5 {ECO:0000312|EMBL:CAI18079.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] {ECO:0000305, ECO:0000312|PIR:D25239} RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-28 AND ALA-154. RX PubMed=3099214; DOI=10.1038/324676a0; RA Wu S., Saunders T.L., Bach F.H.; RT "Polymorphism of human Ia antigens generated by reciprocal intergenic RT exchange between two DR beta loci."; RL Nature 324:676-679(1986). RN [2] {ECO:0000305, ECO:0000312|PIR:C32526} RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-28. RX PubMed=3571980; RA Wu S.K., Yabe T., Madden M., Saunders T.L., Bach F.H.; RT "cDNA cloning and sequencing reveals that the electrophoretically RT constant DR beta 2 molecules, as well as the variable DR beta 1 RT molecules, from HLA-DR2 subtypes have different amino acid sequences RT including a hypervariable region for a functionally important RT epitope."; RL J. Immunol. 138:2953-2959(1987). RN [3] {ECO:0000312|EMBL:AAA59822.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ALLELE DRB5*01:01). RX PubMed=3259543; DOI=10.1007/BF00364432; RA Lock C.B., So A.K., Welsh K.I., Parkes J.D., Trowsdale J.; RT "MHC class II sequences of an HLA-DR2 narcoleptic."; RL Immunogenetics 27:449-455(1988). RN [4] {ECO:0000305, ECO:0000312|EMBL:AAA59791.1} RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-28. RX PubMed=2001975; DOI=10.1016/0198-8859(91)90069-L; RA Demopulos J.T., Hodge T.W., Wooten V., Acton R.T.; RT "A novel DRB1 allele in DR2-positive American blacks."; RL Hum. Immunol. 30:41-44(1991). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB5*01:01). RC TISSUE=Stomach; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] {ECO:0000305, ECO:0000312|EMBL:CAI18079.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ALLELE DRB5*01:01). RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [7] {ECO:0000305, ECO:0000312|EMBL:AAH09234.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE DRB5*01:01). RC TISSUE=B-cell {ECO:0000312|EMBL:AAH09234.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 28-140 (ALLELE DRB5*01:04), AND RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-119 (ALLELE DRB5*02:04). RC TISSUE=Blood; RX PubMed=9162096; DOI=10.1007/s002510050248; RA Robbins F., Hurley C.K., Tang T., Yao H., Lin Y.S., Wade J., RA Goeken N., Hartzman R.J.; RT "Diversity associated with the second expressed HLA-DRB locus in the RT human population."; RL Immunogenetics 46:104-110(1997). RN [9] {ECO:0000312|EMBL:AAA36276.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266 (ALLELES DRB5*01:01 AND RP DRB5*01:02). RX PubMed=2885840; DOI=10.1073/pnas.84.13.4591; RA Lee B.S.M., Rust N.A., McMichael A.J., McDevitt H.O.; RT "HLA-DR2 subtypes form an additional supertypic family of DR beta RT alleles."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4591-4595(1987). RN [10] {ECO:0000305, ECO:0000312|EMBL:AAA59818.1} RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-266, AND VARIANT ALA-154. RX PubMed=3476943; DOI=10.1073/pnas.84.17.6234; RA Bell J.I., Denney D. Jr., Foster L., Belt T.K., Todd J.A., RA McDevitt H.O.; RT "Allelic variation in the DR subregion of the human major RT histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 84:6234-6238(1987). RN [11] {ECO:0000312|PIR:B28756} RP PROTEIN SEQUENCE OF 30-148 AND 158-178. RX PubMed=6576979; RA Goetz H., Kratzin H., Thinnes F.P., Yang C.-Y., Kruse T., Pauly E., RA Koelbel S., Egert G., Wernet P., Hilschmann N.; RT "Primary structure of human class II histocompatibility antigens 3rd RT communication. Amino acid sequence comparison between DR and DC RT subclass antigens derived from a lymphoblastoid B cell line homozygous RT at the HLA loci (HLA-A3,3; B7,7; Dw2,2; DR2,2: MT1,1; Dc1,1: MB1,1)."; RL Hoppe-Seyler's Z. Physiol. Chem. 364:749-755(1983). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 34-122 (ALLELE DRB5*01:05). RX PubMed=8773325; DOI=10.1111/j.1399-0039.1996.tb02563.x; RA Poli F., Bianchi P., Crespiatico L., Terragna C., RA van den Berg-Loonen E., Sirchia G.; RT "Characterization of a new HLA-DRB5 allele (DRB5*0105) by PCR-SSP and RT direct sequencing."; RL Tissue Antigens 47:338-340(1996). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-217 (ALLELE DRB5*01:14). RC TISSUE=Blood; RA Anholts J.D.H.; RT "New sequences found during routine HLA typing."; RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:06). RX PubMed=9226128; DOI=10.1111/j.1365-2370.1997.00267.x; RA Kervaire B., Tiercy J.; RT "Sequence of a new HLA-DR allele, DRB5*0106."; RL Eur. J. Immunogenet. 24:225-228(1997). RN [15] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:03). RC TISSUE=Blood; RA Hurley C.K.; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [16] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*02:05). RA Carter V., Day S., Dunn P.; RT "Identification of a new DRB5*02 variant allele by PCR-SSP and SBT."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:11). RA Greville W.D., Chapman G., Hogbin J.-P., Velickovic Z.; RT "Novel HLA-DRB5 allele found by sequence based typing."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [18] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:12). RX PubMed=14617041; DOI=10.1046/j.1399-0039.2003.00124.x; RA Atkinson D.C., Jobson S.E., Dunn P.P., Briggs D.C.; RT "Identification of a new HLA-DRB5 allele, DRB5*0112, by routine PCR- RT SSP."; RL Tissue Antigens 62:554-555(2003). RN [19] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-123 (ALLELE DRB5*01:13). RX PubMed=16671952; DOI=10.1111/j.1399-0039.2006.00588.x; RA Garino E., Berrino M., Bertinetto F., Caropreso P., Chidichimo R., RA Dametto E., Fasano M.E., Frisaldi E., Mazzola G., Tondat F., RA Boccadoro M., Bruno B., Amoroso A.; RT "Identification of a new allele, HLA-DRB5*0113, through three RT different molecular biology techniques."; RL Tissue Antigens 67:427-429(2006). RN [20] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB5*01:07). RX PubMed=9458128; DOI=10.1111/j.1399-0039.1997.tb02933.x; RA Buyse I.M., Couture C., Hashemi-Tavoularis S.; RT "Identification of novel DRB1*11 (DRB1*11013, DRB1*1129), DRB1*08 RT (DRB1*0816) and DRB5* (DRB5*0107) alleles."; RL Tissue Antigens 50:678-681(1997). RN [21] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-115 (ALLELE DRB5*01:09). RX PubMed=9694360; DOI=10.1111/j.1399-0039.1998.tb03010.x; RA Buyse I.M., Ouellet S., Hashemi-Tavoularis S.; RT "Identification of novel DRB1*13 (DRB1*1333), DRB1*04 (DRB1*0426) and RT DRB5* (DRB5*0109) alleles."; RL Tissue Antigens 51:658-662(1998). RN [22] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-119 (ALLELE DRB5*02:03). RX PubMed=1471145; DOI=10.1111/j.1399-0039.1992.tb02047.x; RA Grooms A., Dunckley H., Gao X., Serjeantson S.W.; RT "DRB5*HK: a new HLA-DRB5 allele in Cantonese."; RL Tissue Antigens 40:210-211(1992). RN [23] RP REVIEW. RX PubMed=8598037; DOI=10.1016/S0092-8674(00)81025-9; RA Cresswell P.; RT "Invariant chain structure and MHC class II function."; RL Cell 84:505-507(1996). RN [24] RP REVIEW. RX PubMed=11684289; DOI=10.1016/S0161-5890(01)00069-4; RA Villadangos J.A.; RT "Presentation of antigens by MHC class II molecules: getting the most RT out of them."; RL Mol. Immunol. 38:329-346(2001). RN [25] RP REVIEW. RX PubMed=17241953; DOI=10.1016/j.immuni.2007.01.005; RA Menendez-Benito V., Neefjes J.; RT "Autophagy in MHC class II presentation: sampling from within."; RL Immunity 26:1-3(2007). RN [26] RP REVIEW. RX PubMed=18046453; DOI=10.1038/sj.emboj.7601945; RA Rocha N., Neefjes J.; RT "MHC class II molecules on the move for successful antigen RT presentation."; RL EMBO J. 27:1-5(2008). RN [27] RP UBIQUITINATION BY MARCH1, AND SUBCELLULAR LOCATION. RX PubMed=18305173; DOI=10.1073/pnas.0708874105; RA De Gassart A., Camosseto V., Thibodeau J., Ceppi M., Catalan N., RA Pierre P., Gatti E.; RT "MHC class II stabilization at the surface of human dendritic cells is RT the result of maturation-dependent MARCH I down-regulation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3491-3496(2008). RN [28] RP REVIEW. RX PubMed=19092054; DOI=10.1242/jcs.035089; RA Berger A.C., Roche P.A.; RT "MHC class II transport at a glance."; RL J. Cell Sci. 122:1-4(2009). RN [29] RP REVIEW. RX PubMed=19533806; DOI=10.3748/wjg.15.2855; RA Beswick E.J., Reyes V.E.; RT "CD74 in antigen presentation, inflammation, and cancers of the RT gastrointestinal tract."; RL World J. Gastroenterol. 15:2855-2861(2009). RN [30] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [31] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [32] {ECO:0000305} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5 RP HETERODIMER IN COMPLEX WITH MBP PEPTIDE, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=11080454; DOI=10.1006/jmbi.2000.4198; RA Li Y., Li H., Martin R., Mariuzza R.A.; RT "Structural basis for the binding of an immunodominant peptide from RT myelin basic protein in different registers by two HLA-DR2 proteins."; RL J. Mol. Biol. 304:177-188(2000). RN [33] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5 RP HETERODIMER IN COMPLEX WITH MPB PEPTIDE AND STREPTOCOCCUS PYOGENES RP SPEC PEPTIDE, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=11163233; DOI=10.1016/S1074-7613(01)00092-9; RA Li Y., Li H., Dimasi N., McCormick J.K., Martin R., Schuck P., RA Schlievert P.M., Mariuzza R.A.; RT "Crystal structure of a superantigen bound to the high-affinity, zinc- RT dependent site on MHC class II."; RL Immunity 14:93-104(2001). RN [34] {ECO:0000312|PDB:1H15} RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 30-219 OF HLA-DRA/HLA-DRB5 RP HETERODIMER IN COMPLEX EPSTEIN-BARR VIRUS BALF5 PEPTIDE, SUBUNIT, AND RP DISULFIDE BONDS. RX PubMed=12244309; DOI=10.1038/ni835; RA Lang H.L.E., Jacobsen H., Ikemizu S., Andersson C., Harlos K., RA Madsen L., Hjorth P., Sondergaard L., Svejgaard A., Wucherpfennig K., RA Stuart D.I., Bell J.I., Jones E.Y., Fugger L.; RT "A functional and structural basis for TCR cross-reactivity in RT multiple sclerosis."; RL Nat. Immunol. 3:940-943(2002). RN [35] {ECO:0000305} RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 30-221 OF HLA-DRA/HLA-DRB5 RP HETERODIMER IN COMPLEX WITH MBP PEPTIDE AND TRAC, SUBUNIT, AND RP DISULFIDE BONDS. RX PubMed=16079912; DOI=10.1038/sj.emboj.7600771; RA Li Y., Huang Y., Lue J., Quandt J.A., Martin R., Mariuzza R.A.; RT "Structure of a human autoimmune TCR bound to a myelin basic protein RT self-peptide and a multiple sclerosis-associated MHC class II RT molecule."; RL EMBO J. 24:2968-2979(2005). CC -!- FUNCTION: Binds peptides derived from antigens that access the CC endocytic route of antigen presenting cells (APC) and presents CC them on the cell surface for recognition by the CD4 T-cells. The CC peptide binding cleft accommodates peptides of 10-30 residues. The CC peptides presented by MHC class II molecules are generated mostly CC by degradation of proteins that access the endocytic route, where CC they are processed by lysosomal proteases and other hydrolases. CC Exogenous antigens that have been endocytosed by the APC are thus CC readily available for presentation via MHC II molecules, and for CC this reason this antigen presentation pathway is usually referred CC to as exogenous. As membrane proteins on their way to degradation CC in lysosomes as part of their normal turn-over are also contained CC in the endosomal/lysosomal compartments, exogenous antigens must CC compete with those derived from endogenous components. Autophagy CC is also a source of endogenous peptides, autophagosomes CC constitutively fuse with MHC class II loading compartments. In CC addition to APCs, other cells of the gastrointestinal tract, such CC as epithelial cells, express MHC class II molecules and CD74 and CC act as APCs, which is an unusual trait of the GI tract. To produce CC a MHC class II molecule that presents an antigen, three MHC class CC II molecules (heterodimers of an alpha and a beta chain) associate CC with a CD74 trimer in the ER to form a heterononamer. Soon after CC the entry of this complex into the endosomal/lysosomal system CC where antigen processing occurs, CD74 undergoes a sequential CC degradation by various proteases, including CTSS and CTSL, leaving CC a small fragment termed CLIP (class-II-associated invariant chain CC peptide). The removal of CLIP is facilitated by HLA-DM via direct CC binding to the alpha-beta-CLIP complex so that CLIP is released. CC HLA-DM stabilizes MHC class II molecules until primary high CC affinity antigenic peptides are bound. The MHC II molecule bound CC to a peptide is then transported to the cell membrane surface. In CC B-cells, the interaction between HLA-DM and MHC class II molecules CC is regulated by HLA-DO. Primary dendritic cells (DCs) also to CC express HLA-DO. Lysosomal microenvironment has been implicated in CC the regulation of antigen loading into MHC II molecules, increased CC acidification produces increased proteolysis and efficient peptide CC loading. CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit; also referred CC as MHC class II molecule. In the endoplasmic reticulum (ER) it CC forms a heterononamer; 3 MHC class II molecules bind to a CD74 CC homotrimer (also known as invariant chain or HLA class II CC histocompatibility antigen gamma chain). In the CC endosomal/lysosomal system; CD74 undergoes sequential degradation CC by various proteases; leaving a small fragment termed CLIP on each CC MHC class II molecule. MHC class II molecule interacts with CC HLA_DM, and HLA_DO in B-cells, in order to release CLIP and CC facilitate the binding of antigenic peptides. CC {ECO:0000269|PubMed:11080454, ECO:0000269|PubMed:11163233, CC ECO:0000269|PubMed:12244309, ECO:0000269|PubMed:16079912}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, CC ECO:0000305}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173, ECO:0000305}. Golgi apparatus, CC trans-Golgi network membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, CC ECO:0000305}. Endosome membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, CC ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:18305173}; CC Single-pass type I membrane protein {ECO:0000269|PubMed:18305173, CC ECO:0000305}. Late endosome membrane CC {ECO:0000269|PubMed:18305173}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:18305173, ECO:0000305}. Note=The MHC class II CC complex transits through a number of intracellular compartments in CC the endocytic pathway until it reaches the cell membrane for CC antigen presentation. CC -!- PTM: Ubiquitinated by MARCH1 and MARCH8 at Lys-254 leading to CC down-regulation of MHC class II. {ECO:0000305|PubMed:18305173}. CC -!- POLYMORPHISM: The following alleles of DRB5 are known: DRB5*01:01, CC DRB5*01:02, DRB5*01:03, DRB5*01:04, DRB5*01:05, DRB5*01:06, CC DRB5*01:07, DRB5*01:09, DRB5*01:11, DRB5*01:12 DRB5*01:13, CC DRB5*01:14, DRB5*02:02, DRB5*02:03, DRB5*02:04, DRB5*02:05. The CC sequence shown is that of DRB5*01:01. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000255}. CC -!- CAUTION: HLA-DRB3, HLA-DRB4 and HLA-DRB5 may represent a unique CC gene. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M20429; AAA59822.1; -; mRNA. DR EMBL; M35159; AAA59791.1; -; Genomic_DNA. DR EMBL; AL713966; CAI18079.1; -; Genomic_DNA. DR EMBL; AK314834; BAG37353.1; -; mRNA. DR EMBL; BC009234; AAH09234.1; -; mRNA. DR EMBL; U31770; AAB63983.1; -; mRNA. DR EMBL; U59685; AAB52229.1; -; Genomic_DNA. DR EMBL; M16954; AAA36276.1; -; mRNA. DR EMBL; M16955; AAA36277.1; -; mRNA. DR EMBL; M17377; AAA59818.1; -; mRNA. DR EMBL; X87210; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; FN430425; CAZ86696.1; -; Genomic_DNA. DR EMBL; Z83201; CAB05668.1; -; Genomic_DNA. DR EMBL; AF122887; AAD31766.1; -; Genomic_DNA. DR EMBL; AJ271159; CAB71144.1; -; Genomic_DNA. DR EMBL; AY141137; AAN28924.1; -; Genomic_DNA. DR EMBL; AJ427352; CAD20460.1; -; Genomic_DNA. DR EMBL; AY457037; AAR20446.2; -; Genomic_DNA. DR EMBL; Y09342; CAA70524.1; -; Genomic_DNA. DR EMBL; Y13727; CAA74055.1; -; Genomic_DNA. DR EMBL; M91001; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS4751.1; -. DR PIR; B27060; B27060. DR PIR; B28043; B28043. DR PIR; B28756; B28756. DR PIR; C32526; C32526. DR PIR; D25239; D25239. DR PIR; I68733; I68733. DR PIR; PT0169; PT0169. DR PIR; PT0170; PT0170. DR PIR; PT0171; PT0171. DR RefSeq; NP_002116.2; NM_002125.3. DR UniGene; Hs.485130; -. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.736560; -. DR PDB; 1FV1; X-ray; 1.90 A; B/E=30-219. DR PDB; 1H15; X-ray; 3.10 A; B/E=30-219. DR PDB; 1HQR; X-ray; 3.20 A; B=30-219. DR PDB; 1ZGL; X-ray; 2.80 A; B/E/H/K=30-221. DR PDBsum; 1FV1; -. DR PDBsum; 1H15; -. DR PDBsum; 1HQR; -. DR PDBsum; 1ZGL; -. DR ProteinModelPortal; Q30154; -. DR SMR; Q30154; -. DR BioGrid; 109372; 16. DR IntAct; Q30154; 6. DR STRING; 9606.ENSP00000364114; -. DR ChEMBL; CHEMBL3988561; -. DR iPTMnet; Q30154; -. DR SwissPalm; Q30154; -. DR BioMuta; HLA-DRB5; -. DR DMDM; 74754558; -. DR PaxDb; Q30154; -. DR PeptideAtlas; Q30154; -. DR PRIDE; Q30154; -. DR ProteomicsDB; 61556; -. DR DNASU; 3127; -. DR Ensembl; ENST00000374975; ENSP00000364114; ENSG00000198502. DR GeneID; 3127; -. DR KEGG; hsa:3127; -. DR UCSC; uc003obj.4; human. DR CTD; 3127; -. DR DisGeNET; 3127; -. DR EuPathDB; HostDB:ENSG00000198502.5; -. DR GeneCards; HLA-DRB5; -. DR HGNC; HGNC:4953; HLA-DRB5. DR HPA; HPA043151; -. DR MIM; 604776; gene. DR neXtProt; NX_Q30154; -. DR OpenTargets; ENSG00000198502; -. DR PharmGKB; PA35076; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR InParanoid; Q30154; -. DR KO; K06752; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR PhylomeDB; Q30154; -. DR TreeFam; TF336626; -. DR Reactome; R-HSA-202424; Downstream TCR signaling. DR Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2132295; MHC class II antigen presentation. DR Reactome; R-HSA-389948; PD-1 signaling. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SIGNOR; Q30154; -. DR ChiTaRS; HLA-DRB5; human. DR EvolutionaryTrace; Q30154; -. DR GeneWiki; HLA-DRB5; -. DR GenomeRNAi; 3127; -. DR PRO; PR:Q30154; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000198502; Expressed in 91 organ(s), highest expression level in lung. DR Genevisible; Q30154; HS. DR GO; GO:0030669; C:clathrin-coated endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome. DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0042613; C:MHC class II protein complex; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; TAS:Reactome. DR GO; GO:0042605; F:peptide antigen binding; ISS:UniProtKB. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Endoplasmic reticulum; KW Endosome; Glycoprotein; Golgi apparatus; Immunity; Lysosome; Membrane; KW MHC II; Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 29 {ECO:0000269|PubMed:6576979}. FT CHAIN 30 266 HLA class II histocompatibility antigen, FT DR beta 5 chain. FT /FTId=PRO_5000143106. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TOPO_DOM 249 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. {ECO:0000255}. FT REGION 30 124 Beta-1. {ECO:0000255}. FT REGION 125 227 Beta-2. {ECO:0000255}. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218}. FT DISULFID 44 108 FT DISULFID 146 202 FT VARIANT 14 14 K -> M (in dbSNP:rs1064587). FT /FTId=VAR_060951. FT VARIANT 14 14 K -> Q (in dbSNP:rs701884). FT /FTId=VAR_060952. FT VARIANT 14 14 K -> V (in allele DRB5*02:02; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060953. FT VARIANT 20 20 M -> T (in dbSNP:rs17211043). FT /FTId=VAR_050355. FT VARIANT 28 28 L -> S. {ECO:0000269|PubMed:2001975, FT ECO:0000269|PubMed:3099214, FT ECO:0000269|PubMed:3571980}. FT /FTId=VAR_039871. FT VARIANT 33 33 R -> Q (in dbSNP:rs1141741). FT /FTId=VAR_050356. FT VARIANT 35 35 R -> C (in allele DRB5*02:02, allele FT DRB5*02:04 and allele DRB5*02:05; FT dbSNP:rs1136744). FT /FTId=VAR_060954. FT VARIANT 41 41 K -> T (in dbSNP:rs200581589). FT /FTId=VAR_050357. FT VARIANT 57 57 H -> Q (in dbSNP:rs202185589). FT /FTId=VAR_060955. FT VARIANT 59 59 D -> G (in allele DRB5*01:02, allele FT DRB5*01:03, allele DRB5*02:02, allele FT DRB5*02:03, allele DRB5*02:04 and allele FT DRB5*02:05; dbSNP:rs41546317). FT /FTId=VAR_060956. FT VARIANT 62 62 N -> H (in dbSNP:rs1059576). FT /FTId=VAR_050358. FT VARIANT 66 66 D -> N (in allele DRB5*01:02, allele FT DRB5*01:03, allele DRB5*02:02, allele FT DRB5*02:03, allele DRB5*02:04 and allele FT DRB5*02:05; dbSNP:rs707956). FT /FTId=VAR_060958. FT VARIANT 66 66 D -> Y (in allele DRB5*01:14; FT dbSNP:rs707956). FT /FTId=VAR_060959. FT VARIANT 67 67 L -> V (in allele DRB5*01:02, allele FT DRB5*01:03, allele DRB5*01:05, allele FT DRB5*01:14, allele DRB5*02:02, allele FT DRB5*02:03, allele DRB5*02:04 and allele FT DRB5*02:05; dbSNP:rs1059580). FT /FTId=VAR_060960. FT VARIANT 87 87 A -> E (in allele DRB5*01:13). FT /FTId=VAR_060961. FT VARIANT 89 89 Y -> S (in allele DRB5*01:12; FT dbSNP:rs41541218). FT /FTId=VAR_060962. FT VARIANT 96 96 F -> I (in allele DRB5*01:06, allele FT DRB5*01:07, allele DRB5*01:11, allele FT DRB5*02:02 and allele DRB5*02:03; FT dbSNP:rs696318). FT /FTId=VAR_060964. FT VARIANT 96 96 F -> L (in allele DRB5*02:05; FT dbSNP:rs696318). FT /FTId=VAR_060963. FT VARIANT 99 99 D -> E (in dbSNP:rs41559913). FT /FTId=VAR_060965. FT VARIANT 99 99 D -> G (in dbSNP:rs41545413). FT /FTId=VAR_060966. FT VARIANT 99 99 D -> H (in dbSNP:rs41547217). FT /FTId=VAR_060967. FT VARIANT 99 99 D -> N (in allele DRB5*01:09; FT dbSNP:rs41547217). FT /FTId=VAR_060968. FT VARIANT 99 99 D -> Q (in allele DRB5*01:06, allele FT DRB5*01:11, allele DRB5*02:02, allele FT DRB5*02:03, allele DRB5*02:04 and allele FT DRB5*02:05; requires 2 nucleotide FT substitutions). FT /FTId=VAR_060969. FT VARIANT 99 99 D -> R (in allele DRB5*01:12; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060970. FT VARIANT 100 100 R -> A (in allele DRB5*01:06, allele FT DRB5*01:11, allele DRB5*02:02, allele FT DRB5*02:03 and allele DRB5*02:04; FT requires 2 nucleotide substitutions). FT /FTId=VAR_060971. FT VARIANT 100 100 R -> G (in dbSNP:rs41551116). FT /FTId=VAR_060972. FT VARIANT 100 100 R -> T (in allele DRB5*01:03; FT dbSNP:rs41544215). FT /FTId=VAR_060973. FT VARIANT 103 103 A -> E (in allele DRB5*01:12; FT dbSNP:rs1059598). FT /FTId=VAR_060974. FT VARIANT 103 103 A -> L (in allele DRB5*01:04; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060975. FT VARIANT 106 106 T -> N (in dbSNP:rs115817940). FT /FTId=VAR_050359. FT VARIANT 107 107 Y -> V (in allele DRB5*01:12; requires 2 FT nucleotide substitutions). FT /FTId=VAR_060976. FT VARIANT 114 114 V -> A (in allele DRB5*01:06, allele FT DRB5*02:02, allele DRB5*02:04 and allele FT DRB5*02:05; dbSNP:rs1136778). FT /FTId=VAR_060977. FT VARIANT 115 115 G -> V (in allele DRB5*01:06, allele FT DRB5*02:02, allele DRB5*02:04 and allele FT DRB5*02:05; dbSNP:rs41556512). FT /FTId=VAR_060978. FT VARIANT 154 154 G -> A (in dbSNP:rs113395425). FT {ECO:0000269|PubMed:3099214, FT ECO:0000269|PubMed:3476943}. FT /FTId=VAR_039872. FT VARIANT 164 164 S -> G (in allele DRB5*02:02; FT dbSNP:rs1059633). FT /FTId=VAR_060979. FT VARIANT 186 186 T -> I (in allele DRB5*02:02; FT dbSNP:rs41559420). FT /FTId=VAR_060980. FT VARIANT 232 232 V -> I (in allele DRB5*02:02; FT dbSNP:rs41553512). FT /FTId=VAR_060981. FT CONFLICT 139 139 Q -> E (in Ref. 11; AA sequence). FT {ECO:0000305}. FT STRAND 36 47 {ECO:0000244|PDB:1FV1}. FT TURN 48 51 {ECO:0000244|PDB:1FV1}. FT STRAND 52 61 {ECO:0000244|PDB:1FV1}. FT STRAND 64 70 {ECO:0000244|PDB:1FV1}. FT TURN 71 73 {ECO:0000244|PDB:1FV1}. FT STRAND 75 80 {ECO:0000244|PDB:1FV1}. FT HELIX 81 83 {ECO:0000244|PDB:1FV1}. FT HELIX 84 91 {ECO:0000244|PDB:1FV1}. FT HELIX 94 101 {ECO:0000244|PDB:1FV1}. FT HELIX 103 106 {ECO:0000244|PDB:1FV1}. FT HELIX 108 115 {ECO:0000244|PDB:1FV1}. FT HELIX 116 118 {ECO:0000244|PDB:1FV1}. FT TURN 119 121 {ECO:0000244|PDB:1FV1}. FT STRAND 127 132 {ECO:0000244|PDB:1FV1}. FT STRAND 137 154 {ECO:0000244|PDB:1FV1}. FT STRAND 157 166 {ECO:0000244|PDB:1FV1}. FT STRAND 169 173 {ECO:0000244|PDB:1FV1}. FT STRAND 180 182 {ECO:0000244|PDB:1FV1}. FT STRAND 184 192 {ECO:0000244|PDB:1FV1}. FT STRAND 199 205 {ECO:0000244|PDB:1FV1}. FT STRAND 213 218 {ECO:0000244|PDB:1FV1}. SQ SEQUENCE 266 AA; 30056 MW; 0D4335BAEEA6AF22 CRC64; MVCLKLPGGS YMAKLTVTLM VLSSPLALAG DTRPRFLQQD KYECHFFNGT ERVRFLHRDI YNQEEDLRFD SDVGEYRAVT ELGRPDAEYW NSQKDFLEDR RAAVDTYCRH NYGVGESFTV QRRVEPKVTV YPARTQTLQH HNLLVCSVNG FYPGSIEVRW FRNSQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAQ SESAQSKMLS GVGGFVLGLL FLGAGLFIYF KNQKGHSGLH PTGLVS // ID E7ENX8_HUMAN Unreviewed; 843 AA. AC E7ENX8; DT 08-MAR-2011, integrated into UniProtKB/TrEMBL. DT 08-MAR-2011, sequence version 1. DT 12-SEP-2018, entry version 63. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSP00000391806}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000391806, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000391806, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000391806} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL669918; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; E7ENX8; -. DR STRING; 9606.ENSP00000391806; -. DR EPD; E7ENX8; -. DR MaxQB; E7ENX8; -. DR PaxDb; E7ENX8; -. DR PeptideAtlas; E7ENX8; -. DR PRIDE; E7ENX8; -. DR Ensembl; ENST00000452392; ENSP00000391806; ENSG00000250264. DR UCSC; uc063nru.1; human. DR EuPathDB; HostDB:ENSG00000250264.1; -. DR GeneCards; ENSG00000250264; -. DR eggNOG; KOG0058; Eukaryota. DR eggNOG; COG1132; LUCA. DR GeneTree; ENSGT00550000074497; -. DR InParanoid; E7ENX8; -. DR OMA; FNQFFVG; -. DR OrthoDB; EOG091G05Q7; -. DR PhylomeDB; E7ENX8; -. DR TreeFam; TF105197; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000250264; Expressed in 80 organ(s), highest expression level in apex of heart. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0042825; C:TAP complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042287; F:MHC protein binding; IEA:InterPro. DR GO; GO:0015440; F:peptide-transporting ATPase activity; IEA:InterPro. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 1.20.1560.10; -; 1. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR013305; ABC_Tap-like. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005293; Tap2/ABCB3. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR PRINTS; PR01897; TAP2PROTEIN. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR TIGRFAMs; TIGR00958; 3a01208; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 56 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 169 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 189 208 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 153 435 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 468 728 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 730 820 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NP_BIND 503 510 ATP. {ECO:0000256|PROSITE- FT ProRule:PRU00434}. FT NON_TER 843 843 {ECO:0000313|Ensembl:ENSP00000391806}. SQ SEQUENCE 843 AA; 92999 MW; A6FDC899742EDCD4 CRC64; MRLPDLRPWT SLLLVDAALL WLLQGPLGTL LPQGLPGLWL EGTLRLGGLW GLLKLRGLLG FVGTLLLPLC LATPLTVSLR ALVAGASRAP PARVASAPWS WLLVGYGAAG LSWSLWAVLS PPGAQEKEQD QVNNKVLMWR LLKLSRPDLP LLVAAFFFLV LAVLGETLIP HYSGRVIDIL GGDFDPHAFA SAIFFMCLFS FGSSLSAGCR GGCFTYTMSR INLRIREQLF SSLLRQDLGF FQETKTGELN SRLSSDTTLM SNWLPLNANV LLRSLVKVVG LYGFMLSISP RLTLLSLLHM PFTIAAEKVY NTRHQEVLRE IQDAVARAGQ VVREAVGGLQ TVRSFGAEEH EVCRYKEALE QCRQLYWRRD LERALYLLVR RVLHLGVQML MLSCGLQQMQ DGELTQGSLL SFMIYQESVG SYVQTLVYIY GDMLSNVGAA EKVFSYMDRQ PNLPSPGTLA PTTLQGVVKF QDVSFAYPNR PDRPVLKGLT FTLRPGEVTA LVGPNGSGKS TVAALLQNLY QPTGGQVLLD EKPISQYEHC YLHSQVVSVG QEPVLFSGSV RNNIAYGLQS CEDDKVMAAA QAAHADDFIQ EMEHGIYTDV GEKGSQLAAG QKQRLAIARA LVRDPRVLIL DEATSALDVQ CEQANGFWVG PLGGGSASES DPTGFLHDSR HRLSSDVGMF VALTKLGQPD AEQWNSRLDL LERSRQAVDG VCRHNYRLGA PFTVGRKVQP EVTVYPERTP LLHQHNLLHC SVTGFYPGDI KIKWFLNGQE ERAGVMSTGP IRNGDWTFQT VVMLEMTPEL GHVYTCLVDH SSLLSPVSVE WRAQSEYSWR KMLSGIAAFL LGL // ID E9PIB1_HUMAN Unreviewed; 136 AA. AC E9PIB1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 12-SEP-2018, entry version 45. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000436686}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000436686}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000436686, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000436686, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000436686} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; E9PIB1; -. DR EPD; E9PIB1; -. DR PeptideAtlas; E9PIB1; -. DR PRIDE; E9PIB1; -. DR Ensembl; ENST00000484729; ENSP00000436686; ENSG00000179344. DR UCSC; uc063nrl.1; human. DR EuPathDB; HostDB:ENSG00000179344.16; -. DR HGNC; HGNC:4944; HLA-DQB1. DR OpenTargets; ENSG00000179344; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000179344; Expressed in 206 organ(s), highest expression level in right lung. DR ExpressionAtlas; E9PIB1; baseline and differential. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Proteomics identification {ECO:0000213|MaxQB:E9PIB1, KW ECO:0000213|PeptideAtlas:E9PIB1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 136 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003242851. FT DOMAIN 45 119 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 136 AA; 15771 MW; 1E895654821FEA00 CRC64; MSWKKALRIP GDLRVATVTL MLAMLSSLLA EGRDSPEDFV FQFKGMCYFT NGTERVRLVT RYIYNREEYA RFDSDVGVYR AVTPQGRPDA EYWNSQKEVL EGTRAELDTV CRHNYEVAFR GILQRRGMVT GLSRSW // ID E9Q479_MOUSE Unreviewed; 245 AA. AC E9Q479; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 12-SEP-2018, entry version 60. DE SubName: Full=Histocompatibility 2, O region beta locus {ECO:0000313|Ensembl:ENSMUSP00000129657}; GN Name=H2-Ob {ECO:0000313|Ensembl:ENSMUSP00000129657, GN ECO:0000313|MGI:MGI:95925}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000129657, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000129657, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000129657, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000129657} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000129657}; RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR974422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; E9Q479; -. DR SMR; E9Q479; -. DR MaxQB; E9Q479; -. DR PRIDE; E9Q479; -. DR Ensembl; ENSMUST00000167280; ENSMUSP00000129657; ENSMUSG00000041538. DR UCSC; uc008cbz.1; mouse. DR MGI; MGI:95925; H2-Ob. DR GeneTree; ENSGT00900000140849; -. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000041538; Expressed in 74 organ(s), highest expression level in lymph node. DR ExpressionAtlas; E9Q479; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0005764; C:lysosome; ISO:MGI. DR GO; GO:0042613; C:MHC class II protein complex; ISO:MGI. DR GO; GO:0023026; F:MHC class II protein complex binding; ISO:MGI. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; ISO:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|EPD:E9Q479, KW ECO:0000213|MaxQB:E9Q479}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 245 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003245685. FT TRANSMEM 199 221 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 82 187 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 245 AA; 27535 MW; 75D919AC03C15073 CRC64; MGAGRAPWVV ALLVNLMRLD SFMIEGRDSP ENFVIQAKAD CYFTNGTEKV HLLVRFIFNL EEYLHFDSDL GMFVALTELG EPDADQWNKR LDLLETSRAA VNMVCRQKYK LGAPFTVERN GFYPGDISVK WFRNGQEERS GVMSTGLVRN GDWTFQTTVM LEMIPELGDI YSCLVEHPGL LRPVSVAWMA QSEYSWKKIL SGAAVFLLGL IVFLVGVVIH LKAQKASVET QPGNEASRES LHSQP // ID F1M7F9_RAT Unreviewed; 248 AA. AC F1M7F9; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 12-SEP-2018, entry version 50. DE SubName: Full=Rano class II histocompatibility antigen, D-1 beta chain {ECO:0000313|Ensembl:ENSRNOP00000057075}; GN Name=RT1-Db1 {ECO:0000313|Ensembl:ENSRNOP00000057075, GN ECO:0000313|RGD:1593282}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000057075, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000057075, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000057075, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000057075} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000057075}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AABR07072809; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PRIDE; F1M7F9; -. DR Ensembl; ENSRNOT00000060327; ENSRNOP00000057075; ENSRNOG00000033215. DR RGD; 1593282; RT1-Db1. DR GeneTree; ENSGT00900000140849; -. DR Reactome; R-RNO-202424; Downstream TCR signaling. DR Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-RNO-202433; Generation of second messenger molecules. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Reactome; R-RNO-389948; PD-1 signaling. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000033215; Expressed in 10 organ(s), highest expression level in spleen. DR ExpressionAtlas; F1M7F9; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:F1M7F9}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 248 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003265843. FT TRANSMEM 211 232 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 108 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 248 AA; 28055 MW; 27C8ECAA65520A62 CRC64; MVWLARDSCV AAVILLLTVL SPPVALVRDP TPRFLEQYKS ECYFYNGTQR VRLLVRYIYN REEYTRFDSD VGEFRAVTEL GRRAAVDTIC RHNYEISDRF LVPRTVEPKV TVYPSKTQPL KHHNLLVCSV SDFYPGSVEV RWFRNGEEEK DGLVSTGLIP NGDWTFQLLV MLEMVPQGGE VYTCQVEHPS LTSPVRVEWK AQSTSAQNKK MSGVGGIVLG LLFLGAGLFV YFRNQKGQSG LQPTGLLN // ID F1MIY6_BOVIN Unreviewed; 252 AA. AC F1MIY6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 2. DT 12-SEP-2018, entry version 49. DE SubName: Full=MHC class II antigen DS beta {ECO:0000313|Ensembl:ENSBTAP00000020679}; GN Name=DSB {ECO:0000313|Ensembl:ENSBTAP00000020679}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000020679, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000020679, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000020679, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] {ECO:0000313|Ensembl:ENSBTAP00000020679} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000020679}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; DAAA02054875; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9913.ENSBTAP00000020679; -. DR PaxDb; F1MIY6; -. DR Ensembl; ENSBTAT00000020679; ENSBTAP00000020679; ENSBTAG00000015565. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1MIY6; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-BTA-202424; Downstream TCR signaling. DR Reactome; R-BTA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-BTA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-BTA-202433; Generation of second messenger molecules. DR Reactome; R-BTA-2132295; MHC class II antigen presentation. DR Reactome; R-BTA-389948; PD-1 signaling. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000015565; Expressed in 5 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 252 AA; 28883 MW; B1CB48BE2D5262EE CRC64; MVCLWFPPGS WTVILPVILM VLSPLLAWAG NTRTLFMVQG KSECHFSNGT QQVRFLDRYI YNREEQVQFD SLVGEYRART EMGRPAAERW NRWPQALQRA RAAVHAYCAS NYEFFASRTV QRRVQPTVTV YPVKSRPLWH HNLLVCSVNG FYPGHIEVRW FRNGQEEEAG VVSTGLIPNG DWTFQIMVML EIVPQGGEVY ACHVEHPSRT SPVTVEWRAQ DESSQEKMLS GIGACVLGLL FLGMGLLFYI RR // ID F1MJU5_BOVIN Unreviewed; 266 AA. AC F1MJU5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 2. DT 12-SEP-2018, entry version 54. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSBTAP00000018484}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000018484, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000018484, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000018484, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] {ECO:0000313|Ensembl:ENSBTAP00000018484} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000018484}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; DAAA02055286; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02055287; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02055288; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02055289; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02055290; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02055291; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; F1MJU5; -. DR STRING; 9913.ENSBTAP00000018484; -. DR PaxDb; F1MJU5; -. DR Ensembl; ENSBTAT00000018484; ENSBTAP00000018484; ENSBTAG00000013919. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1MJU5; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-BTA-202424; Downstream TCR signaling. DR Reactome; R-BTA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-BTA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-BTA-202433; Generation of second messenger molecules. DR Reactome; R-BTA-2132295; MHC class II antigen presentation. DR Reactome; R-BTA-389948; PD-1 signaling. DR ChiTaRS; BOLA-DRB3; cattle. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000013919; Expressed in 9 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:F1MJU5}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003266010. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30555 MW; 59A0BFB644352303 CRC64; MVCLYFSGGS WMAALIVMLM VLCPPLAWAR EIQPHFLEYY KRECHFFNGT ERVRFLDRYF HNGEEYVRFD SDWGEYRAVT ELGQRVAEYC NSQKDFLERA RAAVDTYCRH NYGVGESFTV QRRVEPIVTV YPAKTQPLQH HNLLVCSVNG FYPGHIEVRW FRNGHEEEAG VISTGLIQNG DWTFQTMVML ETVPQSGEVY TCQVEHPSRT SPITVEWRAR SDSAQSKMMS GVGGFVLGLL FLAVGLFIYF RNQKGHPTLQ PTGLLS // ID F1N610_BOVIN Unreviewed; 261 AA. AC F1N610; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 12-SEP-2018, entry version 58. DE SubName: Full=BoLa class II histocompatibility antigen, DQB*0101 beta chain precursor {ECO:0000313|Ensembl:ENSBTAP00000026100}; GN Name=BLA-DQB {ECO:0000313|Ensembl:ENSBTAP00000026100}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000026100, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000026100, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000026100, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] {ECO:0000313|Ensembl:ENSBTAP00000026100} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000026100}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; DAAA02055305; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02055306; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9913.ENSBTAP00000026100; -. DR PaxDb; F1N610; -. DR Ensembl; ENSBTAT00000026100; ENSBTAP00000026100; ENSBTAG00000019588. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1N610; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-BTA-202424; Downstream TCR signaling. DR Reactome; R-BTA-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-BTA-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-BTA-202433; Generation of second messenger molecules. DR Reactome; R-BTA-2132295; MHC class II antigen presentation. DR Reactome; R-BTA-389948; PD-1 signaling. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000019588; Expressed in 9 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003267827. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 233 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29923 MW; 1777BF8915179AA6 CRC64; MSGMVALRIP RGLWTAVVMV TLVMLSTPGA EGRDSPKDFV LQFKGLCYFT NGTERVRYVT RYIYNQEEYV RFDSDWDEYR ALTPLGRPAA EYWNSQKDIL EQTRAEADTV CRHNYQAELI TSLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPSQIK VRWFRNDREE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCRVEHP SLQSPIMVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI IHHRSQKGLM R // ID F1NIV8_CHICK Unreviewed; 310 AA. AC F1NIV8; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 3. DT 12-SEP-2018, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGALP00000040418}; GN Name=DMB1 {ECO:0000313|Ensembl:ENSGALP00000040418}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|Ensembl:ENSGALP00000040418, ECO:0000313|Proteomes:UP000000539}; RN [1] {ECO:0000313|Ensembl:ENSGALP00000040418, ECO:0000313|Proteomes:UP000000539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000040418, RC ECO:0000313|Proteomes:UP000000539}; RX PubMed=15592404; DOI=10.1038/nature03154; RG International Chicken Genome Sequencing Consortium; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., RA Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., RA Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., RA Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C., RA Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., RA Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., RA Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., RA Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., RA Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., RA Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., RA van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., RA Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., RA Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., RA Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., RA Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., RA Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., RA Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., RA Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., RA King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., RA Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., RA Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., RA Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., RA Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., RA Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., RA Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., RA Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., RA Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., RA Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., RA Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., RA Mardis E.R., Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide RT unique perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [2] {ECO:0000313|Ensembl:ENSGALP00000040418} RP IDENTIFICATION. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000040418}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AADN04000555; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001299831.1; NM_001312902.1. DR UniGene; Gga.11016; -. DR Ensembl; ENSGALT00000041213; ENSGALP00000040418; ENSGALG00000000162. DR GeneID; 106182184; -. DR KEGG; gga:106182184; -. DR CTD; 106182184; -. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000000539; Chromosome 16. DR Bgee; ENSGALG00000000162; Expressed in 11 organ(s), highest expression level in female gonad. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000539}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000539}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 310 AA; 32642 MW; D94BD6E174BFBCE8 CRC64; MKAAVLLMGP RGFRVLGAMG LVLSCGTAGA FVVHMASSCP LLANGSLGGF DLTVAFNKNP LLCYDPDVHR FYPCDWGLLH TIATLLAAIL NDDTTWVQRA EARRQACTEL AAQFWTHTAL RRTPPQVRIV PIPISNDPDT VHLICHVWGF YPPAVTIQWL HNGLVVASGD TKLLPNGDWT YRTQVALRAS TAAGSTYTCS VWHSSLEQPL QEDWSPNLSP AMMVKVAVAA MALTLGLVAL SAGVFSFCQR PRAPGAGPSP HPDAGSHSNP GPQNDPGPSS GPHPSPGPHP SPGPHSGLGP GPGSAPGPYP // ID A5HUL2_CHICK Unreviewed; 263 AA. AC A5HUL2; F1NSZ6; DT 26-JUN-2007, integrated into UniProtKB/TrEMBL. DT 26-JUN-2007, sequence version 1. DT 12-SEP-2018, entry version 97. DE SubName: Full=MHC class II beta chain 1 {ECO:0000313|EMBL:BAF62996.1}; GN Name=BLB1 {ECO:0000313|EMBL:BAF62996.1, GN ECO:0000313|Ensembl:ENSGALP00000008911}; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031 {ECO:0000313|EMBL:BAF62996.1}; RN [1] {ECO:0000313|Ensembl:ENSGALP00000008911, ECO:0000313|Proteomes:UP000000539} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000008911, RC ECO:0000313|Proteomes:UP000000539}; RX PubMed=15592404; DOI=10.1038/nature03154; RG International Chicken Genome Sequencing Consortium; RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., RA Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., RA Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., RA Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A., Kremitzki C., RA Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., RA Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., RA Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., RA Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., RA Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., RA Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., RA van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., RA Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., RA Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., RA Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., RA Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., RA Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., RA Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., RA Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., RA King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., RA Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., RA Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., RA Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., RA Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., RA Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., RA Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., RA Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., RA Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., RA Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., RA Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., RA Mardis E.R., Wilson R.K.; RT "Sequence and comparative analysis of the chicken genome provide RT unique perspectives on vertebrate evolution."; RL Nature 432:695-716(2004). RN [2] {ECO:0000313|EMBL:BAF62996.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17513765; DOI=10.4049/jimmunol.178.11.7162; RA Shiina T., Briles W.E., Goto R.M., Hosomichi K., Yanagiya K., RA Shimizu S., Inoko H., Miller M.M.; RT "Extended gene map reveals tripartite motif, C-type lectin, and Ig RT superfamily type genes within a subregion of the chicken MHC-B RT affecting infectious disease."; RL J. Immunol. 178:7162-7172(2007). RN [3] {ECO:0000313|EMBL:BAG69445.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cornell-N {ECO:0000313|EMBL:BAG69445.1}; RX PubMed=18714011; RA Hosomichi K., Miller M.M., Goto R.M., Wang Y., Suzuki S., Kulski J.K., RA Nishibori M., Inoko H., Hanzawa K., Shiina T.; RT "Contribution of mutation, recombination, and gene conversion to RT chicken MHC-B haplotype diversity."; RL J. Immunol. 181:3393-3399(2008). RN [4] {ECO:0000313|Ensembl:ENSGALP00000008911} RP IDENTIFICATION. RC STRAIN=Red jungle fowl {ECO:0000313|Ensembl:ENSGALP00000008911}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AADN04000554; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB268588; BAF62996.1; -; Genomic_DNA. DR EMBL; AB426152; BAG69445.1; -; Genomic_DNA. DR RefSeq; XP_015150480.1; XM_015294994.1. DR UniGene; Gga.4924; -. DR STRING; 9031.ENSGALP00000000193; -. DR Ensembl; ENSGALT00000008925; ENSGALP00000008911; ENSGALG00000000141. DR GeneID; 693256; -. DR CTD; 693256; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000000539; Chromosome 16. DR Bgee; ENSGALG00000000141; Expressed in 11 organ(s), highest expression level in female gonad. DR ExpressionAtlas; A5HUL2; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000539}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000539}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014296980. FT TRANSMEM 225 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 29246 MW; 1631C416319CBFB2 CRC64; MGSGRVPAAG AVLVALLALG ARPAAGTRPS AFFQWTFKAE CHYLNGTERV RYLVRYVYNR QEYAHFDSDV GKHVADTPLG EPQAEYWNSN AEILENRMNE VDTYCRHNYG VVESFTVQRS VEPKVRVSAL QSGSLPETDR LACYVTGFYP PEIEVKWFLN GREETERVVS TDVMQNGDWT YQVLVVLETV PRRGDSYVCR VEHASLRQPI SQAWEPPADA GRSKLLTGVG GFVLGLVFLA LGLFVFLRGQ KGRPVAAAPG MLN // ID F1PSQ5_CANLF Unreviewed; 237 AA. AC F1PSQ5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 12-SEP-2018, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCAFP00000001282}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000001282, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000001282, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000001282, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000001282} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000001282}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAEX03008236; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F1PSQ5; -. DR STRING; 9615.ENSCAFP00000001282; -. DR PaxDb; F1PSQ5; -. DR Ensembl; ENSCAFT00000001396; ENSCAFP00000001282; ENSCAFG00000000900. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1PSQ5; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Reactome; R-CFA-2132295; MHC class II antigen presentation. DR Proteomes; UP000002254; Chromosome 12. DR Bgee; ENSCAFG00000000900; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 51 120 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT DOMAIN 145 195 IGc1. {ECO:0000259|SMART:SM00407}. SQ SEQUENCE 237 AA; 26496 MW; 0B10D8AF8F8FD92E CRC64; SPSLRHLDQL LGLWGTKASS APYSLLYSPL YSYVNLIVYS PQSFTVYQRR STCYELNELN GTHHLLHTEL FAQLDSAAGV FAAVSELGRV TARNWNPREF LALRQSAVDT ACKHIFDLDQ GFTLQRRVQP KVNVSPSKKG RLQHHNLLAG HVSDFSTGHI HNGDWTFQIL VMLEMTLQQG DIYTCQVEHP SLDGPVTVEW TRGTSDSAWS KMLAGVGGFV LGLIALLVSF ILHFRSQ // ID F1PTQ6_CANLF Unreviewed; 269 AA. AC F1PTQ6; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 2. DT 12-SEP-2018, entry version 57. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCAFP00000001171}; GN Name=LOC100856137 {ECO:0000313|Ensembl:ENSCAFP00000001171}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000001171, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000001171, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000001171, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000001171} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000001171}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAEX03008235; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003639463.1; XM_003639415.3. DR ProteinModelPortal; F1PTQ6; -. DR STRING; 9615.ENSCAFP00000001171; -. DR PaxDb; F1PTQ6; -. DR PRIDE; F1PTQ6; -. DR Ensembl; ENSCAFT00000001279; ENSCAFP00000001171; ENSCAFG00000000814. DR GeneID; 100856137; -. DR KEGG; cfa:100856137; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1PTQ6; -. DR KO; K06752; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-CFA-2132295; MHC class II antigen presentation. DR Proteomes; UP000002254; Chromosome 12. DR Bgee; ENSCAFG00000000814; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl. DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl. DR GO; GO:0008134; F:transcription factor binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0002344; P:B cell affinity maturation; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl. DR GO; GO:0046635; P:positive regulation of alpha-beta T cell activation; IEA:Ensembl. DR GO; GO:0002579; P:positive regulation of antigen processing and presentation; IEA:Ensembl. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003267620. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 269 AA; 30522 MW; 438D4E21579D6F76 CRC64; MSGKMTLCIP RGFWTAAVMM ILVVLSIPVA EGRDSPQDFV YQCKAECYFT NGTERVRFLA KYIYNREEFV RFDSDVGEFR AVTELGRPSA EYWNGQKEIL EQERATVDTV CRHNYGVEEL YTLQRRVEPT VTISPSRTEV LNHHNLLVCS VTDFYPGQIK VRWFRNDQEQ TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHA SLQSPITVQW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IRHRSQKGSR GSPPAGLLH // ID F1QNN2_DANRE Unreviewed; 130 AA. AC F1QNN2; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 3. DT 12-SEP-2018, entry version 56. DE SubName: Full=Si:dkey-33b17.3 {ECO:0000313|Ensembl:ENSDARP00000139928}; GN Name=si:dkey-33b17.3 {ECO:0000313|Ensembl:ENSDARP00000139928, GN ECO:0000313|ZFIN:ZDB-GENE-030616-171}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000139928, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000139928, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000139928, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000139928} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000139928}; RG Ensembl; RL Submitted (NOV-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CT583723; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 7955.ENSDARP00000070311; -. DR PaxDb; F1QNN2; -. DR Ensembl; ENSDART00000161194; ENSDARP00000139928; ENSDARG00000104730. DR ZFIN; ZDB-GENE-030616-171; si:dkey-33b17.3. DR GeneTree; ENSGT00900000140849; -. DR OMA; NQEETAY; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR Pfam; PF07654; C1-set; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 106 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 70 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 130 AA; 14699 MW; 1B34AAE21908372C CRC64; MCSAYDFYPP HINVFWLRNG EVMTSEVTST MEMADGDWYY QIHSELEYSP KPGERISCVI EHASSNKPMI YDWDPSLPVF ERNKISIGVS ALVLGIITAA AGIIYYKKKT TGRTSVVPSR LITLPLMFGR // ID F1QRR0_DANRE Unreviewed; 263 AA. AC F1QRR0; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 12-SEP-2018, entry version 47. DE SubName: Full=Si:busm1-228j01.6 {ECO:0000313|Ensembl:ENSDARP00000088910}; GN Name=si:busm1-228j01.6 {ECO:0000313|Ensembl:ENSDARP00000088910, GN ECO:0000313|ZFIN:ZDB-GENE-030616-396}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000088910, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000088910} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000088910}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000088910, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000088910, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CU914776; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 7955.ENSDARP00000088910; -. DR PaxDb; F1QRR0; -. DR Ensembl; ENSDART00000098138; ENSDARP00000088910; ENSDARG00000041705. DR ZFIN; ZDB-GENE-030616-396; si:busm1-228j01.6. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1QRR0; -. DR OMA; DWNNYKD; -. DR TreeFam; TF333780; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000041705; Expressed in 3 organ(s), highest expression level in pharyngeal gill. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003270233. FT TRANSMEM 216 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 113 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 30074 MW; 9357D1197E1B4022 CRC64; MNAKINYSLA AVFLSALFET VHAYYTYAQI QCHVSDSLQK IEFIFSVTYN MIELVRYNST EDTFFGYTAI GQKFAEEYNK DKVLLAQHDF VLNQCRELGD VILPNAVWLA VKPEVIIRSV TEAKGNRKAV LVCSAYDFYP KGIKLTWMRD DKKVTAELTS SEVMADGHWH YQIHSYLEYF PQTGEKISCV VDHASSLKPM IYYWDPSLPE SERSKIILGA VGLLMGIFTA AAGVIYYKRK QTGFYRLPVC LLPMETMNDT ELQ // ID F1QUL1_DANRE Unreviewed; 244 AA. AC F1QUL1; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 12-SEP-2018, entry version 47. DE SubName: Full=Si:busm1-228j01.4 {ECO:0000313|Ensembl:ENSDARP00000110668}; GN Name=si:busm1-228j01.4 {ECO:0000313|Ensembl:ENSDARP00000110668, GN ECO:0000313|ZFIN:ZDB-GENE-030616-394}; GN Synonyms=mhc2dcb {ECO:0000313|ZFIN:ZDB-GENE-030616-394}, GN si:busm1-37i06.8 {ECO:0000313|ZFIN:ZDB-GENE-030616-394}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000110668, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000110668} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000110668}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000110668, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000110668, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CU914776; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 7955.ENSDARP00000110668; -. DR PaxDb; F1QUL1; -. DR Ensembl; ENSDART00000123658; ENSDARP00000110668; ENSDARG00000088872. DR ZFIN; ZDB-GENE-030616-394; si:busm1-228j01.4. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1QUL1; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF333780; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000088872; Expressed in 5 organ(s), highest expression level in pharyngeal gill. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 244 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003270287. FT TRANSMEM 217 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 244 AA; 27786 MW; 61B6C3E0EEF51968 CRC64; MQFSRVACLA MILSALLEKV CGNYGYLQSQ CRVLSSTKKV ELIFSFIFNK IEYIRYNSTD QKIVGYTEFG EKFVENYKNN TFVLVLAEFG IDNCKKIAKA LISDGMLNHV TVKPEVIIRS VTEAKGNQKA VLVCSAYDFY PKAIKLTWMR NDKKVTADVM SIEEMADGDW YYQIHSHLEY FPQPGEKISC VVDHASFHKP MIYYWDPSLP ETERSKIILG AVGLLMGIFT AAAGVIYYKR KQTG // ID F1QVI4_DANRE Unreviewed; 250 AA. AC F1QVI4; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 12-SEP-2018, entry version 53. DE SubName: Full=Si:busm1-104n07.3 {ECO:0000313|Ensembl:ENSDARP00000088705}; GN Name=si:busm1-104n07.3 {ECO:0000313|Ensembl:ENSDARP00000088705, GN ECO:0000313|ZFIN:ZDB-GENE-030616-99}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000088705, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000088705} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000088705}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000088705, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000088705, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CU694322; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU694361; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005167291.1; XM_005167234.3. DR UniGene; Dr.162083; -. DR ProteinModelPortal; F1QVI4; -. DR STRING; 7955.ENSDARP00000088705; -. DR PaxDb; F1QVI4; -. DR Ensembl; ENSDART00000097932; ENSDARP00000088705; ENSDARG00000074510. DR GeneID; 368703; -. DR KEGG; dre:368703; -. DR ZFIN; ZDB-GENE-030616-99; si:busm1-104n07.3. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1QVI4; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF333780; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000074510; Expressed in 11 organ(s), highest expression level in pharyngeal gill. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 28 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 221 242 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 118 207 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 250 AA; 28363 MW; 4076C7655752B57B CRC64; MSLLRLFYGH LILTLSVLIG AETANVYYRY TWIQCISSSK NLSDMVFIES LYFNKYLFTQ FNSNIGKYVG FSEYGIRNAE FRNNDTNLLL KKKAAVNKVC KNNAINHDKF IRNKAVKPKV KLTLVKPAGG RHPAVLMCSA YEFYPPHIRV YWLRNGEVIT SDVTSTMEMA DGDWYYQIHS ELEYSPKSGE RISCGIEHAS SNKPIITEWD SSRPASERNK IAIGASGVVL GIIIPAICFI YYKKTAEAVL // ID F1RBP5_DANRE Unreviewed; 241 AA. AC F1RBP5; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 6. DT 12-SEP-2018, entry version 51. DE SubName: Full=Si:busm1-104n07.3 {ECO:0000313|Ensembl:ENSDARP00000116857}; DE Flags: Fragment; GN Name=si:busm1-104n07.3 {ECO:0000313|Ensembl:ENSDARP00000116857, GN ECO:0000313|ZFIN:ZDB-GENE-030616-99}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000116857, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000116857} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116857}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSDARP00000116857, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000116857, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CU694322; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU694361; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSDART00000148323; ENSDARP00000116857; ENSDARG00000074510. DR ZFIN; ZDB-GENE-030616-99; si:busm1-104n07.3. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000074510; Expressed in 11 organ(s), highest expression level in pharyngeal gill. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 43 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 133 222 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSDARP00000116857}. FT NON_TER 241 241 {ECO:0000313|Ensembl:ENSDARP00000116857}. SQ SEQUENCE 241 AA; 27726 MW; A2FE58D3301549C1 CRC64; XDFWARFSRY SERVKMSLLR LFYGHLILTL SVLIGAETAN VYYRYTWIQC ISSSKNLSDM VFIESLYFNK YLFTQFNSNI GKYVGFSEYG IRNAEFRNND TNLLLKKKAA VNKVCKNNAI NHDKFIRNKA VKPKVKLTLV KPAGGRHPAV LMCSAYEFYP PHIRVYWLRN GEVITSDVTS TMEMADGDWY YQIHSELEYS PKSGERISCG IEHASSNKPI ITEWDSSRPA SERNKIAIGA S // ID F1RQ22_PIG Unreviewed; 277 AA. AC F1RQ22; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 03-MAY-2011, sequence version 1. DT 12-SEP-2018, entry version 45. DE SubName: Full=MHC class II, DO beta precursor {ECO:0000313|Ensembl:ENSSSCP00000001577}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSSSCP00000001577}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000001577, ECO:0000313|Proteomes:UP000008227}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00000001577, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000001577}; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSSCP00000001577} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEMK02000055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9823.ENSSSCP00000001577; -. DR PaxDb; F1RQ22; -. DR PRIDE; F1RQ22; -. DR Ensembl; ENSSSCT00000001619; ENSSSCP00000001577; ENSSSCG00000001459. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-SSC-2132295; MHC class II antigen presentation. DR Proteomes; UP000008227; Chromosome 7. DR Bgee; ENSSSCG00000001459; Expressed in 6 organ(s), highest expression level in kidney. DR ExpressionAtlas; F1RQ22; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 39 {ECO:0000256|SAM:SignalP}. FT CHAIN 40 277 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003271191. FT TRANSMEM 238 260 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 136 224 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 277 AA; 31260 MW; F2FD1440B23F2779 CRC64; MIYTTSFSFS PSRMGSSWVP WVVALLVTVI RLDSSMTQGR DSPEDFVIQA KADCYFTNGT QRVQFVVRFI FNLEEFVRFD SDLGKFVALT ELGQPDAELW NSRPDILESS RASVDVLCRR NYWLGAPLTV ERKVQPEVTV HPERTPSLQL RNLLLCSVTG FYPGAIEIRW FRNGQEQREG VLATGLIRNG DWTFQTVVML EMTPELGDVY TCLVDHPSLL SPVSVEWRAQ SDCSWTKLLI GVAAFLGGLT FLLVGIIIHV RARKGRVETQ LSGDEPH // ID F1RQ23_PIG Unreviewed; 261 AA. AC F1RQ23; DT 03-MAY-2011, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 3. DT 12-SEP-2018, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSSCP00000001576}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000001576, ECO:0000313|Proteomes:UP000008227}; RN [1] {ECO:0000313|Ensembl:ENSSSCP00000001576, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000001576}; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSSCP00000001576} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEMK02000055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F1RQ23; -. DR STRING; 9823.ENSSSCP00000001576; -. DR PaxDb; F1RQ23; -. DR PeptideAtlas; F1RQ23; -. DR PRIDE; F1RQ23; -. DR Ensembl; ENSSSCT00000001618; ENSSSCP00000001576; ENSSSCG00000031336. DR eggNOG; ENOG410KGZ2; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F1RQ23; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-SSC-202424; Downstream TCR signaling. DR Reactome; R-SSC-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-SSC-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-SSC-202433; Generation of second messenger molecules. DR Reactome; R-SSC-2132295; MHC class II antigen presentation. DR Reactome; R-SSC-389948; PD-1 signaling. DR Proteomes; UP000008227; Chromosome 7. DR Bgee; ENSSSCG00000001458; Expressed in 2 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5011723392. FT TRANSMEM 223 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 121 209 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29504 MW; 38EDCC1000AC1C3A CRC64; MSVVHWMAAL TVTLMLWSPP LACARDIPPV FMHQFKCECQ FSNGTERVRF LARYIYNTEE DVHFDSDLGE FRALTELGRP DAEYWNQQKG FLEQMRTKVD TMCRSNYLGI GSLMMQRRVK PRVTVYPAKT QPLQHHNLLV CSVTGFYPGH VEVRWFRNGQ EEAAGVVSTG LIPNGDWTFQ TMVMLETVPQ SGEVYSCRVE HPSLTSPVTV EWRAWSESAQ GKMLSGIGGC VLGLLVLAVG LFISCRRQKE HSGRQPTGLL S // ID F6QQE1_HORSE Unreviewed; 219 AA. AC F6QQE1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000010148}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000010148, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000010148, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000010148, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000010148} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000010148}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6QQE1; -. DR STRING; 9796.ENSECAP00000010148; -. DR PaxDb; F6QQE1; -. DR Ensembl; ENSECAT00000012842; ENSECAP00000010148; ENSECAG00000012400. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6QQE1; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000012400; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 193 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 219 AA; 25101 MW; 42246D6D6DF4455A CRC64; FMVQAKSECH FSNGMERVRL LDRYFYNGEE NVRFDSDVGE FRAMTELGRL DAEHWNRQKD DLERKRAEVD TFCRHNYGIF DSFMVQRRVS PTVTVYPVKT QPLQHHNLLL CSVNGFYPGH IEVRWLRNGQ EEEAGVISTG LIRNGDWTFQ TLVMLQTVPQ SGEVYTCQVE HPSLTSPVTV EWRAQSESAQ SKMLSGVGGF VLGLLILGAG LFIHCRNQK // ID F6R1U8_HORSE Unreviewed; 266 AA. AC F6R1U8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 55. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AFU83069.1}; GN Name=Eqca-DRB3 {ECO:0000313|EMBL:AFU83069.1}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000010867, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000010867, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000010867, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000010867} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000010867}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000313|EMBL:AFU83069.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Standardbred #1406 {ECO:0000313|EMBL:AFU83071.1}, RC Thoroughbred #0834 {ECO:0000313|EMBL:AFU83069.1}, RC Thoroughbred #1536 {ECO:0000313|EMBL:AFU83072.1}, and RC Thoroughbred #3729 {ECO:0000313|EMBL:AFU83070.1}; RA Miller D., Tallmadge R.L., Binns M., Brown H.E., Zhu B., Antczak D.F.; RT "Polymorphism at Expressed Equine MHC Class II DQ and DR Loci."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JQ254095; AFU83069.1; -; mRNA. DR EMBL; JQ254096; AFU83070.1; -; mRNA. DR EMBL; JQ254097; AFU83071.1; -; mRNA. DR EMBL; JQ254098; AFU83072.1; -; mRNA. DR RefSeq; XP_005603562.1; XM_005603505.2. DR UniGene; Eca.13128; -. DR STRING; 9796.ENSECAP00000010867; -. DR Ensembl; ENSECAT00000013673; ENSECAP00000010867; ENSECAG00000012933. DR GeneID; 100052364; -. DR CTD; 248402; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000012933; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015091066. FT TRANSMEM 228 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30282 MW; A17E6833AF65FCFD CRC64; MLCLWFPGGS WMAALTVMLM VLNPPLGWAR NTQPHFLEYS TSECHFFNGT ERVRYLDRYF YNGKEYVRFD SDVGEYRALT ELGRRSAEYW NGQQDILEQK RAKVDTYCRH NYAVSESFLV QRRVEPTVTV YPAKTQPRQH HNLLVCSVNG FYPGHIEVRW LRNGQEEEAG VISTGLIRNG DWTFQTLVML ETVPQSGEVY TCQVEHPSQT SPVTVEWRAP SESAQSKMLS GVGGFVLGLL FLGAGLFIHR RNQKGHGGLQ PTGLLS // ID F6RSV4_ORNAN Unreviewed; 95 AA. AC F6RSV4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOANP00000008813}; OS Ornithorhynchus anatinus (Duckbill platypus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Monotremata; Ornithorhynchidae; Ornithorhynchus. OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000008813, ECO:0000313|Proteomes:UP000002279}; RN [1] {ECO:0000313|Proteomes:UP000002279} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Glennie {ECO:0000313|Proteomes:UP000002279}; RX PubMed=18464734; DOI=10.1038/nature06936; RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., RA Ponting C.P., Grutzner F., Belov K., Miller W., Clarke L., RA Chinwalla A.T., Yang S.P., Heger A., Locke D.P., Miethke P., RA Waters P.D., Veyrunes F., Fulton L., Fulton B., Graves T., Wallis J., RA Puente X.S., Lopez-Otin C., Ordonez G.R., Eichler E.E., Chen L., RA Cheng Z., Deakin J.E., Alsop A., Thompson K., Kirby P., RA Papenfuss A.T., Wakefield M.J., Olender T., Lancet D., Huttley G.A., RA Smit A.F., Pask A., Temple-Smith P., Batzer M.A., Walker J.A., RA Konkel M.K., Harris R.S., Whittington C.M., Wong E.S., Gemmell N.J., RA Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J., Zemann A., RA Churakov G., Kriegs J.O., Brosius J., Murchison E.P., RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D., RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A., RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., RA Taylor J., Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., RA Huang X., Stark A., Kheradpour P., Kellis M., Flicek P., Chen Y., RA Webber C., Hardison R., Nelson J., Hallsworth-Pepin K., Delehaunty K., RA Markovic C., Minx P., Feng Y., Kremitzki C., Mitreva M., Glasscock J., RA Wylie T., Wohldmann P., Thiru P., Nhan M.N., Pohl C.S., Smith S.M., RA Hou S., Nefedov M., de Jong P.J., Renfree M.B., Mardis E.R., RA Wilson R.K.; RT "Genome analysis of the platypus reveals unique signatures of RT evolution."; RL Nature 453:175-183(2008). RN [2] {ECO:0000313|Ensembl:ENSOANP00000008813} RP IDENTIFICATION. RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000008813}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSOANT00000008815; ENSOANP00000008813; ENSOANG00000005547. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6RSV4; -. DR OMA; RHKYELM; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000002279; Unplaced. DR Bgee; ENSOANG00000005547; Expressed in 7 organ(s), highest expression level in female gonad. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002279}; KW Reference proteome {ECO:0000313|Proteomes:UP000002279}. FT DOMAIN 6 80 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 95 AA; 11119 MW; 10C168D4BA810A65 CRC64; LYQAKSECYF YNGTDRVSFV DRYMYDRQEI VRFDSDVGVY VAVTELGRPD AQYWNSLQDF LDDTRGAVDR ICRHNYGVID GFSVQRRGLP ITTMI // ID F6SI57_CALJA Unreviewed; 275 AA. AC F6SI57; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 37. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 2 {ECO:0000313|Ensembl:ENSCJAP00000045561}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSCJAP00000045561}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000045561, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000045561, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000045561} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6SI57; -. DR Ensembl; ENSCJAT00000061144; ENSCJAP00000045561; ENSCJAG00000021548. DR GeneTree; ENSGT00900000140849; -. DR OMA; DWNNYKD; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 275 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015334642. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 275 AA; 31141 MW; 5BE4C6DA9CEB0133 CRC64; MALQIPRGFR AAAVTLMLAM LSTPVADGRD SPKDFVVQFK GMCYFTNGTE RVRGVARYIY NREEYARFDS DVGEFRAVTE LGRSTEDWNN YKDFLEQERA AVYTVCRHNY EAELRTTLQR RVEPTVTISP TRTEALNHHN LLVCSVTDFY PGQIKVRWFR NDQEETAGIV STSLIRNGDW TFQILVMLEM TPQRGDIYTC HVEHPSLQSP ITVEWRAHSE SAQSKMLSGI GGFVLGLIFL GLGLVIRHRG RKGPRGPPPA GNISAMIQVG REQVQ // ID A4UU57_MACMU Unreviewed; 258 AA. AC A4UU57; F6T9M3; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 12-SEP-2018, entry version 82. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:ABP02026.1}; GN Name=Mamu-DPB1 {ECO:0000313|EMBL:ABP02026.1}; GN Synonyms=MAMU-DPB {ECO:0000313|Ensembl:ENSMMUP00000025448}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|EMBL:ABP02026.1}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000025448, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000025448, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|EMBL:ABP02026.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=17989178; DOI=10.1128/JVI.01816-07; RA Giraldo-Vela J.P., Rudersdorf R., Chung C., Qi Y., Wallace L.T., RA Bimber B., Borchardt G.J., Fisk D.L., Glidden C.E., Loffredo J.T., RA Piaskowski S.M., Furlott J.R., Morales-Martinez J.P., Wilson N.A., RA Rehrauer W.M., Lifson J.D., Carrington M., Watkins D.I.; RT "The major histocompatibility complex class II alleles Mamu-DRB1*1003 RT and -DRB1*0306 are enriched in a cohort of simian immunodeficiency RT virus-infected rhesus macaque elite controllers."; RL J. Virol. 82:859-870(2008). RN [3] {ECO:0000313|Ensembl:ENSMMUP00000025448} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000025448}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [4] {ECO:0000313|EMBL:CDH93764.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=9701010Y {ECO:0000313|EMBL:CDH93764.1}; RA Otting N., Freie H.L.F., Van der Wiel M.K., Doxiadis G.G.M., RA Bontrop R.E.; RT "New MHC class II alleles in Chinese rhesus macaques."; RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030678; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; EF490966; ABP02026.1; -; mRNA. DR EMBL; HG514486; CDH93764.1; -; mRNA. DR RefSeq; XP_014991582.1; XM_015136096.1. DR UniGene; Mmu.17162; -. DR STRING; 9544.ENSMMUP00000025448; -. DR Ensembl; ENSMMUT00000027204; ENSMMUP00000025448; ENSMMUG00000019367. DR GeneID; 717969; -. DR CTD; 717969; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000019367; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015086460. FT TRANSMEM 227 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 228 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29336 MW; 439D53ACAA5F8B08 CRC64; MMVLEVSAAP GTVGLMALLM VLLTSVVQGR ATPENYVFQG RQECYAFNGT QRYLERYIYN REEYVRFDSD VGEFRAVTEL GRPDAEYWNS QKDLLEEMRA VVDTMCRYNY ELDEAVTLQR RVQPRVNIAP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETTGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHPSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRR KKVQRGSV // ID F6U0R7_MONDO Unreviewed; 240 AA. AC F6U0R7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000038507}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000038507, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000038507, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000038507} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6U0R7; -. DR STRING; 13616.ENSMODP00000038507; -. DR Ensembl; ENSMODT00000040107; ENSMODP00000038507; ENSMODG00000025678. DR eggNOG; ENOG410KGZ2; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6U0R7; -. DR OMA; QIRVTWL; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002280; Chromosome 2. DR Bgee; ENSMODG00000025678; Expressed in 2 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 240 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003347766. FT TRANSMEM 214 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 240 AA; 27593 MW; E18528F99F6FFDC0 CRC64; SVTVLLMVLD TLTVWSTDIP ENYLHQVRSE CHMTNGTQRV HFVGRLIYDR EEFVRFDSDV GLFEARTELW KSQVQKWNSQ KEIVERARSI VNVCRHNYQF YNKTIVQRKV KPRVKVFPAK TQPLGHHNLL LCSVTSFYPG EIKVSWFRNA KEEKSGVLST GQIRNGDWTF QTLVMLEMTP QRGDVFTCRV DHVSLQSPVF VDWRAQSESA QTKMLIGVGS LVFGMILLGV GLVISLRSSK // ID F6UB75_HUMAN Unreviewed; 175 AA. AC F6UB75; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSP00000412457}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000412457, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000412457, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000412457} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL645941; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F6UB75; -. DR PRIDE; F6UB75; -. DR Ensembl; ENST00000429234; ENSP00000412457; ENSG00000248993. DR UCSC; uc063nso.1; human. DR EuPathDB; HostDB:ENSG00000248993.1; -. DR GeneCards; ENSG00000248993; -. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6UB75; -. DR OMA; NCASHTK; -. DR OrthoDB; EOG091G0G84; -. DR PhylomeDB; F6UB75; -. DR TreeFam; TF335727; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000248993; Expressed in 60 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 175 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003347744. FT DOMAIN 59 137 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 175 175 {ECO:0000313|Ensembl:ENSP00000412457}. SQ SEQUENCE 175 AA; 19438 MW; 7C8B3677DE7E6717 CRC64; MGHEQNQGAA LLQMLPLLWL LPHSWAVPEE QSMITFLPLL LGLSLGCTGA GGFVAHVEST CLLDDAGTPK DFTYCISFNK DLLTCWDPEE NKMAPCEFGV LNSLANVLSQ HLNQKDTLMQ RLRNGLQNCA THTQPFWGSL TNRTRPPSVQ VAKTTPFNTR EPVMLACYVW GFYPA // ID F6UHN3_CALJA Unreviewed; 134 AA. AC F6UHN3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 12-SEP-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000042592}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000042592, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000042592, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000042592} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6UHN3; -. DR STRING; 9483.ENSCJAP00000042592; -. DR Ensembl; ENSCJAT00000057076; ENSCJAP00000042592; ENSCJAG00000001638. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6UHN3; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008225; Unplaced. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR Pfam; PF07654; C1-set; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Immunoglobulin domain {ECO:0000256|SAAS:SAAS00653601}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 134 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015313340. FT DOMAIN 39 127 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 134 AA; 15104 MW; E8299ECADC93F0F5 CRC64; MSWKKALWIP GGLRAAAVTL MLVMLSSPVA EGRDSPVEPT VIISPSKTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEQ TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RLLH // ID F6UTM7_CALJA Unreviewed; 269 AA. AC F6UTM7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000051895}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000051895, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000051895, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000051895} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCJAT00000052338; ENSCJAP00000051895; ENSCJAG00000001638. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015347039. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 269 AA; 30581 MW; 286665A8EF7F807B CRC64; MSWKKALWIP GGLRAAAVTL MLVMLSSPVA EGRDSPEDFV YQFKGFCYFT NGTERVRLVT EHVYNREEYV RFDSDVGEYW AVTQLGLPAA EYWNSQKDIL ERTRAELDTV CRHNYEVAFR GILQWRVEPT VIISPSKTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEQ TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IRQRSRKGPQ GPPPPGLLH // ID F6UY61_MONDO Unreviewed; 266 AA. AC F6UY61; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000015897}; GN Name=MODO-DAB1 {ECO:0000313|Ensembl:ENSMODP00000015897}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000015897, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000015897, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000015897} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSMODT00000016189; ENSMODP00000015897; ENSMODG00000012706. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; GQVDNYC; -. DR Proteomes; UP000002280; Chromosome 2. DR Bgee; ENSMODG00000012706; Expressed in 8 organ(s), highest expression level in liver. DR ExpressionAtlas; F6UY61; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003348434. FT TRANSMEM 228 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 230 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29440 MW; 9F13A2DDBAE71734 CRC64; MVSAQPLGGI WMEVLVVTLL VLTAQVAADR RPPKHFTEYF ISECYFINGT EQVWLVQRYI TNGEETVRFD SNVGVFEAVT ESGRPDAEHW NSQKEFLENL RAAVDTACRH NYKISEPFLV RRRVEPEVLV YPSKTAPVGH HNLLVCSVSG FYPGAVAVTW SVNGQEQRAG VVSTGLMRNG DWTFQTLVML EVTPQRGDVY TCHVEHSSLQ KPVLVAWSAQ SESAQSKMLS GVGGFVLGLI FFGVGLIVHM RSQKANRGSQ PAGLLS // ID F6V690_CANLF Unreviewed; 274 AA. AC F6V690; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 12-SEP-2018, entry version 40. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain precursor {ECO:0000313|Ensembl:ENSCAFP00000001156}; GN Name=HLA-DRB1 {ECO:0000313|Ensembl:ENSCAFP00000001156}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000001156, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000001156, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000001156, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000001156} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000001156}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAEX03008234; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03008235; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F6V690; -. DR PRIDE; F6V690; -. DR Ensembl; ENSCAFT00000001264; ENSCAFP00000001156; ENSCAFG00000000806. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6V690; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-CFA-2132295; MHC class II antigen presentation. DR Proteomes; UP000002254; Chromosome 12. DR Bgee; ENSCAFG00000000806; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 34 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 262 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 138 226 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 274 AA; 31172 MW; 7F09F6578964E19F CRC64; LLPCTLSFLF SSMVCLCFLG GSWMTALMLI LMVLNPPLAW ARDTPPHFVY QFKPECHFTN GTERVRFVER HIHNREEFVR FDSDVGEYRA VTELGRPDAE SWNGQKELLE QERATVDTYC RHNYGVIESF TVQRRVEPTV TVYPTKTQTL QHHNLLVCSV NGFYPGHIEV RWLRNGQEEE AGVVSTGLIR NGDWTFQILV MLEIVPQSGE VYTCQVEHPS LTSPVTVEWR AQSDSAQSKM LSGIGGFVLG LLFLAVGLFI YFRNQKGHSG LQPT // ID F6VAR5_HORSE Unreviewed; 273 AA. AC F6VAR5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000018340}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000018340, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000018340, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018340, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000018340} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018340}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6VAR5; -. DR STRING; 9796.ENSECAP00000018340; -. DR PaxDb; F6VAR5; -. DR Ensembl; ENSECAT00000022206; ENSECAP00000018340; ENSECAG00000020358. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6VAR5; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000020358; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 36 {ECO:0000256|SAM:SignalP}. FT CHAIN 37 273 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003348716. FT TRANSMEM 235 255 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 133 221 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 273 AA; 30880 MW; F0C44E78D4928EA6 CRC64; LSLLFSSMVC LWFPRGSWMA ALTVILMVLN PPLAWARDTQ PHFLELVKHE CHFSNGTQRV RFLDRYFYNR EEYVRFDSDV GEYRAVTELG RPDAEYWNGQ KDVLDDARAA VDTYCRHNYG VSDSFLVPRR VAPTVTVYPA KTQPLQHHNL LVCSVNGFYP GHIEVRWLRN GQEEEAGVIS TGLIRNGDWT FQTLVMLETV PQSGEVYTCQ VEHPSLTNPV TVEWRAHSES AQSKMLSGVG GFVLGLLFLG AGLFIHRRNQ KGHAGLQPTG LLS // ID F6VD88_MACMU Unreviewed; 285 AA. AC F6VD88; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 12-SEP-2018, entry version 51. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000033950}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000033950, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000033950, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000033950, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000033950} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000033950}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030660; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9544.ENSMMUP00000033950; -. DR Ensembl; ENSMMUT00000040920; ENSMMUP00000033950; ENSMMUG00000008227. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6VD88; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000029799; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 285 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008955839. FT TRANSMEM 230 252 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 264 283 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 285 AA; 31853 MW; 72CD269EC924AE04 CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALAG DTRRKSCFLE QFKSDCHFFN GTERVRFLER YLYNQEEYLR FDSDVGEYRA VSELGRPTAE SWNSQKDYLE DKRASVDNFC RHNYRVAESF TVQRRVQPKV TVYPSKTQPL QHHTLLVCSV NGFYPGSIEV RWFRNGQEEK AGVVSTGLIQ NGDWTFQTLV MLETVPQSGE VYTCQVEHPS VTSPLTVEWR ARSESAQSKM LSGVGGFVLG LLFLGAGLFI YFRNQKGEEP LVTGSLSIGF SGGGTTALLR LVLSI // ID F6VDU7_MACMU Unreviewed; 224 AA. AC F6VDU7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 12-SEP-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000033946}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSMMUP00000033946}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000033946, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000033946, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000033946, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000033946} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000033946}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030669; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMMUT00000040916; ENSMMUP00000033946; ENSMMUG00000020159. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000029799; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR ExpressionAtlas; F6VDU7; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008955838. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 224 AA; 25934 MW; 1826AD46304AA812 CRC64; MPRKKALRIP GGLWGTTVTL MLAMLSTPVA GGRDSPEDFV YQFKAMCYFT NGTERVHYVT RYIYNREEYA RFDSDVGKYL PVTPLGPPAA EYWNSQKDIL ERTRAELDTV CRHNYQLELH TTLQWRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VQWFRNDQEE TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RLLH // ID F6VL18_MACMU Unreviewed; 257 AA. AC F6VL18; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000033928}; GN Name=MAMU-DMB {ECO:0000313|Ensembl:ENSMMUP00000033928}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000033928, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000033928, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000033928, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000033928} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000033928}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030677; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F6VL18; -. DR Ensembl; ENSMMUT00000040899; ENSMMUP00000033928; ENSMMUG00000022626. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000022626; Expressed in 14 organ(s), highest expression level in spleen. DR ExpressionAtlas; F6VL18; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 257 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003348824. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 257 AA; 28360 MW; 8FA00C51FDBC1CC4 CRC64; MIIFLPLLLG LSLGCTRAGG FVAHVESTCL LDDDGTAKDF TYCISFNKDL LTCWDPEENK MVPCEFGVLN PVANGISHYL NQQDTLMQRL RNGLQNCTTH TQPFWGSLTH RTRPPSVQVA QTTPFNTREP VMLACYVWGF YPADVTITWM KNGNLVIPHG SGQKTAQPNG DWTYQTLSYL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGLISW RRAGSSSDLI ISLLFIL // ID F6W3Z8_HORSE Unreviewed; 254 AA. AC F6W3Z8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000018511}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000018511, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000018511, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018511, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000018511} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000018511}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6W3Z8; -. DR STRING; 9796.ENSECAP00000018511; -. DR PaxDb; F6W3Z8; -. DR Ensembl; ENSECAT00000022398; ENSECAP00000018511; ENSECAG00000020976. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6W3Z8; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000020976; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 254 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003345049. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 254 AA; 28883 MW; 39D693D4DD772C6F CRC64; SRMGSGWVPW LVALLVNLIR LDSSMTQGRD SPEDFVIQAK ADCYFTNGTE KVQFVVRFIF NLEEYARFDS DLGIFVALTE LGKPDAERWN NRPDILERSR ASVDALCRHN YKLGAPFTVG RKVQPEVTVY PETTPFLQHH NLLLCSVTGF YPGDIKIKWF RNGLEERAGV MSTGLIRNGD WTFQTMVMLE MTPELGDVYT CLVDHPSLLS PVSVEWRAQS EYSWRKMLSG VAAFLLGLIF LLVGIFIHLR ARKG // ID F6W4C3_MONDO Unreviewed; 263 AA. AC F6W4C3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 12-SEP-2018, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000017884}; GN Name=LOC100026858 {ECO:0000313|Ensembl:ENSMODP00000017884}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000017884, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000017884, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000017884} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR RefSeq; XP_007483721.1; XM_007483659.2. DR ProteinModelPortal; F6W4C3; -. DR STRING; 13616.ENSMODP00000017884; -. DR Ensembl; ENSMODT00000018213; ENSMODP00000017884; ENSMODG00000014310. DR GeneID; 100026858; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6W4C3; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000002280; Chromosome 2. DR Bgee; ENSMODG00000014310; Expressed in 8 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003344195. FT TRANSMEM 219 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 116 205 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28860 MW; 19E0CB7A0B7971B2 CRC64; MKLLLPLLMG LGLGFSGAAE GFVTHVESSC VLDEDGSAKD FSYCISFNKA MLTCWDSETK MMVTVNFGIL QGIAEQITNY TNHQSNFISR LSNGLQDCAS HTKPFWGALT QRTRLPSVQI AQVKPFNTRE SVMLACYVWG FYPADVAISW LKNGQLIPQS GIQRAVQSNG DWTYQTRSYL ALTPSTGDIY SCLVEHSGTS QAILQTWTPG LSPKQTLKIS VSVFTLCFGL IIFFLGLVSC RKAGSSDYTV LLGSNYPEGR NIS // ID F6WA04_MACMU Unreviewed; 273 AA. AC F6WA04; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 44. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSMMUP00000014796}; GN Name=MAMU-DOB {ECO:0000313|Ensembl:ENSMMUP00000014796}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000014796, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000014796, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000014796, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000014796} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000014796}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030674; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001181611.1; NM_001194682.1. DR UniGene; Mmu.1755; -. DR STRING; 9544.ENSMMUP00000014796; -. DR Ensembl; ENSMMUT00000015792; ENSMMUP00000014796; ENSMMUG00000011290. DR GeneID; 717702; -. DR KEGG; mcc:717702; -. DR CTD; 717702; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6WA04; -. DR KO; K06752; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000011290; Expressed in 12 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 273 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003345214. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 273 AA; 30827 MW; 58ADFAF16188E2B6 CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSREA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTALLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERAGVMS TGLIGNGDWT FQTVVMLEMT PELGDVYTCL VHHSSLLSPV SVEWRVQSEY SWRKMLSGIA AFLLGLIFLL MGIIIQLRAQ KGYVRTQMSG DEVSRAVLLP QPC // ID F6WPX7_XENTR Unreviewed; 108 AA. AC F6WPX7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSXETP00000058865}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000058865, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000058865} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000058865} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAMC01152169; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 8364.ENSXETP00000058865; -. DR PaxDb; F6WPX7; -. DR Ensembl; ENSXETT00000061919; ENSXETP00000058865; ENSXETG00000032285. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6WPX7; -. DR OMA; ECHYANG; -. DR OrthoDB; EOG091G0YW8; -. DR Reactome; R-XTR-2132295; MHC class II antigen presentation. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000032285; Expressed in 10 organ(s), highest expression level in liver. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 108 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003345509. FT DOMAIN 33 107 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 108 AA; 12439 MW; C47A13487164A12D CRC64; MCGVSVRVLS VLLTLGLCLC SSPTEDFVFQ YKSQCYFRNG TENVRSLVLY IHNQEEWTYF DSDVGLFIAK TELGKPDADY WNGQKDLLEK ERAVVDTVCK HNYQMDNP // ID F6WQV6_HORSE Unreviewed; 232 AA. AC F6WQV6; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000014763}; GN Name=LOC100060531 {ECO:0000313|Ensembl:ENSECAP00000014763}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000014763, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000014763, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014763, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000014763} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014763}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSECAT00000018116; ENSECAP00000014763; ENSECAG00000017143. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000017143; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR ExpressionAtlas; F6WQV6; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 232 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003344710. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 232 AA; 26532 MW; AF13729F4E7B4115 CRC64; MSGKMAPQIP RGLWTAAMMA MLVVLSTPVA EGRDSPQDFV FQLKGQCYFT NGTERVRLVT RLIYNREEFV RFDSDVGEFQ AVTELGRHIA EDWNGQKDVL EQKRAELDTV CRHNYQVEAL TTLQRRVEPR VTISPSRTEV LNRHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SPQSPITVQW RPRGSPPAGT IS // ID F6WWW1_HORSE Unreviewed; 280 AA. AC F6WWW1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000014751}; GN Name=LOC100060531 {ECO:0000313|Ensembl:ENSECAP00000014751}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000014751, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000014751, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014751, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000014751} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000014751}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6WWW1; -. DR STRING; 9796.ENSECAP00000014751; -. DR PaxDb; F6WWW1; -. DR Ensembl; ENSECAT00000018104; ENSECAP00000014751; ENSECAG00000017143. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6WWW1; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000017143; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR ExpressionAtlas; F6WWW1; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 280 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003344844. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 280 AA; 31602 MW; CEC9094372B69711 CRC64; MSGKMAPQIP RGLWTAAMMA MLVVLSTPVA EGRDSPQDFV FQLKGQCYFT NGTERVRLVT RLIYNREEFV RFDSDVGEFQ AVTELGRHIA EDWNGQKDVL EQKRAELDTV CRHNYQVEAL TTLQRRVEPR VTISPSRTEV LNRHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SPQSPITVQW RTHSESAQNK MLCGIGSFVL GLVFLGLSLI IHHRSQKGPR GSPPAGTISA RIHCGVSGQV // ID F6X5T7_HORSE Unreviewed; 263 AA. AC F6X5T7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000019301}; GN Name=LOC100060996 {ECO:0000313|Ensembl:ENSECAP00000019301}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019301, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000019301, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019301, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000019301} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019301}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR RefSeq; XP_005603849.1; XM_005603792.2. DR ProteinModelPortal; F6X5T7; -. DR STRING; 9796.ENSECAP00000019301; -. DR PaxDb; F6X5T7; -. DR Ensembl; ENSECAT00000023314; ENSECAP00000019301; ENSECAG00000021796. DR GeneID; 100060996; -. DR KEGG; ecb:100060996; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6X5T7; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000021796; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003345817. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 115 220 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 29027 MW; F72A9D327535E22F CRC64; MTTLLLLLLG LSLGCTVEGG FVAHVESTCL LDDDGTPKDF TYCVSFNKDL LTCWDPEQAL MVPREFGVLY PLAKSLSAYL NQYENLLQRL STGLQDCANH TQPFWGSLTN RTWAPSVQVA KTTPFNTKES VMLACYVWGF YPADVTITWR KNGQPVPPHS SAHKTVQPNG DWTYQTISHL ATTPSFGDTY TCVVEHIGAP EPILQDWTPG LSPTQTVKVS VSVVTLGLGL ILFFLGLLSW RRARFSGYTI LPGSNYPEGQ NIS // ID F6XUR5_CALJA Unreviewed; 257 AA. AC F6XUR5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000049396}; GN Name=LOC108591149 {ECO:0000313|Ensembl:ENSCJAP00000049396}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000049396, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000049396, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000049396} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6XUR5; -. DR STRING; 9483.ENSCJAP00000049396; -. DR Ensembl; ENSCJAT00000062354; ENSCJAP00000049396; ENSCJAG00000044345. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6XUR5; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 257 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015348955. FT TRANSMEM 227 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 257 AA; 29316 MW; F7E9378EC1DC204B CRC64; MALQIPGGLW AAAVTLMLAM LSTPVAEGRD SPQDFVYQVK GMCYFRNGTE RVRLVTRFIY NREEYLRFDS DVGEYLPVTP LGPPDAEYLN SQKDLLDRTR AELDTVCRHN YQLEFPAILQ RREKPTVTIS SSRREALNHH NLLVCSVTDF YPGQIKVRWF QNDQEQSAGI VSTPLIRNGD WTFQILVMLE MTPQHGDIYI CHVEHPSLQS PITVEWRAQS ESAQRKMLSG IGGFVLGLIF LGLGFIIHHR SQKGLLH // ID F6Z0N4_MACMU Unreviewed; 106 AA. AC F6Z0N4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 12-SEP-2018, entry version 55. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000029791}; GN Name=MAMU-DMB {ECO:0000313|Ensembl:ENSMMUP00000029791}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000029791, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000029791, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029791, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000029791} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029791}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030677; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9544.ENSMMUP00000029791; -. DR Ensembl; ENSMMUT00000031840; ENSMMUP00000029791; ENSMMUG00000022626. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000022626; Expressed in 14 organ(s), highest expression level in spleen. DR ExpressionAtlas; F6Z0N4; baseline. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR Pfam; PF07654; C1-set; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Immunoglobulin domain {ECO:0000256|SAAS:SAAS00653601}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}. FT DOMAIN 1 78 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 106 AA; 11823 MW; 47603683908133F8 CRC64; VAQTTPFNTR EPVMLACYVW GFYPADVTIT WMKNGNLVIP HGSGQKTAQP NGDWTYQTLS YLALTPSYGD TYTCVVEHIG APEPILRDWS YTPLPGSNYP EGRHIS // ID F6Z8R9_HORSE Unreviewed; 257 AA. AC F6Z8R9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000004572}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000004572, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000004572, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000004572, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000004572} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000004572}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F6Z8R9; -. DR STRING; 9796.ENSECAP00000004572; -. DR PaxDb; F6Z8R9; -. DR Ensembl; ENSECAT00000006449; ENSECAP00000004572; ENSECAG00000006492. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F6Z8R9; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000006492; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 257 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003352117. FT TRANSMEM 230 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 257 AA; 29194 MW; 78C2FAC9FDA52A2A CRC64; ISGKMAPQIP RGLWTAAVMV MLVVLSTPVA EGRDSPQDFV VQFMGQCYFT NGTEHVRYVT RYIYNREEYV RFDSDVGEYR ALTELGRPEA EYWNGQKDIL EGTRAELDRV CRPNYQLEFP ALERRVKPTV TISPSRTEAL NHHNLLVCSV TDFYPGQIKV QWFRNDQEET AGVVSTPLIR NGDWTFQILV MLEMTPQRGD VYTCHVEHPS LQSPITVQWQ AQSESAQSKM LSGVGGFVLG LIFLGLGLII HHRSQKG // ID F7A6B9_CALJA Unreviewed; 219 AA. AC F7A6B9; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000042641}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000042641, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000042641, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000042641} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F7A6B9; -. DR Ensembl; ENSCJAT00000052649; ENSCJAP00000042641; ENSCJAG00000044953. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 219 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015358694. SQ SEQUENCE 219 AA; 25088 MW; 02FFBD9FA81BE135 CRC64; MVCLRFPGGS CVAALTVTLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRLLERYI HNQEENLRFD SDVGEFRAVT ELGRPDAESW NSQKDFLEDR RAAVDTYCRH NYEISERFLV PRRVQPKVTV YPAKTQPLQR HNLLVCSVSG FYPGSIEVRW FRNDQEEKTG VVSTGLIHNG DWTFQTLVML ETLPQSGEVY ICQVEHPSVT SPLTVQWRA // ID F7BCC3_HORSE Unreviewed; 266 AA. AC F7BCC3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 54. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AFU83059.1}; DE SubName: Full=MHC class II histocompatibility antigen, DR beta chain {ECO:0000313|EMBL:SJX51226.1}; GN Name=DRB {ECO:0000313|Ensembl:ENSECAP00000019909}; GN Synonyms=Eqca-DRB1 {ECO:0000313|EMBL:AFU83059.1}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000019909, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000019909, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019909, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000019909} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000019909}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000313|EMBL:AFU83059.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Thoroughbred #3729 {ECO:0000313|EMBL:AFU83059.1}; RA Miller D., Tallmadge R.L., Binns M., Brown H.E., Zhu B., Antczak D.F.; RT "Polymorphism at Expressed Equine MHC Class II DQ and DR Loci."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:SJX51226.1} RP NUCLEOTIDE SEQUENCE. RA Viluma A., Mikko S., Hahn D., Skow L., Andersson G., Bergsrom T.F.; RT "Genomic structure of the horse major histocompatibility complex class RT II region resolved using PacBio long-read sequencing technology."; RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JQ254085; AFU83059.1; -; mRNA. DR EMBL; LT745777; SJX51226.1; -; Genomic_DNA. DR RefSeq; NP_001136283.1; NM_001142811.1. DR UniGene; Eca.12924; -. DR STRING; 9796.ENSECAP00000019909; -. DR Ensembl; ENSECAT00000023992; ENSECAP00000019909; ENSECAG00000022072. DR GeneID; 100052006; -. DR KEGG; ecb:100052006; -. DR CTD; 248402; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002281; Chromosome 20. DR Bgee; ENSECAG00000022072; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014090645. FT TRANSMEM 228 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30051 MW; F7EC6B5120DA6CD6 CRC64; MVCLWFPGGS WMAALTAILM VLSPPLAWAK NTRPHFLEAV KFECRFSNGT ERVRFLERRF HNGEEYARFD SDVGEYRAVT ELGRPDAEYW NGQQDILDER RAAVDTYCRH NYGVIDGFLV RRRVEPTVTV YPAKTQPLQH HNLLVCSVNG FYPGHIEVRW FRNGQEEEAG VVSTGLIRNG DWTFQTMVML ETVPQSGEVY TCQVEHPSLT SPVTVEWRAQ SESAQSKMLS GVGGFVLGLL FLGAGLFIHC RNQKGHTGLQ PTGLLN // ID F7BGR3_XENTR Unreviewed; 272 AA. AC F7BGR3; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 43. DE SubName: Full=Major histocompatibility complex, class II, DR beta 1 {ECO:0000313|Ensembl:ENSXETP00000027812}; GN Name=hla-drb1 {ECO:0000313|Ensembl:ENSXETP00000027812, GN ECO:0000313|Xenbase:XB-GENE-945971}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|Ensembl:ENSXETP00000027812, ECO:0000313|Proteomes:UP000008143}; RN [1] {ECO:0000313|Ensembl:ENSXETP00000027812} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000027812}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] {ECO:0000313|Ensembl:ENSXETP00000027812} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAMC01083582; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083583; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083584; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083585; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083586; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083587; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083588; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F7BGR3; -. DR STRING; 8364.ENSXETP00000027812; -. DR PaxDb; F7BGR3; -. DR Ensembl; ENSXETT00000027812; ENSXETP00000027812; ENSXETG00000025586. DR Xenbase; XB-GENE-945971; hla-drb1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F7BGR3; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0F53; -. DR TreeFam; TF336626; -. DR Reactome; R-XTR-2132295; MHC class II antigen presentation. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000025586; Expressed in 18 organ(s), highest expression level in liver. DR ExpressionAtlas; F7BGR3; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 272 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003348407. FT TRANSMEM 232 254 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 120 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 272 AA; 31197 MW; 781AED18E40CCEC7 CRC64; FCFMPSFLDP MMCGISVRVL SVLLTLGVCL CSSPPEDFVY QYKGQCCFRN GTENVRGLDR YIYNQEEIAY FDSDVGFFIA KTELGKKHFA DYWNSQKDLL EQKRAETDTV CRYNYQFDKP DVIDRKSQPN VKIVNSKTLD LEHENLITCF VDGFFPPMIK VTWLKNGIEE GEQVTSSELL PNGDWTFEIH VMLETTIKHG DTFTCRVEHS SLQQPISVNW EPDVSESARN KMLTGIVGFV LGSIFIIVGL VVYLRSKKTM TRFSVVQNEI LL // ID Q6EWJ8_MACMU Unreviewed; 266 AA. AC Q6EWJ8; F6VDU0; F7BKN9; DT 16-AUG-2004, integrated into UniProtKB/TrEMBL. DT 16-AUG-2004, sequence version 1. DT 12-SEP-2018, entry version 105. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:CAE53065.1}; GN Name=DRB1 {ECO:0000313|EMBL:CAE53065.1}; GN Synonyms=LOC100428435 {ECO:0000313|Ensembl:ENSMMUP00000013914}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|EMBL:CAE53065.1}; RN [1] {ECO:0000313|EMBL:CAE53065.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15128802; RA de Groot N., de Groot N.G., Otting N., Heijmans C., Rouweler A.J.M., RA Doxiadis G.G., Bontrop R.E.; RT "Genetic makeup of the DR region in rhesus macaques: gene content, RT transcripts, and pseudogenes."; RL J. Immunol. 172:6152-6157(2004). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000013914, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000013914, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [3] {ECO:0000313|Ensembl:ENSMMUP00000013914} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000013914}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030660; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030661; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030663; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ601357; CAE53065.1; -; mRNA. DR RefSeq; NP_001037726.1; NM_001044261.1. DR UniGene; Mmu.10268; -. DR Ensembl; ENSMMUT00000014851; ENSMMUP00000013914; ENSMMUG00000029799. DR Ensembl; ENSMMUT00000040917; ENSMMUP00000033947; ENSMMUG00000029799. DR GeneID; 692100; -. DR KEGG; mcc:692100; -. DR CTD; 692100; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000029799; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015098265. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29909 MW; 06F2BF6705DE80DE CRC64; MVCLKLHGGS CMAALTVTLM VLSSPLALAG DTQSRFLEQV KFECHFFNGT ERVRYLERRV HNQEEYARFD SDVGEYRAVT ELGRPDAEYW NGQKDLLERR RAEVDTVCRH NYGVVESFTV QRRVQPKVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGLLS // ID F7DBV4_HORSE Unreviewed; 61 AA. AC F7DBV4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 28-MAR-2018, entry version 21. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSECAP00000017771}; OS Equus caballus (Horse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus. OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000017771, ECO:0000313|Proteomes:UP000002281}; RN [1] {ECO:0000313|Ensembl:ENSECAP00000017771, ECO:0000313|Proteomes:UP000002281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000017771, RC ECO:0000313|Proteomes:UP000002281}; RX PubMed=19892987; DOI=10.1126/science.1178158; RG Broad Institute Genome Sequencing Platform; RG Broad Institute Whole Genome Assembly Team; RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F., RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., RA Distl O., Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., RA Penedo M.C.T., Raison J.M., Sharpe T., Vogel J., Andersson L., RA Antczak D.F., Biagi T., Binns M.M., Chowdhary B.P., Coleman S.J., RA Della Valle G., Fryc S., Guerin G., Hasegawa T., Hill E.W., Jurka J., RA Kiialainen A., Lindgren G., Liu J., Magnani E., Mickelson J.R., RA Murray J., Nergadze S.G., Onofrio R., Pedroni S., Piras M.F., RA Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A., Searle S., Skow L., RA Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J., Vaudin M., RA White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.; RT "Genome sequence, comparative analysis, and population genetics of the RT domestic horse."; RL Science 326:865-867(2009). RN [2] {ECO:0000313|Ensembl:ENSECAP00000017771} RP IDENTIFICATION. RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000017771}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR PaxDb; F7DBV4; -. DR Ensembl; ENSECAT00000021566; ENSECAP00000017771; ENSECAG00000020334. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F7DBV4; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000002281; Chromosome 20. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002281}; KW Reference proteome {ECO:0000313|Proteomes:UP000002281}. FT DOMAIN 3 60 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 61 AA; 7252 MW; D5A339B6BB313C55 CRC64; DYYFTNGTEK VHFYNNVGMF VALTELRQPD AELWNNWLDI LERSRASVDV LHRYNYKLGA P // ID F7DN39_MONDO Unreviewed; 264 AA. AC F7DN39; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 12-SEP-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000018363}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000018363, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000018363, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000018363} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F7DN39; -. DR STRING; 13616.ENSMODP00000018363; -. DR Ensembl; ENSMODT00000018696; ENSMODP00000018363; ENSMODG00000014692. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F7DN39; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002280; Chromosome 2. DR Bgee; ENSMODG00000014692; Expressed in 8 organ(s), highest expression level in female gonad. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29324 MW; 751F491DA18E2347 CRC64; GDQSGTDSRD PRLVRRPGLV SQPRSDAAPC PSTEDFVIQS KGLCYFTNGS EQVRLVVRYI YNDQEIARYD SKLGKYVAVT ELGRPTAEYW NSQKDILERR EAEVDTVCRH NYEIDKHIIL AKRAQPHVTV SPSKQEAQQH LLVCSVTGFY PSKIKVTWLK NGQEQTAGVI STEVIQNGDW TYQTLVMLET IPQSRDIYTC SVEHASLQSP ITVEWRAQSG SAQSKLVSGV GGFVLGLIFL SVGLILHLKS QKGHAGPQPA GLLR // ID F7DNM7_MONDO Unreviewed; 264 AA. AC F7DNM7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 12-SEP-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000018356}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000018356, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000018356, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000018356} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F7DNM7; -. DR STRING; 13616.ENSMODP00000018356; -. DR Ensembl; ENSMODT00000018689; ENSMODP00000018356; ENSMODG00000014686. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; F7DNM7; -. DR OMA; RIPEAHC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002280; Chromosome 2. DR Bgee; ENSMODG00000014686; Expressed in 7 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003351491. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 228 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29957 MW; 1046169C6F5A2ABD CRC64; MVAVWISTNF WKIGLLMTLM MFCLPVSWAR DIPEDFVYQY RALCYFTNGS KQVRLVNRHF YNDQETVRYD SKLGKHVAVT ELGRRDAEYW NSRKDILERK RASLDTVCRH NYEAYKPFTL ERRAQPRLTV SPSKQEAQQH LLVCSVTGFY PSKIKVTWLK NGQEQTAGVI STGLIQHGDW TYQTLVMLET IPQSRDIYTC SVEHASLQSP IAVEWRAQSG SAQSKLVSGV GGFVLGLIFL SVGLILHLKS QKGRAGPQPA GNVP // ID F7EID8_CALJA Unreviewed; 261 AA. AC F7EID8; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000050559}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000050559, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000050559, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000050559} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCJAT00000060392; ENSCJAP00000050559; ENSCJAG00000001638. DR KEGG; cjc:100386865; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. SQ SEQUENCE 261 AA; 29853 MW; 475B3840EDB85009 CRC64; MSWKKALWIP GGLRAAAVTL MLVMLSSPVA EGRDSPEDFV YQFKGFCYFT NGTERVRLVT EHVYNREEYV RFDSDVGEYW AVTQLGLPAA EYWNSQKDIL ERTRAELDTV CRHNYEVAFR GILQWRVEPT VIISPSKTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEQ TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IRQRSRKGLL H // ID F7G8K4_MACMU Unreviewed; 268 AA. AC F7G8K4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 12-SEP-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000029996}; GN Name=LOC100428435 {ECO:0000313|Ensembl:ENSMMUP00000029996}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000029996, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000029996, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029996, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000029996} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000029996}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030660; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030661; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030663; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMMUT00000032059; ENSMMUP00000029996; ENSMMUG00000029799. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000029799; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR ExpressionAtlas; F7G8K4; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 268 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008957024. FT TRANSMEM 230 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 268 AA; 30158 MW; 6C61F1ED122AD0B5 CRC64; MVCLKLHGGS CMAALTVTLM VLSSPLALAG DTQSRFLEQV KFECHFFNGT ERVRYLERRV HNQEEYARFD SDVGEYRAVT ELGRPDAEYW NGQKDLLERR RAEVDTVCRH NYGVVESFTV QRRGELQPKV TVYPAKTQPL QHHNLLVCSV SGFYPGSIEV RWFRNGQEEK AGVVSTGLIQ NGDWTFQTLV MLETVPRSGE VYTCQVEHPS VTSPLTVEWR ARSESAQSKM LSGVGGFVLG LLFLGAGLFI YFRNQKGHSG LQPTGNTF // ID F7GF62_MACMU Unreviewed; 267 AA. AC F7GF62; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 12-SEP-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000007322}; GN Name=LOC100428435 {ECO:0000313|Ensembl:ENSMMUP00000007322}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000007322, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000007322, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000007322, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000007322} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000007322}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030660; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030661; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030663; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMMUT00000007793; ENSMMUP00000007322; ENSMMUG00000029799. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000029799; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR ExpressionAtlas; F7GF62; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 267 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003359885. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 267 AA; 30203 MW; 36C878976F9F3DFE CRC64; MVCLKLHGGS CMAALTVTLM VLSSPLALAG DTQSRFLEQV KFECHFFNGT ERVRYLERRV HNQEEYARFD SDVGEYRAVT ELGRPDAEYW NGQKDLLERR RAEVDTVCRH NYGVVESFTV QRRVQPKVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKDHKPTG RNKLGTH // ID F7GQ76_CALJA Unreviewed; 326 AA. AC F7GQ76; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000003003}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000003003, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000003003, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000003003} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCJAT00000003172; ENSCJAP00000003003; ENSCJAG00000044953. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 326 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015348936. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 326 AA; 36822 MW; F9700373DAD43373 CRC64; MVCLRLPGGS YIAALTVTLM ALSSPLALAG DSPPRFLEQF KYECLHLNGT EGVRLLVRYI YNQEEYVRFD SDVGEFRAVT ELGRPAAEYI NSLKDYMEQT RAAVDTVCRH NYGIFERFLV QRRVQPKVTV YPAKTQPLQR HNLLVCSVSG FYPGSIEVRW FRNDQEEKTG VVSTGLIHNG DWTFQTLVML ETLPQSGEVY ICQVEHPSVT SPLTVQWTQS ESAQSKMLSG VGGFVLGLLF LGAGLFIYFR NQKGEEPLVA GFLSIGFSKR GNMALWRFSV CQWPWIKSFF PQKTSNVLLI QTSSVSKHNS LWPVKIRERL TSSSLV // ID F7GS53_CALJA Unreviewed; 267 AA. AC F7GS53; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000047851}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000047851, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000047851, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000047851} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCJAT00000053424; ENSCJAP00000047851; ENSCJAG00000001638. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 229 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 127 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 267 AA; 30744 MW; 717A430F64679212 CRC64; MRTIQFPSYR LKPGRGERRG NRRQSVHLLP VIGQKDFVYQ FKGFCYFTNG TERVRLVTEH VYNREEYVRF DSDVGEYWAV TQLGLPAAEY WNSQKDILER TRAELDTVCR HNYEVAFRGI LQWRVEPTVI ISPSKTEALN HHNLLVCSVT DFYPGQIKVR WFRNDQEQTA GIVSTPLIRN GDWTFQILVM LEMTPQRGDV YTCHVEHPSL QSPITVEWRA QSESAQSKML SGIGGFVLGL IFLGLGLIIR QRSRKGPQGP PPPGLLH // ID F7HN61_MACMU Unreviewed; 267 AA. AC F7HN61; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 12-SEP-2018, entry version 48. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000015492}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSMMUP00000015492}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000015492, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000015492, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000015492, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000015492} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000015492}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030669; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMMUT00000016539; ENSMMUP00000015492; ENSMMUG00000020159. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000029799; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR ExpressionAtlas; F7HN61; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 267 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008957583. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 267 AA; 30613 MW; B41441AD06463B2B CRC64; MPRKKALRIP GGLWGTTVTL MLAMLSTPVA GGRDSPEDFV YQFKAMCYFT NGTERVHYVT RYIYNREEYA RFDSDVGKYL PVTPLGPPAA EYWNSQKDIL ERTRAELDTV CRHNYQLELH TTLQWRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VQWFRNDQEE TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI IHHRSQKVER QPYHRVD // ID F7HNG4_MACMU Unreviewed; 270 AA. AC F7HNG4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 12-SEP-2018, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000015470}; GN Name=LOC100428435 {ECO:0000313|Ensembl:ENSMMUP00000015470}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000015470, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000015470, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000015470, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000015470} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000015470}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030660; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030661; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030662; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JSUE03030663; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMMUT00000016512; ENSMMUP00000015470; ENSMMUG00000029799. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000029799; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR ExpressionAtlas; F7HNG4; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 270 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008957590. FT TRANSMEM 232 254 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 130 218 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 270 AA; 30229 MW; CF309D2881B56FAD CRC64; MVCLKLHGGS CMAALTVTLM VLSSPLALAG DTQCNYCGEG KIGSFFECHF FNGTERVRYL ERRVHNQEEY ARFDSDVGEY RAVTELGRPD AEYWNGQKDL LERRRAEVDT VCRHNYGVVE SFTVQRRVQP KVTVYPAKTQ PLQHHNLLVC SVSGFYPGSI EVRWFRNGQE EKAGVVSTGL IQNGDWTFQT LVMLETVPRS GEVYTCQVEH PSVTSPLTVE WRARSESAQS KMLSGVGGFV LGLLFLGAGL FIYFRNQKGH SGLQPTGNTF // ID F7HU89_MACMU Unreviewed; 276 AA. AC F7HU89; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 30-NOV-2016, sequence version 2. DT 12-SEP-2018, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMMUP00000010784}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSMMUP00000010784}; OS Macaca mulatta (Rhesus macaque). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000010784, ECO:0000313|Proteomes:UP000006718}; RN [1] {ECO:0000313|Ensembl:ENSMMUP00000010784, ECO:0000313|Proteomes:UP000006718} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000010784, RC ECO:0000313|Proteomes:UP000006718}; RX PubMed=17431167; DOI=10.1126/science.1139247; RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M., RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., RA Wilson R.K., Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., RA Hardison R.C., Makova K.D., Miller W., Milosavljevic A., Palermo R.E., RA Siepel A., Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J., RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., RA Dinh H.H., Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., RA Godfrey J., Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., RA Jhangiani S.N., Joshi V., Khan Z.M., Kirkness E.F., Cree A., RA Fowler R.G., Lee S., Lewis L.R., Li Z., Liu Y.-S., Moore S.M., RA Muzny D., Nazareth L.V., Ngo D.N., Okwuonu G.O., Pai G., Parker D., RA Paul H.A., Pfannkoch C., Pohl C.S., Rogers Y.-H.C., Ruiz S.J., RA Sabo A., Santibanez J., Schneider B.W., Smith S.M., Sodergren E., RA Svatek A.F., Utterback T.R., Vattathil S., Warren W., White C.S., RA Chinwalla A.T., Feng Y., Halpern A.L., Hillier L.W., Huang X., RA Minx P., Nelson J.O., Pepin K.H., Qin X., Sutton G.G., Venter E., RA Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P., Jones S.M., RA Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L., Csuros M., RA Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H., Liu Y., RA Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E., RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J., RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J., RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A., RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., RA Denby A., Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., RA Marklein A., Nielsen R., Vallender E.J., Clark A.G., Ferguson B., RA Hernandez R.D., Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., RA Pu L.-L., Ren Y., Smith D.G., Wheeler D.A., Schenck I., Ball E.V., RA Chen R., Cooper D.N., Giardine B., Hsu F., Kent W.J., Lesk A., RA Nelson D.L., O'brien W.E., Pruefer K., Stenson P.D., Wallace J.C., RA Ke H., Liu X.-M., Wang P., Xiang A.P., Yang F., Barber G.P., RA Haussler D., Karolchik D., Kern A.D., Kuhn R.M., Smith K.E., RA Zwieg A.S.; RT "Evolutionary and biomedical insights from the rhesus macaque RT genome."; RL Science 316:222-234(2007). RN [2] {ECO:0000313|Ensembl:ENSMMUP00000010784} RP IDENTIFICATION. RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000010784}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JSUE03030669; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMMUT00000011502; ENSMMUP00000010784; ENSMMUG00000020159. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000006718; Chromosome 4. DR Bgee; ENSMMUG00000029799; Expressed in 14 organ(s), highest expression level in peripheral blood mononuclear cell. DR ExpressionAtlas; F7HU89; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006718}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006718}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 276 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5008957655. FT TRANSMEM 231 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 276 AA; 31586 MW; 20B9870C6C6FDE25 CRC64; MPRKKALRIP GGLWGTTVTL MLAMLSTPVA GGRDSPEDFV YQFKAMCYFT NGTERVHYVT RYIYNREEYA RFDSDVGKYL PVTPLGPPAA EYWNSQKDIL ERTRAELDTV CRHNYQLELH TTLQWRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VQWFRNDQEE TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI IHHRSQKGRP YRSSLSHWLL SKSFLH // ID F7HXA0_CALJA Unreviewed; 294 AA. AC F7HXA0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000002932}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000002932, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000002932, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000002932} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCJAT00000003099; ENSCJAP00000002932; ENSCJAG00000044953. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 294 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015327892. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 294 AA; 33294 MW; 19F0F5CDF813B8B5 CRC64; MVYMRLPGGS CMAVLTVMLM VLSSPLALAG DTRPRFLEYS TSECHFFNGT ERVRLLERYI HNQEENLRFD SDVGEFRAVT ELGRPDAESW NSQKDFLEDR RAAVDTYCRH NYEISERFLV PRRVQPKVTV YPAKAQPLQH HNLLVCSVSG FYPGSIEVRW FRNDQEEKTG VVSTGLIQNG DWTFQTLVML ETLPQSGEVY TCQVEHPSVT SPLTVQWRAQ SESAQSKILS GVGGSVLGLL FLGAGLFIYF RNQKGEEPLV AGSLHRLFRR KNYGFAEVNS QYMSGPGYSL SFPK // ID U3EVA8_CALJA Unreviewed; 263 AA. AC U3EVA8; F7I2S2; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 18-JUL-2018, entry version 28. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:JAB46204.1}; GN Name=HLA-DMB {ECO:0000313|EMBL:JAB46204.1}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB46204.1}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000040135, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000040135} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [3] {ECO:0000313|EMBL:JAB46204.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Bladder {ECO:0000313|EMBL:JAB03342.1}, RC Cerebellum {ECO:0000313|EMBL:JAB46204.1}, RC Cerebral cortex {ECO:0000313|EMBL:JAB29406.1}, and RC Hippocampus {ECO:0000313|EMBL:JAB12960.1}; RX PubMed=25243066; DOI=10.1186/2047-217X-3-14; RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C., RA Moriyama E.N., French J.A., Norgren R.B.Jr.; RT "De novo assembly of the common marmoset transcriptome from NextGen RT mRNA sequences."; RL Gigascience 3:14-14(2014). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; GAMT01008519; JAB03342.1; -; mRNA. DR EMBL; GAMS01010176; JAB12960.1; -; mRNA. DR EMBL; GAMR01004526; JAB29406.1; -; mRNA. DR EMBL; GAMP01006551; JAB46204.1; -; mRNA. DR STRING; 9483.ENSCJAP00000040135; -. DR Ensembl; ENSCJAT00000042394; ENSCJAP00000040135; ENSCJAG00000021558. DR KEGG; cjc:100412691; -. DR CTD; 100412691; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003362072. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28946 MW; C7B1FD9616A01F57 CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDDGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN QLANGLSDYL NKQDTLMQRL RNGLQDCATH TQPFWGSLTH RTRPPSVQVA RTTPFNTREP VMLACYVWGF YPADVIITWR KNGKPVIPHS SAQKTAQPNG DWTYQTLSHL ALTPSYGDIY TCVVEHIGAP EPILQDWTPG LSPMQTVKVS VSAVTLGLGL IIFSLGLISW RRAGSSSYIP LPGSNYPEAR HIS // ID F7I520_CALJA Unreviewed; 227 AA. AC F7I520; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 35. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 2 {ECO:0000313|Ensembl:ENSCJAP00000040119}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSCJAP00000040119}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000040119, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000040119, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000040119} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F7I520; -. DR Ensembl; ENSCJAT00000042377; ENSCJAP00000040119; ENSCJAG00000021548. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 227 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015315274. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 227 AA; 26105 MW; 048FFFD41CD994E5 CRC64; MALQIPRGFR AAAVTLMLAM LSTPVADGRD SPKDFVVQFK GMCYFTNGTE RVRGVARYIY NREEYARFDS DVGEFRAVTE LGRSTEDWNN YKDFLEQERA AVYTVCRHNY EAELRTTLQR RVEPTVTISP TRTEALNHHN LLVCSVTDFY PGQIKVRWFR NDQEETAGIV STSLIRNGDW TFQILVMLEM TPQRGDIYTC HVEHPSLQSP ITVEWRPRGP PPAGLLH // ID F7I5Z4_CALJA Unreviewed; 264 AA. AC F7I5Z4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 37. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 2 {ECO:0000313|Ensembl:ENSCJAP00000046735}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSCJAP00000046735}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000046735, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000046735, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000046735} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCJAT00000057102; ENSCJAP00000046735; ENSCJAG00000021548. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015320211. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29950 MW; 53BA6D1322E3CA1C CRC64; MALQIPRGFR AAAVTLMLAM LSTPVADGRD SPKDFVVQFK GMCYFTNGTE RVRGVARYIY NREEYARFDS DVGEFRAVTE LGRSTEDWNN YKDFLEQERA AVYTVCRHNY EAELRTTLQR RVEPTVTISP TRTEALNHHN LLVCSVTDFY PGQIKVRWFR NDQEETAGIV STSLIRNGDW TFQILVMLEM TPQRGDIYTC HVEHPSLQSP ITVEWRAHSE SAQSKMLSGI GGFVLGLIFL GLGLVIRHRG RKGPRGPPPA GLLH // ID F7ILZ1_CALJA Unreviewed; 257 AA. AC F7ILZ1; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 12-SEP-2018, entry version 36. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSCJAP00000043588}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSCJAP00000043588}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000043588, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000043588, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000043588} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR RefSeq; XP_002746458.2; XM_002746412.4. DR RefSeq; XP_017826508.1; XM_017971019.1. DR Ensembl; ENSCJAT00000057503; ENSCJAP00000043588; ENSCJAG00000021575. DR GeneID; 100408503; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 257 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015312395. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 257 AA; 29220 MW; 75D3E58EC6A68263 CRC64; MVLQVSALPR TVALTALLMA LLTAVVQGRA TTENYVYQRL FECYAFNGTQ HLLDRLFYNR EEFVRFDSDL GEYQAVTELG RPDAKYWNSQ KDILEQMRAE VERVCRHNYE LEDPLILKRQ VQPKVNVSPS KKGPLQHHNL LVCHVTDFYP GSIQVRWFLN GQEETAGVVS TNLIRNGDWT FQILVMLEMM PQQGDVYTCQ VEHPSLDSPV TVEWKAQSDS ARSKMLTGAG SFVLGLLICG VGIVMHRRSK KVQRGSA // ID F7ISU5_CALJA Unreviewed; 224 AA. AC F7ISU5; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000002995}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000002995, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000002995, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000002995} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; F7ISU5; -. DR Ensembl; ENSCJAT00000003163; ENSCJAP00000002995; ENSCJAG00000001638. DR GeneTree; ENSGT00900000140849; -. DR OMA; EMTPRRG; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015335610. SQ SEQUENCE 224 AA; 25982 MW; AB8B41E40E1F62B9 CRC64; MSWKKALWIP GGLRAAAVTL MLVMLSSPVA EGRDSPEDFV YQFKGFCYFT NGTERVRLVT EHVYNREEYV RFDSDVGEYW AVTQLGLPAA EYWNSQKDIL ERTRAELDTV CRHNYEVAFR GILQWRVEPT VIISPSKTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEQ TAGIVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RLLH // ID F7ISX0_CALJA Unreviewed; 219 AA. AC F7ISX0; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 20-JUN-2018, sequence version 2. DT 18-JUL-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCJAP00000002989}; OS Callithrix jacchus (White-tufted-ear marmoset). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Platyrrhini; Cebidae; Callitrichinae; Callithrix; Callithrix. OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000002989, ECO:0000313|Proteomes:UP000008225}; RN [1] {ECO:0000313|Ensembl:ENSCJAP00000002989, ECO:0000313|Proteomes:UP000008225} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.; RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSCJAP00000002989} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSCJAT00000003157; ENSCJAP00000002989; ENSCJAG00000044953. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000008225; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 219 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015316239. SQ SEQUENCE 219 AA; 25070 MW; 4A27261CBBF84720 CRC64; MVCLRFPGGS CVAALTVTLM VLSSPLALAG DTRPRYLEQR KAECHHFNGT ERVRLLERYF YNQEEFVRFD SDVGEFRAVT ELGRPVAESW NSRKDILEQR RAAVDTFCRH NYEGFETFLV PRRVQPKVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FRNDQEEKAG VVSTGLIQNG DWTFQTLVML ETVPQSGEVY ICQVEHPSVT SPLTVQWRA // ID G1L536_AILME Unreviewed; 236 AA. AC G1L536; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 39. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSAMEP00000001996}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSAMEP00000001996}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000001996, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000001996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000001996} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ACTA01034659; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01042658; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01050658; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1L536; -. DR STRING; 9646.ENSAMEP00000001996; -. DR Ensembl; ENSAMET00000002076; ENSAMEP00000001996; ENSAMEG00000001900. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1L536; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 103 190 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 236 AA; 26490 MW; 8D2858345C924B44 CRC64; SPIPFYINLL VYSLPSFTYQ SQSACLEFNG THRFLEQYTY NRELFVQLDS AMGLFAAVSH LGRLTAKSWN IQREFLALRG AVDSVCKHNF DLTRVFPPLP VQPKVNVSPS EKGHPQHHNL LVCHVSDFYP GHIQVCFLNG QEETAGVLST NSMHNGDWTF QILVMLEMTP QQGDVYVCRV EHPSLDSPVT VEWSEEAQSD SAQSKMLAGL GGFALGLTAL RASFILRFRS QRGKKL // ID G1L599_AILME Unreviewed; 268 AA. AC G1L599; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 18-JUL-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMEP00000002060}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002060, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002060} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ACTA01082658; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1L599; -. DR STRING; 9646.ENSAMEP00000002060; -. DR Ensembl; ENSAMET00000002143; ENSAMEP00000002060; ENSAMEG00000001952. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1L599; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 268 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003413411. FT TRANSMEM 224 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 119 225 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 268 AA; 29249 MW; 47676C6282DF6963 CRC64; SPEHSMTTLL PLLLGLSLGS TGAGGFIAHV ESACLLDDDG TPKDFAYCVS FNKDLLTCWD SEEGKMAPHE FGALNFLAKY LSDYLNQQEP LIQRLSNGLQ DCAARTQSFW GSLTHRTRPP TVQVAKTTPF NTKEHVMLAC YVWGFYPADV IISWRKNGQP VPPHSSAPKM AQPNGDWTYQ TVSYLATTPS YGDTYTCVVE HIGAPEPVCE DWTAGLSPMQ TVKVSVSAVT LGLGFIIFSL GLLSWRRAGP SGYILLPGDS YPEGQHVN // ID G1L5N9_AILME Unreviewed; 768 AA. AC G1L5N9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 23-MAY-2018, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMEP00000002200}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002200, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002200} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002200} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ACTA01154656; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01162655; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9646.ENSAMEP00000002200; -. DR Ensembl; ENSAMET00000002292; ENSAMEP00000002200; ENSAMEG00000002044. DR eggNOG; KOG0058; Eukaryota. DR eggNOG; COG1132; LUCA. DR GeneTree; ENSGT00550000074497; -. DR InParanoid; G1L5N9; -. DR OMA; FNQFFVG; -. DR OrthoDB; EOG091G05Q7; -. DR TreeFam; TF105197; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042825; C:TAP complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042287; F:MHC protein binding; IEA:InterPro. DR GO; GO:0015440; F:peptide-transporting ATPase activity; IEA:InterPro. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 1.20.1560.10; -; 1. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR013305; ABC_Tap-like. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005293; Tap2/ABCB3. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR PRINTS; PR01897; TAP2PROTEIN. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR TIGRFAMs; TIGR00958; 3a01208; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 31 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 51 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 172 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 192 216 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 262 285 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 153 435 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 468 728 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 730 768 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NP_BIND 503 510 ATP. {ECO:0000256|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 768 AA; 84778 MW; 678830A1E515F8DA CRC64; MLFPDLRPWA FLLLADSVLL WLIQGTLGAL LPPGLPGLWL EGTLRLGGLW WLLKVGGLLG LVGTLLAPLC LGTPLFLSLR ALVPGALSAP PVRVASAPWS WLLLGYAAVW LGWAMWALLS SPGAQETKQG QENNTDLMWR LLKLSWPDLP YLLAAFFFLI VAVLGETVIP YYSGHVIDIL RGDFDPDAFT SAIFFMCLFS IGSSLCAGCR GSCFTFTMSR INVRVRQLLF SSLLHQDLSF FQDTKTGELN SRLNSDTKLM SCWLALNANV LLRSVVKVVG LYSFMLSLSP RLALLSLLKV PLAITAQKLY DVRHQAVLRE IQNAVAKAGQ VVREAVGGLQ TVRSFGAEEH ELCLYKEALE RCRQLWWRRD LESALYLLFR RMLHLGMQVL MLNCGLQQIL AGDLTQGGLL SFLLYQEDMG HYVQTLVYMC GDMLSNVGAA EKVFQYLDRK PNLPPPGTLA PPTLRGLVEF QDVSFAYPNR PDQPVLKGLT FTLRPGQVTA LVGPNGSGKS TVAALLQNLY QPSGGRLLLD GQPLSQYEHR YLHRQVTSVG QEPVLFSGSV RDNIAYGLKS CSDEQVMAAA QAANADGFIQ EMEHGLYTDV GERGNQLAVG QKQCLAIARA LVRDPRVLIL DEATSALDVQ CEQANGFWVD SMDGGPPSEC NPTGFLHDSS QRLSSCVGMF VALTELGKPD AELWNSRPDI LERSRASVDA LCRRNYKLGA PFTVGRKVQP EVTVYPERTP SLQHRNLLLC SVTGFYPGDI KIRWFRNG // ID G1L5S3_AILME Unreviewed; 276 AA. AC G1L5S3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 20-JUN-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMEP00000002234}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002234, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002234} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002234} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ACTA01002660; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01194647; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1L5S3; -. DR STRING; 9646.ENSAMEP00000002234; -. DR Ensembl; ENSAMET00000002327; ENSAMEP00000002234; ENSAMEG00000002099. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1L5S3; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 39 {ECO:0000256|SAM:SignalP}. FT CHAIN 40 276 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003413250. FT TRANSMEM 238 260 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 136 224 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 276 AA; 31480 MW; 4DAB6D1FC7A8BAD9 CRC64; PQTLSSLFSR MAYLWFPRGL SMAALMVILM MLSPPSAWAT DTPQHRLYSI NLKCHFTNGT ERVRLLQRCI YNREEYVRFD SDVGEYRAVT ELGRPSAEYW NQQKDFMEQQ RAAVDTYCRH NYGVGESFTV QRRVEPTVTV YPTKTRPLQH HNLLVCSVNG FYPGHIEVRW FRNGQEEEAG VVSTGLIRNG DWTFQTLVML ETVPRSGEVY TCQVEHPSLT SPVTVEWRAR SDSAQSKMLS GIGGFVLGLL FLVVGLFLYF RNQKGHSGLQ PAGLLS // ID G1L6D6_AILME Unreviewed; 256 AA. AC G1L6D6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 20-JUN-2018, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMEP00000002451}; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002451, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002451} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002451} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ACTA01107527; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9646.ENSAMEP00000002451; -. DR Ensembl; ENSAMET00000002556; ENSAMEP00000002451; ENSAMEG00000002342. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1L6D6; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 256 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003413274. FT TRANSMEM 228 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 256 AA; 29679 MW; AFC4D6210FC6671A CRC64; KMAPWIPRGL WTAAVMMILV VLSVPVAEGR DSPQDFVFQF KGECYFTNGT ERVRGVDRYI YNREEFLRYD DDVGEHRPVT ELGRSWAEDF NQQKDFMERK RAEVDTVCRH NYQIEDRFIL QRRVEPTVTI SPSRTEVLNH HNLLVCSVTD FYPGQIKVRW FRNDQEETAG VVSTPLIRNG DWTFQILVML EMTPQRGDVY TCHVEHPSLQ SPITVEWRAQ SESARSKMLS GIGGFVLGLI FLGLGLIIRH RSQKGK // ID G1L6H3_AILME Unreviewed; 285 AA. AC G1L6H3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMEP00000002488}; DE Flags: Fragment; OS Ailuropoda melanoleuca (Giant panda). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; OC Ailuropoda. OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000002488, ECO:0000313|Proteomes:UP000008912}; RN [1] {ECO:0000313|Ensembl:ENSAMEP00000002488} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20010809; DOI=10.1038/nature08696; RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., RA Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., RA Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., RA Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., RA Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., RA Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., RA Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., RA Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., RA Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., RA Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., RA Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., RA Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., RA Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., RA Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., RA Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., RA Wang J., Wang J.; RT "The sequence and de novo assembly of the giant panda genome."; RL Nature 463:311-317(2010). RN [2] {ECO:0000313|Ensembl:ENSAMEP00000002488} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ACTA01059528; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ACTA01067528; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1L6H3; -. DR STRING; 9646.ENSAMEP00000002488; -. DR Ensembl; ENSAMET00000002596; ENSAMEP00000002488; ENSAMEG00000002361. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1L6H3; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008912; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008912}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000008912}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 20 42 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 252 270 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 146 234 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSAMEP00000002488}. SQ SEQUENCE 285 AA; 31944 MW; 6E4E195C818E93B0 CRC64; QSSLSETCLL PCALSSLLSS MVYLCFLGGS WMPALTLILM VLSTPLAWAR DTPPAGMEMF KGECYFTNGT ERVRAVVRCI YNQEEYVRFD SDVGEFRPVT ELGRPDAEYF NQQKDYLEQT RAAVDTVCRH NYGVLDSFLV QRQVEPTVTV YPTKTRPLQH HNLLVCSVNG FYPGHIEVRW FRNGQEEEAG VVSTGLIRNG DWTFQTLVML ETVPRSGEVY TCQVEHPSLT SPVTVEWNPG PNAGRASKAN EITGLMMDLL LYLLNIYLPF SFPGHSGLQP TGLLS // ID G1P4A6_MYOLU Unreviewed; 267 AA. AC G1P4A6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000004781}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000004781, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000004781} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The genome sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000004781} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02057072; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1P4A6; -. DR STRING; 59463.ENSMLUP00000004781; -. DR Ensembl; ENSMLUT00000005241; ENSMLUP00000004781; ENSMLUG00000005240. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1P4A6; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 267 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003416677. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 267 AA; 29777 MW; A6BAD410F744B97A CRC64; MVCLRLRGGS WMAALKVMLM ALSPPLAQAR DTPPHFLYQP KSECHFSNGE QVRFLERHIY NGQEDLLFDS DVGEFRAVTE LGRPIAEFVN SLEDLLEREW AQVDRFCRDN YRLSQEFLVQ RQTEPTVTVY PAKTQGLQHH SLLVCSVNSF YPGHIEVRWL RNGQEEEAGV VSTGLIRNGD WTFQTLVMLE TVPRSGEVYT CQVRHPSSTS PVTVEWRAQS GSAQSKVLSG AGGFVLGLLF LGAGLLIYFR AQKGKGPAGS QGTETVG // ID G1PES9_MYOLU Unreviewed; 268 AA. AC G1PES9; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000009032}; DE Flags: Fragment; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000009032, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000009032} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000009032} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02055727; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59463.ENSMLUP00000009032; -. DR Ensembl; ENSMLUT00000009906; ENSMLUP00000009032; ENSMLUG00000009907. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1PES9; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 268 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003418430. FT DOMAIN 119 225 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMLUP00000009032}. SQ SEQUENCE 268 AA; 29508 MW; A6F96670F0710889 CRC64; LPRQIMSALL RLLLGLSLGC TGAGGFVAHV ESTCLLDDDG IPQDFAYCIS FNKDLLTCWD PEKRTMVPLE FGMLNGLANY LANYLNSQEI LLQRLSEGRQ DCATRTQPFW ESLTQRTRPP SVQVAKATPV NTREPVMLAC YVWGFYPADV TITWRKNGQL VPPHGSAHKV IQSNGDWTYQ TLSHLATTPS FGDTYTCVVE HFGTLEPILQ DWTPGLSPEQ TVKVSVSVVT LGLGLLIFSL GLLSWRRAGS SGYTVLAGST YPQGRHIS // ID G1PU90_MYOLU Unreviewed; 264 AA. AC G1PU90; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 20-JUN-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000014839}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000014839, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000014839, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000014839} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02063766; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1PU90; -. DR STRING; 59463.ENSMLUP00000014839; -. DR Ensembl; ENSMLUT00000016285; ENSMLUP00000014839; ENSMLUG00000016283. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1PU90; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003417485. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29618 MW; 403092F3DB2318FD CRC64; MVAPQAAGAP CMAALLMPLV MLSSPWAQGR DTPAVHVYQR RSDCYESNGT HRFLERYVYN RDVFVQFDST VGVFVAVTEL GRWTARNWNI QREFLELRRG AVDAVCRHNY ELDRAFTLER RVQPKVNVSP SKKGPLQHPD LLVCHVTDFY PGHVQVRWFL NGQEETAGVV STNLIHNGDW TFQILVMLEM TPQQGDVYTC RVEHPSLDSA VTVEWKAQSD SARSKMLTGV GGFVLGLLAL AVSVTLHFRG HSGRQRPQPI GGIS // ID G1PXS7_MYOLU Unreviewed; 266 AA. AC G1PXS7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000016259}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000016259, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000016259} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000016259} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02054299; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1PXS7; -. DR STRING; 59463.ENSMLUP00000016259; -. DR Ensembl; ENSMLUT00000027881; ENSMLUP00000016259; ENSMLUG00000026460. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1PXS7; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003419190. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29697 MW; BD64712894D04426 CRC64; MVCLRLPGGS WMAALKVMLM ALSPPLAQAR DTPPNFLEQL KVECHFSNGT ERVRFLLRYI HNRQEYVRFD SDVGEHRAVT ELGRPIAEHW NSLEGELEPA RAAVDTFCRC NYGVSEGFLV QRRTEPTVTV YPAKTQRLQH HNLLVCSVNG FYPGNIEVRW LRNGQEEEAG VVSTGLIRNG DWTFQTLVML ETVPRSGEVY TCQVRHPSRT SPVTVEWRAQ SGSARSKVLS GAGGFVLGLL FLGAGLLIYF RTQKGHSGLQ PTGLLS // ID G1PXT2_MYOLU Unreviewed; 266 AA. AC G1PXT2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000016264}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000016264, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000016264} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000016264} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02052218; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02052219; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02052220; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_014303190.1; XM_014447704.1. DR ProteinModelPortal; G1PXT2; -. DR STRING; 59463.ENSMLUP00000016264; -. DR Ensembl; ENSMLUT00000026404; ENSMLUP00000016264; ENSMLUG00000023039. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1PXT2; -. DR OMA; YLERHIY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003417689. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29796 MW; 4250E4F7B6AC7BDC CRC64; MVCLRVPGGS WMAALMVILM ALSPPLAQAR DPPPHFLHQV KQECHFSNGT EWVRYLERHI YEGQETLRFD SDLGEFRALT ELSRPEEKAW NSQKDFLQRK QAEAVWVCRH NYRVSEGFLV PQQTEPTLTV YPAKTLRLQH HNLLVCSVNG FYPGHIVVRW LRNGQEEEAG VVSTGLIRNG DWTFQILVML ETVPRSGEVY TCQVQHPSSS SPVTAEWRAQ SGSAQSKVLS GAGGFVLGLL FLGAGLLIYF RAQKGHSGLQ PTGLLS // ID G1PY42_MYOLU Unreviewed; 265 AA. AC G1PY42; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000016374}; GN Name=LOC102431769 {ECO:0000313|Ensembl:ENSMLUP00000016374}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000016374, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000016374, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000016374} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02059510; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_014305524.1; XM_014450038.1. DR ProteinModelPortal; G1PY42; -. DR STRING; 59463.ENSMLUP00000016374; -. DR Ensembl; ENSMLUT00000029278; ENSMLUP00000016374; ENSMLUG00000030543. DR GeneID; 102431769; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1PY42; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 265 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003417645. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 29513 MW; 99FDE65AEBF7471C CRC64; MVCLRLPGGS WVAALKVMLM ALSPPLAQAR DTPANFLEQL KAECHFSNGT ERVLYLQRYF YNGQEYVRFD SDVGEYCAVT ELGRPIAEHL NSRKDFMEQM RAGVDRCREA YRVSEGFLVP RQTKPTVTVY PAKTQHLQHH NLLVCSMNGF YPGPIEVHWL RNGQEEEAGV VSTGLIRNGD WTFQILVMLE TVPRSGEVYT CQVRHPSSTS PVTVEWRAQS GSTQSKVLSG AGGFLLGLLF LGTGLLTYFR AQNGHSGLQP TGLLS // ID G1PZ38_MYOLU Unreviewed; 265 AA. AC G1PZ38; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 20-JUN-2018, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000016720}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000016720, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000016720, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000016720} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02058319; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1PZ38; -. DR STRING; 59463.ENSMLUP00000016720; -. DR Ensembl; ENSMLUT00000023204; ENSMLUP00000016720; ENSMLUG00000023291. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1PZ38; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 265 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003418535. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 29738 MW; 02A4325373F12F02 CRC64; MVCLRLPGGS WMAALKVMLM ALSPPLAQAR DTPPNFLEQV KHECHFSNGT ERVRYLERYI HNGQEDLRFD SDVGEFLALT ELGWPDAEDW NSLESELEQR RAYVDTFCRE AYRVTGFLVQ RKTEPTVTVY PAKTQRLQHH NLLVCSVNGF YPGHIEVRWL RNGQEEEAGV VSTGLIRNGD WTFQTLVMLE TVPRRGEVYT CQVRHPSSTS PVTVEWRAQS GSTQSKVLSG AGGFVLGLLF LGAGLLIYFR AQKGHSGLQP AGNAL // ID G1PZZ5_MYOLU Unreviewed; 265 AA. AC G1PZZ5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000017027}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000017027, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000017027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000017027} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02051231; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02051232; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1PZZ5; -. DR STRING; 59463.ENSMLUP00000017027; -. DR Ensembl; ENSMLUT00000030076; ENSMLUP00000017027; ENSMLUG00000026786. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1PZZ5; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 265 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003417752. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 29697 MW; 202E5629A4503E09 CRC64; MVCLLLPGGS WMAALMVMLM ALSPPLAQAR DTPTHFLEQL KAECQFSNGT ERVRYLQRYI HNGQEDVRFD SDVGEFRAVT ELGRPDAEYW NSQEDFLERM RAAVDRFCRH NYGVSASFEK ERVAEPTVTV YPAKTQRLQH HNLLVCSVNF YPGHIEVRWL RNGQEEEAGV VSTGLIRNGD WTFQTMVMLE TVPRSGEVYT CQVQHPSRTS PVTVEWRAQS GSAQSKVLSG AGGFVLGLLF LGAGLLIYFR AQKGHSGLQP TGLLS // ID G1Q0G8_MYOLU Unreviewed; 265 AA. AC G1Q0G8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000017200}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000017200, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000017200} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000017200} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02056061; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02056062; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59463.ENSMLUP00000017200; -. DR Ensembl; ENSMLUT00000022698; ENSMLUP00000017200; ENSMLUG00000026901. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1Q0G8; -. DR OMA; NGTERRY; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 265 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003417770. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 29843 MW; 35DC0DC66834CCC9 CRC64; MVCLRLPGGS WMAALMVMLM ALSPPLARAR DTPPNFLKQV KKECHFSNGT ERRYLQRYIY NGQEFVRFDS DVGEYRAVTE LGRPDEKLWN SQEGELEQRR AKVDTYCRHN YGVSEGFLVP RQTEPTVTVY PAKTQRLQHH NLLVCSVNGF YPGHIEVHWL RNGQEEEAGV VSTGLIRNGD WTFQILVMLE TVPRSGEVYT CQVRHPSRTS PVTMEWRAQS GSARSKVLSG AGGFVLGLLF LGAGLLIYFR AQKGHSGLQP TGLLS // ID G1Q1T8_MYOLU Unreviewed; 133 AA. AC G1Q1T8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000017671}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000017671, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000017671, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000017671} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02060282; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMLUT00000028902; ENSMLUP00000017671; ENSMLUG00000027094. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1Q1T8; -. DR OMA; RHKYELM; -. DR OrthoDB; EOG091G0YW8; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}. FT DOMAIN 52 126 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 133 AA; 15226 MW; 352266A3E277D092 CRC64; VRLSRFPRGK MTGIPRSPWA AAGIVTVVLT VLRTPLAHRR GTPGDFVYQF KGTCYFTNGT QRVRLVATEI YNRQEIVRFD SDVGVFVAVT ELGRPHAESW NSQEDLLLVY RAQVDVLCRH NYKEMAPFTV QRR // ID G1Q1W4_MYOLU Unreviewed; 270 AA. AC G1Q1W4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000017697}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000017697, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000017697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000017697} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02058239; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1Q1W4; -. DR STRING; 59463.ENSMLUP00000017697; -. DR Ensembl; ENSMLUT00000027745; ENSMLUP00000017697; ENSMLUG00000028956. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1Q1W4; -. DR OMA; EPSHSAM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 270 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003417836. FT TRANSMEM 232 254 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 130 218 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 270 AA; 29809 MW; 5C9657B4A36B2476 CRC64; MVCLLLPGGS WMAFLTVMLM ALSPPLAQAQ GHSTTHFLVQ AKSECYFSNG TERVRFLDGY IYNGQEYVRF DSDVGEFRAV TELGRPSAEH WNSQKDILED ARASVDTYCR CRAAYRVSEG FLCLGKISEP TVTVYPAKTQ RLQHHNLLVC SVNGFYPGNI EVRWLRNGQE EEAGVVSTGL IRNGDWTFQT MVMLETVPRS GEVYTCQVQH PSRTSPVTVE WRAQSGSAQS KVLSGAGGFV LGLLFLGAGL LIYFRAQKGH SGLQPTGLLS // ID G1Q2A7_MYOLU Unreviewed; 89 AA. AC G1Q2A7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000017840}; DE Flags: Fragment; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000017840, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000017840} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000017840} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02052227; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMLUT00000026549; ENSMLUP00000017840; ENSMLUG00000028086. DR GeneTree; ENSGT00910000146742; -. DR InParanoid; G1Q2A7; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}. FT DOMAIN 8 67 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMLUP00000017840}. SQ SEQUENCE 89 AA; 10104 MW; E8A716C78BF874AA CRC64; HFLEQAKSEC QYSNRTERVR FLDRYIHNGQ EFVRFDSDVG EFRAVTELGL PIAEYWNSLE GNTGAQAGPG GTRTADTTTG WLKDTWCSI // ID G1Q4A2_MYOLU Unreviewed; 127 AA. AC G1Q4A2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000018535}; GN Name=LOC102441108 {ECO:0000313|Ensembl:ENSMLUP00000018535}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000018535, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000018535, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000018535} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02061890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02061891; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMLUT00000022521; ENSMLUP00000018535; ENSMLUG00000027858. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1Q4A2; -. DR OMA; ECHYANG; -. DR OrthoDB; EOG091G12PD; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 127 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003418749. FT DOMAIN 42 116 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 127 AA; 15022 MW; 1B01E29BE529DD06 CRC64; MVCLRFPGGS WMAALMVMLM ALSPPLAQAR DTPPHFLQQI KFECHFSNGK EQVQFLERYI YNGQEDFRFD SDVGEFRALT ELRRPDEKGW NIQKDILERK RGAVDTFCRY NYRVSEGFLV PWKSEHR // ID G1Q4X4_MYOLU Unreviewed; 265 AA. AC G1Q4X4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000018757}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000018757, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000018757} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000018757} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02058187; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006107797.1; XM_006107735.2. DR RefSeq; XP_014305234.1; XM_014449748.1. DR STRING; 59463.ENSMLUP00000018757; -. DR Ensembl; ENSMLUT00000023434; ENSMLUP00000018757; ENSMLUG00000026740. DR GeneID; 102441506; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1Q4X4; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 265 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003419124. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 29770 MW; 08380DD3F665E17E CRC64; MVCLRLPGGS WMAALKVMLM ALSPPLAQAR DTPPHFLEQL KAECQFSNWT ERVRYLQRYI YNGQEYLRFD SDVGEYRAVT ELGRPIAEHL NSRKDFMEQM RAGVDRCRAA YRVSEGFLVP RQTKPTVTVY PAKTQHLQHH SLLVCSMNGF YPGPIEVRWL RNGQEEEAGV MSTGLIRNGD WTFQTLVMLE TVPRSGEVYT CQVRHPSSTS PVTVEWRAQS GSTQSKVLSG AGGFLLGLLF LGTGLLIYFR AQKGHSGLQP TGLLS // ID G1Q7L5_MYOLU Unreviewed; 89 AA. AC G1Q7L5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000019698}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000019698, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000019698, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000019698} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02057069; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSMLUT00000007743; ENSMLUP00000019698; ENSMLUG00000029341. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1Q7L5; -. DR OMA; WRDECHY; -. DR OrthoDB; EOG091G0YW8; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}. FT DOMAIN 8 82 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 89 AA; 10789 MW; 3CFA66938FCBD3B2 CRC64; HFLEQVKKEC HFSNGTERVR FLVRLIYNGQ EYVHFDSNVE EYRAVTELGR PDAEHWNSQK DELERARAAV DRYCRHNYWV SEGFLVERK // ID G1Q865_MYOLU Unreviewed; 264 AA. AC G1Q865; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 20-JUN-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000019898}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000019898, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000019898, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000019898} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02052217; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59463.ENSMLUP00000019898; -. DR Ensembl; ENSMLUT00000023483; ENSMLUP00000019898; ENSMLUG00000029049. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1Q865; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003419689. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29508 MW; F7BA5CADDB4997BD CRC64; MVCLRFPGGS WMATLKVMLM ALSSPLAQAR DTPPHFLEQV KHECQFSNGT ERVRYLERYI HNGQEDLRFD SDVGEFLALT ELGWPDAEDW NSLEGELEQR AYVDTFCREA YRVTGFLMQR KTEPTVTVYP AKTQHLQHHN LLVCSVNGFY PGPIEVRWLR NGQEEEAGVV STGLIRNGDW TFQTLVMLET VPRSGEVYTC QVRHPSSTSP VTVEWRAPSG SAQSKVLSGA GGFVLGLLFL GAGLLIYFRA QKGHSGLQPT GLLS // ID G1Q9L8_MYOLU Unreviewed; 281 AA. AC G1Q9L8; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000020401}; GN Name=LOC102433751 {ECO:0000313|Ensembl:ENSMLUP00000020401}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000020401, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000020401, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000020401} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02054299; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59463.ENSMLUP00000020401; -. DR Ensembl; ENSMLUT00000025156; ENSMLUP00000020401; ENSMLUG00000026054. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1Q9L8; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 44 {ECO:0000256|SAM:SignalP}. FT CHAIN 45 281 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003418160. FT TRANSMEM 243 265 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 141 229 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 281 AA; 31463 MW; 05175EA1531941B9 CRC64; VRPPCSLPLS SLSSSMVCLR FPRGSWMAAL MVMLMALSPP LAQARDTPPH FLFLGKAECQ FSNGTERVRF MDRYFYNGQE YVRFDSDVGQ FRAVTELGRP TAKYWNSLED FMEQKRAEVD TYCRHNYGVF EGFSVQRKTE PTVTVYPAKT QRLQHHNLLV CSVNGFYPGH IEVRWLRNGQ EEEAGVVSTG LIRNGDWTFQ TMVMLETVPR SGEVYTCQVQ HPSSTSPVTV EWRAQSGSAQ SKVLSGAGGF VLGLLFLGAG LLIYFRAQKG HSGLQPTGLL S // ID G1QA82_MYOLU Unreviewed; 272 AA. AC G1QA82; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000020615}; DE Flags: Fragment; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000020615, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000020615} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000020615} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02057291; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02057292; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1QA82; -. DR STRING; 59463.ENSMLUP00000020615; -. DR Ensembl; ENSMLUT00000029954; ENSMLUP00000020615; ENSMLUG00000022263. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1QA82; -. DR OMA; GENCAVT; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 36 {ECO:0000256|SAM:SignalP}. FT CHAIN 37 272 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003418994. FT TRANSMEM 234 256 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 132 220 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMLUP00000020615}. SQ SEQUENCE 272 AA; 30219 MW; 40ABB69EFD80F2F4 CRC64; LSSLSSSMVC LRFPGGSWMA ALKVMLMALS PLLAQARDTP SHFMQQQKAE CHFSKGTERV RFLYRYIYNG QEYAHFDSDV GENCAVTELG RPIAKDWNSQ KDELERMRAG VDTFCRHNYG VSGFLVPRQT EPTVTVYPAK TQRLQHHNLL VCSVNGFYPG HIEVRWLRNG QEEEAGVVST GLIWNGDWTF QTLVMLETVP RSGEVYTCQV RHPSSTSPVT VEWRAQSGSA QSKVLSGAGG FVLGLLFLGA GLLIYFRAQK GHSGLQPTGL LS // ID G1QBG5_MYOLU Unreviewed; 266 AA. AC G1QBG5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000021048}; GN Name=LOC102418225 {ECO:0000313|Ensembl:ENSMLUP00000021048}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000021048, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000021048, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000021048} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02055469; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006107020.1; XM_006106958.2. DR ProteinModelPortal; G1QBG5; -. DR STRING; 59463.ENSMLUP00000021048; -. DR Ensembl; ENSMLUT00000028718; ENSMLUP00000021048; ENSMLUG00000029929. DR GeneID; 102418225; -. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1QBG5; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003419397. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29791 MW; 62E57CE04E39D423 CRC64; MVCLRFPGGS WMAALKVMLM ALSPPLAQAR DTPLHFLEQV KFECHFFNGT ERVRFLERYF YNGQEYLRFD SDVGEYRAVT ELGRLDAEYL NSQEDLMEDE RAEVDTLCIY NYVGAEGFLV PRQTEPTVTV YPAKTQRLQH HSLLVCSVNG FYPGHIEVHW LRNGQEEEAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVRHPSST SPVTVEWRAQ SGSAQSKVLS GAGGFVLGLL FLGAGLLIYF RAQKGHSGLQ PTGLLS // ID G1QBP5_MYOLU Unreviewed; 281 AA. AC G1QBP5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000021128}; DE Flags: Fragment; GN Name=LOC102424373 {ECO:0000313|Ensembl:ENSMLUP00000021128}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000021128, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000021128, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000021128} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02052222; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1QBP5; -. DR STRING; 59463.ENSMLUP00000021128; -. DR Ensembl; ENSMLUT00000029965; ENSMLUP00000021128; ENSMLUG00000030134. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1QBP5; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 44 {ECO:0000256|SAM:SignalP}. FT CHAIN 45 281 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003419049. FT TRANSMEM 243 265 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 141 229 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMLUP00000021128}. SQ SEQUENCE 281 AA; 31525 MW; 6EF2AE8E57657F09 CRC64; VRPPCSLPLS SLSSSMVCLR FPRGSWMAAL KVMLMALSSP LAQARDTPPH FLYQVIQECH FSNGTERVRY LYRDIYNGQE DVRFDSDVGE YRAVTELGRP DEKDWNSQED ELEQRRAYVD TYCRHNYGVS EGFLVQRKTE PTVTVYPAKT QRLQHHNLLV CSVNGFYPGN IEVRWLRNGQ EEEAGVVSTG LIRNGDWTFQ TLVMLETVPR SGEVYTCQVR HPSSTSPVTV EWRAQSGSAQ SKVLSGAGGF VLGLLFLGAG LLIYFRAQKG HSGLQPTGLL S // ID G1QDA7_MYOLU Unreviewed; 266 AA. AC G1QDA7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 40. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000021690}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000021690, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000021690} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Genome Sequencing Platform; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000021690} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02063199; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006108732.1; XM_006108670.2. DR ProteinModelPortal; G1QDA7; -. DR STRING; 59463.ENSMLUP00000021690; -. DR Ensembl; ENSMLUT00000024234; ENSMLUP00000021690; ENSMLUG00000025436. DR GeneID; 102431149; -. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1QDA7; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003419923. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29900 MW; 7C14247A9E37A104 CRC64; MVCLRFPGGS WMAALTVMLM ALSPPLAQAR DTPSHFLRQI KFECHFSNWK ERVRLLERLI YNGQEDVRFD SDVGEYRAVT ELGQLSAEHL PRQKDFMERK RAEVDTVCRH NYKVSEGFLL PRHTEPTVTV YPAKTQRLQH HNLLVCSVNG FYPGNIEVRW LRNGQEEEAG VVSTGLIRNG DWTFQTLVML ETVPGSGEVY TCQVRHPSRT SPVTVEWRAQ SGSAQSKVLS GAGGFVLGLL FLGVGLLIYF RAQKGHSGLQ PTGLLS // ID G1QFU5_MYOLU Unreviewed; 266 AA. AC G1QFU5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 20-JUN-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000022578}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000022578, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000022578, ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSMLUP00000022578} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02052221; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1QFU5; -. DR STRING; 59463.ENSMLUP00000022578; -. DR Ensembl; ENSMLUT00000028450; ENSMLUP00000022578; ENSMLUG00000023837. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1QFU5; -. DR OMA; QIRVTWL; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003420031. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30003 MW; AA2281C8AF1758A1 CRC64; MVCLRFPGGS WMAALTVMLM ALSPPLARAR DTPPNFLHQL IQECHFSNRT ERVQYLYRLI YNGQEFLRFD SYVGEFSAVT ELGRPIAEHW NSQEGLLEEK RAYVVTLCRH NYVEFERFLV HRQTEPTVTV YPAKTQRLQH HNLLVCSVNS FYPGHIEVRW LRNGQEEGAG VVSTGLIRNG DWTFQTLVML ETVPRSGEVY TCQVRHPSST SPVTVEWRAQ SGSAQSKGLS GAGGFVLGLL FLGAGLLIYF RAQKGHSGLQ PTDMAL // ID G1QGE3_MYOLU Unreviewed; 265 AA. AC G1QGE3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000022776}; DE Flags: Fragment; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000022776, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000022776} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The genome sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000022776} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02055688; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02055689; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1QGE3; -. DR Ensembl; ENSMLUT00000031273; ENSMLUP00000022776; ENSMLUG00000025967. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1QGE3; -. DR OMA; RIPEAHC; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMLUP00000022776}. SQ SEQUENCE 265 AA; 29918 MW; 458CA284A9D61A84 CRC64; LVPCFPSLLP GLSGLWTLVS EVPDSLGNGI SGNFVLQFKG LCYFTNGTQH VRGVARYLYN LEEQVRYDSD VGEFRALTPL GQLLAENWNG QKELMERERA YVDTVCRHNY QLEALTTLQW RVEPTVTIFP AKTEALTHHN MLVCSVTDFY PAHIKVRWFR NDQEETASVL STPLIRNGDW TYQILVMLEM TPQRGDVYTC RVEHSSLQSP LTVEWRAQSG SAQSKMLSGV GGFVLGLIFL GLGLVIRHRK QKGKQLGKRE DGLCP // ID G1QJQ3_NOMLE Unreviewed; 258 AA. AC G1QJQ3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 3. DT 28-MAR-2018, entry version 49. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSNLEP00000001148}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000001148}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000001148} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000001148} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G1QJQ3; -. DR STRING; 61853.ENSNLEP00000001148; -. DR Ensembl; ENSNLET00000001215; ENSNLEP00000001148; ENSNLEG00000000928. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1QJQ3; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001073; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 216 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 202 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT COILED 75 95 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 258 AA; 29180 MW; FA3E445646D21B2E CRC64; SLGWRLPGGG RFCNRIVHVP TARFLEQFKG ECHFFNGTER VRLLVRFFYN QEEFVRFDSD VGEYRAVTEL GRPIAEHLNS QKDSLERRRA EVDTVCRHNY GGVESFTVQR RVHPEVTVYP SKTQPLQHHN LLVCSVSGFY PGSIEVKWFR NGQEEKAGVV STGLIQNGDW TFQTLVMLET VPRSGEVYTC QVEHPSVTSP LTVEWRARSE SAQSKMLSGV GGFVLGLLFL GAGLFIYFRN QKAPPPGFTP FSCLSLSE // ID G1R4N2_NOMLE Unreviewed; 224 AA. AC G1R4N2; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 28-MAR-2018, entry version 39. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 1 {ECO:0000313|Ensembl:ENSNLEP00000008154}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSNLEP00000008154}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000008154}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000008154} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000008154} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ADFV01069487; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_012358581.1; XM_012503127.1. DR STRING; 61853.ENSNLEP00000008154; -. DR Ensembl; ENSNLET00000008541; ENSNLEP00000008154; ENSNLEG00000006693. DR GeneID; 100602317; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1R4N2; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000001073; Chromosome 1a. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014123023. SQ SEQUENCE 224 AA; 26114 MW; A0898B2E6D30C46A CRC64; MSWKKALRIP GGLRAATVTL MLAMLSTPVA EGRDSPEDFV FQFKAMCYFT NGTERVRYVT RYIYNREEFV RFDSDVRVYR ALTPQGRPVA EDWNSQKDIL ERTRAELDTV CRHNYEVAYR GILQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DIYTCHVEHP SLQSPITVEW RLLH // ID G1R4P5_NOMLE Unreviewed; 227 AA. AC G1R4P5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 28-MAR-2018, entry version 41. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 2 {ECO:0000313|Ensembl:ENSNLEP00000008167}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSNLEP00000008167}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000008167}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000008167} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000008167} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ADFV01069490; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 61853.ENSNLEP00000008167; -. DR Ensembl; ENSNLET00000008555; ENSNLEP00000008167; ENSNLEG00000006713. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1R4P5; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000001073; Chromosome 1a. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 227 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014177107. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 227 AA; 26061 MW; 45D9E43D254E19E8 CRC64; MALQIPGSFW AAAVTAMLVM LSTPVAEARD FPKDFLVQFK GMCYFTNGTE RVRGVARYIY NREEYGRFDS DVGEFQAVTE LGRSIEDWNN YKDFLEQERA AVDKVCRHNY EAELRTTLQR RVEPTVTISP SRTEALNHHN LLVCSVTDFY PGQIKVRWFR NDQEETAGVV STSLIRNGDW TFQILVMLEM TPQRGDVYTC HVEHPSLQSP ITVEWRPRGP PPAGLLH // ID G1R4S3_NOMLE Unreviewed; 653 AA. AC G1R4S3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 23-MAY-2018, entry version 52. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSNLEP00000008195}; GN Name=TAP2 {ECO:0000313|Ensembl:ENSNLEP00000008195}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000008195, ECO:0000313|Proteomes:UP000001073}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000008195} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000008195} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ADFV01069493; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01069494; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_012358660.1; XM_012503206.1. DR STRING; 61853.ENSNLEP00000008195; -. DR Ensembl; ENSNLET00000008583; ENSNLEP00000008195; ENSNLEG00000006714. DR GeneID; 100604022; -. DR CTD; 6891; -. DR eggNOG; KOG0058; Eukaryota. DR eggNOG; COG1132; LUCA. DR GeneTree; ENSGT00550000074497; -. DR InParanoid; G1R4S3; -. DR OMA; FNQFFVG; -. DR OrthoDB; EOG091G05Q7; -. DR TreeFam; TF105197; -. DR Proteomes; UP000001073; Chromosome 1a. DR GO; GO:0042825; C:TAP complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042287; F:MHC protein binding; IEA:InterPro. DR GO; GO:0015440; F:peptide-transporting ATPase activity; IEA:InterPro. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 1.20.1560.10; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR013305; ABC_Tap-like. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005293; Tap2/ABCB3. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR PRINTS; PR01897; TAP2PROTEIN. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR TIGRFAMs; TIGR00958; 3a01208; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT DOMAIN 153 435 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 468 653 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 653 AA; 71832 MW; EC783ECF1E566DAF CRC64; MPLPDLRPWT SLLLVDAALL WLLQGPLGTL LPQGQPGLWL EGTLRLGGLW GLLKLSGLLG FVGTLLPPLC LATPLTVSLR ALVAGALRAP PARVASAPWS WLLVGYGAAG LSWSLWAVLS PPGAQEKEQD QVNNNVLMWR LLKLSRPDLP LLVAAFFFLV LAVLGETLIP HYSGRVIDIL GGDFDPHAFV SAIFFMCLFS FGSSLSAGCR GGCFTYTMSR INLRIREQLF SSLLRQDLGF FQETKTGELN SRLSSDTTLM SNWLPLNANV LLRSVVKVVG LYGFMLSISP RLTLLSLLHM PFTIAAEKVY NTRHQAVLRE IQDAVARAGQ VVREAIGGLQ TVRSFGAEEH EVCRYKEALE QCRQLYWRRD LERALYLLVR RVLHLGVQML MLSCGLQQMQ DGELTQGSLL SFMIYQESVG SYVHTLVYIY GDMLSNVGAA EKVFSYMDRQ PNLPSPGTLA PTTLQGIVKF QDVSFAYPNC PDRPVLKGLT FTLRPGEVTA LVGPNGSGKS TVAALLQNLY QPTGGQVLLD EKPISQYEHC YLHSQVVSVG QEPVLFSGSV RSNIAYGLQS CEDDKVMAAA QAAHADDFIQ EMEHGIYTDV GEKGSQLAAG QKQRLAIARA LVRDPRVLIL DEATSALDVQ CEQAKTFWKF MIF // ID G1R4X0_NOMLE Unreviewed; 263 AA. AC G1R4X0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSNLEP00000008242}; GN Name=LOC100606816 {ECO:0000313|Ensembl:ENSNLEP00000008242}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000008242, ECO:0000313|Proteomes:UP000001073}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000008242} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000008242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ADFV01069501; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADFV01069502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003272208.1; XM_003272160.3. DR STRING; 61853.ENSNLEP00000008242; -. DR Ensembl; ENSNLET00000008631; ENSNLEP00000008242; ENSNLEG00000006770. DR GeneID; 100606816; -. DR KEGG; nle:100606816; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1R4X0; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000001073; Chromosome 1a. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003419481. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28823 MW; 87336FC594BB365E CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN GLANGLSNYL NQQDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPADVTITWR KNGKLVSPHS SAHKTARPNG DWTYQTLSYL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGLISW RRAGSSSYTP LPGSNYPEGR HIS // ID G1R508_NOMLE Unreviewed; 258 AA. AC G1R508; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 28-MAR-2018, entry version 42. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSNLEP00000008280}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSNLEP00000008280}; OS Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates OS leucogenys). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hylobatidae; Nomascus. OX NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000008280}; RN [1] {ECO:0000313|Ensembl:ENSNLEP00000008280} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. RN [2] {ECO:0000313|Ensembl:ENSNLEP00000008280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Gibbon Genome Sequencing Consortium; RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ADFV01069513; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003272211.1; XM_003272163.3. DR STRING; 61853.ENSNLEP00000008280; -. DR Ensembl; ENSNLET00000008671; ENSNLEP00000008280; ENSNLEG00000006801. DR GeneID; 100607843; -. DR KEGG; nle:100607843; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1R508; -. DR KO; K06752; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001073; Chromosome 1a. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001073}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001073}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003420944. FT TRANSMEM 227 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 228 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29253 MW; 58D4DD8FD328A481 CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYLYQV RQECYAFNGT QRYLERYIYN REEVLRFDSD VGEFQAVTEL GRPEAEYFNS QEDILEKKRA VTDTMCRHNY ELDEAVTLQR RVQPRVNVSP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHPSLDSP VTVDWKAQSD SARSKTLTGA GGFMLGLIIC GVGIFMHRRS KKVQRGSA // ID G1SFC3_RABIT Unreviewed; 266 AA. AC G1SFC3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 2. DT 12-SEP-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOCUP00000001201}; GN Name=RLA-DRB1 {ECO:0000313|Ensembl:ENSOCUP00000001201}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001201, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000001201, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000001201} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001201}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAGW02017726; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_002714652.2; XM_002714606.3. DR UniGene; Ocu.7437; -. DR ProteinModelPortal; G1SFC3; -. DR STRING; 9986.ENSOCUP00000001201; -. DR Ensembl; ENSOCUT00000001396; ENSOCUP00000001201; ENSOCUG00000001396. DR GeneID; 100350656; -. DR KEGG; ocu:100350656; -. DR CTD; 100350656; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1SFC3; -. DR KO; K06752; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001811; Chromosome 12. DR Bgee; ENSOCUG00000001396; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30099 MW; 050F1F77286431F3 CRC64; MLCLWLSRGP CLAALTVTLL VLSSYLALAR DTRSRFLELV KHECHFSNGT QRVRYIFRDV YNQEEHVRFD SDVGEFEAVT ELGRPDAEYW NSQTDILEDR RTAVDRYCRH NYGVLDSFLV QRRVVPTVTV YPAKTQPLQH HNLLVCAVSG FYPGHIEVRW FRNGEEEEAG VVSTGLIRNG DWTFQTLVML ETVPQSGEVY TCQVEHPSVT SPITVEWKAQ SESAQSKMLS GVGGFVLGLL FLGLGLFVYR RNQKGHSGLQ PTGLLS // ID G1SHN5_RABIT Unreviewed; 304 AA. AC G1SHN5; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 2. DT 12-SEP-2018, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOCUP00000002148}; GN Name=LOC100351163 {ECO:0000313|Ensembl:ENSOCUP00000002148}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000002148, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000002148, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000002148} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000002148}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAGW02017729; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G1SHN5; -. DR STRING; 9986.ENSOCUP00000002148; -. DR Ensembl; ENSOCUT00000002484; ENSOCUP00000002148; ENSOCUG00000002485. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1SHN5; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001811; Chromosome 12. DR Bgee; ENSOCUG00000002485; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl. DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl. DR GO; GO:0008134; F:transcription factor binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0002344; P:B cell affinity maturation; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl. DR GO; GO:0046635; P:positive regulation of alpha-beta T cell activation; IEA:Ensembl. DR GO; GO:0002579; P:positive regulation of antigen processing and presentation; IEA:Ensembl. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 266 286 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 164 252 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 304 AA; 34279 MW; E1776A82B30A3A53 CRC64; MPGSFLRFLF SQVGTSDLFG ASFADCHSLL PLFSSMSRGM ALLLPRSLRR AAVLAILVVL SSPAAEGHDS PKDFVVQFKC QCYFTNGTQR VQYVTRYIYN LEEHLRFDSD VGEYRAVTEL GRPEAKSWNS QPDILERTRA EVDTVCRHNY QAELLTSLQR REKPMVTISP SKREVLDHHN MLVCSVTDFY PSQIKVRWFR NDQEETAGVV STPLIRNGDW TFQILVMLEM TPQRGDVYTC QVEHPSVESP ITVEWRVQSE SAQSKMLSGV GGFVLGLIFL GLGLIIHHRS QKGSRGSPPT GLLH // ID G1SHP0_RABIT Unreviewed; 264 AA. AC G1SHP0; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 2. DT 12-SEP-2018, entry version 43. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSOCUP00000002153}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSOCUP00000002153}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000002153, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000002153, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000002153} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000002153}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAGW02017730; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_008260980.1; XM_008262758.2. DR RefSeq; XP_017200510.1; XM_017345021.1. DR UniGene; Ocu.1844; -. DR ProteinModelPortal; G1SHP0; -. DR Ensembl; ENSOCUT00000002489; ENSOCUP00000002153; ENSOCUG00000029437. DR GeneID; 100351416; -. DR KEGG; ocu:100351416; -. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000001811; Chromosome 12. DR Bgee; ENSOCUG00000029437; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003422600. FT TRANSMEM 224 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 122 210 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 30030 MW; AB9E2F1A6A7F45BE CRC64; MDSKWVPWVV ALLVNLIRLD YSMTQGDSPE DFVIQAKADC YFTNGTEQVR FVVRFIFNLE EYAHFDSDVG MFVALTELGQ PDAESWNNRP DILERSRASV DFLCRRNYRL GAPFTVGRKV PPEVTVYPER TPVLRQHNLL LCSATGFYPG DIRVKWLRNG QEERAGIMST GLIRNGDWTF QTTEMLEMTP ELGDVYTCLV DHPSLLSPVS VEWRPQSEYS WAKMLSGVAG FLFGLIFLMV GTIIHIRAWK GYVETQLSAA AEVS // ID G1SVQ7_RABIT Unreviewed; 253 AA. AC G1SVQ7; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 2. DT 12-SEP-2018, entry version 43. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSOCUP00000007527}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSOCUP00000007527}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000007527, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000007527, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000007527} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000007527}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAGW02017734; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_008260991.1; XM_008262769.2. DR Ensembl; ENSOCUT00000008716; ENSOCUP00000007527; ENSOCUG00000008721. DR GeneID; 100341358; -. DR KEGG; ocu:100341358; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G1SVQ7; -. DR KO; K06752; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001811; Chromosome 12. DR Bgee; ENSOCUG00000008721; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 253 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003422629. FT TRANSMEM 221 241 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 119 207 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 253 AA; 28659 MW; D3840305B9B3D7B6 CRC64; MRPCRSLRTA ALAVVLTVLL HPVALGRATP ENYLWQRRYE CYASNGTQRL LDRCAYNREE FVRFDSDIGE FRAVSELGRQ VAESWNLEYL QQARAEVDRV CRHNYELFQG LPVLLQAQPR VSVSPSKKGP LQHHSLLVCH VTDFYPGHVQ VRWFLNGREE TAGVVSTHPI HNGDWTFQIL VMLEMTPHQG DVYTCHVEHP SLDSPITVEW KAQSDSARSK MLAGVGGLVL GLVSLAVGVF MHRRSKKAQQ GCR // ID G1TXW3_RABIT Unreviewed; 257 AA. AC G1TXW3; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 12-SEP-2018, entry version 39. DE SubName: Full=Histocompatibility antigen DM heterodimer light chain-like precursor {ECO:0000313|Ensembl:ENSOCUP00000021918}; GN Name=RLA-DMB {ECO:0000313|Ensembl:ENSOCUP00000021918}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000021918, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000021918, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000021918} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000021918}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAGW02017730; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9986.ENSOCUP00000015452; -. DR Ensembl; ENSOCUT00000029029; ENSOCUP00000021918; ENSOCUG00000026567. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR Proteomes; UP000001811; Chromosome 12. DR Bgee; ENSOCUG00000026567; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 257 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003424330. FT DOMAIN 114 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 257 AA; 28231 MW; 2B6ADDF573684A46 CRC64; MSALLPLLLG FSLGCTGAGG FVAHVESTCL LDDDGTPRDF TYCISFNKDL LTCWDPQEGQ LTPVEFGVLN PLAISISEYL NHSDTLLQRL HNGLKNCGTH TQPFWTSLTH RTRPPTVQVA ETTPFNTREP VMLACYVWGF YPADVTITWM KNGQLVIPHS SMEKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHIGAP EPILQNWTPG LSPTLTVKVS VSVVTLGVGS IIFSLGLICW RKYGFSSYTP LPGSNYP // ID G3HQS3_CRIGR Unreviewed; 280 AA. AC G3HQS3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 20-JUN-2018, entry version 47. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain-like protein {ECO:0000313|EMBL:ERE88225.1}; DE SubName: Full=HLA class II histocompatibility antigen, DP(W4) beta chain {ECO:0000313|EMBL:EGW09102.1}; GN ORFNames=H671_1g3220 {ECO:0000313|EMBL:ERE88225.1}, GN I79_013179 {ECO:0000313|EMBL:EGW09102.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW09102.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). RN [2] {ECO:0000313|EMBL:EGW09102.1} RP NUCLEOTIDE SEQUENCE. RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line."; RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Proteomes:UP000030759} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17A/GY {ECO:0000313|Proteomes:UP000030759}; RX PubMed=23929341; DOI=10.1038/nbt.2645; RA Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., RA Kofler R., Romand S., Hesse F., Budach W.E., Galosy S., Muller D., RA Noll T., Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., RA Goesmann A., Helk B., Mott J.E., Puhler A., Borth N.; RT "Chinese hamster genome sequenced from sorted chromosomes."; RL Nat. Biotechnol. 31:694-695(2013). RN [4] {ECO:0000313|EMBL:ERE88225.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=17A/GY {ECO:0000313|EMBL:ERE88225.1}; RA Brinkrolf K., Rupp O., Laux H., Kollin F., Ernst W., Linke B., RA Kofler R., Romand S., Hesse F., Budach W.E., Galosy S., Muller D., RA Noll T., Wienberg J., Jostock T., Leonard M., Grillari J., Tauch A., RA Goesmann A., Helk B., Mott J.E., Puehler A., Borth N.; RT "Chinese hamster genome sequenced from sorted chromosomes."; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH000617; EGW09102.1; -; Genomic_DNA. DR EMBL; KE666174; ERE88225.1; -; Genomic_DNA. DR PRIDE; G3HQS3; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR Proteomes; UP000030759; Unassembled WGS sequence. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 280 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5010496915. FT TRANSMEM 222 241 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 120 208 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 280 AA; 31616 MW; 1470FD27631D6485 CRC64; MVLCIPVSPW VAALMVLLSR GIQGGAPPDN HLLRALHECY AEDNRTQRYV MRCILDREEF MRFDSTVGEF RALTAMGRPW AESWNSQKEY MERRRAEVDT VCRHNYELNQ GFTVKRRVQP KVHVSPSKKV ALQHHGLLVC HATDFYPGNI QVRWFRNGQE ETAGVVSTNL IRNGDWTFQI LVMLEMTPQG GDVYTCHVEH PSLQSPITVE WKVRSDSARN KMLTGVCGLV LGLIFLAVGT TMHLRCKKGE KCVEEQPPTA AMAGGSQVQG LPGLHSETWT // ID G3HQS7_CRIGR Unreviewed; 261 AA. AC G3HQS7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 20-JUN-2018, entry version 36. DE SubName: Full=Class II histocompatibility antigen, M beta 1 chain {ECO:0000313|EMBL:EGW09106.1}; GN ORFNames=I79_013183 {ECO:0000313|EMBL:EGW09106.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW09106.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH000617; EGW09106.1; -; Genomic_DNA. DR RefSeq; XP_003505928.1; XM_003505880.3. DR RefSeq; XP_007622903.1; XM_007624713.2. DR ProteinModelPortal; G3HQS7; -. DR GeneID; 100761082; -. DR KEGG; cge:100761082; -. DR InParanoid; G3HQS7; -. DR KO; K06752; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003444537. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 204 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 28778 MW; 653B18553ED166C7 CRC64; MAMLLQLLLG LSLGCVGVGG FVAHVESTCL LDDSGTPKDF TYCVAFNKDL LACWDPESGQ IVPIEFGVLY NLAVFISKSL NTNEALIRRL GKGLQDCAMH TQPFWDALTH RTRPPSVQVA RTAPINTKEP VMLACYVWGF YPADVTVTWM KNGNLVIPHN IKESTAQTNG DWTYQTVSYL ALTPSYGDIY TCVVQHSATS EPVRQDWTIG LSPIQTVKVS VSAVTLGLGF IIFCFGFFSW RKARLSSYIP LPGSTYPEGR H // ID G3HQT2_CRIGR Unreviewed; 258 AA. AC G3HQT2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 33. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|EMBL:EGW09111.1}; GN ORFNames=I79_013188 {ECO:0000313|EMBL:EGW09111.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW09111.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH000617; EGW09111.1; -; Genomic_DNA. DR ProteinModelPortal; G3HQT2; -. DR PRIDE; G3HQT2; -. DR InParanoid; G3HQT2; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29310 MW; F5CC8E2259A8F137 CRC64; MGAGRAPWVV ALLVNLMRPD SFMSEGRGPP EDFVIQAKAD CYFTNGTEKV RFVVRFIFNL EEYLHFDSDL GVFVALTELG EPDAEQWNKR WDLLEQSRAS VNLVCRQNYK LGAPFTVERE VPPEVTVFPE RTPLLQQHNL LFCSVTGFYP GDIKVRWFRN GQEERSGVMS TGLVRNGDWT FQMTVMLEMT PELGDTYSCL VEHPSLESPV SVEWMAQSEY SWKKILSGGV AFLLGLIVFL VGVVIHLKAR KGNKLPRL // ID G3HQT5_CRIGR Unreviewed; 503 AA. AC G3HQT5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 37. DE SubName: Full=HLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EGW09114.1}; GN ORFNames=I79_013191 {ECO:0000313|EMBL:EGW09114.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW09114.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH000617; EGW09114.1; -; Genomic_DNA. DR ProteinModelPortal; G3HQT5; -. DR PRIDE; G3HQT5; -. DR InParanoid; G3HQT5; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 2. DR Gene3D; 3.10.320.10; -; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 2. DR Pfam; PF00969; MHC_II_beta; 2. DR ProDom; PD000328; MHC_II_b_N; 2. DR SMART; SM00407; IGc1; 2. DR SMART; SM00921; MHC_II_beta; 2. DR SUPFAM; SSF48726; SSF48726; 2. DR SUPFAM; SSF54452; SSF54452; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS00290; IG_MHC; 2. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 448 469 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 346 434 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT COILED 311 331 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 503 AA; 57855 MW; 571E208CF25D4483 CRC64; MVRLWLPRGS CVAAVVLTLM ALSPPVTLVR DPRPRFLEQA KHECHFYNGT QRVRYLERRI HNREEYARFD SEVGEYRAVT ELGRPDAEYW NGQKELLEQR RASVDTYCRH NYGVGESFTV QRRVEPQVTV YPTKSQPLEH HNLLVCSVSG FYPGHIEVRW FRNDQEETAG VVSTGLIQNG DWTFQTLVML ETVPQSGEVY TCQVEHPSLA SPVTVEWRAQ STSAQNKMLS GIGGFVLGLL FLGLGLFIYF RNQKARYLEQ LKAECHYLKG KESVRSVTRF IYNQEEFAQF DSDIGKFRAV TELGQPIAED LNSQKDVLEN YRASVDRCRN NYRLVDWFLL NLKAEPQVSV YPTKTQPLEH HNLLVCSASR FYPSHIEVRW FRNGQEEKDG VISTGLIQNG DWTYQILVML EMVPQSGEVY TCQVEHPSLA SPVTVEWTAQ STSTQNRVWS GVIFVLGLLL PVVQCIYFRT REVRSPAGPN RLHSISGEGR GFLRLEMRYQ ENL // ID G3I647_CRIGR Unreviewed; 236 AA. AC G3I647; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 32. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EGW07951.1}; GN ORFNames=I79_018959 {ECO:0000313|EMBL:EGW07951.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07951.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH001341; EGW07951.1; -; Genomic_DNA. DR ProteinModelPortal; G3I647; -. DR PRIDE; G3I647; -. DR InParanoid; G3I647; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 175 197 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 73 161 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 236 AA; 26204 MW; EC525FC0473CD8EF CRC64; MMLLTSDTDW LPSTDFTQHS TKAENPLVPL TWQAEYWSSQ EGFLEQKPAK VDTFCRFNYA IVGLLTVLQR VEPQVTMYPT KTRPLEHRNL LVCSVSGFYP GHIEVRWFRN DQEEKAGVVP TGLIQNGDWT FQILVMLETV PQSGEVYTFQ VEHPSLASPV TVEWRAQSTS AQNKMLSGIG GFVLGLLFLG LGLFIYFRNQ KVCSGLTAVG CGAREISGSS SESGDMNLGT DLPPCT // ID G3I648_CRIGR Unreviewed; 137 AA. AC G3I648; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EGW07952.1}; GN ORFNames=I79_018960 {ECO:0000313|EMBL:EGW07952.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07952.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH001341; EGW07952.1; -; Genomic_DNA. DR ProteinModelPortal; G3I648; -. DR InParanoid; G3I648; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}. FT DOMAIN 46 101 IGc1. {ECO:0000259|SMART:SM00407}. SQ SEQUENCE 137 AA; 15710 MW; E397DD00AB947410 CRC64; MTKLGRSKPS TDWSSQEGFL EQKPAKVDTF CRFNYAIVGL LTVLQRVRWF RNDQEVKAGV MSTDLIQNGD WTFQILVMLE TVPQSGEVYT CQVEHPSLTS PVTVEWRAQS TSAQNKMLSR IGGFMLGLLF FWLELER // ID G3I649_CRIGR Unreviewed; 373 AA. AC G3I649; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 23-MAY-2018, entry version 33. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EGW07953.1}; GN ORFNames=I79_018961 {ECO:0000313|EMBL:EGW07953.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW07953.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH001341; EGW07953.1; -; Genomic_DNA. DR ProteinModelPortal; G3I649; -. DR PRIDE; G3I649; -. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 156 178 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 54 142 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 373 AA; 41079 MW; C64EDB2BF11FB8E8 CRC64; MGKYQAVTKL GKIQAEYWNS QEGFLEQKRA KVDTFCRFNY AIVGLLTVLQ RAEPRVTVYL TKTQPLEHRN LLVCSVSGFY PGHIEVRWFQ NDQEEKAGIV STGLIRNGDW TFQILVMLET VPQSGEVYTC QVEHPSLTSP VTVEWRAQST SAQNKMLSGI GGFVLGLLFL GLGLFIYFRN QKGLLNWGEV ISLKEGAFPV STAQLPPLPE YPRTWLLLAL DTVDLCSLSA PGPSLASPWA EASLPTAALC LAHLSVTLEA QLSVTLEAHL SVTLEAHLSD TLEAHLSDTL EAHLSVTLEA HLSVTLEAHL SDTLEAHLSV TLEAHLSVTL EAHLSVTLEA HLSVPLCQHL GCLEQPGFLL MFFGDFQLLQ GQR // ID G3II66_CRIGR Unreviewed; 125 AA. AC G3II66; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 10-MAY-2017, entry version 22. DE SubName: Full=H-2 class II histocompatibility antigen, I-A beta chain {ECO:0000313|EMBL:EGW12663.1}; GN ORFNames=I79_023533 {ECO:0000313|EMBL:EGW12663.1}; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW12663.1, ECO:0000313|Proteomes:UP000001075}; RN [1] {ECO:0000313|Proteomes:UP000001075} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075}; RX PubMed=21804562; DOI=10.1038/nbt.1932; RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., RA Xie M., Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., RA Koh W., Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., RA Quake S.R., Famili I., Palsson B.O., Wang J.; RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell RT line."; RL Nat. Biotechnol. 29:735-741(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH002938; EGW12663.1; -; Genomic_DNA. DR Proteomes; UP000001075; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001075}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001075}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 64 86 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 16 45 MHC_II_beta. {ECO:0000259|Pfam:PF00969}. SQ SEQUENCE 125 AA; 13683 MW; 3D9AE00C952212F5 CRC64; MFLATSQSEC HFSSGQAEYW SSQEGFLEQK PAKVDTFCRF NYAIVGLLTV LQRGAQSTSA QNKMLSGIGG FVLGLLFLGL GLFIYFRNQK GKEPGGVQDP IAFQGRSTLC SRDVTELVIS GFNQL // ID G3MWT2_BOVIN Unreviewed; 266 AA. AC G3MWT2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-SEP-2018, entry version 53. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSBTAP00000053987}; GN Name=BOLA-DYB {ECO:0000313|Ensembl:ENSBTAP00000053987}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000053987, ECO:0000313|Proteomes:UP000009136}; RN [1] {ECO:0000313|Ensembl:ENSBTAP00000053987, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000053987, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [2] {ECO:0000313|Ensembl:ENSBTAP00000053987} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000053987}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; DAAA02054876; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G3MWT2; -. DR STRING; 9913.ENSBTAP00000053987; -. DR PaxDb; G3MWT2; -. DR Ensembl; ENSBTAT00000064718; ENSBTAP00000053987; ENSBTAG00000045923. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3MWT2; -. DR OMA; RIPEAHC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000045923; Expressed in 3 organ(s), highest expression level in spleen. DR ExpressionAtlas; G3MWT2; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003447555. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30276 MW; 832CDA635ADAD479 CRC64; YGCLCFPSGL WVTEFILLIQ VLRIPEAHCR DAPKNFVYQF KGMCYFTNGT EHVRLVARQI YNKEEILHFD SDLGEFVAVT ELGRVCAEIW NTQKDLLAEF RAYVDTLCRH NYKETAGFTV QRRVEPTVTV SPASTEALNH HNLLVCSVTD FYPRQVKVKW FRNQQEQTAG VGFTPLTQNG DWTYQIHVML ETVPQLGDVY VCHVDHPSLQ SPITVEWRAQ SESAQSKMQS GIGGFVLGLI FLGVGLFVHF WDKRVHDLCS EAGLVA // ID G3N555_GASAC Unreviewed; 251 AA. AC G3N555; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000000425}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000425, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000000425} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000000425} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3N555; -. DR Ensembl; ENSGACT00000000425; ENSGACP00000000425; ENSGACG00000000336. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 251 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003448142. FT TRANSMEM 217 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 251 AA; 28228 MW; A640D1C7AB2BE1CB CRC64; MAPSFISVSL LFIGLHAADG FMEFVATECV FNSTELKDIE YIQSYYYNKL EYTRFSSSVG KFVGFTERGV KNAAAWNNNP SYLSRAKAQK EVYCLNHVPV YYNNMLTKSA EPYVRLHSET PPGGGPLSML VCSVYDFYPK KIIVRWTRDG RPETTGVTST DELADGDWYY QTHSHLEYTP SRSGEKISCV VEHISLSKPL VTDWTDPSMP ESERNKVAIG ASGLILGLTL SLAGFIYYKR KARGRILVPS H // ID G3N560_GASAC Unreviewed; 249 AA. AC G3N560; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000000430}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000430, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000000430} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000000430} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000000430; ENSGACP00000000430; ENSGACG00000000336. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003448067. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28039 MW; 42DCA082B0E23C12 CRC64; MAPSFISVSL LFIGLHAADG FMEFVATECV FNSTELKDIE YIQSYYYNKL EYTRFSSSVG KFVGFTERGV KNAAAWNNNP SYLSRAKAQK EVYCLNHVPV YYNNMLTKSA EPYVRLHSET PPGGGPLSML VCSVYDFYPK KIIVRWTRDG RPETTGVTST DELADGDWYY QTHSHLEYTP RSGEKISCVV EHISLSKPLV TDWNPSMPES ERNKVAIGAS GLILGLTLSL AGFIYYKRKA RGRILVPSH // ID G3N561_GASAC Unreviewed; 256 AA. AC G3N561; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000000431}; DE Flags: Fragment; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000431, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000000431} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000000431} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3N561; -. DR STRING; 69293.ENSGACP00000000431; -. DR Ensembl; ENSGACT00000000431; ENSGACP00000000431; ENSGACG00000000336. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3N561; -. DR OMA; VWISAGC; -. DR TreeFam; TF333780; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 217 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 92 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGACP00000000431}. SQ SEQUENCE 256 AA; 28729 MW; BE04063660E36872 CRC64; FMEFVATECV FNSTELKDIE YIQSYYYNKL EYTRFSSSVG KFVGFTERGV KNAAAWNNNP SYLSRAKAQK EVYCLNHVPV YYNNMLTKSA EPYVRLHSET PPGGGPLSML VCSVYDFYPK KIIVRWTRDG RPETTGVTST DELADGDWYY QTHSHLEYTP SRSGEKISCV VEHISLSKPL VTDWNPSMPE SERNKVAIGA SGLILGLTLS LAGFIYYKRK ARAGPPESGP GSPAPSDTCL VFQTSSVWFQ WSGICI // ID G3N562_GASAC Unreviewed; 70 AA. AC G3N562; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000000432}; DE Flags: Fragment; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000432, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000000432} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000000432} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000000432; ENSGACP00000000432; ENSGACG00000000336. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}. FT DOMAIN 1 63 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGACP00000000432}. SQ SEQUENCE 70 AA; 8203 MW; E7C884850EC51D6A CRC64; EYIQSYYYNK LEYTRFSSSV GKFVGFTERG VKNAAAWNNN PSYLSRAKAQ KEVYCLNHVP VYYNNMLTKS // ID G3N580_GASAC Unreviewed; 250 AA. AC G3N580; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000000450}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000450, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000000450} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000000450} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR STRING; 69293.ENSGACP00000000450; -. DR Ensembl; ENSGACT00000000450; ENSGACP00000000450; ENSGACG00000000350. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3N580; -. DR OMA; DWNNYKD; -. DR TreeFam; TF333780; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 250 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003448070. FT TRANSMEM 216 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 250 AA; 28128 MW; AB9590E7A49641E0 CRC64; MAPSFISVSL LFIGLHAADG FMEFRTDECV FNSTELKDIE FIRSSYYNKK EDTRFSSSVG KFVGFTEQGV KYAANWNKDA SYLSAMRAQK EVYCLNNVQI KYDNALTKSA EPYVRLHSET PPGGGPLSML VCSVYDFYPK KIIVRWTRDG RPETTGVTST DELADGDWYY QTHSHLEYTP SRSGEKISCV VEHISLSKPL VTDWNPSMPE SERNKIAIGA SGLILGLTLS LAGFIYYKRK ARGRILVPSH // ID G3N582_GASAC Unreviewed; 249 AA. AC G3N582; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000000452}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000452, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000000452} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000000452} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3N582; -. DR Ensembl; ENSGACT00000000452; ENSGACP00000000452; ENSGACG00000000350. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003448050. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28041 MW; C404414D4AA1CA1F CRC64; MAPSFISVSL LFIGLHAADG FMEFRTDECV FNSTELKDIE FIRSSYYNKK EDTRFSSSVG KFVGFTEQGV KYAANWNKDA SYLSAMRAQK EVYCLNNVQI KYDNALTKSA EPYVRLHSET PPGGGPLSML VCSVYDFYPK KIIVRWTRDG RPETTGVTST DELADGDWYY QTHSHLEYTP RSGEKISCVV EHISLSKPLV TDWNPSMPES ERNKIAIGAS GLILGLTLSL AGFIYYKRKA RGRILVPSH // ID G3N583_GASAC Unreviewed; 70 AA. AC G3N583; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000000453}; DE Flags: Fragment; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000000453, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000000453} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000000453} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000000453; ENSGACP00000000453; ENSGACG00000000350. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}. FT DOMAIN 1 63 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGACP00000000453}. SQ SEQUENCE 70 AA; 8090 MW; D33470DD9BF8BFBB CRC64; EFIRSSYYNK KEDTRFSSSV GKFVGFTEQG VKYAANWNKD ASYLSAMRAQ KEVYCLNNVQ IKYDNALTKS // ID G3NHM8_GASAC Unreviewed; 245 AA. AC G3NHM8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000004837}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000004837, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000004837} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000004837} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000004851; ENSGACP00000004837; ENSGACG00000003680. DR eggNOG; ENOG410KH5C; Eukaryota. DR eggNOG; ENOG4110RMF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 245 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003448489. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 245 AA; 26961 MW; EA4FFEE9C3DC8FE8 CRC64; MSSSTFLLLL CLSSCSAADG HGYFMYADFW CNMQTARPQQ VEYLVDWYFN KEFTMQYNST VGKWTGFTAA GLVSAAVFNG NHFDVLQRKE ERRLICVDNV GHALNATEDN MAAPSVRLAE ASGSGHNTTL VCSAYDFYPR RIRLAWLRDG QEVTSGATFS EVTTNGNWTY AVHSSLSFTP GGRDRVSCKV EHAGLQEPAL RTWAAHGARD WETGFLVGGV CALLLGAACL SSGLIVHRRK YSNIS // ID G3NHN7_GASAC Unreviewed; 247 AA. AC G3NHN7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000004846}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000004846, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000004846} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000004846} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3NHN7; -. DR Ensembl; ENSGACT00000004860; ENSGACP00000004846; ENSGACG00000003680. DR eggNOG; ENOG410KH5C; Eukaryota. DR eggNOG; ENOG4110RMF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3NHN7; -. DR OMA; NITVENM; -. DR TreeFam; TF333780; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 217 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 116 203 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 247 AA; 27359 MW; 2C4839CDC826E406 CRC64; SMFTCFCETL SVSLTSFRAT DGHGYFMYAD FWCNMQTARP QQVEYLVDWY FNKEFTMQYN STVGKWTGFT AAGLVSAAVF NGNHFDVLQR KEERRLICVD NVGHALNATE DNMAAPSVRL AEASGSGHNT TLVCSAYDFY PRRIRLAWLR DGQEVTSGAT FSEVTTNGNW TYAVHSSLSF TPGGRDRVSC KVEHAGLQEP ALRTWAAHGA RDWETGFLVG GVCALLLGAA CLSSGLIVHR RKYSNIS // ID G3Q1I8_GASAC Unreviewed; 250 AA. AC G3Q1I8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000023736}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023736, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000023736} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000023736} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR STRING; 69293.ENSGACP00000023736; -. DR Ensembl; ENSGACT00000023783; ENSGACP00000023736; ENSGACG00000017967. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3Q1I8; -. DR OMA; NQEETAY; -. DR TreeFam; TF333780; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 250 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003450350. FT TRANSMEM 216 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 250 AA; 28182 MW; C03B6DD0E3A3C017 CRC64; MAPSFISVSL LFIGLHAADG FLEFMTDECV FNSTELKDIE YIRSYYYNKL ELTRFSSSVG KYVGFTEYGV RNAANWNKDA SELIAMRAQK EVYCLNSIQI KYNNVLTKSA EPYVRLHSET PPGGGPLSML VCSVYDFYPK KIIVRWTRDG RPETTGVTST DELADGDWYY QTHSHLEYTP SRSGEKISCV VEHISLSKPL VTDWNPSMPE SERNKVAIGA SGLILGLTLS LAGFIYYKRK ARGRILVPSH // ID G3Q1I9_GASAC Unreviewed; 249 AA. AC G3Q1I9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000023737}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023737, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000023737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000023737} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000023784; ENSGACP00000023737; ENSGACG00000017967. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003450362. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28095 MW; 1AEADD89D4B03D5A CRC64; MAPSFISVSL LFIGLHAADG FLEFMTDECV FNSTELKDIE YIRSYYYNKL ELTRFSSSVG KYVGFTEYGV RNAANWNKDA SELIAMRAQK EVYCLNSIQI KYNNVLTKSA EPYVRLHSET PPGGGPLSML VCSVYDFYPK KIIVRWTRDG RPETTGVTST DELADGDWYY QTHSHLEYTP RSGEKISCVV EHISLSKPLV TDWNPSMPES ERNKVAIGAS GLILGLTLSL AGFIYYKRKA RGRILVPSH // ID G3Q1J1_GASAC Unreviewed; 70 AA. AC G3Q1J1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000023739}; DE Flags: Fragment; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000023739, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000023739} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000023739} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSGACT00000023786; ENSGACP00000023739; ENSGACG00000017967. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}. FT DOMAIN 1 63 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGACP00000023739}. SQ SEQUENCE 70 AA; 8201 MW; 7AE01293A769D0FB CRC64; EYIRSYYYNK LELTRFSSSV GKYVGFTEYG VRNAANWNKD ASELIAMRAQ KEVYCLNSIQ IKYNNVLTKS // ID G3Q5N3_GASAC Unreviewed; 250 AA. AC G3Q5N3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000025189}; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000025189, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000025189} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000025189} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3Q5N3; -. DR STRING; 69293.ENSGACP00000025189; -. DR Ensembl; ENSGACT00000025238; ENSGACP00000025189; ENSGACG00000019051. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3Q5N3; -. DR OMA; YRARTEM; -. DR TreeFam; TF333780; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 250 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003450503. FT TRANSMEM 216 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 250 AA; 28034 MW; 580318B556EECEB5 CRC64; MAPSFHSVSL LFIFLHAAGG FMEFVKDQCV FNSTDLKGIE FIRSTYFNKL QYTKFSSSVG KFVGFTEQGM KNAAASNNNN MYMASIRAAK ETICQPNIQR MYDNILTKSA QPYVRLHSET PLGGRTSSML VCSVYDFYPQ NIIVRWTRDG RPEATGVSST DELADGDWYY QTHSYLEYTP SRSGEKIACV VEHISLSKPL VTDWDPSMPE SERNKIAIGG SGLILGLTLS LAGFIYYKRK GRGRILVPSY // ID G3Q5N4_GASAC Unreviewed; 70 AA. AC G3Q5N4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGACP00000025190}; DE Flags: Fragment; OS Gasterosteus aculeatus (Three-spined stickleback). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae; OC Gasterosteus. OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000025190, ECO:0000313|Proteomes:UP000007635}; RN [1] {ECO:0000313|Ensembl:ENSGACP00000025190} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.; RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGACP00000025190} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3Q5N4; -. DR Ensembl; ENSGACT00000025239; ENSGACP00000025190; ENSGACG00000019051. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007635; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007635}; KW Reference proteome {ECO:0000313|Proteomes:UP000007635}. FT DOMAIN 1 63 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSGACP00000025190}. SQ SEQUENCE 70 AA; 8000 MW; D64EF3FA78AFAB3F CRC64; EFIRSTYFNK LQYTKFSSSV GKFVGFTEQG MKNAAASNNN NMYMASIRAA KETICQPNIQ RMYDNILTKS // ID G3QEJ0_GORGO Unreviewed; 265 AA. AC G3QEJ0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGGOP00000000687}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000000687, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000000687, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000000687} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044280; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044281; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044282; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044283; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044284; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044285; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044286; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044287; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSGGOT00000000703; ENSGGOP00000000687; ENSGGOG00000000700. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000000700; Expressed in 7 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 265 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014143737. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 29680 MW; 8617F05BB152AD01 CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALAG DTRPRFLEQA KCECHILNGT ERVQYLNRYI HKREENLRFD SDVGEFQAVT ELGRPVAEKW NSQKEILEEK RDKVDTYCRY SYGVFESFTV PRVQPKVTVY PSKTQLLQHH NLLVCSVSGF YPGSIEVRWF RNGQEEKAGV VSTGLIQNGD WTFQTLVMLE TVPRSGEVYT CQVEHPSVTS PLTVEWRARS ESAQSKMLSG VGGFVLGLLF LGAGLFIYFR SQKGHSGLQP TGFLS // ID G3QNQ2_GORGO Unreviewed; 224 AA. AC G3QNQ2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 41. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 1 {ECO:0000313|Ensembl:ENSGGOP00000004173}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSGGOP00000004173}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000004173, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000004173, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000004173} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044295; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G3QNQ2; -. DR STRING; 9593.ENSGGOP00000004173; -. DR Ensembl; ENSGGOT00000004276; ENSGGOP00000004173; ENSGGOG00000004252. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3QNQ2; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000004252; Expressed in 7 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014175590. SQ SEQUENCE 224 AA; 25889 MW; D326A4ED4D29F67F CRC64; MSWKKALQIP GDLRVATVTL MLAMLSSLLA EGRDSPEDFV VQFKAMCYFT NGTERVRYVT RYIYNREESA RFDSDVGVYR AVTPQGRPDA EYWNSHKDIL ESTRAELDTV CRNNYEVAFR GILQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RLLH // ID G3R5S5_GORGO Unreviewed; 273 AA. AC G3R5S5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-SEP-2018, entry version 40. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSGGOP00000010658}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSGGOP00000010658}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000010658, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000010658, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000010658} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044299; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSGGOT00000010976; ENSGGOP00000010658; ENSGGOG00000043194. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000010941; Expressed in 6 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 273 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003451801. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 273 AA; 30873 MW; 6DCD2646B77D89DF CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSHV GMFVALTKLG QPDAEQWNSR LDLLERSREA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERAGVMS TGPIRNGDWT FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWRKMLSGIA AFLLGLIFLL VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QSC // ID G3R5T3_GORGO Unreviewed; 653 AA. AC G3R5T3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 52. DE SubName: Full=Antigen peptide transporter 2 {ECO:0000313|Ensembl:ENSGGOP00000010666}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000010666, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000010666, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000010666} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044299; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044300; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9593.ENSGGOP00000010666; -. DR Ensembl; ENSGGOT00000010984; ENSGGOP00000010666; ENSGGOG00000010941. DR GeneTree; ENSGT00550000074497; -. DR InParanoid; G3R5T3; -. DR OMA; FNQFFVG; -. DR OrthoDB; EOG091G05Q7; -. DR TreeFam; TF105197; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000010941; Expressed in 6 organ(s), highest expression level in liver. DR GO; GO:0042825; C:TAP complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042287; F:MHC protein binding; IEA:InterPro. DR GO; GO:0015440; F:peptide-transporting ATPase activity; IEA:InterPro. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro. DR GO; GO:0015833; P:peptide transport; IEA:InterPro. DR Gene3D; 1.20.1560.10; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR013305; ABC_Tap-like. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005293; Tap2/ABCB3. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR PRINTS; PR01897; TAP2PROTEIN. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR TIGRFAMs; TIGR00958; 3a01208; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT DOMAIN 153 435 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 468 653 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. SQ SEQUENCE 653 AA; 71998 MW; C2C1CE76C8FD802D CRC64; MRLPDLRPWT SLLLVDAALL WLLQGPLGTL LPQGLPGLWL EGTLRLGGLW GLLKLRGLLG FVGTLLLPLC LATPLTVSLR ALVAGASRAP PARVASAPWS WLLVGYGAAG LSWSLWAVLS PPGAQEKEQD QVNNKVLMWR LLKLSRPDLP LLVAAFFFLV LAVLGETLIP RYSGRVIDIL GGDFDPHAFA SAIFFMCLFS FGSSLSAGCR GGCFTYTMSR INLRIREQLF SSLLRQDLGF FQETKTGELN SRLSSDTTLM SNWLPLNANV LLRSLVKVVG LYGFMLSISP RLTLLSLLHM PFTIAAEKVY NTRHQAVLRE IQDAVARAGQ VVREAVGGLQ TVRSFGAEEH EVCRYKEALE QCRQLYWRRD LERALYLLVR RVLHLGVQML MLSCGLQQMQ DGELTQGSLL SFMIYQESVG SYVQTLVYIY GDMLSNVGAA EKVFSYMDRQ PNLPSPGTLA PTTLQGVVKF QDVSFAYPNR PDRPVLKGLT FTLRPGEVTA LVGPNGSGKS TVAALLQNLY QPTGGQVLLD EKPISQYEHC YLHSQVVSVG QEPVLFSGSV RNNIAYGLQS CEDDKVMAAA QAAHADDFIQ EMEHGIYTDV GEKGSQLAAG QKQRLAIARA LVRDPRVLIL DEATSALDVQ CEQAKTFWKF MIF // ID G3RCR2_GORGO Unreviewed; 258 AA. AC G3RCR2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-SEP-2018, entry version 46. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSGGOP00000013296}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSGGOP00000013296}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000013296, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000013296, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000013296} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044310; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_004043842.1; XM_004043794.2. DR STRING; 9593.ENSGGOP00000013296; -. DR Ensembl; ENSGGOT00000013677; ENSGGOP00000013296; ENSGGOG00000013630. DR GeneID; 101141025; -. DR KEGG; ggo:101141025; -. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3RCR2; -. DR KO; K06752; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000013630; Expressed in 7 organ(s), highest expression level in heart. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003452516. FT TRANSMEM 227 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29443 MW; 6D4C3516372BC94B CRC64; MMVLQVSAAP RTVALMALLM VLLTSVVQGR ATPENYLYQV RQECYAFNGT QRFLERYIYN REEWVRFDSD VGEFRAVTEM GRPDAEYWNS QKDLLEEKRA VPDRICRHNY ELDEAVTLQR RVQPRVNVSP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYIC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID G3RPG3_GORGO Unreviewed; 261 AA. AC G3RPG3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-SEP-2018, entry version 43. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 1 {ECO:0000313|Ensembl:ENSGGOP00000017683}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSGGOP00000017683}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000017683, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000017683, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000017683} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044295; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_004043821.1; XM_004043773.2. DR Ensembl; ENSGGOT00000033362; ENSGGOP00000017683; ENSGGOG00000004252. DR GeneID; 101133052; -. DR KEGG; ggo:101133052; -. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000004252; Expressed in 7 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003452955. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29719 MW; 7FE288E35A4DCB60 CRC64; MSWKKALQIP GDLRVATVTL MLAMLSSLLA EGRDSPEDFV VQFKAMCYFT NGTERVRYVT RYIYNREESA RFDSDVGVYR AVTPQGRPDA EYWNSHKDIL ESTRAELDTV CRNNYEVAFR GILQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI IRQRSQKGLL H // ID G3RQJ2_GORGO Unreviewed; 263 AA. AC G3RQJ2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 47. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGGOP00000018065}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000018065, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000018065, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000018065} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044306; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_004043840.1; XM_004043792.2. DR ProteinModelPortal; G3RQJ2; -. DR STRING; 9593.ENSGGOP00000018065; -. DR Ensembl; ENSGGOT00000031725; ENSGGOP00000018065; ENSGGOG00000022404. DR GeneID; 101140024; -. DR KEGG; ggo:101140024; -. DR CTD; 101140024; -. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3RQJ2; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000022404; Expressed in 7 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014136933. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28943 MW; 74AAF6D62965740A CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN SLANVLSQHL NQQDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPAEVTITWR KNGKLVMPHS SAHKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGVISW RRAGHSSYTP LPGSNYSEGW HIS // ID G3S117_GORGO Unreviewed; 266 AA. AC G3S117; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 33. DE SubName: Full=Major histocompatibility complex, class II, DR beta 5 {ECO:0000313|Ensembl:ENSGGOP00000021762}; GN Name=HLA-DRB5 {ECO:0000313|Ensembl:ENSGGOP00000021762}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000021762, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000021762, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000021762} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044256; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044257; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044258; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044259; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044260; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044261; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CABD030044262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_018884633.1; XM_019029088.1. DR ProteinModelPortal; G3S117; -. DR Ensembl; ENSGGOT00000031952; ENSGGOP00000021762; ENSGGOG00000037929. DR GeneID; 101131235; -. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000000700; Expressed in 7 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014153537. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30034 MW; 42C908D581333558 CRC64; MVCLKLPGGS YMAVLTVTLM VLSSPLALAG DTRPRFLKQD KYECHFFNGT ERVRYLHRDI YNQEEDLRFD SDVGEYRAVT ELGRPDAEYW NSQKDVLEDE RASVDTYCRH NYGVVESFTV QRRVEPKVTV YPARTQTLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQILVML ETVPQSGEVY TCQVEHPSVT IPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF KNQKGHSGLH PTGLVS // ID G3S846_GORGO Unreviewed; 227 AA. AC G3S846; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 32. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 2 {ECO:0000313|Ensembl:ENSGGOP00000024258}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSGGOP00000024258}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000024258, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000024258, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000024258} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044298; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSGGOT00000026929; ENSGGOP00000024258; ENSGGOG00000014413. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000014413; Expressed in 7 organ(s), highest expression level in heart. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 227 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014171578. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 227 AA; 26040 MW; B0380F61B1B6371F CRC64; MALQIPGGFW AAAVTVMLVM LSTPVAEARD FPKDFLVQFK GMCYFTNGTE RVRGVARYIY NREEYGRFDS DVGEFQAVTE LGRSIEDWNN YKDFLEQERA AVDKVCRHNY EAELRTTLQR QVEPTVTISP SRTEALNHHN LLVCSVTDFY PAQIKVRWFR NDQEETAGVV STSLIRNGDW TFQILVMLEI TPQRGDIYTC HVEHPSLQSP ITVEWRPRGP PPAGLLH // ID G3SJ91_GORGO Unreviewed; 264 AA. AC G3SJ91; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-SEP-2018, entry version 43. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 2 {ECO:0000313|Ensembl:ENSGGOP00000028181}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSGGOP00000028181}; OS Gorilla gorilla gorilla (Western lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000028181, ECO:0000313|Proteomes:UP000001519}; RN [1] {ECO:0000313|Ensembl:ENSGGOP00000028181, ECO:0000313|Proteomes:UP000001519} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Scally A.; RT "Insights into the evolution of the great apes provided by the gorilla RT genome."; RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSGGOP00000028181} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CABD030044298; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9593.ENSGGOP00000028181; -. DR Ensembl; ENSGGOT00000029552; ENSGGOP00000028181; ENSGGOG00000014413. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3SJ91; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001519; Chromosome 6. DR Bgee; ENSGGOG00000014413; Expressed in 7 organ(s), highest expression level in heart. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001519}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001519}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003454132. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29849 MW; 31D9BC286239D543 CRC64; MALQIPGGFW AAAVTVMLVM LSTPVAEARD FPKDFLVQFK GMCYFTNGTE RVRGVARYIY NREEYGRFDS DVGEFQAVTE LGRSIEDWNN YKDFLEQERA AVDKVCRHNY EAELRTTLQR QVEPTVTISP SRTEALNHHN LLVCSVTDFY PAQIKVRWFR NDQEETAGVV STSLIRNGDW TFQILVMLEI TPQRGDIYTC HVEHPSLQSP ITVEWRAQSE SAQSKMLSGV GGFVLGLIFL GLGLIIRHRG QKGPRGPPPA GLLH // ID G3SND0_LOXAF Unreviewed; 225 AA. AC G3SND0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000001107}; DE Flags: Fragment; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000001107, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000001107} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000001107}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000001107} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3SND0; -. DR Ensembl; ENSLAFT00000001315; ENSLAFP00000001107; ENSLAFG00000001315. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3SND0; -. DR OMA; SYRVMES; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 187 209 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 85 173 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSLAFP00000001107}. SQ SEQUENCE 225 AA; 25715 MW; 1C394C3A8B0F4876 CRC64; FLEQAKSECH FTNQKKQVRF EQRFVYNQEE YVRFDSDVWE FEAVTALGQP DVQYWNSQKE ILNNRFCRQS YRVMESLTVQ QRVEPVVTVY LAKTQPLQHH SLLVCSVNGF YPGHIEVRWF RNGQEEEAGV ASTGLIQNGD WTFQILVMLE TTPQSGEVYS CQVEHPRLTS PVTVEWKAQS GSVQSKMLNG IGGLVLGLLF LGVGLFIHFR NQKGHCGLQP TGNAL // ID G3SSP8_LOXAF Unreviewed; 234 AA. AC G3SSP8; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000002996}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000002996, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000002996} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000002996}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000002996} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3SSP8; -. DR STRING; 9785.ENSLAFP00000002996; -. DR Ensembl; ENSLAFT00000003590; ENSLAFP00000002996; ENSLAFG00000003591. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3SSP8; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 215 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 94 182 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 234 AA; 26396 MW; C9D796263872F627 CRC64; MFPVPTARFL YQFKPDCQFT NGTERVRFVE RHLYNREEFL RFDSDVGEYR AVTELGRPDA EIWNSQKETL DYKRGADTTT GVDESFTVQR RVEPVVTVYL AKTQPLQHHN LLVCSVNGFY PGNIEVRWFR NGQEEEAGVV STGLIQNGDW TFQILVMLET IPQSGEVYTC QVEHPSLTSP VTVEWRAQSG SAQSKMLSGI GGLVLGLLFL GAGLFTHFRN QKARSGLQPT GLLS // ID G3STJ3_LOXAF Unreviewed; 253 AA. AC G3STJ3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 41. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSLAFP00000003382}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSLAFP00000003382}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000003382}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000003382} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003382}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000003382} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003382}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3STJ3; -. DR STRING; 9785.ENSLAFP00000003382; -. DR Ensembl; ENSLAFT00000004052; ENSLAFP00000003382; ENSLAFG00000004052. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3STJ3; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 253 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003454428. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 253 AA; 28749 MW; 460DCCCA60288A16 CRC64; LSFLWPSLDL QGIILLVILL DSSVTEGRDF PEDFVVQAKA DCYFTNGTEK VQFVVRFIFN LEEYARFDSD VGMFVALTEL GKPDAERWNN RTDILERSRA SVDALCRYNY KLGASFTVGR KVQPEVTVYP ERTPSLQHPN LLLCSVTNFY PGDIKVKWFR NGQEERAGVM STGLIRNGDW TFQTMVMLEI TPELGDVYTC LVYHPSLLSP VSVEWRAQSE YSWRKVLSGV GALLFGIIFL LVGIVIHFRG QKG // ID G3SUJ1_LOXAF Unreviewed; 266 AA. AC G3SUJ1; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000003829}; GN Name=LOC100665293 {ECO:0000313|Ensembl:ENSLAFP00000003829}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000003829, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000003829} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003829}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000003829} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000003829}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR RefSeq; XP_003423509.2; XM_003423461.2. DR ProteinModelPortal; G3SUJ1; -. DR STRING; 9785.ENSLAFP00000003829; -. DR Ensembl; ENSLAFT00000004587; ENSLAFP00000003829; ENSLAFG00000026868. DR GeneID; 100665293; -. DR KEGG; lav:100665293; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3SUJ1; -. DR KO; K06752; -. DR OMA; GQVDNYC; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003454266. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 230 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30219 MW; 77016F523683CAAF CRC64; MVCLWFPRGT WMAALTLILM MLSPPLALSR DTRPRFQWHG KSECHFTNGT ERVRFVERYI YNREEYARFD SDVGEYRAVT ELGRPSAEYW NGQKELLDEK RGQVDNYCRH NYGVGESFTV QRRVEPAVTV YLAKTQPLQH HNLLVCSVNG FYPGHIEVRW FRNGQEEEAG VVSTGLIQNG DWTFQILMML ETIPQSGEVY TCQVEHPSLM SPVTVEWRAQ SGSAQSKMLS GIGGLVLGLL FLGAGLFIHF RNQKAPSGLQ PTGLLS // ID G3TN16_LOXAF Unreviewed; 264 AA. AC G3TN16; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000016567}; GN Name=LOC100669075 {ECO:0000313|Ensembl:ENSLAFP00000016567}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000016567, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000016567} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000016567}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000016567} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000016567}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3TN16; -. DR STRING; 9785.ENSLAFP00000016567; -. DR Ensembl; ENSLAFT00000023012; ENSLAFP00000016567; ENSLAFG00000022970. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3TN16; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003455648. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 228 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 30216 MW; EA5A1201E586682C CRC64; MALHTPRDLW TAAVMVMLML STQMTEGRDS PEDFVAQEKF LCYFTNGTER VRLVERYIYN REEIVRFDSD VGEHVALTPL GRPDAEYWNS QKDILEEKRA YVDTLCRHNY RIEESFTVQR RELAPEVTIS PARTETINHH NAVCTVTDFY PGQVKVRWFR NDQEETAGIV FTPLIRNGDW TFQILVMLEM TPQRGDVYTC HVEHPSLQSP IVVEWRAQSE SAQSKMLSGV GGFVLGLAFL GLGLIIHHRS QKGLRGSPPT GNKS // ID G3TNR9_LOXAF Unreviewed; 264 AA. AC G3TNR9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 20-JUN-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000016940}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000016940, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000016940} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000016940}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000016940} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000016940}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3TNR9; -. DR STRING; 9785.ENSLAFP00000016940; -. DR Ensembl; ENSLAFT00000023042; ENSLAFP00000016940; ENSLAFG00000031139. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3TNR9; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003455683. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29983 MW; 6AF490734BE0B9B1 CRC64; CLWFPRGTWM AALTLILMVL SPPLALSRDT RSHFQSQIKA QCDFTNGTER VRFVQRYIYN REEYVRFDSD VGEFVVVTEL GRPDAEYWNG QKELLDDRRG EVDRFCRHNY GVFESFSVQR RVEPMVTVYL AKTQPLQHHN LLVCSVNGFY PGNIEVRWFR NGQEEEAGVV STGLIQNGDW TFQILVMLET IPQSGEVYTC QVEHPSLTSP VTVEWRAQSG SAQSKMLSGI GGLVLGLLFL GAGLFIHFRN QKARSGLQPT GNAL // ID G3TQC0_LOXAF Unreviewed; 255 AA. AC G3TQC0; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000017730}; GN Name=LOC100669075 {ECO:0000313|Ensembl:ENSLAFP00000017730}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000017730, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000017730} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017730}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000017730} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000017730}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSLAFT00000021644; ENSLAFP00000017730; ENSLAFG00000022970. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 255 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003455655. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 228 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 255 AA; 29405 MW; 400A69287C666380 CRC64; KMALHTPRDL WTAAVMVMLM LSTQMTEGRD SPEDFVAQEK FLCYFTNGTE RVRLVERYIY NREEIVRFDS DVGEHVALTP LGRPDAEYWN SQKDILEEKR AYVDTLCRHN YRIEESFTVQ RRVAPEVTIS PARTETINHH NLVCTVTDFY PGQVKVRWFR NDQEETAGIV FTPLIRNGDW TFQILVMLEM TPQRGDVYTC HVEHPSLQSP IVVEWRAQSE SAQSKMLSGV GGFVLGLAFL GLGLIIHHRS QKGKE // ID G3UCY9_LOXAF Unreviewed; 266 AA. AC G3UCY9; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000025697}; GN Name=LOC100665293 {ECO:0000313|Ensembl:ENSLAFP00000025697}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000025697, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000025697} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000025697}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000025697} RP IDENTIFICATION. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000025697}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR Ensembl; ENSLAFT00000031061; ENSLAFP00000025697; ENSLAFG00000026868. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003456321. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 230 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30312 MW; 770161B0E683CAAF CRC64; MVCLWFPRGT WMAALTLILM MLSPPLALSR DTRPRFQWHG KSECHFTNGT ERVRFVERYI YNREEYARFD SDVGEYRAVT ELGRPSAEYW NGQKELLDEK RGQVDNYCRH NYGVGESFTV QRRVEPAVTV YLAKTQPLQH HNLLVCSVNG FYPGHIEVRW FRNGQEEEAG VVSTGLIQNG DWTFQILMML ETIPQSGEVY TCQVEHPSLM SPVTVEWRAQ SGSAQSKMLS GIGGLVLGLL FLGAGLFIHF RNQKAPSGLQ PTDFLS // ID G3UG94_LOXAF Unreviewed; 206 AA. AC G3UG94; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000026852}; DE Flags: Fragment; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000026852, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000026852} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000026852}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000026852} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3UG94; -. DR STRING; 9785.ENSLAFP00000026852; -. DR Ensembl; ENSLAFT00000034237; ENSLAFP00000026852; ENSLAFG00000029575. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3UG94; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 90 178 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSLAFP00000026852}. SQ SEQUENCE 206 AA; 23409 MW; 4810D9560FA3938A CRC64; CTRGGATAMS FNSTQRFLER YIYNEEEYIQ LDSNVGVFKA MTELDQTTAK NWNIQKEFLE LRRQAVDVVC KHKDELDKGF TLKSRVQVLP KVNVFPSNTG SLQHHNLLVC HVTDFYPGSI EIRWFRNGQE ETAGIVTADL IRNGDWTFRI LVMLEMTPQK GDVYTCHVEH PSLDSPVTVE WEEAQSDSAQ SKMLTGVGGF ALGLIF // ID G3UMT2_LOXAF Unreviewed; 260 AA. AC G3UMT2; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLAFP00000029141}; OS Loxodonta africana (African elephant). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta. OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000029141, ECO:0000313|Proteomes:UP000007646}; RN [1] {ECO:0000313|Ensembl:ENSLAFP00000029141} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000029141}; RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The Genome Sequence of Loxodonta africana (African elephant)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLAFP00000029141} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; G3UMT2; -. DR Ensembl; ENSLAFT00000026695; ENSLAFP00000029141; ENSLAFG00000018482. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3UMT2; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG09070C67; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007646; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000007646}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000007646}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 260 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003456835. FT TRANSMEM 219 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 118 221 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 260 AA; 28789 MW; 75534C6261D4FC28 CRC64; MALQIPRGLW TAGVMVMLTL LCTLKAEGRD SPQDFVVQSK AMCYFTNRME RLLVGRSIYN REEIVRFDSD VGNRGAHALG RPDAEYGNSQ KDLWSGVGLC GRAEQTQLPD RMCKIVAPEV TISPAKTETV NHHNLLVFSV TDFYPGQVNV RWFRNDQEET AGIMYTFIRN GDWTFQILVM LEMTPQSGDV YTCHVESPSL QSPIVVEWRA QSESAQSRML SGVGGFVLGL VFLGLGPSIT GARKLSFVGP HGPLLTGNKS // ID G3UY15_MOUSE Unreviewed; 205 AA. AC G3UY15; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 12-SEP-2018, entry version 49. DE SubName: Full=Histocompatibility 2, O region beta locus {ECO:0000313|Ensembl:ENSMUSP00000133906}; GN Name=H2-Ob {ECO:0000313|Ensembl:ENSMUSP00000133906, GN ECO:0000313|MGI:MGI:95925}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000133906, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000133906, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000133906, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000133906} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000133906}; RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR974422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G3UY15; -. DR SMR; G3UY15; -. DR MaxQB; G3UY15; -. DR PRIDE; G3UY15; -. DR Ensembl; ENSMUST00000173764; ENSMUSP00000133906; ENSMUSG00000041538. DR UCSC; uc012apw.1; mouse. DR MGI; MGI:95925; H2-Ob. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000041538; Expressed in 74 organ(s), highest expression level in lymph node. DR ExpressionAtlas; G3UY15; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0005764; C:lysosome; ISO:MGI. DR GO; GO:0042613; C:MHC class II protein complex; ISO:MGI. DR GO; GO:0023026; F:MHC class II protein complex binding; ISO:MGI. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; ISO:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 176 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 52 142 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 205 AA; 22865 MW; 800C6657B9DDD5EE CRC64; MFVALTELGE PDADQWNKRL DLLETSRAAV NMVCRQKYKL GAPFTVERNV PPEVTVYPER TPLLQQHNLL LCSVTGFYPG DISVKWFRNG QEERSGVMST GLVRNGDWTF QTTVMLEMIP ELGDIYSCLV EHPGLLRPVS VAWMAQSEYS WKKILSGAAV FLLGLIVFLV GVVIHLKAQK GKPHLILTGD PVFSLSSICG DSAWQ // ID G3VGC7_SARHA Unreviewed; 235 AA. AC G3VGC7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 20-JUN-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000002231}; GN Name=LOC100917964 {ECO:0000313|Ensembl:ENSSHAP00000002231}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000002231}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000002231} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000002231} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEFK01180389; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01180390; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01180391; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01180392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003770438.1; XM_003770390.2. DR ProteinModelPortal; G3VGC7; -. DR STRING; 9305.ENSSHAP00000002231; -. DR Ensembl; ENSSHAT00000002255; ENSSHAP00000002231; ENSSHAG00000001984. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3VGC7; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 235 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003457256. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 235 AA; 26947 MW; B04990795B57C8E5 CRC64; MVCVLLFKGI WTEVLAVTLL VLNPQVAAGR NTPKHFTKQS KCECYFVNGM EHVQYVERHM YNQKEYVHFD SNVGKYAAVM ELGRPEAEYW NNHKEILDDL RARVDTLCRH NYQVIEPFLL PRSVEPEVIV YPSKIAPLGH HNLLVCSVSG FYPGDIEVRW FLNGQEEMTG VVSTGLISNG DWTYQLQVIL EMIPKSGDVY TCQVEHSSLQ RPIILDWSET ELPHPPVLTL LRTCS // ID G3VGF7_SARHA Unreviewed; 228 AA. AC G3VGF7; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000002261}; DE Flags: Fragment; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000002261, ECO:0000313|Proteomes:UP000007648}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000002261} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000002261} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEFK01184033; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEFK01184034; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G3VGF7; -. DR STRING; 9305.ENSSHAP00000002261; -. DR Ensembl; ENSSHAT00000002285; ENSSHAP00000002261; ENSSHAG00000002008. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3VGF7; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 214 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 92 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSSHAP00000002261}. SQ SEQUENCE 228 AA; 25572 MW; 633979C0CBD424B2 CRC64; HFTLQFKAEC YFENGTEHVR HVHRAIYNRQ EYARFDSDLG KFVAVTELGR GIAEHWNSQK EILENVRAEV DTVCIYNYKS YNSLSMHMHA HPKVTVYPSK MAPPGHHNLL VCSVSGFYPG DIKVQWFLNG REETAGVVST GLIGNGDWTY QTLVMLEMTH RRGDVYTCQV EHSSLQGPVH LDWKAQSESA QSKMLSGVGG LVLGLIFLGV GLIVHKRSQK GNQGSQPA // ID G3VM66_SARHA Unreviewed; 268 AA. AC G3VM66; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 18-JUL-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000004271}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000004271}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000004271} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000004271} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEFK01181403; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G3VM66; -. DR STRING; 9305.ENSSHAP00000004271; -. DR Ensembl; ENSSHAT00000004314; ENSSHAP00000004271; ENSSHAG00000003762. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3VM66; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 268 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003457728. FT TRANSMEM 223 244 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 120 209 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 268 AA; 29606 MW; 80875864601E17CE CRC64; YLKQRMKLLH LLLVGFSLGF SGAGAFVTHV ESDCVLDEDG SVKDFTYCIS FNKNVLTCWD SKIKKMVTVD YGLLQPFAEY LSQSLNNNSA LIYHLSNGLQ DCASHTKPFW GSLTQRTRSP SVQIAQTTPF NTREQVMLAC YVWGFYPADV AISWLKNGQP IPNSGIQRAV QSNGDWTYQT RSYLALTPSS GDIYTCHVEH SGSSQAILQT WTSGLSLKQT VKISVSVLTL GLGLIFFFLG LVFCQKAGSS DYTPLSGSNY PEGNSHFC // ID G3VR65_SARHA Unreviewed; 259 AA. AC G3VR65; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 20-JUN-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000005670}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000005670}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000005670} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000005670} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEFK01180400; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; G3VR65; -. DR STRING; 9305.ENSSHAP00000005670; -. DR Ensembl; ENSSHAT00000005724; ENSSHAP00000005670; ENSSHAG00000004955. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3VR65; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 259 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003457902. FT TRANSMEM 221 243 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 119 223 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT COILED 84 104 {ECO:0000256|SAM:Coils}. SQ SEQUENCE 259 AA; 29188 MW; 8A77EE718F07B6EF CRC64; MLIVGAKVLI LTLLMMNFLE ATVRDSEDNF MEQTKAECHF VNGTEHVQFV GRLIYNREEI LRFDSEVGKF VALTELGRPI EELMNSQLEA LEQARAQVAM CRNNYILWES LWNRRRVEPE VTVYSSKITP LGYPNQLICF ITGFYPGDIE VRWFLNGQEK TAGVLSTGLI NNGDWTFQTL VMLEMIPKPG DVYTCQVEHS SLQNPVIGVW EAQYGSAQKK MLSGVGGLVL GLIFLGVGLA VYLKSQKGNQ GQQPIDNFL // ID G3VYR3_SARHA Unreviewed; 95 AA. AC G3VYR3; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000008318}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000008318}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000008318} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000008318} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEFK01166408; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9305.ENSSHAP00000008318; -. DR Ensembl; ENSSHAT00000008386; ENSSHAP00000008318; ENSSHAG00000007210. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; G3VYR3; -. DR OMA; WRDECHY; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}. FT DOMAIN 13 87 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 95 AA; 11342 MW; A9F5A409157739C5 CRC64; GVPAEHFTWQ GKSECHFENG TEHVRFVERH FYNRQEFMRF DSDVGKYEAV TELGRRIAEH WNSQKEILER ARTAVDIVCR HNYGISESFL VRRRG // ID G3VYR4_SARHA Unreviewed; 77 AA. AC G3VYR4; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000008319}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000008319}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000008319} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000008319} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEFK01166408; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSSHAT00000008387; ENSSHAP00000008319; ENSSHAG00000007210. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}. FT DOMAIN 5 77 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 77 AA; 9314 MW; C7AF5B5C10948A12 CRC64; WQGKSECHFE NGTEHVRFVE RHFYNRQEFM RFDSDVGKYE AVTELGRRIA EHWNSQKEIL ERARTAVDIV CRHNYGI // ID G3VYR5_SARHA Unreviewed; 76 AA. AC G3VYR5; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 28-MAR-2018, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSHAP00000008320}; OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus. OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000008320}; RN [1] {ECO:0000313|Ensembl:ENSSHAP00000008320} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21709235; DOI=10.1073/pnas.1102838108; RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., RA Miller J., Walenz B., Knight J., Qi J., Zhao F., Wang Q., RA Bedoya-Reina O.C., Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., RA Woodbridge P., Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., RA Helgen K.M., Lesk A.M., Pringle T.H., Patterson N., Zhang Y., RA Kreiss A., Woods G.M., Jones M.E., Schuster S.C.; RT "Genetic diversity and population structure of the endangered RT marsupial Sarcophilus harrisii (Tasmanian devil)."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011). RN [2] {ECO:0000313|Ensembl:ENSSHAP00000008320} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEFK01166408; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSSHAT00000008388; ENSSHAP00000008320; ENSSHAG00000007210. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000007648; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007648}; KW Reference proteome {ECO:0000313|Proteomes:UP000007648}. FT DOMAIN 4 76 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 76 AA; 9128 MW; 12940B5C531C4151 CRC64; QGKSECHFEN GTEHVRFVER HFYNRQEFMR FDSDVGKYEA VTELGRRIAE HWNSQKEILE RARTAVDIVC RHNYGI // ID G5BB06_HETGA Unreviewed; 300 AA. AC G5BB06; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 20-JUN-2018, entry version 30. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:EHB06471.1}; GN ORFNames=GW7_20366 {ECO:0000313|EMBL:EHB06471.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB06471.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB06471.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH169323; EHB06471.1; -; Genomic_DNA. DR ProteinModelPortal; G5BB06; -. DR InParanoid; G5BB06; -. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 300 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003474167. FT DOMAIN 114 204 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 300 AA; 32558 MW; A135DCE45A6AAF11 CRC64; MSTLLPLLLG LSLACTGAGG FMAHVESTCL LDDNGIPKDF AYCIAYNKDL LTCWDPEEDR MAPCEFGTLH MLAVSLSNYL NNNTNLLQRL RNGLQDCATH TQPFWESLTH RRKPPSVQVA QTTPFNTREP VMLACYVWGF YPADVTINWM KNGLLVTPHS SAQKTAQPNG DWTYQTISRL ALTPSYGDVY TCVAEHVGAS EPIRQDWTPG LSPVQTVKVS VSAVTLGLGI IVFSIGVISW RKAGSSSYTS LPGSIYPEGN SSVALFAPGP SERMSRKSQG WVQLVVPRVG GAAVGSSELI // ID G5BB10_HETGA Unreviewed; 607 AA. AC G5BB10; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 25-OCT-2017, entry version 34. DE SubName: Full=Antigen peptide transporter 2 {ECO:0000313|EMBL:EHB06475.1}; DE Flags: Fragment; GN ORFNames=GW7_20370 {ECO:0000313|EMBL:EHB06475.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB06475.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB06475.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH169323; EHB06475.1; -; Genomic_DNA. DR InParanoid; G5BB10; -. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042825; C:TAP complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042287; F:MHC protein binding; IEA:InterPro. DR GO; GO:0015440; F:peptide-transporting ATPase activity; IEA:InterPro. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 1.20.1560.10; -; 1. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005293; Tap2/ABCB3. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR PRINTS; PR01897; TAP2PROTEIN. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 29 54 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 106 124 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 205 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 307 550 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 569 607 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NP_BIND 342 349 ATP. {ECO:0000256|PROSITE- FT ProRule:PRU00434}. FT NON_TER 1 1 {ECO:0000313|EMBL:EHB06475.1}. FT NON_TER 607 607 {ECO:0000313|EMBL:EHB06475.1}. SQ SEQUENCE 607 AA; 67652 MW; 1EEAB202C72283B5 CRC64; GEMLIPHYSG RVIDILGADF DPDAFASAVF LMCLFSVGSS LSGGFRGGFF TLIMSRINLR IREKLFSSLL RQDLGFFQET KTGELHSRLS SDTTLMSFWL PLNANIILRS LVKVVGLYGF MFTISPRLTL LSLLDLPVML TADKVYTTRR QALLLEIQDA VAKAGQVVRE AVGGLQTVRS FGAEELEVWR YKEALERCRQ LWWRRDLEKG LYDLVRKEEM ERLKGGKVLV LSCGLQQIAA GEITRGALLS FLLYRKDVGP YVHSLVYRYG DMLSNVGAAE KVFSYLDREP RLPQPGTLAP AAIRGLMEFR DVSFAYPSRP DQPVLQGLTF TLRPGEVTAL VGPNGSGKST VATLLQNLYQ PTKGQVLLDE NPVSEYEHHY LHRQVSVVGQ EPVLFSGSVR DNITYGLQSC EDAKVVAAAQ EALAYRFIEE LPDGMHTDVG EKGSQLAVGQ KQCLAVARAL VRDPRVLILD EATSGLDVCC EQANGFWLGE LHAGSTSKSD QAGVLHNRRQ RLSSDVGMFV ALTELGKPDA EHWNNRPDIL ETSRASVDMV CRHNYRLGAP FTLGRRVQPE VTVYPERTPF LQQHNLLLCS VTGFYPGDIK IRWFRNG // ID G5C3J0_HETGA Unreviewed; 206 AA. AC G5C3J0; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 25-OCT-2017, entry version 27. DE SubName: Full=HLA class II histocompatibility antigen, DRB1-15 beta chain {ECO:0000313|EMBL:EHB16101.1}; DE Flags: Fragment; GN ORFNames=GW7_04820 {ECO:0000313|EMBL:EHB16101.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB16101.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB16101.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH173151; EHB16101.1; -; Genomic_DNA. DR ProteinModelPortal; G5C3J0; -. DR InParanoid; G5C3J0; -. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 124 206 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:EHB16101.1}. SQ SEQUENCE 206 AA; 23392 MW; B966612E151BFB86 CRC64; MAYLWLPRGS GVTALTVTLM VLSPPVTLVR DTRRRFLGQM KGECRYVNGT QQVRFLNRYI YNQEVFVRFD SEVGKFQAVT ELGRPIAEDL NSQKDVLDNY RAGVDRCRNN YDLVRLLSGR SVAPSMTVYP TKTQPLQHHN LLVCSVSGFY PGHIEVRWFR NGQEEEAGVV STGLIQNGDW TFQTLVMLET VPQSGEVYAC QVEHPS // ID G5C3J2_HETGA Unreviewed; 228 AA. AC G5C3J2; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 25-OCT-2017, entry version 28. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EHB16103.1}; DE Flags: Fragment; GN ORFNames=GW7_04822 {ECO:0000313|EMBL:EHB16103.1}; OS Heterocephalus glaber (Naked mole rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Bathyergidae; Heterocephalus. OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB16103.1, ECO:0000313|Proteomes:UP000006813}; RN [1] {ECO:0000313|EMBL:EHB16103.1, ECO:0000313|Proteomes:UP000006813} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993625; DOI=10.1038/nature10533; RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L., RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X., RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A., RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., RA Bronson R.T., Buffenstein R., Wang B., Han C., Li Q., Chen L., RA Zhao W., Sunyaev S.R., Park T.J., Zhang G., Wang J., Gladyshev V.N.; RT "Genome sequencing reveals insights into physiology and longevity of RT the naked mole rat."; RL Nature 479:223-227(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH173151; EHB16103.1; -; Genomic_DNA. DR ProteinModelPortal; G5C3J2; -. DR InParanoid; G5C3J2; -. DR Proteomes; UP000006813; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000006813}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000006813}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 191 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 89 193 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:EHB16103.1}. FT NON_TER 228 228 {ECO:0000313|EMBL:EHB16103.1}. SQ SEQUENCE 228 AA; 26173 MW; B2477DA18A95F8D2 CRC64; YVFQARQDCY ARNWTQRFVE RYIYNREEFA RFDSEVGEYR AVTELGRRSA EYWNSQKEIL ERTRAELDTY CRHNYGVAES FTVQRRVVPK VTLYPTKTQP LQHHNLLVCS VSGFYPGHIE VRWFRNGQEE EAGVVSTGLI QNGDWTFQTL VMLETVPQSG EVYACQVEHP SWSSPVTVEW RAQSASARSK MLSGVGGFVL GLLFLGTGLF IYLRNQKGHS GVQPTGNV // ID G7P2R4_MACFA Unreviewed; 266 AA. AC G7P2R4; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 25-OCT-2017, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHH52935.1}; DE Flags: Fragment; GN ORFNames=EGM_13475 {ECO:0000313|EMBL:EHH52935.1}; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH52935.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH52935.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CM001279; EHH52935.1; -; Genomic_DNA. DR ProteinModelPortal; G7P2R4; -. DR Proteomes; UP000009130; Chromosome 4. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003501619. FT TRANSMEM 232 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 130 218 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 266 266 {ECO:0000313|EMBL:EHH52935.1}. SQ SEQUENCE 266 AA; 30068 MW; 2569458A2385B6E0 CRC64; MPWKKALRIP GGLRVATVTL MLAMLSTPVT EGRDSPEDFV VQFKAMCYFT NGTERVHYVT RYIYNREEFA RFDSDVWEYR AVTPLGRXXX XXXXXXXXXX EGPFLMADVL CDLTSYSYVF SCLLLPSVEP TVTISPSRTE ALNHHNLLVC SVTDFYPGQI KVRWFRNDQE ETTGVVSTPL IRNGDWTFQI LVMLEMTPQR GDVYTCHVEH PSLQRPITVE WRAQSESAQS KMLSGVGGFV LGLIFLGLGL IIHYRSHKGP QGPPPA // ID G7P2R5_MACFA Unreviewed; 259 AA. AC G7P2R5; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHH52936.1}; DE Flags: Fragment; GN ORFNames=EGM_13476 {ECO:0000313|EMBL:EHH52936.1}; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH52936.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH52936.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CM001279; EHH52936.1; -; Genomic_DNA. DR Proteomes; UP000009130; Chromosome 4. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 259 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003501934. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 259 259 {ECO:0000313|EMBL:EHH52936.1}. SQ SEQUENCE 259 AA; 28509 MW; 44271976D2CC9701 CRC64; MIIFLPLLLG LSLGCTRAGG FVAHVESTCL LDDDGTAKDF TYCISFNKDL LTCWDPEENK MVPCEFGVLN PLANGISHYL NQQDTLMQRL RNGLQNCTTH TQPFWGSLTH RTRPPSVQVA QTTPFNTREP VMLACYVWGF YPADVTITWM KNGNLVIPHG SGQKTAQPNG DWTYQTLSYL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGLISW RRAGSSSYTP LPGSNYPEG // ID G7P2R9_MACFA Unreviewed; 84 AA. AC G7P2R9; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 30-AUG-2017, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHH52940.1}; DE Flags: Fragment; GN ORFNames=EGM_13482 {ECO:0000313|EMBL:EHH52940.1}; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH52940.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH52940.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CM001279; EHH52940.1; -; Genomic_DNA. DR Proteomes; UP000009130; Chromosome 4. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}. FT DOMAIN 4 76 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:EHH52940.1}. FT NON_TER 84 84 {ECO:0000313|EMBL:EHH52940.1}. SQ SEQUENCE 84 AA; 10097 MW; 2822AC04E61508C6 CRC64; QERQECYAFN GTQRFVDGLI YNREDYVHFD SAVGEFLAVM ELGRPTGEYL NSQKDFMERK RAEVDKMCRH KYELMEPLLR QRRG // ID G8F5I2_MACFA Unreviewed; 273 AA. AC G8F5I2; DT 25-JAN-2012, integrated into UniProtKB/TrEMBL. DT 25-JAN-2012, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EHH62546.1}; GN ORFNames=EGM_20928 {ECO:0000313|EMBL:EHH62546.1}; OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Macaca. OX NCBI_TaxID=9541 {ECO:0000313|Proteomes:UP000009130}; RN [1] {ECO:0000313|EMBL:EHH62546.1, ECO:0000313|Proteomes:UP000009130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH62546.1}; RX PubMed=22002653; DOI=10.1038/nbt.1992; RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., RA Li Q., Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., RA Huang Z., Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., RA Huang Y., Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., RA Li B., Liu X., Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., RA Li Y., Wang W., Katze M.G., Su B., Nielsen R., Yang H., Wang J., RA Wang X., Wang J.; RT "Genome sequencing and comparison of two nonhuman primate animal RT models, the cynomolgus and Chinese rhesus macaques."; RL Nat. Biotechnol. 29:1019-1023(2011). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JH331756; EHH62546.1; -; Genomic_DNA. DR Proteomes; UP000009130; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000009130}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009130}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 273 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003509754. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 273 AA; 30851 MW; 1C5D60BC1B4DA282 CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSREA VDGVCRHNYR LGAPFTVERK VQPEVTVFPE RTALLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERAGVMS TGLIGNGDWT FQTVVMLEMT PELGDVYTCL VHHSSLLSPV SVEWRVQSEY SWRKMLSGIA AFLLGLIFLL VGIIIQLRAQ KGYVRTQMSG DEVSRAVLLP QPC // ID H0UZF2_CAVPO Unreviewed; 259 AA. AC H0UZF2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 12-SEP-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCPOP00000002555}; GN Name=LOC100716469 {ECO:0000313|Ensembl:ENSCPOP00000002555}; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000002555}; RN [1] {ECO:0000313|Ensembl:ENSCPOP00000002555} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000002555}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSCPOP00000002555} RP IDENTIFICATION. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000002555}; RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAKN02021519; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003473765.2; XM_003473717.3. DR STRING; 10141.ENSCPOP00000002555; -. DR Ensembl; ENSCPOT00000002845; ENSCPOP00000002555; ENSCPOG00000002810. DR GeneID; 100716469; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0UZF2; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR Bgee; ENSCPOG00000002810; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005447}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005447}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 259 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5011539621. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 206 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 259 AA; 28373 MW; 4A33225F520A09D8 CRC64; MITLLPLLLG LSLGCTGAGG FMAHVESTCL LDDNGTPKDF TYCVAYNKDL LTCWNSDEER MEPCEFGTLN MLAVSLSNYL NNNTNLLQRL HNGLQDCATH TQPFWGSLTQ RKKPPTVQVA QTTPFNTREP VMLACYVWGF YPAEVTITWM KNGQVVTPHS SVQKIAQPNG DWTYQTISRL ALTPSYGDVY TCAVEHSGAS EPIYVDWTPG LSPVQKVKVS VSAVVLGLGI IIFSIGLVSW RKAVPSSYTP LPGSTYPEG // ID H0V169_CAVPO Unreviewed; 224 AA. AC H0V169; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 12-SEP-2018, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCPOP00000003228}; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000003228}; RN [1] {ECO:0000313|Ensembl:ENSCPOP00000003228} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003228}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSCPOP00000003228} RP IDENTIFICATION. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003228}; RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAKN02021534; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0V169; -. DR STRING; 10141.ENSCPOP00000003228; -. DR Ensembl; ENSCPOT00000003618; ENSCPOP00000003228; ENSCPOG00000003574. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0V169; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR Bgee; ENSCPOG00000003574; Expressed in 3 organ(s), highest expression level in brain. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005447}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005447}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5013220601. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 224 AA; 25478 MW; EC52435AED7380F5 CRC64; MLCLWLPGGP CMAALTVTLM VLSPPVALAR DTRPRFLVYG KSECHFSNGT ERVRLLAKYI YNQEELVLFD SEVGEFHAVT HLGRPDAKAW NNHKDFLEQM RAMVDTVCRH NYQIGEKTMV QRRVEPKVTV YSTKTQPLQH HNLLVCSVSG FYPGHIEVTW FRNGQEQEIG VVSTGLIQNG DWTFQILVML ETVPQSGEVY ACQVEHVSWS SPVTVEWSEW GPLT // ID H0W2X0_CAVPO Unreviewed; 257 AA. AC H0W2X0; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 12-SEP-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSCPOP00000017315}; GN Name=LOC100714501 {ECO:0000313|Ensembl:ENSCPOP00000017315}; OS Cavia porcellus (Guinea pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; OC Hystricomorpha; Caviidae; Cavia. OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000017315}; RN [1] {ECO:0000313|Ensembl:ENSCPOP00000017315} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000017315}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSCPOP00000017315} RP IDENTIFICATION. RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000017315}; RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAKN02021513; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAKN02021514; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003473759.2; XM_003473711.3. DR ProteinModelPortal; H0W2X0; -. DR STRING; 10141.ENSCPOP00000017315; -. DR Ensembl; ENSCPOT00000027774; ENSCPOP00000017315; ENSCPOG00000024142. DR GeneID; 100714501; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0W2X0; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000005447; Unassembled WGS sequence. DR Bgee; ENSCPOG00000024142; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005447}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005447}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 257 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5011585119. FT TRANSMEM 226 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 257 AA; 29222 MW; BB6AD44DB5B36668 CRC64; MAPQVPEAPW ISALTVALLV LSSTVVQSRT HPEHCVYLRR WECYARNGTQ RLVERYIYNR EEFVRYDSAV GEFRAVTELG RPDAELWNGR KDGLEERRAA VDTVCRYNYE LEAPLTVQRR VQPKVHVSPA KKGTLQHHNQ LICHVTDFYP GDIEVRWFLN GQEETAGIES TSLIHNGDWT FQILVMLEVM PQQGDVYTCH VEHPSLDSPV TVEWTAQSDA ARNKKLTGIG GFVLGLIFLT VGIVMHVRSK KGQRGPQ // ID H0WSJ6_OTOGA Unreviewed; 276 AA. AC H0WSJ6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 20-JUN-2018, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000005060}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000005060}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000005060} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000005060} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAQR03060323; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0WSJ6; -. DR STRING; 30611.ENSOGAP00000005060; -. DR Ensembl; ENSOGAT00000005665; ENSOGAP00000005060; ENSOGAG00000005662. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0WSJ6; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl. DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl. DR GO; GO:0008134; F:transcription factor binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0002344; P:B cell affinity maturation; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl. DR GO; GO:0046635; P:positive regulation of alpha-beta T cell activation; IEA:Ensembl. DR GO; GO:0002579; P:positive regulation of antigen processing and presentation; IEA:Ensembl. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 276 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003544610. FT TRANSMEM 227 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 276 AA; 31158 MW; 0AFEA7015FB30E4A CRC64; MAVQIPGGFW TAAVMVTLLM LSSPVTEGSD SPEDFVFQFK GLCYFTNGTQ RVRLVTRYIY NLEEFARFDS DVGEYRPVTE LGRPDAEYWN SQKDLLERNR AEVDTVCRHN YEAYQGFTWQ RRVEPTVTIS PTKTEALNHH NLLVCSVTDF YPGQVKVHWL RNGQEETAGV VSTPLIRNGD WTFQILVMLE MTPRRGDVYT CHVEHPSFQS PITVEWRAQS ESAQSKMLSG VGGLVLGLIF LGLGLIVHHR SQKGPHGPSP AGNIFVHIQW GQETGV // ID H0X155_OTOGA Unreviewed; 89 AA. AC H0X155; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 28-MAR-2018, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000008702}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000008702, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000008702} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000008702} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAQR03060320; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOGAT00000009734; ENSOGAP00000008702; ENSOGAG00000009732. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0X155; -. DR OMA; WRDECHY; -. DR OrthoDB; EOG091G0YW8; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}. FT DOMAIN 8 82 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 89 AA; 10825 MW; 5D3FA2F1C985631A CRC64; RFLVQFKGEC HFHNGTEKVR LLVRNIYNRE EYARFDSDVG KYRAVTELGR PDAEYWNSQK DVLEQKRAEV DTVCRHNYEI FDRFLVPRR // ID H0X8B5_OTOGA Unreviewed; 89 AA. AC H0X8B5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 28-MAR-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000011709}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000011709, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000011709} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000011709} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAQR03060316; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOGAT00000013073; ENSOGAP00000011709; ENSOGAG00000013069. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0X8B5; -. DR OMA; RHKYELM; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}. FT DOMAIN 8 82 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 89 AA; 11014 MW; F446C67334576539 CRC64; RFLEQAKSEC HFYNGTQRVQ FLERHFYNRE EFVRFDSDVG EFREVTELGR PDAEYWNSQK DFLESRRTAV DWFCRVSYQI SDRFLVSRR // ID H0XEQ5_OTOGA Unreviewed; 79 AA. AC H0XEQ5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 28-MAR-2018, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000014442}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000014442, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000014442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000014442} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAQR03060335; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOGAT00000016138; ENSOGAP00000014442; ENSOGAG00000016138. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0XEQ5; -. DR OrthoDB; EOG091G0YW8; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}. FT DOMAIN 7 79 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 79 AA; 9564 MW; 915C7C74315F3A78 CRC64; YVLQSRDDCY AFNGTQRYVE TYAYNREEYV RFDSDVGEYR AVTELGRRSA EYWNSQKDIL EDARATADRM CRYNYELDE // ID H0XSU5_OTOGA Unreviewed; 770 AA. AC H0XSU5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000019187}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000019187, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000019187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000019187} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAQR03060325; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03060326; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03060327; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 30611.ENSOGAP00000019187; -. DR Ensembl; ENSOGAT00000029342; ENSOGAP00000019187; ENSOGAG00000031343. DR eggNOG; KOG0058; Eukaryota. DR eggNOG; COG1132; LUCA. DR GeneTree; ENSGT00550000074497; -. DR InParanoid; H0XSU5; -. DR OMA; FNQFFVG; -. DR OrthoDB; EOG091G05Q7; -. DR TreeFam; TF105197; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042825; C:TAP complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0042287; F:MHC protein binding; IEA:InterPro. DR GO; GO:0015440; F:peptide-transporting ATPase activity; IEA:InterPro. DR GO; GO:0019885; P:antigen processing and presentation of endogenous peptide antigen via MHC class I; IEA:InterPro. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 1.20.1560.10; -; 1. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR036640; ABC1_TM_sf. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005293; Tap2/ABCB3. DR Pfam; PF00664; ABC_membrane; 1. DR Pfam; PF00005; ABC_tran; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR PRINTS; PR01897; TAP2PROTEIN. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR SUPFAM; SSF90123; SSF90123; 1. DR PROSITE; PS50929; ABC_TM1F; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 58 79 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 99 119 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 149 169 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 258 437 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 470 713 ABC transporter. FT {ECO:0000259|PROSITE:PS50893}. FT DOMAIN 732 770 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NP_BIND 505 512 ATP. {ECO:0000256|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 770 AA; 85016 MW; 4BE36A65FB8CD3CA CRC64; MRLPDLTPWA SLVLVDLAFL WLLQGSLGTV LPRGLPGLWL EGTLRLGGLW GLLKLRGVLG YVGTLLPPLC LVTPLFLSLR ALVSGALSAP PISVASAPWS WLLLGYGAAG LSWAVWAVLS PAGAQEKEQG QEKSKALMWR LLQLSRPDVP FLAAAFFFLA VAVLGETLIP HYSGRVIDIL GGDFDPDAFA SAIGFMCLFS FGSPLDRGFH GPDATFRPSS CTKHKILKLL YSFPLFRQTQ ECTHPKQTKE LLGRNRMDTN LMSSWLPLNA NVLLRSLVKV VGLYAFMLNV SPRLTLLSLL HVPLTIAAEK VYNARHQAVL REIQDAVARA GQVVREAVGG LQTVRSFGAE EHEVWRYKEA LERCRQLWWR RDLERALYLL LRRLLPLGGQ VLMLSCGLQE IRAREMTQGG LLSFLIYQEE VGNYVHSLVY MYGDMLSNVG AAEKVFSYLD RQPNLPCPGE LAPTTLQGLV EFQDVSFAYP NRPDQPVLKG LTFTLRPGEV TALVGPNGSG KSTVAALLQN LYQPTGGQVL LDEKPVWQYE HRYLHSQVAS VGQEPVLFSG SVRDNITYGL QSCEDDKVAA AVQAAHADDF IQEMKDGIYT DIGEKGSQLA AGQKQRLAIA RALVRNPRVL ILDEATSALD AQCEQANAFW LHPLHGGSAT EFDWAGLLPD SRHRLSSDVG MFVALTVLGE PDAKRWNSRP DILETSRASV DALCRHNYRL GAPFTVGRKV QPEVTVYPER TPSLQQHNLL LCSVTGFYPG DINIRWLRNG // ID H0XUU6_OTOGA Unreviewed; 56 AA. AC H0XUU6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 28-MAR-2018, entry version 17. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000019888}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000019888, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000019888} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000019888} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAQR03018021; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOGAT00000031931; ENSOGAP00000019888; ENSOGAG00000026189. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}. FT DOMAIN 2 56 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 56 AA; 6645 MW; 7E03CF5F2C344340 CRC64; MEKVQLVAKC TYNLEEFTLF HSHVGEYQLV TKLGAKAKYW NSQKDILEQK QPGWTW // ID H0Y2E5_OTOGA Unreviewed; 268 AA. AC H0Y2E5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 20-JUN-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOGAP00000022538}; OS Otolemur garnettii (Small-eared galago) (Garnett's greater bushbaby). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Strepsirrhini; OC Lorisiformes; Galagidae; Otolemur. OX NCBI_TaxID=30611 {ECO:0000313|Ensembl:ENSOGAP00000022538, ECO:0000313|Proteomes:UP000005225}; RN [1] {ECO:0000313|Ensembl:ENSOGAP00000022538} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Sequencing Platform; RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K., Jaffe D.B., RA Gnerre S., MacCallum I., Przybylski D., Ribeiro F.J., Burton J.N., RA Walker B.J., Sharpe T., Hall G.; RT "Version 3 of the genome sequence of Otolemur garnettii (Bushbaby)."; RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSOGAP00000022538} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAQR03060329; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAQR03060330; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0Y2E5; -. DR STRING; 30611.ENSOGAP00000022538; -. DR Ensembl; ENSOGAT00000026329; ENSOGAP00000022538; ENSOGAG00000032749. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0Y2E5; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000005225; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005225}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005225}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 268 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003545820. FT DOMAIN 120 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 268 AA; 29352 MW; 9134FDA93775B4C2 CRC64; FTEQSMTILL PLLLGLSLGC MGAGGFVAHV ESTCLLDDNG TPQDFTYCIS FNKDLLTCWD PEQDKMAPCE FGVLNGLATY LSNCLNQQDT LLQRLRNGLQ DCAVHTQPFW GSLTHRTRAP SVQVAQTTPF NTREPVMLAC YVWGFYPADV TITWKKNGQP VTAHSSPQKT PQPNGDWTYQ TLSHLALTPS YGDTYTCVVE HIGALEPILQ DWTPGLSPVQ TVKVSVSAVT LGLGLIIFSL GLISWRRAGS SSYIPLPGSN YPEGRHIS // ID H0Y4X4_HUMAN Unreviewed; 181 AA. AC H0Y4X4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 05-OCT-2016, sequence version 8. DT 12-SEP-2018, entry version 49. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|Ensembl:ENSP00000394860}; DE Flags: Fragment; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSP00000394860}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000394860, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000394860, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000394860} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL669918; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0Y4X4; -. DR PRIDE; H0Y4X4; -. DR Ensembl; ENST00000447394; ENSP00000394860; ENSG00000241106. DR UCSC; uc063nrv.1; human. DR EuPathDB; HostDB:ENSG00000241106.6; -. DR HGNC; HGNC:4937; HLA-DOB. DR OpenTargets; ENSG00000241106; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR ChiTaRS; HLA-DOB; human. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000241106; Expressed in 84 organ(s), highest expression level in small intestine Peyer's patch. DR ExpressionAtlas; H0Y4X4; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:H0Y4X4, KW ECO:0000213|PeptideAtlas:H0Y4X4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 101 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000394860}. FT NON_TER 181 181 {ECO:0000313|Ensembl:ENSP00000394860}. SQ SEQUENCE 181 AA; 20709 MW; BCE7230176DF4211 CRC64; XNLTRLDSSM TQGTDSPEDF VIQAKADCYF TNGTEKVQFV VRFIFNLEEY VRFDSDVGMF VALTKLGQPD AEQWNSRLDL LERSRQAVDG VCRHNYRLGA PFTVGRKEVT VYPERTPLLH QHNLLHCSVT GFYPGDIKIK WFLNGQEERA GVMSTGPIRN GDWTFQTVVM LEMTPELGHV Y // ID H0Y5P2_HUMAN Unreviewed; 235 AA. AC H0Y5P2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 43. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000399832}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000399832}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000399832, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000399832, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000399832} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL645931; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0Y5P2; -. DR PRIDE; H0Y5P2; -. DR Ensembl; ENST00000416804; ENSP00000399832; ENSG00000223865. DR UCSC; uc011dqq.2; human. DR EuPathDB; HostDB:ENSG00000223865.10; -. DR HGNC; HGNC:4940; HLA-DPB1. DR OpenTargets; ENSG00000223865; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000223865; Expressed in 112 organ(s), highest expression level in lung. DR ExpressionAtlas; H0Y5P2; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:H0Y5P2, KW ECO:0000213|PeptideAtlas:H0Y5P2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 213 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000399832}. SQ SEQUENCE 235 AA; 26923 MW; 2927C29A3706E143 CRC64; XNYLFQGRQE CYAFNGTQRF LERYIYNREE FARFDSDVGE FRAVTELGRP AAEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKKG EKACRFNEDL HKQGS // ID H0Y7G7_HUMAN Unreviewed; 229 AA. AC H0Y7G7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 46. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000412654}; DE Flags: Fragment; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSP00000412654}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000412654, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000412654, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000412654} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL645931; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0Y7G7; -. DR SMR; H0Y7G7; -. DR MaxQB; H0Y7G7; -. DR PRIDE; H0Y7G7; -. DR Ensembl; ENST00000428835; ENSP00000412654; ENSG00000223865. DR UCSC; uc063nue.1; human. DR EuPathDB; HostDB:ENSG00000223865.10; -. DR HGNC; HGNC:4940; HLA-DPB1. DR OpenTargets; ENSG00000223865; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000223865; Expressed in 112 organ(s), highest expression level in lung. DR ExpressionAtlas; H0Y7G7; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:H0Y7G7, KW ECO:0000213|PeptideAtlas:H0Y7G7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 204 223 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 101 189 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000412654}. FT NON_TER 229 229 {ECO:0000313|Ensembl:ENSP00000412654}. SQ SEQUENCE 229 AA; 26084 MW; 03DD6307AA104641 CRC64; KQAWRGSATR LGPQNSGRQE CYAFNGTQRF LERYIYNREE FARFDSDVGE FRAVTELGRP AAEYWNSQKD ILEEKRAVPD RMCRHNYELG GPMTLQRRVQ PRVNVSPSKK GPLQHHNLLV CHVTDFYPGS IQVRWFLNGQ EETAGVVSTN LIRNGDWTFQ ILVMLEMTPQ QGDVYTCQVE HTSLDSPVTV EWKAQSDSAR SKTLTGAGGF VLGLIICGVG IFMHRRSKK // ID H0Y7Y7_HUMAN Unreviewed; 218 AA. AC H0Y7Y7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 44. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000415997}; DE Flags: Fragment; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000415997}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000415997, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000415997, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000415997} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL672104; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0Y7Y7; -. DR PRIDE; H0Y7Y7; -. DR Ensembl; ENST00000427449; ENSP00000415997; ENSG00000232629. DR UCSC; uc063nrr.1; human. DR EuPathDB; HostDB:ENSG00000232629.8; -. DR HGNC; HGNC:4945; HLA-DQB2. DR OpenTargets; ENSG00000232629; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000232629; Expressed in 120 organ(s), highest expression level in skin of abdomen. DR ExpressionAtlas; H0Y7Y7; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:H0Y7Y7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 218 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003545822. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000415997}. SQ SEQUENCE 218 AA; 25211 MW; 6CB551B77127115C CRC64; XLQIPGGFWA AAVTVMLVML STPVAEARDF PKDFLVQFKG MCYFTNGTER VRGVARYIYN REEYGRFDSD VGEFQAVTEL GRSIEDWNNY KDFLEQERAA VDKVCRHNYE AELRTTLQRQ VEPTVTISPS RTEALNHHNL LVCSVTDFYP AQIKVRWFRN DQEETAGVVS TSLIRNGDWT FQILVMLEIT PQRGDIYTCQ VEHPSLQSPI TVEWRLLH // ID H0ZU54_TAEGU Unreviewed; 212 AA. AC H0ZU54; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 46. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000014151}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000014151, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000014151} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01068573; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59729.ENSTGUP00000014151; -. DR Ensembl; ENSTGUT00000014316; ENSTGUP00000014151; ENSTGUG00000013745. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 212 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003546946. FT DOMAIN 121 209 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 212 AA; 23641 MW; 5CF4AE4AD618DC5F CRC64; MGRGAAAGAV LVALVALGAA PAAGAELSAV FQQMSKGECH FTNGTEKVRF VLRYIYNRQQ DVMFDSDVGE YVGFTPLGQR NVKRFNNDPE IMERRRAAVD WFCRHYYQQC APVTVERRVP PSVSISLVPS SSQPGPGRLL CSVLDFYPAP IQVRWFQGQQ ELSEHVVATE VVPNGDWSYQ LLVLLETPPR RGLTYSCQVE HGSLEHPLSQ SW // ID H0ZVH6_TAEGU Unreviewed; 213 AA. AC H0ZVH6; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000014623}; GN Name=LOC100218309 {ECO:0000313|Ensembl:ENSTGUP00000014623}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000014623, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000014623} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01073143; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABQF01073144; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABQF01073145; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59729.ENSTGUP00000014623; -. DR Ensembl; ENSTGUT00000014819; ENSTGUP00000014623; ENSTGUG00000014233. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 213 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003546964. FT DOMAIN 122 210 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 213 AA; 23675 MW; 2249449B3832F25C CRC64; AMGRGAAAGA VLVALVALGA APAAGAELSG VLQEMVYHEC HFTNGTEKVR LVQRLIYNRE QYAMFDSDVG EFVGFTPYGE KFAKKLNSDP EWMERKRAEV DIVCRHNYRV STPFLTERRV PPSVSISLVP SSSQPGPGRL LCSVLDFYPA PIQVRWFQGQ QELSEHVVAT EVVPNGDWSY QLLVLLETPP RRGLTYSCQV EHGSLEHPLS QSW // ID H0ZWA2_TAEGU Unreviewed; 168 AA. AC H0ZWA2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000014901}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000014901, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000014901} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01073453; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABQF01073454; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABQF01073455; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABQF01073456; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABQF01073457; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0ZWA2; -. DR STRING; 59729.ENSTGUP00000014901; -. DR Ensembl; ENSTGUT00000015114; ENSTGUP00000014901; ENSTGUG00000014503. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0ZWA2; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 77 165 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 168 AA; 19382 MW; 611014C75FA6AD73 CRC64; TERVRYVERL IYNRLQYLMF DSDVGEYVGF TPYGERNAER LNSDPAIMER RRAAVDWHCR HNYEAFAPFS VERRVPPSVS ISLVPSSSQP GPGRLLCSVL DFYPAPIQVR WFQGQQELSE HVVATEVVPN GDWSYQLLVL LETPPRRGLT YSCQVEHGSL EHPLSQSW // ID H0ZWI5_TAEGU Unreviewed; 191 AA. AC H0ZWI5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 45. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000014986}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000014986, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000014986} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01065257; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H0ZWI5; -. DR STRING; 59729.ENSTGUP00000014986; -. DR Ensembl; ENSTGUT00000015212; ENSTGUP00000014986; ENSTGUG00000014620. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0ZWI5; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 100 188 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 191 AA; 22007 MW; 3C3C806AAAB83FAB CRC64; ELCPALTGVL QYMFKAECRF TNSTERVRYV QRYIYNRLQY LMFDSDVGEF VGFTPLGERN AKRFNSDPVI MEDKRSEVDR FCRHNYRGVA PFSVERRVPP NVSISLVPSS SQPGPGRLLC SVLDFYPAPI QVRWFQGQQE LSEHVVATEV VPNGDWSYQL LVLLETPPRR GLTYSCQVEH GSLEHPLSQS W // ID H0ZWL2_TAEGU Unreviewed; 116 AA. AC H0ZWL2; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000015013}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000015013, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000015013} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01090996; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59729.ENSTGUP00000015013; -. DR Ensembl; ENSTGUT00000015240; ENSTGUP00000015013; ENSTGUG00000014649. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H0ZWL2; -. DR OMA; RHKYELM; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 20 94 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 116 AA; 13307 MW; 27B31497C40F888C CRC64; GAPPELCPAL TAVLQELVYK ECHFTNGTEK VRYVERYIYN REQFLMFDSD VGEFVGFTPF GERNAKRLNS DPAIMEDKRA AVDRFCRHNY RVVTPFSVER RVPPSPSQSI PGHSQP // ID H0ZXA5_TAEGU Unreviewed; 127 AA. AC H0ZXA5; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000015256}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000015256, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000015256} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01077189; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSTGUT00000015504; ENSTGUP00000015256; ENSTGUG00000014905. DR GeneTree; ENSGT00900000140849; -. DR OMA; WRDECHY; -. DR OrthoDB; EOG091G13XG; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 127 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003546979. FT DOMAIN 37 111 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 127 AA; 14596 MW; 31329A8463E11AD2 CRC64; MGRVAAARAL LVALVLLGAS SGADTELSGV FQEMVKSECH FINGTQRVRF VKRFIYNREQ YVHFDSDVGH FVGDTPYGEQ VARYWNSNLE WMEYRRAAVD RHCRHNYELS TPFLAERRVP PDLSLSL // ID H0ZZB1_TAEGU Unreviewed; 155 AA. AC H0ZZB1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000015964}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000015964, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000015964} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01093107; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSTGUT00000016255; ENSTGUP00000015964; ENSTGUG00000015634. DR GeneTree; ENSGT00900000140849; -. DR OMA; FSWARET; -. DR OrthoDB; EOG091G13XG; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 155 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003547141. FT DOMAIN 38 112 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 155 AA; 17267 MW; 5B57EBB65C9141D4 CRC64; AMGRGAAAGA VLVALVALGA APAAGAELSG VFQHMFKAEC YFTNGTEKVR FVERYIYNRL QYMMFDSDVG EYVGFTPYGE KNAKRLNSDP ELMEYRRTAV DWYCRHNYLV FAPFSVERRV PPSVSISLVP SSSKPGPGRL LCSELHFYPA PIQVR // ID H1A0J1_TAEGU Unreviewed; 195 AA. AC H1A0J1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000016400}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000016400, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000016400} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01074967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H1A0J1; -. DR STRING; 59729.ENSTGUP00000016400; -. DR Ensembl; ENSTGUT00000016722; ENSTGUP00000016400; ENSTGUG00000016075. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H1A0J1; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 104 192 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 195 AA; 22317 MW; CF9AEBA3B7870D0A CRC64; GAPPELCPAL SAVFQQMSKC ECHFTNGTEK VRFVLRYIYN RQQDVMFDSD VGEYVGFTPY GEKNAKRLNS DPEWMEYRRT AVDRYCRQNY HVDAPFTVER RVPPSVSISL VPSSSQPGPG RLLCSVLDFY PAPIQVRWFQ GQQELSEHVV ATEVVPNGDW SYQLLVLLET PPRRGLTYSC QVEHGSLEHP LSQSW // ID H1A2M7_TAEGU Unreviewed; 248 AA. AC H1A2M7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 43. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000017139}; GN Name=LOC100229282 {ECO:0000313|Ensembl:ENSTGUP00000017139}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000017139, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000017139} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01063494; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59729.ENSTGUP00000017139; -. DR Ensembl; ENSTGUT00000017514; ENSTGUP00000017139; ENSTGUG00000016844. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H1A2M7; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 248 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003547035. FT TRANSMEM 221 243 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 121 207 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 248 AA; 27968 MW; 741EAADBEB44CC21 CRC64; MGRVAAARAL LAALVLLGAS SAADTELSGV FQEMVKSECH FINGTQRVRF VKRFIYNREQ YVHFDSDVGH FVGDTPYGEQ VARYWNSNLE WMEYRRAAVD RHCRHNYELS TPFLAERRVS PSVSISLVPS SSQPGPGRLL CSVLDFYPAP IQVRWFQGQQ ELSVVATDIF PSGDWTYQLL VLLETPTRAG LTYTCQVEHG SLEHPLSRHW EMLPDTAHSK MLTGIGGFVL GFVFLALGLG FYLHKKVR // ID H1A3G1_TAEGU Unreviewed; 137 AA. AC H1A3G1; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000017423}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000017423, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000017423} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01066484; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H1A3G1; -. DR Ensembl; ENSTGUT00000017817; ENSTGUP00000017423; ENSTGUG00000017139. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H1A3G1; -. DR OMA; IMEHRRT; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 2 56 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 137 AA; 15780 MW; 76713D2D9DF68A7E CRC64; XNREQYLMFD SDVGEYVGFT PYGEKQARYR NSNPEIMEHR RTAVDWYCRH NYRGVAPFSV ERRVPPSVSI SLVPSSSQPG PGRLLCSVLD FYPAPIQVRF QGQQDLSEHV VATEWPHGDW SYQLLVLLES PPRRGLT // ID H1A3G3_TAEGU Unreviewed; 113 AA. AC H1A3G3; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000017425}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000017425, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000017425} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01066487; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 59729.ENSTGUP00000017425; -. DR Ensembl; ENSTGUT00000017821; ENSTGUP00000017425; ENSTGUG00000017149. DR eggNOG; ENOG410JFJX; Eukaryota. DR eggNOG; ENOG41119HF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H1A3G3; -. DR OMA; ECHYANG; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 113 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003547045. FT DOMAIN 29 103 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 113 AA; 13006 MW; 4F99BF3F70491FA6 CRC64; AVLVALVALG AAPAAGAELS GVFQFLGKFE CYFMNGTEKV RYVHRYLYNR EQLAMFDSDV GVYVGFNPLG EKWARCWNSD PEFMERKRAE VDIVCRHNYR VYAPFLAERR GER // ID H1A3U4_TAEGU Unreviewed; 180 AA. AC H1A3U4; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 12-SEP-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTGUP00000017558}; OS Taeniopygia guttata (Zebra finch) (Poephila guttata). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; OC Estrildidae; Estrildinae; Taeniopygia. OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000017558, ECO:0000313|Proteomes:UP000007754}; RN [1] {ECO:0000313|Proteomes:UP000007754} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20360741; DOI=10.1038/nature08819; RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W., RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A., RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P., RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., RA London S.E., Li Y., Lin Y.C., George J., Sweedler J., Southey B., RA Gunaratne P., Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., RA Itoh Y., Whitney O., Pfenning A.R., Howard J., Volker M., RA Skinner B.M., Griffin D.K., Ye L., McLaren W.M., Flicek P., RA Quesada V., Velasco G., Lopez-Otin C., Puente X.S., Olender T., RA Lancet D., Smit A.F., Hubley R., Konkel M.K., Walker J.A., RA Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z., Eichler E.E., RA Stapley J., Slate J., Ekblom R., Birkhead T., Burke T., Burt D., RA Scharff C., Adam I., Richard H., Sultan M., Soldatov A., Lehrach H., RA Edwards S.V., Yang S.P., Li X., Graves T., Fulton L., Nelson J., RA Chinwalla A., Hou S., Mardis E.R., Wilson R.K.; RT "The genome of a songbird."; RL Nature 464:757-762(2010). RN [2] {ECO:0000313|Ensembl:ENSTGUP00000017558} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABQF01057820; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H1A3U4; -. DR Ensembl; ENSTGUT00000017959; ENSTGUP00000017558; ENSTGUG00000017280. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H1A3U4; -. DR OMA; RIPEAHC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007754; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007754}; KW Reference proteome {ECO:0000313|Proteomes:UP000007754}. FT DOMAIN 94 180 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 180 AA; 20164 MW; 4C146715568E88B5 CRC64; GLFQEMVKSG CHFINGTERV RLVQRNIYKW EQLLHLGGDG GLYVGDASSG ENVARYWNSN LEWMEHRLAA VDRHYHPPYV ACCPFTPNSS KAHPTVSILL GLSSSQHNPG HLLCPIMDFY PAHIQLRWFQ GQQEPSVMAT NVVPNGDWTH QLLVLLETPP QGGVTCSCQV EHVSLEHPLS // ID H2L2T3_ORYLA Unreviewed; 249 AA. AC H2L2T3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 20-JUN-2018, entry version 44. DE SubName: Full=Nonclassical MHC class II antigen beta chain {ECO:0000313|EMBL:AGA53816.1}; GN Name=Orla-DCB {ECO:0000313|EMBL:AGA53816.1}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000000030, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000000030, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000000030, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000000030} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000000030}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:AGA53816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hd-rR {ECO:0000313|EMBL:AGA53816.1}; RX PubMed=23989892; DOI=10.1007/s00251-013-0731-8; RA Bannai H.P., Nonaka M.; RT "Comprehensive analysis of medaka major histocompatibility complex RT (MHC) class II genes: implications for evolution in teleosts."; RL Immunogenetics 65:883-895(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BAAF04081053; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04081054; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; JQ743259; AGA53816.1; -; Genomic_DNA. DR STRING; 8090.ENSORLP00000000030; -. DR Ensembl; ENSORLT00000000030; ENSORLP00000000030; ENSORLG00000000025. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF333780; -. DR Proteomes; UP000001038; Chromosome 3. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28381 MW; 15D0369621397E0F CRC64; MDSSSLRVFL LILTLYPADG FIHYILNRCL FNSSDLKDIE NIYSYYYNKE EFLRFSSSSG KFVGYTEIGV KTAELANNDP EKMSRRRAEK ETFCKPNIDN DYSTILTKSV QPRVRVQSLE PSGGNHPAML ICSVYDFYPK KIKVSWLQDQ EEVSSDVTST AEMEDGDWFY QIHSYLEYTP RSGGKISCRV EHISLKDPLI TDWDPSMPES EKNKIAIGAS GLILGLVLSL AGFVYYKRKT RGRILVPSS // ID H2LZC5_ORYLA Unreviewed; 241 AA. AC H2LZC5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 20-JUN-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSORLP00000011497}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000011497, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000011497, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000011497, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000011497} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000011497}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BAAF04003798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04003799; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2LZC5; -. DR Ensembl; ENSORLT00000011498; ENSORLP00000011497; ENSORLG00000009164. DR GeneTree; ENSGT00900000140882; -. DR OMA; QIRVTWL; -. DR Proteomes; UP000001038; Chromosome 16. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 241 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003565527. FT TRANSMEM 217 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 111 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 241 AA; 27590 MW; 58F0B46D16130077 CRC64; TGKSQNCSLG FLPLFLLFSS TNAFYGHGTL KCQFTSSHDL VYLEQVYFNK RLMVQYNSTL GKYEGYTKKA KDLADGFSKS KPFLEQAVKN REKCRTHMDL VFELQSHPVE PSVRVTPVVR QGSSHQAMLA CSAYNFYPKQ IRLTWLRNGE KVINYVTSTE ELPDGNWLYQ IHSYLEYTPS PREEITCMVE HASPKEPKLY NWEVLSPPMF GAVRNKIAVG TALLFGSFVF VAGLFFYKRT T // ID H2MBX4_ORYLA Unreviewed; 238 AA. AC H2MBX4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 20-JUN-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSORLP00000016051}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000016051, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000016051, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016051, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000016051} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016051}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BAAF04004797; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04004798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2MBX4; -. DR Ensembl; ENSORLT00000016052; ENSORLP00000016051; ENSORLG00000012822. DR eggNOG; ENOG410KH5C; Eukaryota. DR eggNOG; ENOG4110RMF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2MBX4; -. DR OMA; NITVENM; -. DR OrthoDB; EOG091G0GLS; -. DR TreeFam; TF333780; -. DR Proteomes; UP000001038; Chromosome 5. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 238 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003565972. FT TRANSMEM 213 235 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 115 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 238 AA; 27466 MW; 2D89482E78B8AC68 CRC64; ILSSLIYFYL LFLTSYYSKD QHGYFMFSDF FCYIPSRNPK EVQYLIDWYF NMELTMQYNS SVGGWTGFTP AGLITAAKFN ADKYDVVQRI LERELVCQRS VEMVYNGTEE AKVEPNVSLQ TVEDNDSTLE CSALDFYPKH IRLTWFSNGQ EVTEGVTFSD VLPNGDWTYQ AHTYLTLTPG KQDHISCMVQ HTSLKEPKIY NWEPSMNQTD RDYIIGGVCA LLLGAVFLCV GLIHYKQK // ID H2MBX8_ORYLA Unreviewed; 237 AA. AC H2MBX8; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 20-JUN-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSORLP00000016055}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000016055, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Ensembl:ENSORLP00000016055, ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016055, RC ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000016055} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000016055}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BAAF04004797; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BAAF04004798; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSORLT00000016056; ENSORLP00000016055; ENSORLG00000012822. DR eggNOG; ENOG410KH5C; Eukaryota. DR eggNOG; ENOG4110RMF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000001038; Chromosome 5. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 212 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 237 AA; 27345 MW; 1A691E7591BDEBB8 CRC64; FHTEEQSLFV LFHSNYSKDQ HGYFMFSDFF CYIPSRNPKE VQYLIDWYFN MELTMQYNSS VGGWTGFTPA GLITAAKFNA DKYDVVQRIL ERELVCQRSV EMVYNGTEEA KVEPNVSLQT VEDNDSTLEC SALDFYPKHI RLTWFSNGQE VTEGVTFSDV LPNGDWTYQA HTYLTLTPGK QDHISCMVQH TSLKEPKIYN WEPSMNQTDR DYIIGGVCAL LLGAVFLCVG LIHYKQK // ID H2MX91_ORYLA Unreviewed; 247 AA. AC H2MX91; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 48. DE SubName: Full=MHC class II antigen beta chain {ECO:0000313|EMBL:AGA53814.1}; GN Name=LOC101160212 {ECO:0000313|Ensembl:ENSORLP00000023542}; GN Synonyms=Orla-DAB {ECO:0000313|EMBL:AGA53814.1}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000023542, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000023542} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000023542}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:AGA53814.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hd-rR {ECO:0000313|EMBL:AGA53814.1}; RX PubMed=23989892; DOI=10.1007/s00251-013-0731-8; RA Bannai H.P., Nonaka M.; RT "Comprehensive analysis of medaka major histocompatibility complex RT (MHC) class II genes: implications for evolution in teleosts."; RL Immunogenetics 65:883-895(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JQ743257; AGA53814.1; -; Genomic_DNA. DR RefSeq; XP_004084697.1; XM_004084649.2. DR STRING; 8090.ENSORLP00000023542; -. DR Ensembl; ENSORLT00000023543; ENSORLP00000023542; ENSORLG00000018856. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF333780; -. DR Proteomes; UP000001038; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 247 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014574554. FT TRANSMEM 213 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 110 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 247 AA; 28167 MW; 8E6F9DEB01470EE0 CRC64; MDSSSLCLLF LTMCSADAFL RYDVDRCVFN STDLKDIEYI YSMYYNKKEF TRFSSSLGKY VGYTEYGVKT AERANKDTSE LSARKAQKET YCKHNIDNWY KNMLSKSVQP RVRVQSLAPS GGHHPAMLVC SVYDFYPKTI RVSWLRGKEE VSSDVTSTAE MEDGDWYYQI HSHLEYTPRS GEKISCKVEH ASLKDPLVTE WDPSMPESER NKVAIGASGL ILGLVLSLAG FIYYKRKARG RILVPSS // ID H2MYN4_ORYLA Unreviewed; 249 AA. AC H2MYN4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 20-JUN-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSORLP00000024128}; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; OC Oryziinae; Oryzias. OX NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000024128, ECO:0000313|Proteomes:UP000001038}; RN [1] {ECO:0000313|Proteomes:UP000001038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Proteomes:UP000001038}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSORLP00000024128} RP IDENTIFICATION. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000024128}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; H2MYN4; -. DR STRING; 8090.ENSORLP00000024128; -. DR Ensembl; ENSORLT00000024129; ENSORLP00000024128; ENSORLG00000019376. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2MYN4; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF333780; -. DR Proteomes; UP000001038; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001038}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001038}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003566834. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28570 MW; 9F503A8C64DD8770 CRC64; TDMDFSSLCL LFLTLYSADG FLEYDMHRCL FNSSDMKDIE YIYSKHYNKE EVIRFSSSLG KYVGYTKFGV MAAGYWNKDL EGLRERRADK ERLCKTNIDL DYLNILTKSV KPSVMIESVT SSGGHHPAML VCSVYDFYPK YIKVSWLRDQ EEVSSDVTST TELEDGDWYY QIHSHLEYTP RSGEKISCRV EHASLKDPLI TDWDPSMPES EKNKLAIGAS GLILGLVLSL AGFIYYKRKA LGRSSLNRF // ID H2PIN9_PONAB Unreviewed; 266 AA. AC H2PIN9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 28-MAR-2018, entry version 40. DE SubName: Full=Major histocompatibility complex, class II, DR beta 5 {ECO:0000313|Ensembl:ENSPPYP00000018440}; GN Name=HLA-DRB5 {ECO:0000313|Ensembl:ENSPPYP00000018440}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000018440, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000018440, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000018440} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01134636; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01134637; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01134638; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01134639; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01144822; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01144823; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9601.ENSPPYP00000018440; -. DR Ensembl; ENSPPYT00000019175; ENSPPYP00000018440; ENSPPYG00000016490. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PIN9; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003567965. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30089 MW; B74822650BEC9CFF CRC64; MVCLKLPGGS YMAALTVTLM VLSSPLALAG DTRSRFLRQD KYECHFFNGT ERVRFLHRGI YNQEENVRFD SDVGEYRAVT ELGRPDAEYW NSQKDFLEDR RAAVDTFCRH NYGVVESFTV QRRVEPKVTV YPAKTQTLQH HNLLVCSVNG FYPDSIEVRW FRNGQEEKTG VVSTGLIQNG DWTFQILVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGTGLFIYF RNQKGHSGLQ PTGLVS // ID H2PIP2_PONAB Unreviewed; 304 AA. AC H2PIP2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 28-MAR-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPPYP00000018443}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000018443, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000018443, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000018443} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01030719; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01218054; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01218055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01218056; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01218057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01218058; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2PIP2; -. DR STRING; 9601.ENSPPYP00000018443; -. DR Ensembl; ENSPPYT00000019178; ENSPPYP00000018443; ENSPPYG00000016492. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PIP2; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 264 284 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 162 250 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 304 AA; 34424 MW; 0DF08FBABAF13960 CRC64; METSTGFYSF CQVHQIHQVR AVLTTTTFPF VSIMSWKKAL RIPGGLRAAT VTLMLAMLST PVAEGRGSPE DFVVQFKGMC YFTNGTERVR LVARHVYNRE EYARFDSDVG VYRAVTPLGQ SSVEYWNSQK EVLETKRAEL DTVCRHNYQL ELRTTLQRRV EPTVTISPSR TEALNHHNLL VCSVTNFYPA QIKVRWFRND QEETTGVVST PLIRNGDWTF QILVMLEITP QRGDVYTCHV EHPSLQSPIT VEWRAQSESA QSKMVSGIGG FVLGLIFLGL GLIIHHRSQK DLKGLHQQGS CTDS // ID H2PL14_PONAB Unreviewed; 290 AA. AC H2PL14; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 28-MAR-2018, entry version 50. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPPYP00000019292}; GN Name=LOC100443385 {ECO:0000313|Ensembl:ENSPPYP00000019292}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019292}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019292} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019292} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01113363; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2PL14; -. DR STRING; 9601.ENSPPYP00000019292; -. DR Ensembl; ENSPPYT00000020051; ENSPPYP00000019292; ENSPPYG00000017216. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PL14; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 252 274 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 150 238 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 290 AA; 32963 MW; 5F474B8F9D6BCAEB CRC64; RKTEDEPLGC WWWALRGGGC RLRFPVPAPR PGSPDGGVPI SVFSGGRPCD RILRVPTARF LEQVKSECHF FNGTERVRFL ERYFYNQEEY VHFDSDVGEY RAVTELGRPD AEYWNSQKNL LEQKRGQVDN YCRHNYGVGE SFTVQRRVQP KVTVYPSKTQ PLQHHNLLVC SVNGFYPGSI EVRWFRNGQE EKTGVVSTGL IQNGDWTFQT LVMLETVPQS GEVYTCQVEH PSMTSPLTVE WRARSESAQS KMLSGVGGFV LGLLFLGAGL FIYFRNQKGH SGLQPRGFLS // ID H2PL15_PONAB Unreviewed; 266 AA. AC H2PL15; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 20-JUN-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPPYP00000019293}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019293, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019293, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019293} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01396647; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01396648; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01396649; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2PL15; -. DR STRING; 9601.ENSPPYP00000019293; -. DR Ensembl; ENSPPYT00000020052; ENSPPYP00000019293; ENSPPYG00000017217. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PL15; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003568018. FT TRANSMEM 229 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 127 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29924 MW; 01784A31B7FB6CD4 CRC64; MVCLKLPGGS SLAALTVTLM VLSSPLALSG DTRPRFLEYS TSECYFFNGT ERVRFVERYI YNQEENLRFD SDVGEFRAVT ELGRPDAENW NSQKKSFLED RRAAVDTFCR HNYGVGESFT VQRRVQPRVT VYPSKTQPLQ HHNLLVCSVS GFYPGSIEVR WFRNGQEEKA GVVSTGLIRN GDWTFQTLVM LETVPRSGEV YTCQVEHPSV TSPLTVEWRA RSESAQSKML SGVGGFVLGL LFLGTGLFIY FRNQKGHSRL PPTGLS // ID H2PL21_PONAB Unreviewed; 264 AA. AC H2PL21; A0A2J8Y2N6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 39. DE SubName: Full=HLA-DQB2 isoform 2 {ECO:0000313|EMBL:PNJ88561.1}; DE SubName: Full=Major histocompatibility complex, class II, DQ beta 2 {ECO:0000313|Ensembl:ENSPPYP00000019299}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSPPYP00000019299}; GN ORFNames=CR201_G0016201 {ECO:0000313|EMBL:PNJ88561.1}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019299, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019299, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019299} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:PNJ88561.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Susie {ECO:0000313|EMBL:PNJ88561.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., RA Chaisson M., Hoppe E., Hill C., Pang A., Hillier L., Baker C., RA Armstrong J., Shendure J., Paten B., Wilson R., Chao H., Schneider V., RA Ventura M., Kronenberg Z., Murali S., Gordon D., Cantsilieris S., RA Munson K., Nelson B., Raja A., Underwood J., Diekhans M., Fiddes I., RA Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01190016; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; NDHI03003283; PNJ88561.1; -; Genomic_DNA. DR STRING; 9601.ENSPPYP00000019299; -. DR Ensembl; ENSPPYT00000020058; ENSPPYP00000019299; ENSPPYG00000017220. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PL21; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014575121. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29853 MW; FE22E4F5C06B6049 CRC64; MALQIPGGFW AAAVTAMLVM LSTPVAEARD FPKDFLVQFK GMCYFTNGTE RVRGVARYIY NREEYGRFDS DVGEFRAVTE LGRSIEDWNN YKDFLEQERA AVDKVCRHNY EAELRTTLQR RVEPIVTISP SRTEALNHHN LLVCSVTDFY PAQIKVQWFR NDQEETAGVV STSLIRNGDW TFQILVMLEM TPQRGDVYTC HVEHPSLQSP ITVEWRAQSE SAQSKMLSGA GGFVLGLIFL GLGLIIRHRG QKGPRGLPPA GLLH // ID H2PL23_PONAB Unreviewed; 272 AA. AC H2PL23; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 28-MAR-2018, entry version 37. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSPPYP00000019301}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSPPYP00000019301}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019301, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019301, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019301} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01190010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_009235418.1; XM_009237143.1. DR STRING; 9601.ENSPPYP00000019301; -. DR Ensembl; ENSPPYT00000020060; ENSPPYP00000019301; ENSPPYG00000017221. DR GeneID; 100443682; -. DR KEGG; pon:100443682; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PL23; -. DR KO; K06752; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 272 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003567424. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 272 AA; 30739 MW; BDC70F7769F32C24 CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVHFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSREA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERAGVMS TGPIRNGDWT FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWRKMLSGIA AFLLGLIFLL VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QP // ID H2PL28_PONAB Unreviewed; 263 AA. AC H2PL28; A0A2J8Y2R3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 23-MAY-2018, entry version 38. DE SubName: Full=HLA-DMB isoform 5 {ECO:0000313|EMBL:PNJ88576.1}; GN Name=LOC100448477 {ECO:0000313|Ensembl:ENSPPYP00000019306}; GN ORFNames=CR201_G0016211 {ECO:0000313|EMBL:PNJ88576.1}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019306, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019306, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019306} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:PNJ88576.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Susie {ECO:0000313|EMBL:PNJ88576.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., RA Chaisson M., Hoppe E., Hill C., Pang A., Hillier L., Baker C., RA Armstrong J., Shendure J., Paten B., Wilson R., Chao H., Schneider V., RA Ventura M., Kronenberg Z., Murali S., Gordon D., Cantsilieris S., RA Munson K., Nelson B., Raja A., Underwood J., Diekhans M., Fiddes I., RA Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01189998; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01189999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01190000; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; NDHI03003283; PNJ88576.1; -; Genomic_DNA. DR RefSeq; XP_002809179.1; XM_002809133.2. DR ProteinModelPortal; H2PL28; -. DR STRING; 9601.ENSPPYP00000019306; -. DR Ensembl; ENSPPYT00000020065; ENSPPYP00000019306; ENSPPYG00000017226. DR GeneID; 100448477; -. DR KEGG; pon:100448477; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PL28; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014575103. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28858 MW; 7405F23B81C32E5A CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESTCL LDDAGTPKDF TYCISFNKVL LTCWDPEENE MAPCEFGVLN GVANVLSHYL NQQDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPADVTITWR KNGKLVIPHS SAQKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGLISW RRAGHSSYSP LPGSNYPEGR HIS // ID H2PL33_PONAB Unreviewed; 283 AA. AC H2PL33; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 2. DT 20-JUN-2018, entry version 37. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPPYP00000019311}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019311, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019311, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019311} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01157331; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2PL33; -. DR STRING; 9601.ENSPPYP00000019311; -. DR Ensembl; ENSPPYT00000020070; ENSPPYP00000019311; ENSPPYG00000017230. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PL33; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 252 271 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 149 253 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 283 AA; 32392 MW; 0C023A6C4AB71F4F CRC64; MKAMKEGYLL TLCKLLFERI SKPSSTMVLQ VSAAPQTVAL MALLMVLLTS VVQGRATPEN YVYQRLFECY AFNGTQRLLD RLIYNQEEYI RFDSDLGEYR TVTELGRRTA EYWNSQKDIL ELERAEVDRV CRHNYELEEP LIRKRQVQPR VNVSPSKKGP LQHHNLLVCH VTDFYPGNIQ VRWFLNGQEE TAGVVSTNLI RNGDWTFQIL VMLEITPKQG DVYTCQVEHP SLDSPVTMEW KTQSDSARSK TLTGAGGFVL GLIICGVGIF MHRRSKKVQR GSV // ID H2PL44_PONAB Unreviewed; 157 AA. AC H2PL44; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 28-MAR-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPPYP00000019322}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000019322, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000019322, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000019322} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01171213; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPPYT00000020081; ENSPPYP00000019322; ENSPPYG00000017237. DR eggNOG; ENOG410IUVV; Eukaryota. DR eggNOG; ENOG4110PTP; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2PL44; -. DR OMA; RHKYELM; -. DR OrthoDB; EOG091G0W5S; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 157 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003568022. FT DOMAIN 42 114 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 157 AA; 17813 MW; E9232C32BF7A66BE CRC64; MMILQVSGGP WTVALTALLM VLLISVVQAA ATPENSVYQE RQECYAFSGT QRFVDGLIYN REEYVHFDSA VGEFLTVMEL GRPMAECLNS QKDFMERKRA VMDTVCRHKY ELMEPLIRQR RGDVPITAVR GCWTMILSDY FLLKRGVVLG SCSWGSS // ID H2QSQ3_PANTR Unreviewed; 275 AA. AC H2QSQ3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPTRP00000030724}; GN Name=LOC104006793 {ECO:0000313|Ensembl:ENSPTRP00000030724}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000030724, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030724, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000030724} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPTRT00000033254; ENSPTRP00000030724; ENSPTRG00000051243. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018001; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 275 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014189725. FT TRANSMEM 230 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 218 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 275 AA; 31058 MW; C8C8645EC665E6E5 CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALSG DTRHKSRFLE LVKSECHFFN GTERVRFLER YFYNQEEYVR FDSDVGEYRA VTELGRPVAE SWNSQKDLLE QKRGQVDNYC RHNYGAVESF TVQRRVHPQV TVYPAKTQPL QHHNLLVCSV NGFYPGSIEV RWFRNGQEEK AGVVSTGLIQ NGDWTFQTLV MLETVPRSGE VYTCQVEHPS VMSPLTVEWR ARSESAQSKM LSGVGGFVLG LLFLGAGLFI YFRNQKGKES LVAGSLRSLS FPKRL // ID H2QSQ4_PANTR Unreviewed; 279 AA. AC H2QSQ4; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 38. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 2 {ECO:0000313|Ensembl:ENSPTRP00000030727}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSPTRP00000030727}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000030727, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030727, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000030727} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9598.ENSPTRP00000030727; -. DR PaxDb; H2QSQ4; -. DR Ensembl; ENSPTRT00000033257; ENSPTRP00000030727; ENSPTRG00000023404. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2QSQ4; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000023404; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 279 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014168743. FT TRANSMEM 230 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 279 AA; 31473 MW; B8C94ECC8CAFFEAA CRC64; MSWKMALQIP GGFWAAAVTV MLVMLSTPVA EARDFPKDFL VQFKGMCYFT NGTERVRGVA RYIYNREEYG RFDSDVGEFQ AVTELGRSIE DWNNYKDFLE QERAAVDKVC RHNYEAELRT TLQRQVEPTV TISPSRTEAL NHHNLLVCSV TDFYPAQIKV RWFRNDQEET AGVVSTSLIR NGDWTFQILV MLEITPQHGD IYTCHVEHPS LQSPITVEWR AQSESAQSKM LSGVGGFVLG LIFLGLGLII RHRGQKGPRG PPPAGNISAM IQSGERAQS // ID H2QSQ5_PANTR Unreviewed; 282 AA. AC H2QSQ5; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 45. DE SubName: Full=Major histocompatibility complex, class II, DR beta 5 precursor {ECO:0000313|Ensembl:ENSPTRP00000030734}; GN Name=PATR-DRB5 {ECO:0000313|Ensembl:ENSPTRP00000030734}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000030734, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030734, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000030734} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9598.ENSPTRP00000030734; -. DR PaxDb; H2QSQ5; -. DR Ensembl; ENSPTRT00000033264; ENSPTRP00000030734; ENSPTRG00000023735. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2QSQ5; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000023735; Expressed in 6 organ(s), highest expression level in testis. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 282 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014120216. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 282 AA; 31961 MW; 31BDFBCF48803919 CRC64; MVCLKLPGGS YMAVLTVTLM VLSSPLALAG DTRPRFLKQD KYECHFFNGT ERVRYLHRDI YNQEENVRFD SDVGEYRAVT ELGRPVAEYW NSQKDILERR RAAVDTYCRH NYGVAESFTV QRRVHPKVTV YPAKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQILVML ETVPRSGEVY TCQVEHPSVM SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF KNQKENVHPC GFLSSCPWPE VPALMAVPHL QL // ID H2QSR6_PANTR Unreviewed; 261 AA. AC H2QSR6; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 12-SEP-2018, entry version 51. DE SubName: Full=MHC-class II protein {ECO:0000313|EMBL:SCE63383.1}; DE SubName: Full=Major histocompatibility complex, class II, DQ beta 1 {ECO:0000313|Ensembl:ENSPTRP00000030768}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSPTRP00000030768}; GN Synonyms=MHC-DQB1 {ECO:0000313|EMBL:SCE63383.1}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000030768, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030768, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000030768} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:SCE63383.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cor {ECO:0000313|EMBL:SCE63383.1}, and RC Dylan {ECO:0000313|EMBL:SCE63384.1}; RA Ottng N., Heijmans C.M.C., De Groot N.G., Bontrop R.E.; RT "New MHC class II alleles in Pan troglodytes."; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:SCE63383.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cor {ECO:0000313|EMBL:SCE63383.1}, and RC Dylan {ECO:0000313|EMBL:SCE63384.1}; RA Seilhamer J.J.; RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; LT607051; SCE63383.1; -; mRNA. DR EMBL; LT607052; SCE63384.1; -; mRNA. DR RefSeq; XP_003339166.1; XM_003339118.3. DR STRING; 9598.ENSPTRP00000030768; -. DR Ensembl; ENSPTRT00000033302; ENSPTRP00000030768; ENSPTRG00000018018. DR GeneID; 100616520; -. DR KEGG; ptr:100616520; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2QSR6; -. DR KO; K06752; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018018; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014576156. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29779 MW; 4B94ED0CEDEE8100 CRC64; MSWKKALRIP GGLRAATVTL VLAMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVT RYIYNREEYV RFDSDVGVYR AVTPLGPPAA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQHG DVYTCHVEHP SLQNPITVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI IHHRSQKGLL H // ID H2QSR7_PANTR Unreviewed; 273 AA. AC H2QSR7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 12-SEP-2018, entry version 39. DE SubName: Full=Patr class II histocompatibility antigen, DO beta chain precursor {ECO:0000313|Ensembl:ENSPTRP00000030772}; GN Name=PATR-DOB {ECO:0000313|Ensembl:ENSPTRP00000030772}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000030772, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030772, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000030772} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPTRT00000033306; ENSPTRP00000030772; ENSPTRG00000018020. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2QSR7; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018020; Expressed in 5 organ(s), highest expression level in heart. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 273 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003569898. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 273 AA; 30822 MW; 906A00E46A06D30D CRC64; MGSGWVPWVV ALLVNLTRLD SSMTQGTDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYVRFDSDV GMFVALTKLG QPDAEQWNSR LDLLERSRQA VDGVCRHNYR LGAPFTVGRK VQPEVTVYPE RTPLLHQHNL LHCSVTGFYP GDIKIRWFLN GQEERAGVMS TGPIRNGDWT FQTVVMLEMT PELGHVYTCL VDHSSLLSPV SVEWRAQSEY SWKKMLSGIA AFLLGLIFLL VGIVIQLRAQ KGYVRTQMSG NEVSRAVLLP QSC // ID H2QSS0_PANTR Unreviewed; 263 AA. AC H2QSS0; A0A2J8NYD7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 12-SEP-2018, entry version 41. DE SubName: Full=HLA-DMB isoform 5 {ECO:0000313|EMBL:PNI76791.1}; DE SubName: Full=Major histocompatibility complex, class II, DM beta precursor {ECO:0000313|Ensembl:ENSPTRP00000030778}; GN Name=PATR-DMB {ECO:0000313|Ensembl:ENSPTRP00000030778}; GN ORFNames=CK820_G0006956 {ECO:0000313|EMBL:PNI76791.1}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000030778, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030778, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000030778} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:PNI76791.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Yerkes chimp pedigree #C0471 {ECO:0000313|EMBL:PNI76791.1}; RC TISSUE=Blood {ECO:0000313|EMBL:PNI76791.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., RA Chaisson M., Hoppe E., Hill C., Pang A., Hillier L., Baker C., RA Armstrong J., Shendure J., Paten B., Wilson R., Chao H., Schneider V., RA Ventura M., Kronenberg Z., Murali S., Gordon D., Cantsilieris S., RA Munson K., Nelson B., Raja A., Underwood J., Diekhans M., Fiddes I., RA Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; NBAG03000221; PNI76791.1; -; Genomic_DNA. DR RefSeq; NP_001127814.1; NM_001134342.2. DR UniGene; Ptr.3688; -. DR STRING; 9598.ENSPTRP00000030778; -. DR PaxDb; H2QSS0; -. DR Ensembl; ENSPTRT00000033314; ENSPTRP00000030778; ENSPTRG00000018025. DR GeneID; 449592; -. DR KEGG; ptr:449592; -. DR CTD; 449592; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2QSS0; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018025; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015093079. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28947 MW; ABE1F6CBE21E79A2 CRC64; MITFLPLLLG LSLGCTGAGG FVAHVESSCL LDDAGTPKDF TYCISFNKDL LTCWDPEENK MAPCEFGVLN SLANFLSQHL NQQDTLMQRL RNGLQNCATH TQPFWGSLTN RTRPPSVQVA KTTPFNTREP VMLACYVWGF YPAEVTITWR KNGKLVMPHS SAHKTAQPNG DWTYQTLSHL ALTPSYGDTY TCVVEHIGAP EPILRDWTPG LSPMQTLKVS VSAVTLGLGL IIFSLGVISW RRAGHSSYTP LPGSNYSEGR HIS // ID H2RAS7_PANTR Unreviewed; 266 AA. AC H2RAS7; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 41. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 1 precursor {ECO:0000313|Ensembl:ENSPTRP00000054448}; GN Name=PATR-DQB1 {ECO:0000313|Ensembl:ENSPTRP00000054448}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000054448, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000054448, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000054448} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001258000.1; NM_001271071.1. DR UniGene; Ptr.3300; -. DR Ensembl; ENSPTRT00000061904; ENSPTRP00000054448; ENSPTRG00000018001. DR GeneID; 462594; -. DR KEGG; ptr:462594; -. DR CTD; 462594; -. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2RAS7; -. DR KO; K06752; -. DR OMA; GQVDNYC; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018001; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29778 MW; 1AF0F139281CBF27 CRC64; MLCLKLPGVS CMTALTVTLM VLSSPLALAG DTRSRFLLQP KGECHFFNGT ERVRFLHRYF YNQEEFMRFD SDVGEYRAVT ELGRPVAEYC NSQKDILEQA RAAVDNYCRH NYGVGESFTV QRRVQPKVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGHSGLQ PTGFLS // ID H2RAS9_PANTR Unreviewed; 289 AA. AC H2RAS9; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 44. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPTRP00000054452}; GN Name=LOC104006793 {ECO:0000313|Ensembl:ENSPTRP00000054452}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000054452, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000054452, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000054452} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9598.ENSPTRP00000054452; -. DR PaxDb; H2RAS9; -. DR Ensembl; ENSPTRT00000061908; ENSPTRP00000054452; ENSPTRG00000051243. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018001; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 289 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014134190. FT TRANSMEM 230 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 218 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 289 AA; 32791 MW; 65D2BB90F9929E96 CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALSG DTRHKSRFLE LVKSECHFFN GTERVRFLER YFYNQEEYVR FDSDVGEYRA VTELGRPVAE SWNSQKDLLE QKRGQVDNYC RHNYGAVESF TVQRRVHPQV TVYPAKTQPL QHHNLLVCSV NGFYPGSIEV RWFRNGQEEK AGVVSTGLIQ NGDWTFQTLV MLETVPRSGE VYTCQVEHPS VMSPLTVEWR ARSESAQSKM LSGVGGFVLG LLFLGAGLFI YFRNQKGKES LVAGSLRRLF WRRNYGFAEV SSQYMSGPE // ID H2RAT0_PANTR Unreviewed; 276 AA. AC H2RAT0; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPTRP00000054454}; GN Name=LOC104006793 {ECO:0000313|Ensembl:ENSPTRP00000054454}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000054454, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000054454, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000054454} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPTRT00000061910; ENSPTRP00000054454; ENSPTRG00000051243. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018001; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 276 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014166005. FT TRANSMEM 230 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 218 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 276 AA; 31306 MW; DDD856472A82E0CF CRC64; MVCLKLPGGS CMAALTVTLM VLSSPLALSG DTRHKSRFLE LVKSECHFFN GTERVRFLER YFYNQEEYVR FDSDVGEYRA VTELGRPVAE SWNSQKDLLE QKRGQVDNYC RHNYGAVESF TVQRRVHPQV TVYPAKTQPL QHHNLLVCSV NGFYPGSIEV RWFRNGQEEK AGVVSTGLIQ NGDWTFQTLV MLETVPRSGE VYTCQVEHPS VMSPLTVEWR ARSESAQSKM LSGVGGFVLG LLFLGAGLFI YFRNQKGKDC IPNSFLSLNR SWINKT // ID H2RC37_PANTR Unreviewed; 266 AA. AC H2RC37; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 39. DE SubName: Full=Major histocompatibility complex, class II, DR beta 5 precursor {ECO:0000313|Ensembl:ENSPTRP00000056708}; GN Name=PATR-DRB5 {ECO:0000313|Ensembl:ENSPTRP00000056708}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000056708, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000056708, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000056708} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPTRT00000065144; ENSPTRP00000056708; ENSPTRG00000023735. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018001; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014163250. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30049 MW; A72F38ABB33D6F82 CRC64; MVCLKLPGGS YMAVLTVTLM VLSSPLALAG DTRPRFLKQD KYECHFFNGT ERVRYLHRDI YNQEENVRFD SDVGEYRAVT ELGRPVAEYW NSQKDILERR RAAVDTYCRH NYGVAESFTV QRRVHPKVTV YPAKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQILVML ETVPRSGEVY TCQVEHPSVM SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF KNQKGHSGLH PTGLVS // ID H2RC77_PANTR Unreviewed; 258 AA. AC H2RC77; A0A2J8NYI2; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 12-SEP-2018, entry version 50. DE SubName: Full=HLA-DPB1 isoform 1 {ECO:0000313|EMBL:PNI76809.1}; DE SubName: Full=MHC class II protein {ECO:0000313|EMBL:SCW24592.1}; DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSPTRP00000056904}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSPTRP00000056904}; GN Synonyms=Patr-DPB1 {ECO:0000313|EMBL:SCW24592.1}; GN ORFNames=CK820_G0006964 {ECO:0000313|EMBL:PNI76809.1}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000056904, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000056904, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000056904} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|EMBL:SCW24592.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Karin {ECO:0000313|EMBL:SCW24592.1}; RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:SCW24592.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Karin {ECO:0000313|EMBL:SCW24592.1}; RA Ottng N., Heijmans C.M.C., De Groot N.G., Bontrop R.E.; RT "New MHC class II alleles in Pan troglodytes."; RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:PNI76809.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Yerkes chimp pedigree #C0471 {ECO:0000313|EMBL:PNI76809.1}; RC TISSUE=Blood {ECO:0000313|EMBL:PNI76809.1}; RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., RA Chaisson M., Hoppe E., Hill C., Pang A., Hillier L., Baker C., RA Armstrong J., Shendure J., Paten B., Wilson R., Chao H., Schneider V., RA Ventura M., Kronenberg Z., Murali S., Gordon D., Cantsilieris S., RA Munson K., Nelson B., Raja A., Underwood J., Diekhans M., Fiddes I., RA Haussler D., Eichler E.; RT "High-resolution comparative analysis of great ape genomes."; RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; NBAG03000221; PNI76809.1; -; Genomic_DNA. DR EMBL; LT622890; SCW24592.1; -; mRNA. DR RefSeq; XP_518391.3; XM_518391.6. DR STRING; 9598.ENSPTRP00000056904; -. DR Ensembl; ENSPTRT00000065338; ENSPTRP00000056904; ENSPTRG00000018030. DR GeneID; 462599; -. DR KEGG; ptr:462599; -. DR CTD; 462599; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2RC77; -. DR KO; K06752; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018030; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015093473. FT TRANSMEM 227 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29248 MW; 03F277EEAF1C81CD CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYVYQG RQECYAFNGT QRYLERYIYN REEYARFDSD VGEFRAVTEL GRPAAEYWNS QKDLLEEKRA VPDRMCRHNY ELNEAVTLQR RVQPKVNVSP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYIC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID H2RDN1_PANTR Unreviewed; 271 AA. AC H2RDN1; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 39. DE SubName: Full=Major histocompatibility complex, class II, DQ beta 1 precursor {ECO:0000313|Ensembl:ENSPTRP00000059118}; GN Name=PATR-DQB1 {ECO:0000313|Ensembl:ENSPTRP00000059118}; OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000059118, ECO:0000313|Proteomes:UP000002277}; RN [1] {ECO:0000313|Ensembl:ENSPTRP00000059118, ECO:0000313|Proteomes:UP000002277} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16136131; DOI=10.1038/nature04072; RG Chimpanzee sequencing and analysis consortium; RT "Initial sequence of the chimpanzee genome and comparison with the RT human genome."; RL Nature 437:69-87(2005). RN [2] {ECO:0000313|Ensembl:ENSPTRP00000059118} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AACZ04022817; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSPTRT00000067532; ENSPTRP00000059118; ENSPTRG00000018001. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000002277; Chromosome 6. DR Bgee; ENSPTRG00000018001; Expressed in 6 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; IEA:Ensembl. DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002506; P:polysaccharide assembly with MHC class II protein complex; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002277}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002277}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 271 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014138357. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 271 AA; 30402 MW; EDCDFC3841AC69DF CRC64; MLCLKLPGVS CMTALTVTLM VLSSPLALAG DTRSRFLLQP KGECHFFNGT ERVRFLHRYF YNQEEFMRFD SDVGEYRAVT ELGRPVAEYC NSQKDILEQA RAAVDNYCRH NYGVGESFTV QRRVQPKVTV YPAKTQPLQH HNLLVCSVSG FYPGSIEVRW FLNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSVT SPLTVEWRAR SESAQSKMLS GVGGFVLGLL FLGAGLFIYF RNQKGEEPLG PFFPQTALMS C // ID H2RX67_TAKRU Unreviewed; 250 AA. AC H2RX67; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 20-JUN-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000004737}; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000004737, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000004737} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21551351; RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., RA Hosoya S., Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.; RT "Integration of the genetic map and genome assembly of fugu RT facilitates insights into distinct features of genome evolution in RT teleosts and mammals."; RL Genome Biol. Evol. 3:424-442(2011). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000004737} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; H2RX67; -. DR STRING; 31033.ENSTRUP00000004737; -. DR Ensembl; ENSTRUT00000004765; ENSTRUP00000004737; ENSTRUG00000002062. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2RX67; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 250 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003571436. FT TRANSMEM 216 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 250 AA; 28541 MW; 571E5A1F16915F27 CRC64; MSSSSLRVFL LFISLYTAGG FQSYRVDRCD FNSTDLKDIE YSRSHYYNKL MYVRFRSSVG KFEGYTKDGL IQADYWNNIS SYLEQMRDEK ERYCEPNIKV WYSNILSKSV EPTVRVHSVV PPAGGHPAML VCSVYDFYPR YIKVSWQRDG EEVSQDVTST DELADGDWFY QLHSHLEYLP ACLSALLSVC LSETHLSVPT CLPSDPSMPE SERNQIAIGA SGLILGLILS LAGFIYFKRK SRGRILVPNN // ID H2V693_TAKRU Unreviewed; 214 AA. AC H2V693; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 28-MAR-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTRUP00000044727}; DE Flags: Fragment; OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Takifugu. OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000044727, ECO:0000313|Proteomes:UP000005226}; RN [1] {ECO:0000313|Ensembl:ENSTRUP00000044727} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSTRUP00000044727}; RX PubMed=17554307; DOI=10.1038/nature05846; RA Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., RA Yamada T., Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., RA Shimada A., Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., RA Asakawa S., Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., RA Sugano S., Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., RA Nomoto H., Nogata K., Morishita T., Endo T., Shin-I T., Takeda H., RA Morishita S., Kohara Y.; RT "The medaka draft genome and insights into vertebrate genome RT evolution."; RL Nature 447:714-719(2007). RN [2] {ECO:0000313|Ensembl:ENSTRUP00000044727} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; H2V693; -. DR STRING; 31033.ENSTRUP00000044727; -. DR Ensembl; ENSTRUT00000044878; ENSTRUP00000044727; ENSTRUG00000017449. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2V693; -. DR OMA; QIRVTWL; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005226; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005226}; KW Reference proteome {ECO:0000313|Proteomes:UP000005226}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 214 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003575949. FT DOMAIN 115 203 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSTRUP00000044727}. SQ SEQUENCE 214 AA; 24400 MW; FADE5A7B4C19A393 CRC64; SRMSSSSLRV FLLFISLYTA AGGFQSYVVD SCDFNSTDLK DIEYTRSLYY NRVMYARFSS RVGKFEGYTK YGLFQADYWN NQSSILEGLR ETKESICQPN IKIDYSNILS KSVEPTVRVH SVVPPAGGHP AMLVCSVYDF YPRYIKVSWQ RDGEEVSQDV TSTDELADGD WFYQLHSHLE YTPRSGEKIS CVVEHASLKT PLVKDWGNHL SVCS // ID H2ZRY9_LATCH Unreviewed; 89 AA. AC H2ZRY9; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000000160}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000000160, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000000160} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000000160}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000000160} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01284697; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLACT00000000162; ENSLACP00000000160; ENSLACG00000000143. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2ZRY9; -. DR OMA; ECHYANG; -. DR OrthoDB; EOG091G12PD; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}. FT DOMAIN 8 82 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 89 AA; 10819 MW; 5D4D0FD0C9E54FE2 CRC64; SYVYQANFEC HYANGTQDIV FIKRNIYAGQ EFVYFNSRIR KFTAVTEWGK PTADKWNNDK EYLEGMRNEV EAYCRHNYEW MQSWVVVRN // ID H2ZS24_LATCH Unreviewed; 88 AA. AC H2ZS24; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 20-JUN-2018, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000000195}; GN Name=LOC102361794 {ECO:0000313|Ensembl:ENSLACP00000000195}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000000195, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000000195} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000000195}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000000195} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01283994; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLACT00000000197; ENSLACP00000000195; ENSLACG00000000176. DR GeneTree; ENSGT00910000146742; -. DR InParanoid; H2ZS24; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}. FT DOMAIN 7 81 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 88 AA; 10472 MW; 48FC338FC03B7AF8 CRC64; YVHQSKDECY YTNGTQDIVY IRRTIYAGQE YAYFDSRIGK FTAVTEWGKP SVDYWNKNKE YLAGLQTEKD RACTMNYNWM RGWAVGKQ // ID H2ZSB6_LATCH Unreviewed; 223 AA. AC H2ZSB6; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000000287}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000000287, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000000287} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000000287}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000000287} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01276623; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01276624; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2ZSB6; -. DR STRING; 7897.ENSLACP00000000287; -. DR Ensembl; ENSLACT00000000289; ENSLACP00000000287; ENSLACG00000000257. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2ZSB6; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}. FT DOMAIN 90 180 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 223 AA; 25741 MW; ECDF22589F9ADADB CRC64; VEQYQWECHY TNGTQDIDFI HRVIYNGQEE SYFDSRIGKF TGVTEWGKKD ADYWNKDKEN LAQWRIQEDR WCRNNYNWMQ GWAVGKQVSP AAVITPTKGM SSSHPNMLVC YVTGFFPSKI TVTWFRNGKE VDSHVTSSEL LQNGDWTYQI HVFLEMTPKS GDVYTCRVEH SSLEDPMELT WGNLTSSKIH PKICKSIKPG VLSEISDMPG LKAHHTIPKS LVK // ID H2ZSF5_LATCH Unreviewed; 87 AA. AC H2ZSF5; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000000326}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000000326, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000000326} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000000326}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000000326} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01279633; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLACT00000000328; ENSLACP00000000326; ENSLACG00000000294. DR InParanoid; H2ZSF5; -. DR OMA; RHKYELM; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}. FT DOMAIN 6 80 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 87 AA; 10723 MW; 30C35A30FEF88CDF CRC64; VEQYQWECHY TNGTQDIDFI YRVIYNGQED TYFDSRIGKF TAVTEWGKKD ADYWNKNKEY LARLQTEEER WCRNNYDWMQ GWAVGKQ // ID H2ZSX0_LATCH Unreviewed; 262 AA. AC H2ZSX0; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 20-JUN-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000000491}; GN Name=LOC102367485 {ECO:0000313|Ensembl:ENSLACP00000000491}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000000491, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000000491} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000000491}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000000491} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01264851; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2ZSX0; -. DR STRING; 7897.ENSLACP00000000491; -. DR Ensembl; ENSLACT00000000493; ENSLACP00000000491; ENSLACG00000000438. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2ZSX0; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 221 243 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 118 207 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 262 AA; 29754 MW; BB1DB71E4D0353CA CRC64; ICREIKCQRI CVLLLLCEEF VSEFPRSYVQ EMTSGCYYTN GTEQVRFFHR YIYNKEEQVY FDSQAGLFIG RTEFGRKQAA SWNKDKTNLD DERANVDRFC KHNYFMVEKF VLARKVKPTA KVTPTKVMGT HPGMVVCHVT GFFPSKIKVK WLRNGEEVTS DVTSTELLQN GDWTFQVHVF LELTPKSGDT YTCRVEHNSL DGPLEISWAE PGMSESERSK LLTGIGGLVL GVIFVVAGLI VYLKNKKGAP TIPVTQSQGI LL // ID H2ZU11_LATCH Unreviewed; 97 AA. AC H2ZU11; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000000882}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000000882, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000000882} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000000882}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000000882} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01274755; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSLACT00000000891; ENSLACP00000000882; ENSLACG00000000794. DR InParanoid; H2ZU11; -. DR OMA; WRDECHY; -. DR OrthoDB; EOG091G0YW8; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}. FT DOMAIN 7 81 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 97 AA; 11790 MW; 937F5B98B29A9C46 CRC64; YVQQWRDECH YTNGTQDIVY IFRLIYAGQE YAYFDSRIDK FTAVTEWGKP TADHWNKDKE YLARLQTEEE RWCRNNYDWM QGWAVGKEGE RNPPVRG // ID H2ZWH8_LATCH Unreviewed; 260 AA. AC H2ZWH8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000001749}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000001749, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000001749} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000001749}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000001749} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01219840; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01219841; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2ZWH8; -. DR STRING; 7897.ENSLACP00000001749; -. DR Ensembl; ENSLACT00000001762; ENSLACP00000001749; ENSLACG00000001562. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2ZWH8; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 221 241 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 118 208 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 260 AA; 30352 MW; 9F4127D6F5D842F1 CRC64; MLCCVSQIKG SIFKSIVCCL IDIVWVSYVY QFNFECYYTN GTRDIVFFHR AIYAGQEYTY FDSRIGKFTT VTEWGKPDTD KWNNDKEYLE GMRNEVEAYC RHNYEWMQSW VVERKVKPKA KITPTKAMRT SHPNMLVCYV TEFYPSEITV TWLKNDEEVT SHVTSSDLLQ DGDWSYQIHV FLEMTPKSGD VYTCRVEHSS LPDPVELTWE AGMSESERNK LVTGIVGFVL GAIFVVIRLI VYLRNKKGNN SFIRKETAFI // ID H2ZY39_LATCH Unreviewed; 237 AA. AC H2ZY39; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000002310}; GN Name=LOC102351546 {ECO:0000313|Ensembl:ENSLACP00000002310}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000002310, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000002310} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000002310}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000002310} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01221673; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H2ZY39; -. DR STRING; 7897.ENSLACP00000002310; -. DR Ensembl; ENSLACT00000002328; ENSLACP00000002310; ENSLACG00000002063. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H2ZY39; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 199 221 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 97 186 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 237 AA; 26982 MW; 4DD2B497931B2FEA CRC64; VSPPFLFSLG SYVEQINSEC YYTNGTEQVR FFQRYIYNKH EQVYFDSQAG LYIGRKQAAG WNKDKTNLDN VRAAVDRFCK PNYFVVENFV LERKVKPTAK VTPTKVMGTH PGMIICHVTG FFPSKIKVKW FRNGEEVTSD VTSTELLQNG DWTYQVHVFL ELTLKSGDRY TCRVEHNSLD GPLEISWEPG MSESERSKLL TGIGGLVLGV IFVVVGLIVY LRKKKGNNSP KCFALLE // ID H3A4I8_LATCH Unreviewed; 266 AA. AC H3A4I8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000004559}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000004559, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000004559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000004559}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000004559} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01219855; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H3A4I8; -. DR STRING; 7897.ENSLACP00000004559; -. DR Ensembl; ENSLACT00000004598; ENSLACP00000004559; ENSLACG00000004057. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H3A4I8; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 223 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 120 210 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30246 MW; 34CA59702FA2BFB6 CRC64; VCSAEGRVKV AFIPGLINCD SFLSPAGVSY VYQFTWECYF TNGTQDVQFV IRDIYDGQEQ FNLDSRIGHF IGFTEYGRKQ AKYFNGQKDY VAQWMTEDDR WCRNNYLWME DWAIERKVKP QVKITPTKGM SSSHPNMLVC YVTGFFPSKI AVTWLRNGKE VNSHVTSSEL LQDGDWTYQI HVFLEMTLKS GDVYTCRVEH SSLPDPLELT WEPGMSESER SKLLTGIGGL VLGVIFVVVG LIVYLRNKKG APTIQVSQTQ GNSLSL // ID H3AA83_LATCH Unreviewed; 267 AA. AC H3AA83; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000006554}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000006554, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000006554} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000006554}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000006554} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01219863; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01219864; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H3AA83; -. DR STRING; 7897.ENSLACP00000006554; -. DR Ensembl; ENSLACT00000006607; ENSLACP00000006554; ENSLACG00000005810. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H3AA83; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 267 AA; 30746 MW; 8AD321FFAF9DFBF6 CRC64; KKYSLIFINC NTGLKISTVH LTLTGCLSDP GVSYVRQSKW ECYFTNGTQN IVFFLRHVYD GEEIFYFDSR IGHFIGTTEY GRIQAEYRNS HKEMVDKWRN EEERWCKNNY QWMEGWAIGR QVKPQVKITP TKGMSSSHPN MLVCYVTGFF PSGITVTWLR NGKEVDSHVT SSELLQDGDW TYQIHVFLEM TPKSGDVYVC RVEHNSLLDP IELTWEPGMS ESERSKLLTG IGGLVLGVIF VVVGLIVYLR NKKEIFTPIA INRSTFN // ID H3AG87_LATCH Unreviewed; 267 AA. AC H3AG87; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLACP00000008658}; OS Latimeria chalumnae (West Indian ocean coelacanth). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Coelacanthiformes; Coelacanthidae; Latimeria. OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000008658, ECO:0000313|Proteomes:UP000008672}; RN [1] {ECO:0000313|Ensembl:ENSLACP00000008658} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Wild caught {ECO:0000313|Ensembl:ENSLACP00000008658}; RX PubMed=9215903; RA Zardoya R., Meyer A.; RT "The complete DNA sequence of the mitochondrial genome of a 'living RT fossil,' the coelacanth (Latimeria chalumnae)."; RL Genetics 146:995-1010(1997). RN [2] {ECO:0000313|Ensembl:ENSLACP00000008658} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AFYH01219878; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AFYH01219879; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; H3AG87; -. DR STRING; 7897.ENSLACP00000008658; -. DR Ensembl; ENSLACT00000008726; ENSLACP00000008658; ENSLACG00000007653. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H3AG87; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000008672; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000008672}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008672}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 229 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 207 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 267 AA; 30675 MW; AE74268866BB37FE CRC64; FRQVYIFPIC RDVKCQRICV LLLICEEFVA EFPRSYVTEI STECYYTNGT EQVRFFDRYI YNKKEYLYFD SKVGLFAGTT ELGRQYAERL NKDKGILDNA RAAVDRFCKP NYFAVEKFVL ERKVKPTAKV TPTKVMGMHP GMIVCHVTGF YPSKIKVKWL RNGEEVTSDV TSTELLQNGD WTYQVHVFLE LTPKSGDTYT CRVEHNSLYG PLEIRWAEPG MSELERSKVL TGIGGLVLGV IFVVVGLIVY LRNKKGNNST KCFALLE // ID H3C150_TETNG Unreviewed; 250 AA. AC H3C150; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTNIP00000001966}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000001966, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000001966} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000001966} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR STRING; 99883.ENSTNIP00000001966; -. DR Ensembl; ENSTNIT00000002403; ENSTNIP00000001966; ENSTNIG00000000531. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H3C150; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G13XG; -. DR TreeFam; TF333780; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 250 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003581283. FT TRANSMEM 216 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 27 102 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 250 AA; 28067 MW; 37373D2FC11970D4 CRC64; MASSALRVSL LFLGLSAAGG FEHYEVDLCD FTSAELKDIE YSRSLYYNKH LYARFSSSVG TFVGFTKYGL HQADYWNNQS SYLDRLKEEK QRYCHRNIQN WYSHILSKSE ASSYLLENLI QVIQVIQVSR SFSGSLTFFS SSSQVAPPAG GHAASHDVTS TDELADGDWF YQLHSHLEYT PRSGEKISCV VEHASLKTPL VKDWDPSMPE AERNQIAIGA SGLILGLILS LAGFIYFQRK SRGRILVPTN // ID H3CJ65_TETNG Unreviewed; 249 AA. AC H3CJ65; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 28-MAR-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSTNIP00000008294}; OS Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon OS nigroviridis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; OC Tetraodon. OX NCBI_TaxID=99883 {ECO:0000313|Ensembl:ENSTNIP00000008294, ECO:0000313|Proteomes:UP000007303}; RN [1] {ECO:0000313|Ensembl:ENSTNIP00000008294} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496914; DOI=10.1038/nature03025; RA Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N., RA Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., RA Nicaud S., Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., RA Dasilva C., Salanoubat M., Levy M., Boudet N., Castellano S., RA Anthouard V., Jubin C., Castelli V., Katinka M., Vacherie B., RA Biemont C., Skalli Z., Cattolico L., Poulain J., De Berardinis V., RA Cruaud C., Duprat S., Brottier P., Coutanceau J.-P., Gouzy J., RA Parra G., Lardier G., Chapple C., McKernan K.J., McEwan P., Bosak S., RA Kellis M., Volff J.-N., Guigo R., Zody M.C., Mesirov J., RA Lindblad-Toh K., Birren B., Nusbaum C., Kahn D., Robinson-Rechavi M., RA Laudet V., Schachter V., Quetier F., Saurin W., Scarpelli C., RA Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.; RT "Genome duplication in the teleost fish Tetraodon nigroviridis reveals RT the early vertebrate proto-karyotype."; RL Nature 431:946-957(2004). RN [2] {ECO:0000313|Ensembl:ENSTNIP00000008294} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; H3CJ65; -. DR STRING; 99883.ENSTNIP00000008294; -. DR Ensembl; ENSTNIT00000008460; ENSTNIP00000008294; ENSTNIG00000005593. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H3CJ65; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF333780; -. DR Proteomes; UP000007303; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007303}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007303}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003582162. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28154 MW; 77B40F18FF0BA95B CRC64; MASSALRVSL LFLGLSAAGA FEHYGLRRCD FTSAEPKDME YSLSVYYNKH LMARFSSSVG KFVGYDKYGQ YQADYWNNQS SFLEAMRSSK QRLCQHNIPL WYSHILSKSV LKDVFVYSVA PPAGGHPAML VCSVYDFYPK KIKVSWRRDG QEVSHDVTST DELADGDWFY QLHSHLEYTP RSGEKISCVV EHASLKTPLV KDWDPSMPEA ERNQIAIGAS GLILGLILSL AGFIYFQRKS RGRILVPTN // ID H9H0W9_MELGA Unreviewed; 245 AA. AC H9H0W9; DT 16-MAY-2012, integrated into UniProtKB/TrEMBL. DT 16-MAY-2012, sequence version 1. DT 28-MAR-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMGAP00000005904}; DE Flags: Fragment; OS Meleagris gallopavo (Wild turkey). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Meleagridinae; Meleagris. OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000005904, ECO:0000313|Proteomes:UP000001645}; RN [1] {ECO:0000313|Ensembl:ENSMGAP00000005904, ECO:0000313|Proteomes:UP000001645} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475; RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A., RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K., RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C., RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A., RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., RA de Jong P., Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., RA Lee M.K., Lee T., Mane S., Marcais G., Marz M., McElroy A.P., RA Modise T., Nefedov M., Notredame C., Paton I.R., Payne W.S., RA Pertea G., Prickett D., Puiu D., Qioa D., Raineri E., Ruffier M., RA Salzberg S.L., Schatz M.C., Scheuring C., Schmidt C.J., Schroeder S., RA Searle S.M., Smith E.J., Smith J., Sonstegard T.S., Stadler P.F., RA Tafer H., Tu Z.J., Van Tassell C.P., Vilella A.J., Williams K.P., RA Yorke J.A., Zhang L., Zhang H.B., Zhang X., Zhang Y., Reed K.M.; RT "Multi-platform next-generation sequencing of the domestic turkey RT (Meleagris gallopavo): genome assembly and analysis."; RL PLoS Biol. 8:E1000475-E1000475(2010). RN [2] {ECO:0000313|Ensembl:ENSMGAP00000005904} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; H9H0W9; -. DR STRING; 9103.ENSMGAP00000005904; -. DR Ensembl; ENSMGAT00000006649; ENSMGAP00000005904; ENSMGAG00000005944. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; H9H0W9; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001645; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000001645}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000001645}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 194 216 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 92 180 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSMGAP00000005904}. SQ SEQUENCE 245 AA; 27491 MW; E6723553DEED4A8A CRC64; XFQWSATVEC HFLNGTERMR FLVRHVYNRQ QYVHFDSDVG LFVADTVLGE PSAQLFNSQP DVLEKNRAAA EMLCGYNYEI VAPLTLQERA APEVRICALQ SGSLPRTDRL ACFVTGFYPP EIEVKWFQNG QEETERVVST DVIQNGDWTY QVLVVLETGP RRGDSYVCRV EHVSLRQPIS RLWEPPVDAG RSKLLVGVGG FVLGLVWLAL GLFLFLRSKK GEQWGGGAVL WVSGHPDPPP PGNFS // ID HB21_BOVIN Reviewed; 261 AA. AC Q9TVC8; O77825; Q95541; DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 25-OCT-2017, entry version 97. DE RecName: Full=BoLa class II histocompatibility antigen, DQB*0101 beta chain; DE Short=DQB1*1A; DE Flags: Precursor; GN Name=BoLA-DQB {ECO:0000312|EMBL:CAA77078.1}; GN Synonyms=DQB1 {ECO:0000312|EMBL:AAB21511.1}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] {ECO:0000312|EMBL:CAA77078.1} RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Blood {ECO:0000312|EMBL:CAA77078.1}; RX PubMed=11132144; DOI=10.1007/s002510000257; RA Russell G.C.; RT "Sequence duplication at the 3' end of BoLA-DQB genes suggests RT multiple allelic lineages."; RL Immunogenetics 52:101-106(2000). RN [2] {ECO:0000312|EMBL:AAB21511.1} RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-121. RX PubMed=1537611; DOI=10.1007/BF00185115; RA Sigurdardottir S., Borsch C., Gustafsson K., Andersson L.; RT "Gene duplications and sequence polymorphism of bovine class II DQB RT genes."; RL Immunogenetics 35:205-213(1992). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000255}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; Y18201; CAA77078.1; -; mRNA. DR EMBL; S83910; AAB21511.1; -; Genomic_DNA. DR PIR; I47060; I47060. DR UniGene; Bt.350; -. DR ProteinModelPortal; Q9TVC8; -. DR SMR; Q9TVC8; -. DR PRIDE; Q9TVC8; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR InParanoid; Q9TVC8; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 32 {ECO:0000255}. FT CHAIN 33 261 BoLa class II histocompatibility antigen, FT DQB*0101 beta chain. FT /FTId=PRO_5000147334. FT TOPO_DOM 33 230 Extracellular. {ECO:0000255}. FT TRANSMEM 231 251 Helical. {ECO:0000255}. FT TOPO_DOM 252 261 Cytoplasmic. {ECO:0000255}. FT DOMAIN 129 233 Ig-like C1-type. {ECO:0000255}. FT REGION 33 126 Beta-1. {ECO:0000255}. FT REGION 127 220 Beta-2. {ECO:0000255}. FT REGION 221 230 Connecting peptide. {ECO:0000255}. FT CARBOHYD 51 51 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 47 111 {ECO:0000250|UniProtKB:P06343, FT ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 149 205 {ECO:0000250|UniProtKB:P06343, FT ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 261 AA; 30122 MW; 9BB83ABA7CCC49F8 CRC64; MSGMVALWIP RGLWTAVVMV TLVMLSTPGA EGRDSPKDFV YQFKGLCYFT NGTERVRYVT RYIYNQEENV RFDSDWDEYR AVTPLGRPDA EYFNSQKDFL EQTRAEADTV CRHNYQVEAP FTWQRQVEPT VTIFLSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGVVATPLI RNGDWTFQLF MMLEMTPQRG DVYTCRVEHP SLQSPIMVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI VHHRSQKGLM R // ID HB21_MOUSE Reviewed; 264 AA. AC P04230; O78226; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 25-APR-2018, entry version 131. DE RecName: Full=H-2 class II histocompatibility antigen, E-B beta chain; DE Flags: Precursor; GN Name=H2-Eb1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=C57BL/10; RX PubMed=6086309; RA Widera G., Flavell R.A.; RT "The nucleotide sequence of the murine I-E beta b immune response RT gene: evidence for gene conversion events in class II genes of the RT major histocompatibility complex."; RL EMBO J. 3:1221-1225(1984). RN [2] RP NUCLEOTIDE SEQUENCE. RX PubMed=3150763; RA King L.B., Sharma S., Corley R.B.; RT "Complete coding region sequence of E beta k cDNA clones: lack of RT polymorphism in the NH2-terminus between E beta k and E beta b RT molecules."; RL J. Immunogenet. 15:209-214(1988). RN [3] RP NUCLEOTIDE SEQUENCE OF 113-121. RX PubMed=3692165; RA Golubic M., Budimir O., Schoepfer R., Kasahara M., Mayer W.E., RA Figueroa F., Klein J.; RT "Nucleotide sequence analysis of class II genes borne by mouse t RT chromosomes."; RL Genet. Res. 50:137-146(1987). RN [4] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [5] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X00623; CAA25257.1; -; Genomic_DNA. DR EMBL; X00701; CAB51615.2; ALT_SEQ; Genomic_DNA. DR EMBL; X00702; CAB51615.2; JOINED; Genomic_DNA. DR EMBL; M36940; AAA39590.1; -; mRNA. DR EMBL; L38590; AAA57294.1; -; Genomic_DNA. DR CCDS; CCDS37584.1; -. DR PIR; A02226; HLMSE1. DR UniGene; Mm.22564; -. DR PDB; 1I3R; X-ray; 2.40 A; B/D/F/H=30-225. DR PDB; 1KT2; X-ray; 2.80 A; B/D=30-215. DR PDB; 1KTD; X-ray; 2.40 A; B/D=30-215. DR PDB; 3QIB; X-ray; 2.70 A; B=30-225. DR PDB; 3QIU; X-ray; 2.70 A; B=30-225. DR PDB; 3QIW; X-ray; 3.30 A; B=30-225. DR PDBsum; 1I3R; -. DR PDBsum; 1KT2; -. DR PDBsum; 1KTD; -. DR PDBsum; 3QIB; -. DR PDBsum; 3QIU; -. DR PDBsum; 3QIW; -. DR ProteinModelPortal; P04230; -. DR SMR; P04230; -. DR STRING; 10090.ENSMUSP00000074143; -. DR MaxQB; P04230; -. DR PaxDb; P04230; -. DR PRIDE; P04230; -. DR MGI; MGI:95901; H2-Eb1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P04230; -. DR PhylomeDB; P04230; -. DR ChiTaRS; H2-Eb1; mouse. DR EvolutionaryTrace; P04230; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-EB1; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; ISO:MGI. DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Immunity; Membrane; MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 26 FT CHAIN 27 264 H-2 class II histocompatibility antigen, FT E-B beta chain. FT /FTId=PRO_0000019000. FT TOPO_DOM 27 225 Extracellular. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TOPO_DOM 247 264 Cytoplasmic. {ECO:0000255}. FT DOMAIN 124 214 Ig-like C1-type. FT REGION 27 121 Beta-1. FT REGION 122 225 Beta-2. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 38 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 144 200 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT STRAND 34 45 {ECO:0000244|PDB:1I3R}. FT HELIX 47 49 {ECO:0000244|PDB:1I3R}. FT STRAND 50 59 {ECO:0000244|PDB:1I3R}. FT STRAND 62 68 {ECO:0000244|PDB:1I3R}. FT TURN 69 71 {ECO:0000244|PDB:1I3R}. FT STRAND 73 78 {ECO:0000244|PDB:1I3R}. FT HELIX 79 81 {ECO:0000244|PDB:1I3R}. FT HELIX 82 89 {ECO:0000244|PDB:1I3R}. FT HELIX 92 104 {ECO:0000244|PDB:1I3R}. FT HELIX 106 113 {ECO:0000244|PDB:1I3R}. FT TURN 114 119 {ECO:0000244|PDB:1I3R}. FT STRAND 125 130 {ECO:0000244|PDB:1I3R}. FT STRAND 134 136 {ECO:0000244|PDB:1I3R}. FT STRAND 141 152 {ECO:0000244|PDB:1I3R}. FT STRAND 155 160 {ECO:0000244|PDB:1I3R}. FT STRAND 163 165 {ECO:0000244|PDB:1I3R}. FT STRAND 167 171 {ECO:0000244|PDB:1I3R}. FT STRAND 178 180 {ECO:0000244|PDB:1I3R}. FT STRAND 182 189 {ECO:0000244|PDB:1I3R}. FT STRAND 197 203 {ECO:0000244|PDB:1I3R}. FT STRAND 211 216 {ECO:0000244|PDB:1I3R}. SQ SEQUENCE 264 AA; 30166 MW; BF1264C41AF8D1C0 CRC64; MVWLPRVPCV AAVILLLTVL SPPMALVRDS RPWFLEYCKS ECHFYNGTQR VRLLERYFYN LEENLRFDSD VGEFHAVTEL GRPDAENWNS QPEFLEQKRA EVDTVCRHNY EISDKFLVRR RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL GAGLFIYFRN QKGQSGLQPT GLLS // ID HB22_MOUSE Reviewed; 264 AA. AC P01915; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 25-OCT-2017, entry version 104. DE RecName: Full=H-2 class II histocompatibility antigen, E-D beta chain; DE Flags: Precursor; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6310581; DOI=10.1073/pnas.80.18.5520; RA Saito H., Maki R.A., Clayton L.K., Tonegawa S.; RT "Complete primary structures of the E beta chain and gene of the mouse RT major histocompatibility complex."; RL Proc. Natl. Acad. Sci. U.S.A. 80:5520-5524(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-31. RX PubMed=6087163; DOI=10.1038/310594a0; RA Gillies S.D., Folsom V., Tonegawa S.; RT "Cell type-specific enhancer element associated with a mouse MHC gene, RT E beta."; RL Nature 310:594-597(1984). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- MISCELLANEOUS: The structure of the E beta gene is more similar to CC class I MHC genes than to class II, in that, unlike either the E CC alpha or DR alpha genes, (1) the core portion of the E beta CC cytoplasmic segment is encoded by its own exon and (2) the sixth CC exon of the E beta chain is not split into two exons, but rather CC encodes both the carboxyl end of the cytoplasmic segment and the CC entire 3'-UTR. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X00777; CAA25354.1; -; Genomic_DNA. DR EMBL; K00123; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A02225; HLMSEB. DR UniGene; Mm.22564; -. DR ProteinModelPortal; P01915; -. DR SMR; P01915; -. DR MaxQB; P01915; -. DR PeptideAtlas; P01915; -. DR PRIDE; P01915; -. DR HOVERGEN; HBG012730; -. DR Proteomes; UP000000589; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 31 FT CHAIN 32 264 H-2 class II histocompatibility antigen, FT E-D beta chain. FT /FTId=PRO_0000019001. FT TOPO_DOM 32 225 Extracellular. {ECO:0000255}. FT TRANSMEM 226 248 Helical. {ECO:0000255}. FT TOPO_DOM 249 264 Cytoplasmic. {ECO:0000255}. FT DOMAIN 124 214 Ig-like C1-type. FT REGION 32 121 Beta-1. FT REGION 122 215 Beta-2. FT REGION 216 225 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 144 200 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 264 AA; 30049 MW; 29117F30B8A56942 CRC64; MVWLPRVPCV AAVILLLTVL SPPVALVRDT RPRFLEYVTS ECHFYNGTQH VRFLERFIYN REENLRFDSD VGEYRAVTEL GRPDAENWNS QPEILEDARA SVDTYCRHNY EISDKFLVRR RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEETGIV STGLVRNGDW TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL GAGLFIYFRN QKGQSGLQPT GLLS // ID HB23_MOUSE Reviewed; 232 AA. AC P04231; O78225; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-1987, sequence version 1. DT 28-FEB-2018, entry version 115. DE RecName: Full=H-2 class II histocompatibility antigen, E-S beta chain; DE Flags: Fragment; GN Name=H2-Eb1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2986145; DOI=10.1073/pnas.82.9.2910; RA Mengle-Gaw L., McDevitt H.O.; RT "Predicted protein sequence of the murine I-E-beta S-polypeptide chain RT from cDNA and genomic clones."; RL Proc. Natl. Acad. Sci. U.S.A. 82:2910-2914(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 81-89. RX PubMed=3692165; RA Golubic M., Budimir O., Schoepfer R., Kasahara M., Mayer W.E., RA Figueroa F., Klein J.; RT "Nucleotide sequence analysis of class II genes borne by mouse t RT chromosomes."; RL Genet. Res. 50:137-146(1987). RN [3] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [4] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M11355; AAA39644.1; -; mRNA. DR EMBL; L38589; AAA57293.1; -; Genomic_DNA. DR PIR; A02227; HLMSE2. DR UniGene; Mm.22564; -. DR ProteinModelPortal; P04231; -. DR SMR; P04231; -. DR MaxQB; P04231; -. DR PRIDE; P04231; -. DR MGI; MGI:95901; H2-Eb1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR ChiTaRS; H2-Eb1; mouse. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-EB1; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; ISO:MGI. DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT CHAIN <1 232 H-2 class II histocompatibility antigen, FT E-S beta chain. FT /FTId=PRO_0000080754. FT TOPO_DOM <1 193 Extracellular. {ECO:0000255}. FT TRANSMEM 194 216 Helical. {ECO:0000255}. FT TOPO_DOM 217 232 Cytoplasmic. {ECO:0000255}. FT DOMAIN 92 182 Ig-like C1-type. FT REGION <1 90 Beta-1. FT REGION 91 193 Beta-2. FT CARBOHYD 14 14 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 10 74 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 112 168 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT NON_TER 1 1 SQ SEQUENCE 232 AA; 26647 MW; 8960CFC0BD6A8CB4 CRC64; WFLEYSTSEC HFYNGTQRVR LLERYFYNLE ENLRFDSDVG EFRAVTELGR PDAENWNSQP EFLEQRRAAV DTYCRHNYEI LDKFLVPRRV EPTVTVYPTK TQPLEHHNLL VCSVSDFYPG NIEVRWFRNG KEEKTGIVST GLVRNGDWTF QTLVMLETVP QSGEVYTCQV EHPSLTDPVT VEWKAQSTSA QNKMLSGVGG FVLGLLFLGA GLFIYFRNQK GQSGLQPTGL LS // ID HB24_MOUSE Reviewed; 264 AA. AC P20040; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 31-JAN-2018, entry version 106. DE RecName: Full=H-2 class II histocompatibility antigen, E-Q beta chain; DE AltName: Full=E-W17; DE Flags: Precursor; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2460545; RA Vu T.H., Tacchini-Cottier F.M., Day C.E., Begovich A.B., Jones P.P.; RT "Molecular basis for the defective expression of the mouse Ew17 beta RT gene."; RL J. Immunol. 141:3654-3661(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2106558; RA Begovich A.B., Vu T.H., Jones P.P.; RT "Characterization of the molecular defects in the mouse E beta f and E RT beta q genes. Implications for the origin of MHC polymorphism."; RL J. Immunol. 144:1957-1964(1990). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M23693; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M35682; AAA39595.1; -; Genomic_DNA. DR EMBL; M35680; AAA39595.1; JOINED; Genomic_DNA. DR EMBL; M35681; AAA39595.1; JOINED; Genomic_DNA. DR PIR; A30529; A30529. DR UniGene; Mm.22564; -. DR ProteinModelPortal; P20040; -. DR SMR; P20040; -. DR MaxQB; P20040; -. DR PRIDE; P20040; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR Proteomes; UP000000589; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 26 FT CHAIN 27 264 H-2 class II histocompatibility antigen, FT E-Q beta chain. FT /FTId=PRO_0000019002. FT TOPO_DOM 27 225 Extracellular. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TOPO_DOM 247 264 Cytoplasmic. {ECO:0000255}. FT DOMAIN 124 214 Ig-like C1-type. FT REGION 27 121 Beta-1. FT REGION 122 225 Beta-2. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 38 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 144 200 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 264 AA; 30205 MW; FF81C532A9B72D7A CRC64; MVWLPRVPCV AAVILLLTVL SPPVALVRDS RPWFLEYCKS ECHFYNGTQR VRFLKRYFYN LEENLRFDSD VGEFRAVTEL GRPDAENWNS QPEILEQKRA AVDTYCRHNY EIFDNFLVRR RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL GAGLFIYFRN QKGQSGLQPT GLLS // ID HB2A_MOUSE Reviewed; 265 AA. AC P14483; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 12-SEP-2018, entry version 152. DE RecName: Full=H-2 class II histocompatibility antigen, A beta chain; DE Flags: Precursor; GN Name=H2-Ab1; Synonyms=H2-iabeta; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6411350; DOI=10.1016/0092-8674(83)90148-4; RA Larhammar D., Hammerling U., Denaro M., Lund T., Flavell R.A., RA Rask L., Peterson P.A.; RT "Structure of the murine immune response I-A beta locus: sequence of RT the I-A beta gene and an adjacent beta-chain second domain exon."; RL Cell 34:179-188(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Rowen L., Qin S., Ahearn M.E., Loretz C., Faust J., Lasky S., RA Mahairas G., Hood L.E.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [4] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; V01527; CAA24768.1; -; Genomic_DNA. DR EMBL; AF027865; AAB81531.1; -; Genomic_DNA. DR CCDS; CCDS37583.1; -. DR PIR; I48656; I48656. DR RefSeq; NP_996988.2; NM_207105.3. DR UniGene; Mm.254067; -. DR PDB; 1LNU; X-ray; 2.50 A; B/D/F/H=27-216. DR PDB; 1MUJ; X-ray; 2.15 A; B=28-216. DR PDB; 3C5Z; X-ray; 2.55 A; D/H=30-216. DR PDB; 3C60; X-ray; 3.05 A; D/H=30-216. DR PDB; 3C6L; X-ray; 3.40 A; D/H=30-216. DR PDB; 3RDT; X-ray; 2.70 A; D=30-218. DR PDB; 4P23; X-ray; 2.25 A; D=31-219. DR PDB; 4P46; X-ray; 2.85 A; D=31-219. DR PDB; 4P5T; X-ray; 3.26 A; D/H=27-218. DR PDBsum; 1LNU; -. DR PDBsum; 1MUJ; -. DR PDBsum; 3C5Z; -. DR PDBsum; 3C60; -. DR PDBsum; 3C6L; -. DR PDBsum; 3RDT; -. DR PDBsum; 4P23; -. DR PDBsum; 4P46; -. DR PDBsum; 4P5T; -. DR ProteinModelPortal; P14483; -. DR SMR; P14483; -. DR BioGrid; 200147; 1. DR IntAct; P14483; 1. DR MINT; P14483; -. DR STRING; 10090.ENSMUSP00000041008; -. DR EPD; P14483; -. DR PaxDb; P14483; -. DR PRIDE; P14483; -. DR Ensembl; ENSMUST00000040828; ENSMUSP00000041008; ENSMUSG00000073421. DR GeneID; 14961; -. DR KEGG; mmu:14961; -. DR UCSC; uc008ccb.2; mouse. DR CTD; 14961; -. DR MGI; MGI:103070; H2-Ab1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR PhylomeDB; P14483; -. DR TreeFam; TF336626; -. DR Reactome; R-MMU-202424; Downstream TCR signaling. DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-MMU-202433; Generation of second messenger molecules. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-389948; PD-1 signaling. DR ChiTaRS; H2-Ab1; mouse. DR EvolutionaryTrace; P14483; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000073421; Expressed in 199 organ(s), highest expression level in mesenteric lymph node. DR CleanEx; MM_H2-AB1; -. DR ExpressionAtlas; P14483; baseline and differential. DR Genevisible; P14483; MM. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IDA:MGI. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI. DR GO; GO:1990405; F:protein antigen binding; IPI:BHF-UCL. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0015643; F:toxic substance binding; IPI:BHF-UCL. DR GO; GO:0008134; F:transcription factor binding; IDA:BHF-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IDA:MGI. DR GO; GO:0002344; P:B cell affinity maturation; IDA:BHF-UCL. DR GO; GO:0071346; P:cellular response to interferon-gamma; IDA:BHF-UCL. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISO:MGI. DR GO; GO:0006955; P:immune response; IMP:MGI. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISO:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI. DR GO; GO:0046635; P:positive regulation of alpha-beta T cell activation; IDA:BHF-UCL. DR GO; GO:0002579; P:positive regulation of antigen processing and presentation; IDA:BHF-UCL. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IDA:BHF-UCL. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Immunity; Membrane; MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 27 FT CHAIN 28 265 H-2 class II histocompatibility antigen, FT A beta chain. FT /FTId=PRO_0000018993. FT TOPO_DOM 28 226 Extracellular. {ECO:0000255}. FT TRANSMEM 227 247 Helical. {ECO:0000255}. FT TOPO_DOM 248 265 Cytoplasmic. {ECO:0000255}. FT DOMAIN 125 213 Ig-like C1-type. FT REGION 28 122 Beta-1. FT REGION 123 216 Beta-2. FT REGION 217 226 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 145 201 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT STRAND 34 45 {ECO:0000244|PDB:1MUJ}. FT TURN 46 49 {ECO:0000244|PDB:1MUJ}. FT STRAND 50 59 {ECO:0000244|PDB:1MUJ}. FT STRAND 62 68 {ECO:0000244|PDB:1MUJ}. FT TURN 69 71 {ECO:0000244|PDB:1MUJ}. FT STRAND 73 75 {ECO:0000244|PDB:1MUJ}. FT HELIX 79 81 {ECO:0000244|PDB:1MUJ}. FT HELIX 82 89 {ECO:0000244|PDB:1MUJ}. FT HELIX 92 104 {ECO:0000244|PDB:1MUJ}. FT HELIX 106 111 {ECO:0000244|PDB:1MUJ}. FT HELIX 113 116 {ECO:0000244|PDB:1MUJ}. FT HELIX 118 120 {ECO:0000244|PDB:1MUJ}. FT STRAND 126 132 {ECO:0000244|PDB:1MUJ}. FT TURN 137 139 {ECO:0000244|PDB:1LNU}. FT STRAND 142 153 {ECO:0000244|PDB:1MUJ}. FT STRAND 156 161 {ECO:0000244|PDB:1MUJ}. FT STRAND 164 166 {ECO:0000244|PDB:1MUJ}. FT STRAND 170 172 {ECO:0000244|PDB:1MUJ}. FT STRAND 179 181 {ECO:0000244|PDB:1MUJ}. FT STRAND 183 190 {ECO:0000244|PDB:1MUJ}. FT STRAND 199 204 {ECO:0000244|PDB:1MUJ}. FT STRAND 212 216 {ECO:0000244|PDB:1MUJ}. SQ SEQUENCE 265 AA; 30128 MW; DA5118187D254BD6 CRC64; MALQIPSLLL SAAVVVLMVL SSPGTEGGDS ERHFVYQFMG ECYFTNGTQR IRYVTRYIYN REEYVRYDSD VGEHRAVTEL GRPDAEYWNS QPEILERTRA ELDTVCRHNY EGPETHTSLR RLEQPNVVIS LSRTEALNHH NTLVCSVTDF YPAKIKVRWF RNGQEETVGV SSTQLIRNGD WTFQVLVMLE MTPRRGEVYT CHVEHPSLKS PITVEWRAQS ESAWSKMLSG IGGCVLGVIF LGLGLFIRHR SQKGPRGPPP AGLLQ // ID HB2A_RAT Reviewed; 233 AA. AC P06341; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 23-MAY-2018, entry version 89. DE RecName: Full=Rano class II histocompatibility antigen, A beta chain; DE AltName: Full=RT1 class II histocompatibility antigen, A beta chain; DE Flags: Fragment; GN Name=RT1-B; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3865896; DOI=10.1007/BF00430314; RA Eccles S.J., McMaster W.R.; RT "DNA sequence analysis of a rat RT1 class II A beta gene."; RL Immunogenetics 22:653-663(1985). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M15358; AAA74477.1; -; Genomic_DNA. DR EMBL; M15354; AAA74477.1; JOINED; Genomic_DNA. DR EMBL; M15355; AAA74477.1; JOINED; Genomic_DNA. DR EMBL; M15356; AAA74477.1; JOINED; Genomic_DNA. DR EMBL; M15357; AAA74477.1; JOINED; Genomic_DNA. DR PIR; A02235; HLRTAB. DR ProteinModelPortal; P06341; -. DR SMR; P06341; -. DR PRIDE; P06341; -. DR RGD; 3467; RT1-B. DR HOVERGEN; HBG012730; -. DR InParanoid; P06341; -. DR PhylomeDB; P06341; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome; Glycoprotein; Immunity; Membrane; MHC II; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN <1 233 Rano class II histocompatibility antigen, FT A beta chain. FT /FTId=PRO_0000080755. FT TOPO_DOM <1 194 Extracellular. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. FT TOPO_DOM 216 233 Cytoplasmic. {ECO:0000255}. FT DOMAIN 93 181 Ig-like C1-type. FT REGION <1 80 Beta-1. FT REGION 81 184 Beta-2. FT REGION 185 194 Connecting peptide. FT CARBOHYD 14 14 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT NON_TER 1 1 SQ SEQUENCE 233 AA; 26827 MW; 293922C66A768E75 CRC64; DFVYQFKGLC YYTNGTQRIR SVDRRFYNQE EFLRYDSDVG EFRALTELGR SWADDWNSQK EILEQKRAEM DTVCRYNYEE TEVPTSLRRL ERPNVAISLS RTEALNHHNL LVCSVTDFYP AQIKVRWFRN GQEETTGVVS TQLIKNGDWT FQILVMLEMT PQRGDVYTCH VDHASLESPV TVEWRAQSES AQSKMLSGIG GLVLGVIFLG LGLFIRHKRQ KGPQGPPPAG LLQ // ID HB2B_RAT Reviewed; 263 AA. AC P29826; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 23-MAY-2018, entry version 112. DE RecName: Full=Rano class II histocompatibility antigen, B-1 beta chain; DE AltName: Full=RT1 class II histocompatibility antigen, B-1 beta chain; DE AltName: Full=RT1.B-beta(1); DE Flags: Precursor; GN Name=RT1-Bb; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Lewis; TISSUE=Bone marrow; RX PubMed=1859846; DOI=10.1016/0167-4781(91)90189-S; RA Syha-Jedelhauser J., Wendling U., Reske K.; RT "Complete coding nucleotide sequence of cDNA for the class II RT1.B RT beta I chain of the Lewis rat."; RL Biochim. Biophys. Acta 1089:414-416(1991). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X56596; CAA39934.1; -; mRNA. DR PIR; S16999; HLRTBB. DR UniGene; Rn.202964; -. DR ProteinModelPortal; P29826; -. DR SMR; P29826; -. DR STRING; 10116.ENSRNOP00000000525; -. DR PaxDb; P29826; -. DR PRIDE; P29826; -. DR UCSC; RGD:3469; rat. DR RGD; 3469; RT1-Bb. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR InParanoid; P29826; -. DR PhylomeDB; P29826; -. DR PRO; PR:P29826; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0009986; C:cell surface; IDA:RGD. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:RGD. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEP:RGD. DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IEP:RGD. DR GO; GO:0071315; P:cellular response to morphine; IEP:RGD. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:RGD. DR GO; GO:0009623; P:response to parasitic fungus; IEP:RGD. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; KW Isopeptide bond; Membrane; MHC II; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Ubl conjugation. FT SIGNAL 1 27 {ECO:0000255}. FT CHAIN 28 263 Rano class II histocompatibility antigen, FT B-1 beta chain. FT /FTId=PRO_0000019005. FT TOPO_DOM 28 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 263 Cytoplasmic. {ECO:0000255}. FT DOMAIN 123 211 Ig-like C1-type. FT REGION 28 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 104 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 143 199 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT CROSSLNK 251 251 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT {ECO:0000250|UniProtKB:P13762}. SQ SEQUENCE 263 AA; 29935 MW; 11127ABBE6139204 CRC64; MALQTPSFLL PAAVVVLMVL SSPGTEGRDS PRDFVYQFKG LCYYTNGTQR IRDVIRYIYN QEEYLRYDSD VGEYRALTEL GRPSAEYFNK QYLEQTRAEL DTVCRHNYEG SEVRTSLRRL EQPNVAISLS RTEALNHHNL LVCSVTDFYP AQIKVRWFRN GQEETAGVVS TQLIRNGDWT FQILVMLEMT PQRGEVYICH VDHPSLESPV TVEWRAQSES AQSKMLSGIG GFVLGVIFLG LGLFIRHKRQ KGPRGPPPAG LLQ // ID HB2C_PIG Reviewed; 261 AA. AC P15982; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 25-OCT-2017, entry version 96. DE RecName: Full=SLA class II histocompatibility antigen, DQ haplotype C beta chain; DE Flags: Precursor; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2391424; RA Gustafsson K., Leguern C., Hirsch F., Germana S., Pratt K., RA Sachs D.H.; RT "Class II genes of miniature swine. IV. Characterization and RT expression of two allelic class II DQB cDNA clones."; RL J. Immunol. 145:1946-1951(1990). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M31497; AAA31084.1; -; mRNA. DR EMBL; M32117; AAA53110.1; -; mRNA. DR PIR; A60404; A60404. DR RefSeq; NP_001107166.1; NM_001113694.1. DR UniGene; Ssc.11063; -. DR ProteinModelPortal; P15982; -. DR SMR; P15982; -. DR STRING; 9823.ENSSSCP00000001575; -. DR PaxDb; P15982; -. DR PeptideAtlas; P15982; -. DR PRIDE; P15982; -. DR GeneID; 100037921; -. DR KEGG; ssc:100037921; -. DR CTD; 100037921; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR Proteomes; UP000008227; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 31 FT CHAIN 32 261 SLA class II histocompatibility antigen, FT DQ haplotype C beta chain. FT /FTId=PRO_0000019008. FT TOPO_DOM 32 230 Extracellular. {ECO:0000255}. FT TRANSMEM 231 251 Helical. {ECO:0000255}. FT TOPO_DOM 252 261 Cytoplasmic. {ECO:0000255}. FT DOMAIN 129 233 Ig-like C1-type. FT REGION 32 126 Beta-1. FT REGION 127 220 Beta-2. FT REGION 221 230 Connecting peptide. FT CARBOHYD 51 51 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 47 111 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 149 205 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 261 AA; 29550 MW; AA9581F2A3B1969D CRC64; MSGMVALRLP RGLWTAALTV MLVVLGAPVA EGRDSPQDFV FQFKGECYFY NGTQRVRGVA RYIYNQEEHL RFDSDVGEFR AVTPLGRPEA DSWNSQKDVL EQMRAEVDRV CKHNYQIEEG TTLQRRVQPT VTISPSKAEA LNHHNLLVCA VTDFYPSQVK VQWFRNGQEE TAGVVSTPLI RNGDWTYQVL VMLEMNLQRG DVYTCRVEHS SLQNPILVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLF IRHRSQKGLV R // ID HB2D_CANLF Reviewed; 266 AA. AC P18470; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-JUN-2018, entry version 95. DE RecName: Full=DLA class II histocompatibility antigen, DR-1 beta chain; DE Flags: Precursor; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2370085; DOI=10.1007/BF02115018; RA Sarmiento U.M., Storb R.; RT "Nucleotide sequence of a dog DRB cDNA clone."; RL Immunogenetics 31:396-399(1990). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M29611; AAA30874.1; -; mRNA. DR PIR; A45844; A45844. DR RefSeq; NP_001014768.1; NM_001014768.1. DR UniGene; Cfa.18984; -. DR ProteinModelPortal; P18470; -. DR SMR; P18470; -. DR STRING; 9615.ENSCAFP00000001156; -. DR PaxDb; P18470; -. DR GeneID; 474860; -. DR KEGG; cfa:474860; -. DR CTD; 3123; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR Proteomes; UP000002254; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 29 FT CHAIN 30 266 DLA class II histocompatibility antigen, FT DR-1 beta chain. FT /FTId=PRO_0000019010. FT TOPO_DOM 30 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 266 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 214 Ig-like C1-type. FT REGION 30 124 Beta-1. FT REGION 125 227 Beta-2. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 266 AA; 30151 MW; 4E8297BBF1ACDD67 CRC64; MVCLCFLGGS WMTALMLILM VLNPPFAWAR DTPPHFLEVA KSECYFTNGT ERVRFVERYI HNREEFVRFD SDVGEFRAVT ELGRPVAESW NGQKEILEQE RATVDTYCRH NYGVIESFTV QRRVEPTVTV YPTKTQTLQH HNLLVCSVNG FYPGHIEVRW LRNGQEEEAG VVSTGLIRNG DWTFQILVML EIVPQSGEVY TCQVEHPSLT SPVTVEWRAQ SDSAQSKMLS GIGGFVLGLL FLAVGLFIYF RNQKGHSGLQ PTGLLS // ID HB2D_MOUSE Reviewed; 265 AA. AC P01921; O19456; O19457; O19458; Q31133; Q31138; Q31139; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 12-SEP-2018, entry version 134. DE RecName: Full=H-2 class II histocompatibility antigen, A-D beta chain; DE Flags: Precursor; GN Name=H2-Ab1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BALB/cJ; RX PubMed=6410508; DOI=10.1126/science.6410508; RA Malissen M., Hunkapiller T., Hood L.E.; RT "Nucleotide sequence of a light chain gene of the mouse I-A subregion: RT A beta d."; RL Science 221:750-754(1983). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-265. RX PubMed=6407114; DOI=10.1126/science.6407114; RA Choi E.C., McIntyre K., Germain R.N., Seidman J.G.; RT "Murine i-a-beta chain polymorphism: nucleotide sequences of three RT allelic i-a-beta genes."; RL Science 221:283-286(1983). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 124-261. RX PubMed=2555693; DOI=10.1128/MCB.9.10.4402; RA Ghogawala Z., Choi E., Daly K.R., Blanco L.R., Griffith I.J., RA Glimcher L.H.; RT "An intronic 10-base-pair deletion in a class II A beta gene affects RT RNA processing."; RL Mol. Cell. Biol. 9:4402-4408(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 215-265. RX PubMed=6311906; RA Robinson R.R., Germain R.N., McKean D.J., Mescher M., Seidman J.G.; RT "Extensive polymorphism surrounding the murine Ia A-beta chain gene."; RL J. Immunol. 131:2025-2031(1983). RN [5] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [6] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; K00008; AAA39548.1; -; Genomic_DNA. DR EMBL; K00007; AAA39548.1; JOINED; Genomic_DNA. DR EMBL; M29248; AAA39543.1; -; Genomic_DNA. DR EMBL; K00113; AAA39544.1; -; Genomic_DNA. DR EMBL; K00109; AAA39544.1; JOINED; Genomic_DNA. DR EMBL; K00110; AAA39544.1; JOINED; Genomic_DNA. DR EMBL; K00112; AAA39544.1; JOINED; Genomic_DNA. DR EMBL; K00111; AAA39544.1; JOINED; Genomic_DNA. DR EMBL; K01143; AAA39545.1; -; mRNA. DR PIR; A02236; HLMSAB. DR UniGene; Mm.254067; -. DR PDB; 1IAO; X-ray; 2.60 A; B=28-216. DR PDB; 2IAD; X-ray; 2.40 A; B=28-216. DR PDBsum; 1IAO; -. DR PDBsum; 2IAD; -. DR ProteinModelPortal; P01921; -. DR SMR; P01921; -. DR IntAct; P01921; 1. DR MINT; P01921; -. DR MaxQB; P01921; -. DR PeptideAtlas; P01921; -. DR PRIDE; P01921; -. DR MGI; MGI:103070; H2-Ab1. DR HOVERGEN; HBG012730; -. DR InParanoid; P01921; -. DR ChiTaRS; H2-Ab1; mouse. DR EvolutionaryTrace; P01921; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-AB1; -. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IDA:MGI. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IDA:MGI. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISO:MGI. DR GO; GO:0006955; P:immune response; IMP:MGI. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISO:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Immunity; Membrane; MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 27 FT CHAIN 28 265 H-2 class II histocompatibility antigen, FT A-D beta chain. FT /FTId=PRO_0000018994. FT TOPO_DOM 28 226 Extracellular. {ECO:0000255}. FT TRANSMEM 227 247 Helical. {ECO:0000255}. FT TOPO_DOM 248 265 Cytoplasmic. {ECO:0000255}. FT DOMAIN 125 213 Ig-like C1-type. FT REGION 28 122 Beta-1. FT REGION 123 216 Beta-2. FT REGION 217 226 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 145 201 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT STRAND 35 45 {ECO:0000244|PDB:2IAD}. FT TURN 46 49 {ECO:0000244|PDB:2IAD}. FT STRAND 50 59 {ECO:0000244|PDB:2IAD}. FT STRAND 62 68 {ECO:0000244|PDB:2IAD}. FT TURN 69 71 {ECO:0000244|PDB:2IAD}. FT STRAND 73 78 {ECO:0000244|PDB:2IAD}. FT HELIX 79 81 {ECO:0000244|PDB:2IAD}. FT HELIX 82 90 {ECO:0000244|PDB:2IAD}. FT HELIX 92 104 {ECO:0000244|PDB:2IAD}. FT HELIX 106 111 {ECO:0000244|PDB:2IAD}. FT HELIX 113 116 {ECO:0000244|PDB:2IAD}. FT HELIX 118 120 {ECO:0000244|PDB:2IAD}. FT STRAND 126 131 {ECO:0000244|PDB:2IAD}. FT STRAND 133 139 {ECO:0000244|PDB:2IAD}. FT STRAND 143 153 {ECO:0000244|PDB:2IAD}. FT STRAND 156 161 {ECO:0000244|PDB:2IAD}. FT STRAND 164 166 {ECO:0000244|PDB:2IAD}. FT STRAND 170 172 {ECO:0000244|PDB:2IAD}. FT STRAND 179 181 {ECO:0000244|PDB:2IAD}. FT STRAND 183 189 {ECO:0000244|PDB:2IAD}. FT STRAND 199 204 {ECO:0000244|PDB:2IAD}. FT STRAND 212 216 {ECO:0000244|PDB:1IAO}. SQ SEQUENCE 265 AA; 29954 MW; 3A6274DD8920F564 CRC64; MALQIPSLLL SAAVVVLMVL SSPRTEGGNS ERHFVVQFKG ECYYTNGTQR IRLVTRYIYN REEYVRYDSD VGEYRAVTEL GRPDAEYWNS QPEILERTRA EVDTACRHNY EGPETSTSLR RLEQPNVAIS LSRTEALNHH NTLVCSVTDF YPAKIKVRWF RNGQEETVGV SSTQLIRNGD WTFQVLVMLE MTPHQGEVYT CHVEHPSLKS PITVEWRAQS ESARSKMLSG IGGCVLGVIF LGLGLFIRHR SQKGPRGPPP AGLLQ // ID HB2D_PIG Reviewed; 258 AA. AC P15983; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1990, sequence version 1. DT 20-JUN-2018, entry version 89. DE RecName: Full=SLA class II histocompatibility antigen, DQ haplotype D beta chain; DE Flags: Precursor; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2391424; RA Gustafsson K., Leguern C., Hirsch F., Germana S., Pratt K., RA Sachs D.H.; RT "Class II genes of miniature swine. IV. Characterization and RT expression of two allelic class II DQB cDNA clones."; RL J. Immunol. 145:1946-1951(1990). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M31498; AAA31085.1; -; mRNA. DR UniGene; Ssc.11063; -. DR ProteinModelPortal; P15983; -. DR SMR; P15983; -. DR PeptideAtlas; P15983; -. DR PRIDE; P15983; -. DR HOVERGEN; HBG012730; -. DR Proteomes; UP000008227; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 31 FT CHAIN 32 258 SLA class II histocompatibility antigen, FT DQ haplotype D beta chain. FT /FTId=PRO_0000019009. FT TOPO_DOM 32 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TOPO_DOM 249 258 Cytoplasmic. {ECO:0000255}. FT DOMAIN 126 230 Ig-like C1-type. FT REGION 32 123 Beta-1. FT REGION 124 217 Beta-2. FT REGION 218 227 Connecting peptide. FT CARBOHYD 48 48 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 44 108 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 146 202 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 258 AA; 29262 MW; E3AC75110AED47C3 CRC64; MVALRLPRGL WTAALTVMLV VLGAPVAEGR DSPQDFVVQF KGECYFYNGT QRVWSVDRYI YNQEEFLRFD SDMGEYRAVT PLGRPDADYL NGQKEALEQK RAELDTVCKH NYQIEEGTTL QRRVQPTVTI SPSKAEALNH HNLLVCAVTD FYPSQVKVQW FRNGQEETAG VVSTPLIRNG DWTYQVLVML EMNLQRGDVY TCRVEHSSLQ SPILVEWRAQ SESAQSKMLS GVGGFVLGLI FLGLGLFIRH RSQKGLVR // ID HB2D_RAT Reviewed; 264 AA. AC P18211; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 20-JUN-2018, entry version 112. DE RecName: Full=Rano class II histocompatibility antigen, D-1 beta chain; DE AltName: Full=RT1 class II histocompatibility antigen, D-1 beta chain; DE Flags: Precursor; GN Name=RT1-Db1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Lewis familiaris; TISSUE=Bone marrow; RX PubMed=2388838; DOI=10.1093/nar/18.15.4598; RA Syha-Jedelhauser J., Reske K.; RT "Sequence of rat cDNA clone pLR beta 112 coding for the RT1.D beta I RT chain."; RL Nucleic Acids Res. 18:4598-4598(1990). CC -!- FUNCTION: Involved in the presentation of foreign antigens to the CC immune system. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X53054; CAA37221.1; -; mRNA. DR PIR; B60497; B60497. DR PIR; S10989; S10989. DR UniGene; Rn.33311; -. DR ProteinModelPortal; P18211; -. DR SMR; P18211; -. DR iPTMnet; P18211; -. DR PhosphoSitePlus; P18211; -. DR PRIDE; P18211; -. DR UCSC; RGD:1593282; rat. DR RGD; 1593282; RT1-Db1. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR InParanoid; P18211; -. DR PhylomeDB; P18211; -. DR PRO; PR:P18211; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0071548; P:response to dexamethasone; IEP:RGD. DR GO; GO:0010033; P:response to organic substance; IEP:RGD. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 26 FT CHAIN 27 264 Rano class II histocompatibility antigen, FT D-1 beta chain. FT /FTId=PRO_0000019006. FT TOPO_DOM 27 226 Extracellular. {ECO:0000255}. FT TRANSMEM 227 248 Helical. {ECO:0000255}. FT TOPO_DOM 249 264 Cytoplasmic. {ECO:0000255}. FT DOMAIN 124 228 Ig-like C1-type. FT REGION 27 120 Beta-1. FT REGION 121 215 Beta-2. FT REGION 216 226 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 144 200 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 264 AA; 29876 MW; 158F357355177DA1 CRC64; MVWLARDSCV AAVILLLTVL SPPVALVRDP TPRFLEQVKG ECHFYNGTQR VRFLARYIYN REEYTRFDSD VGEFRAVTEL GRPSAEYYNK QKEYMEQLRA TVDTACKHDY EISESFLVPR TVEPKVTVYP SKTQPLEHHN LLVCSVSDFY PGSVEVRWFR NGEEEKDGLV STGLIRNGDW TFQLLVMLET VPQGGEVYTC QVEHPSLPSP VRVEWKAQST SAQNKKMSGV GGIVLGLLFL GAGLFVYFRN QKGQSGLQPT GLLN // ID HB2F_MOUSE Reviewed; 252 AA. AC P06346; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 12-SEP-2018, entry version 124. DE RecName: Full=H-2 class II histocompatibility antigen, A-F beta chain; DE Flags: Precursor; Fragment; GN Name=H2-Ab1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3086866; DOI=10.1073/pnas.83.11.3594; RA Estess P., Begovich A.B., Koo M., Jones P.P., McDevitt H.O.; RT "Sequence analysis and structure-function correlations of murine q, k, RT u, s, and f haplotype I-A beta cDNA clones."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3594-3598(1986). RN [2] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [3] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M13541; AAA39629.1; -; mRNA. DR PIR; A02241; HLMSBF. DR UniGene; Mm.254067; -. DR ProteinModelPortal; P06346; -. DR SMR; P06346; -. DR MINT; P06346; -. DR MaxQB; P06346; -. DR PRIDE; P06346; -. DR MGI; MGI:103070; H2-Ab1. DR HOVERGEN; HBG012730; -. DR ChiTaRS; H2-Ab1; mouse. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-AB1; -. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IDA:MGI. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IDA:MGI. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISO:MGI. DR GO; GO:0006955; P:immune response; IMP:MGI. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISO:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL <1 16 {ECO:0000250}. FT CHAIN 17 252 H-2 class II histocompatibility antigen, FT A-F beta chain. FT /FTId=PRO_0000018995. FT TOPO_DOM 17 213 Extracellular. {ECO:0000255}. FT TRANSMEM 214 234 Helical. {ECO:0000255}. FT TOPO_DOM 235 252 Cytoplasmic. {ECO:0000255}. FT DOMAIN 112 200 Ig-like C1-type. FT REGION 17 109 Beta-1. FT REGION 110 203 Beta-2. FT REGION 204 213 Connecting peptide. FT CARBOHYD 35 35 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 31 93 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 132 188 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT NON_TER 1 1 SQ SEQUENCE 252 AA; 28602 MW; E9D91C8A213E629B CRC64; AAVVVLMVLS SPGTEGGNSE RHFVSQFKGE CYFTNGTQRI RSVDRYIYNR EEYLRFDSDV GEYRAVTELG RSDAEYYNKQ YLERTRAELD TVCRHNYEGV ETPTSLRRLE QPNVVISLSR TEALNHHNTL VCSVTDFYPA KIKVRWFRNG QEETVGVSST QLIRNGDWTF QVLVMLEMAP RRGEVYTCHV EHPSLKSPIT VEWRAQSESA RSKMLSGIGG CVLGVIFLGL GLFIRYRSQK GPRGPPPAGL LQ // ID HB2I_MOUSE Reviewed; 264 AA. AC P18468; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 28-FEB-2018, entry version 121. DE RecName: Full=H-2 class II histocompatibility antigen, I-A beta chain; DE Flags: Precursor; GN Name=H2-Eb1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NOD; TISSUE=Spleen; RX PubMed=1855817; DOI=10.1007/BF00212313; RA Acha-Orbea H., Scarpellino L.; RT "Nonobese diabetic and nonobese nondiabetic mice have unique MHC class RT II haplotypes."; RL Immunogenetics 34:57-59(1991). RN [2] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [3] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 32-215, AND DISULFIDE BONDS. RX PubMed=14690592; DOI=10.1016/S1097-2765(03)00474-X; RA Krogsgaard M., Prado N., Adams E.J., He X.L., Chow D.C., Wilson D.B., RA Garcia K.C., Davis M.M.; RT "Evidence that structural rearrangements and/or flexibility during TCR RT binding can contribute to T cell activation."; RL Mol. Cell 12:1367-1378(2003). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X52641; CAA36863.1; -; mRNA. DR PIR; I48224; S11650. DR UniGene; Mm.22564; -. DR PDB; 1R5V; X-ray; 2.50 A; B/D=32-215. DR PDBsum; 1R5V; -. DR ProteinModelPortal; P18468; -. DR SMR; P18468; -. DR iPTMnet; P18468; -. DR PhosphoSitePlus; P18468; -. DR MaxQB; P18468; -. DR PRIDE; P18468; -. DR MGI; MGI:95901; H2-Eb1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR ChiTaRS; H2-Eb1; mouse. DR EvolutionaryTrace; P18468; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-EB1; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; ISS:BHF-UCL. DR GO; GO:0005765; C:lysosomal membrane; ISS:BHF-UCL. DR GO; GO:0042613; C:MHC class II protein complex; TAS:BHF-UCL. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:BHF-UCL. DR GO; GO:0034341; P:response to interferon-gamma; IDA:BHF-UCL. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Immunity; Membrane; MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 31 FT CHAIN 32 264 H-2 class II histocompatibility antigen, FT I-A beta chain. FT /FTId=PRO_0000019003. FT TOPO_DOM 32 225 Extracellular. {ECO:0000255}. FT TRANSMEM 226 248 Helical. {ECO:0000255}. FT TOPO_DOM 249 264 Cytoplasmic. {ECO:0000255}. FT DOMAIN 124 214 Ig-like C1-type. FT REGION 32 121 Beta-1. FT REGION 122 215 Beta-2. FT REGION 216 225 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 106 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:14690592}. FT DISULFID 144 200 {ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:14690592}. FT STRAND 34 45 {ECO:0000244|PDB:1R5V}. FT HELIX 47 49 {ECO:0000244|PDB:1R5V}. FT STRAND 50 59 {ECO:0000244|PDB:1R5V}. FT STRAND 62 68 {ECO:0000244|PDB:1R5V}. FT TURN 69 71 {ECO:0000244|PDB:1R5V}. FT STRAND 73 78 {ECO:0000244|PDB:1R5V}. FT HELIX 79 81 {ECO:0000244|PDB:1R5V}. FT HELIX 82 89 {ECO:0000244|PDB:1R5V}. FT HELIX 92 104 {ECO:0000244|PDB:1R5V}. FT HELIX 106 113 {ECO:0000244|PDB:1R5V}. FT TURN 114 116 {ECO:0000244|PDB:1R5V}. FT STRAND 125 131 {ECO:0000244|PDB:1R5V}. FT STRAND 133 135 {ECO:0000244|PDB:1R5V}. FT STRAND 141 152 {ECO:0000244|PDB:1R5V}. FT STRAND 155 160 {ECO:0000244|PDB:1R5V}. FT STRAND 167 171 {ECO:0000244|PDB:1R5V}. FT STRAND 178 180 {ECO:0000244|PDB:1R5V}. FT STRAND 182 189 {ECO:0000244|PDB:1R5V}. FT STRAND 198 203 {ECO:0000244|PDB:1R5V}. FT STRAND 211 215 {ECO:0000244|PDB:1R5V}. SQ SEQUENCE 264 AA; 30232 MW; 04529F5E2E527D7A CRC64; MVWLPRVPCV AAVILLLTVL SPPVALVRDS RPWFLEYCKS ECHFYNGTQR VRFLKRYFYN LEENLRFDSD VGEFRAVTEL GRPDAENWNS QPEILDEKRA AVDTYCRHNY EIFDNFLVPR RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL RAGLFIYFRN QKGQSGLQPT GLLS // ID HB2J_MOUSE Reviewed; 264 AA. AC P18469; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 12-SEP-2018, entry version 127. DE RecName: Full=H-2 class II histocompatibility antigen, I-E beta chain; DE Flags: Precursor; GN Name=H2-Eb1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3018929; DOI=10.1126/science.3018929; RA Kobori J.A., Strauss E., Minard K., Hood L.; RT "Molecular analysis of the hotspot of recombination in the murine RT major histocompatibility complex."; RL Science 234:173-179(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=NOD; TISSUE=Spleen; RX PubMed=1855817; DOI=10.1007/BF00212313; RA Acha-Orbea H., Scarpellino L.; RT "Nonobese diabetic and nonobese nondiabetic mice have unique MHC class RT II haplotypes."; RL Immunogenetics 34:57-59(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1918991; RA Padgett K.A., Shreffler D.C., Saha B.K.; RT "Molecular mapping of murine I region recombinants. III. Crossing over RT at two discrete sites within the beta 1-beta 2 intron of the E beta RT gene."; RL J. Immunol. 147:2764-2770(1991). RN [4] RP GLYCOSYLATION AT ASN-46. RX PubMed=3980466; RA Swiedler S.J., Freed J.H., Tarentino A.L., Plummer T.H. Jr., RA Hart G.W.; RT "Oligosaccharide microheterogeneity of the murine major RT histocompatibility antigens. Reproducible site-specific patterns of RT sialylation and branching in asparagine-linked oligosaccharides."; RL J. Biol. Chem. 260:4046-4054(1985). RN [5] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [6] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X52642; CAA36864.1; -; mRNA. DR PIR; I48422; I48422. DR UniGene; Mm.22564; -. DR ProteinModelPortal; P18469; -. DR SMR; P18469; -. DR MINT; P18469; -. DR iPTMnet; P18469; -. DR MaxQB; P18469; -. DR PRIDE; P18469; -. DR MGI; MGI:95901; H2-Eb1. DR HOVERGEN; HBG012730; -. DR ChiTaRS; H2-Eb1; mouse. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-EB1; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0031902; C:late endosome membrane; ISO:MGI. DR GO; GO:0005765; C:lysosomal membrane; ISO:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 31 FT CHAIN 32 264 H-2 class II histocompatibility antigen, FT I-E beta chain. FT /FTId=PRO_0000019004. FT TOPO_DOM 32 225 Extracellular. {ECO:0000255}. FT TRANSMEM 226 248 Helical. {ECO:0000255}. FT TOPO_DOM 249 264 Cytoplasmic. {ECO:0000255}. FT DOMAIN 124 214 Ig-like C1-type. FT REGION 32 121 Beta-1. FT REGION 122 215 Beta-2. FT REGION 216 225 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:3980466}. FT DISULFID 42 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 144 200 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 264 AA; 30141 MW; 93178C1AE63987FF CRC64; MVWLPRVPCV AAVILLLTVL SPPVALVRNS RPRFLEYSTS ECHFYNGTQR VRFLERYIYN REEYVRFDSD VGEYRAVTEL GRPDAEYWNS QPEILEDARA TVDTYCRHNY EIFDNFLVPR RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL GAGLFIYFRN QKGQSGLQPT GLLS // ID HB2K_MOUSE Reviewed; 263 AA. AC P06343; Q31137; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 12-SEP-2018, entry version 135. DE RecName: Full=H-2 class II histocompatibility antigen, A-K beta chain; DE Flags: Precursor; GN Name=H2-Ab1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3086866; DOI=10.1073/pnas.83.11.3594; RA Estess P., Begovich A.B., Koo M., Jones P.P., McDevitt H.O.; RT "Sequence analysis and structure-function correlations of murine q, k, RT u, s, and f haplotype I-A beta cDNA clones."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3594-3598(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-214. RC STRAIN=CRO435; RX PubMed=3692165; RA Golubic M., Budimir O., Schoepfer R., Kasahara M., Mayer W.E., RA Figueroa F., Klein J.; RT "Nucleotide sequence analysis of class II genes borne by mouse t RT chromosomes."; RL Genet. Res. 50:137-146(1987). RN [3] RP GLYCOSYLATION AT ASN-46. RX PubMed=3980466; RA Swiedler S.J., Freed J.H., Tarentino A.L., Plummer T.H. Jr., RA Hart G.W.; RT "Oligosaccharide microheterogeneity of the murine major RT histocompatibility antigens. Reproducible site-specific patterns of RT sialylation and branching in asparagine-linked oligosaccharides."; RL J. Biol. Chem. 260:4046-4054(1985). RN [4] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [5] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 32-216. RX PubMed=9529148; DOI=10.1016/S1074-7613(00)80536-1; RA Fremont D.H., Monnaie D., Nelson C.A., Hendrickson W.A., Unanue E.R.; RT "Crystal structure of I-Ak in complex with a dominant epitope of RT lysozyme."; RL Immunity 8:305-317(1998). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M13538; AAA39632.1; -; mRNA. DR EMBL; M27456; AAA57291.1; -; Genomic_DNA. DR PIR; A02238; HLMSBK. DR PIR; I68208; I68208. DR PIR; PL0285; PL0285. DR PIR; PL0286; PL0286. DR UniGene; Mm.254067; -. DR PDB; 1D9K; X-ray; 3.20 A; D/H=30-216. DR PDB; 1IAK; X-ray; 1.90 A; B=34-216. DR PDB; 1JL4; X-ray; 4.30 A; B=34-216. DR PDBsum; 1D9K; -. DR PDBsum; 1IAK; -. DR PDBsum; 1JL4; -. DR ProteinModelPortal; P06343; -. DR SMR; P06343; -. DR DIP; DIP-6134N; -. DR IntAct; P06343; 1. DR MINT; P06343; -. DR iPTMnet; P06343; -. DR MaxQB; P06343; -. DR PRIDE; P06343; -. DR MGI; MGI:103070; H2-Ab1. DR HOVERGEN; HBG012730; -. DR ChiTaRS; H2-Ab1; mouse. DR EvolutionaryTrace; P06343; -. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-AB1; -. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IDA:MGI. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IDA:MGI. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISO:MGI. DR GO; GO:0006955; P:immune response; IMP:MGI. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISO:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Immunity; Membrane; MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 27 FT CHAIN 28 263 H-2 class II histocompatibility antigen, FT A-K beta chain. FT /FTId=PRO_0000018996. FT TOPO_DOM 28 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 263 Cytoplasmic. {ECO:0000255}. FT DOMAIN 123 211 Ig-like C1-type. FT REGION 28 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:3980466}. FT DISULFID 42 104 FT DISULFID 143 199 FT CONFLICT 36 36 H -> Y (in Ref. 2; AAA57291). FT {ECO:0000305}. FT CONFLICT 55 55 I -> T (in Ref. 2; AAA57291). FT {ECO:0000305}. FT CONFLICT 64 65 YV -> FM (in Ref. 2; AAA57291). FT {ECO:0000305}. FT CONFLICT 85 85 A -> V (in Ref. 2; AAA57291). FT {ECO:0000305}. FT CONFLICT 90 90 K -> S (in Ref. 2; AAA57291). FT {ECO:0000305}. FT CONFLICT 114 114 P -> H (in Ref. 2; AAA57291). FT {ECO:0000305}. FT CONFLICT 120 120 L -> F (in Ref. 2; AAA57291). FT {ECO:0000305}. FT CONFLICT 124 124 S -> N (in Ref. 2; AAA57291). FT {ECO:0000305}. FT STRAND 34 45 {ECO:0000244|PDB:1IAK}. FT HELIX 47 49 {ECO:0000244|PDB:1IAK}. FT STRAND 50 59 {ECO:0000244|PDB:1IAK}. FT STRAND 62 68 {ECO:0000244|PDB:1IAK}. FT TURN 69 71 {ECO:0000244|PDB:1IAK}. FT STRAND 73 78 {ECO:0000244|PDB:1IAK}. FT HELIX 79 81 {ECO:0000244|PDB:1IAK}. FT HELIX 82 91 {ECO:0000244|PDB:1IAK}. FT HELIX 93 97 {ECO:0000244|PDB:1IAK}. FT HELIX 99 102 {ECO:0000244|PDB:1IAK}. FT HELIX 104 110 {ECO:0000244|PDB:1IAK}. FT TURN 111 115 {ECO:0000244|PDB:1IAK}. FT HELIX 116 118 {ECO:0000244|PDB:1IAK}. FT STRAND 124 131 {ECO:0000244|PDB:1IAK}. FT STRAND 135 137 {ECO:0000244|PDB:1D9K}. FT STRAND 139 151 {ECO:0000244|PDB:1IAK}. FT STRAND 154 159 {ECO:0000244|PDB:1IAK}. FT STRAND 162 164 {ECO:0000244|PDB:1IAK}. FT STRAND 168 170 {ECO:0000244|PDB:1IAK}. FT STRAND 177 179 {ECO:0000244|PDB:1IAK}. FT STRAND 181 189 {ECO:0000244|PDB:1IAK}. FT STRAND 196 202 {ECO:0000244|PDB:1IAK}. FT STRAND 210 215 {ECO:0000244|PDB:1IAK}. SQ SEQUENCE 263 AA; 29967 MW; 48F8FB38370EADF8 CRC64; MALQIPSLLL LAAVVVLTVL SSPGTEGGNS ERHFVHQFQP FCYFTNGTQR IRLVIRYIYN REEYVRFDSD VGEYRAVTEL GRPDAEYWNK QYLERTRAEL DTVCRHNYEK TETPTSLRRL EQPSVVISLS RTEALNHHNT LVCSVTDFYP AKIKVRWFRN GQEETVGVSS TQLIRNGDWT FQVLVMLEMT PRRGEVYTCH VEHPSLKSPI TVEWRAQSES ARSKMLSGIG GCVLGVIFLG LGLFIRHRSQ KGPRGPPPAG LLQ // ID HB2L_CHICK Reviewed; 231 AA. AC P23068; DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1991, sequence version 1. DT 25-OCT-2017, entry version 92. DE RecName: Full=Class II histocompatibility antigen, B-L beta chain; DE Flags: Fragment; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; OC Phasianidae; Phasianinae; Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (CLONE P14). RX PubMed=2841107; RA Bourlet Y., Behar G., Guillemot F., Frechin N., Billault A., RA Chausse A.M., Zoorob R., Auffray C.; RT "Isolation of chicken major histocompatibility complex class II (B-L) RT beta chain sequences: comparison with mammalian beta chains and RT expression in lymphoid organs."; RL EMBO J. 7:1031-1039(1988). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; X07447; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; B49055; B49055. DR PIR; S00475; HLCHBL. DR ProteinModelPortal; P23068; -. DR SMR; P23068; -. DR STRING; 9031.ENSGALP00000008911; -. DR PaxDb; P23068; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR PhylomeDB; P23068; -. DR Proteomes; UP000000539; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN <1 231 Class II histocompatibility antigen, B-L FT beta chain. FT /FTId=PRO_0000080756. FT TOPO_DOM <1 194 Extracellular. {ECO:0000255}. FT TRANSMEM 195 219 Helical. {ECO:0000255}. FT TOPO_DOM 220 231 Cytoplasmic. {ECO:0000255}. FT DOMAIN 91 179 Ig-like C1-type. FT REGION <1 89 Beta-1. FT REGION 90 182 Beta-2. FT REGION 183 194 Connecting peptide. FT CARBOHYD 14 14 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 10 74 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 111 167 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT NON_TER 1 1 SQ SEQUENCE 231 AA; 26278 MW; 06ADED95FAF8B22A CRC64; FFQWSATVEC HFLNGTERVR FLVRHVYNRQ QYVHFDSDVG LFVADTVLGE PSAKLFNSQP DVLEKNRAAV EMLCNYNYEI VAPLTLQRRE PKVRIFALQS GSLPQTDRLA CYVTGFYPPE IEVKWFQNGQ EETERVVSTD VIQNGDWTYQ VLVVLEISPR HGDSYVCQVE HTSLQQPITQ RWEPPGDVSR SKLLMGVGGF VLGLVYLALG IFFFLCSKKG QPDPTSPGIL N // ID HB2P_RABIT Reviewed; 257 AA. AC P20756; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 25-OCT-2017, entry version 85. DE RecName: Full=RLA class II histocompatibility antigen, DP beta chain; DE AltName: Full=D10 haplotype; DE Flags: Precursor; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2834455; RA Sittisombut N., Mordacq J., Knight K.L.; RT "Rabbit MHC. II. Sequence analysis of the R-DP alpha- and beta- RT genes."; RL J. Immunol. 140:3237-3243(1988). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M21468; AAA31393.1; -; Genomic_DNA. DR EMBL; M21465; AAA31393.1; JOINED; Genomic_DNA. DR EMBL; M21466; AAA31393.1; JOINED; Genomic_DNA. DR EMBL; M21467; AAA31393.1; JOINED; Genomic_DNA. DR PIR; A32283; A32283. DR ProteinModelPortal; P20756; -. DR SMR; P20756; -. DR STRING; 9986.ENSOCUP00000007527; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR Proteomes; UP000001811; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 257 RLA class II histocompatibility antigen, FT DP beta chain. FT /FTId=PRO_0000019011. FT TOPO_DOM 30 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 257 Cytoplasmic. {ECO:0000255}. FT DOMAIN 123 211 Ig-like C1-type. FT REGION 30 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 49 49 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 45 105 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 143 199 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 257 AA; 29090 MW; 60955374F2BD466C CRC64; MRPCRSLRTA ALAVVLTVLL HPVALGRATP GESEQNYLWQ RRYECYASNG TQRLLDRCAY NREEFVRFDS DIGEFRAVSE LGRQVAESWN LEYLQQARAE VDRVCRHNYE LFQGLPVLLQ TQPRVSVSPS KKGPLQHHSL LVCHVTDFYP GHVQVRWFLN GREETAGVVS THPIHNGDWT FQILVMLEMT PHQGDVYTCH VEHPSLDSPI TVEWKAQSDS ARSKMLAGVG GLVLGLVSLA VGVFMHRRSK KAQQGCR // ID HB2Q_MOUSE Reviewed; 265 AA. AC P06342; O19469; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 20-JUN-2018, entry version 119. DE RecName: Full=H-2 class II histocompatibility antigen, A-Q beta chain; DE Flags: Precursor; GN Name=H2-Ab1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3086866; DOI=10.1073/pnas.83.11.3594; RA Estess P., Begovich A.B., Koo M., Jones P.P., McDevitt H.O.; RT "Sequence analysis and structure-function correlations of murine q, k, RT u, s, and f haplotype I-A beta cDNA clones."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3594-3598(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-122. RX PubMed=2512582; DOI=10.1073/pnas.86.23.9475; RA Holmdahl R., Karlsson M., Andersson M.E., Rask L., Andersson L.; RT "Localization of a critical restriction site on the I-A-beta chain RT that determines susceptibility to collagen-induced arthritis in RT mice."; RL Proc. Natl. Acad. Sci. U.S.A. 86:9475-9479(1989). RN [3] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [4] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M13537; AAA39633.1; -; mRNA. DR EMBL; M31825; AAA39631.1; -; Genomic_DNA. DR PIR; A02237; HLMSQB. DR UniGene; Mm.254067; -. DR ProteinModelPortal; P06342; -. DR SMR; P06342; -. DR PhosphoSitePlus; P06342; -. DR MaxQB; P06342; -. DR PeptideAtlas; P06342; -. DR PRIDE; P06342; -. DR MGI; MGI:103070; H2-Ab1. DR HOVERGEN; HBG012730; -. DR ChiTaRS; H2-Ab1; mouse. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-AB1; -. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IDA:MGI. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IDA:MGI. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISO:MGI. DR GO; GO:0006955; P:immune response; IMP:MGI. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISO:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 27 FT CHAIN 28 265 H-2 class II histocompatibility antigen, FT A-Q beta chain. FT /FTId=PRO_0000018997. FT TOPO_DOM 28 227 Extracellular. {ECO:0000255}. FT TRANSMEM 228 247 Helical. {ECO:0000255}. FT TOPO_DOM 248 265 Cytoplasmic. {ECO:0000255}. FT DOMAIN 125 213 Ig-like C1-type. FT REGION 28 122 Beta-1. FT REGION 123 217 Beta-2. FT REGION 218 227 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 106 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 145 201 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 265 AA; 29950 MW; ED9E95181C62D27D CRC64; MALQIPSLLL SAAVVVLMVL SSPRTEGGNS ERHFVAQLKG ECYFTNGTQR IRSVNRYIYN REEWVRFDSD VGEYRAVTEL GRPDAEYWNS QPEILERTRA EVDTVCRHNY EGVETHTSLR RLEQPNVAIS LSRTEALNHH NTLVCSVTDF YPAKIKVRWF RNGQEETVGV SSTQLIRNGD WTFQVLVMLE MTPHQGEVYT CHVEHPSLKS PITVEWRAQS ESARSKMLSG IGGCVLGVIF LGLGLFIRHR SQKGPRGPPP AGLLQ // ID HB2S_MOUSE Reviewed; 263 AA. AC P06345; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 20-JUN-2018, entry version 119. DE RecName: Full=H-2 class II histocompatibility antigen, A-S beta chain; DE Flags: Precursor; GN Name=H2-Ab1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=3086866; DOI=10.1073/pnas.83.11.3594; RA Estess P., Begovich A.B., Koo M., Jones P.P., McDevitt H.O.; RT "Sequence analysis and structure-function correlations of murine q, k, RT u, s, and f haplotype I-A beta cDNA clones."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3594-3598(1986). RN [2] RP UBIQUITINATION. RX PubMed=17174123; DOI=10.1016/j.immuni.2006.11.001; RA van Niel G., Wubbolts R., Ten Broeke T., Buschow S.I., Ossendorp F.A., RA Melief C.J., Raposo G., van Balkom B.W., Stoorvogel W.; RT "Dendritic cells regulate exposure of MHC class II at their plasma RT membrane by oligoubiquitination."; RL Immunity 25:885-894(2006). RN [3] RP UBIQUITINATION. RX PubMed=17051151; DOI=10.1038/nature05261; RA Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A., RA Mellman I.; RT "Surface expression of MHC class II in dendritic cells is controlled RT by regulated ubiquitination."; RL Nature 444:115-118(2006). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- PTM: Ubiquitinated in immature dendritic cells leading to down- CC regulation of MHC class II. {ECO:0000269|PubMed:17051151, CC ECO:0000269|PubMed:17174123}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; M13540; AAA39634.1; -; mRNA. DR PIR; A02240; HLMSBS. DR UniGene; Mm.254067; -. DR ProteinModelPortal; P06345; -. DR SMR; P06345; -. DR MaxQB; P06345; -. DR PeptideAtlas; P06345; -. DR PRIDE; P06345; -. DR MGI; MGI:103070; H2-Ab1. DR HOVERGEN; HBG012730; -. DR ChiTaRS; H2-Ab1; mouse. DR Proteomes; UP000000589; Unplaced. DR CleanEx; MM_H2-AB1; -. DR GO; GO:0009986; C:cell surface; ISO:MGI. DR GO; GO:0005769; C:early endosome; IDA:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IDA:MGI. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0042613; C:MHC class II protein complex; IDA:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0042605; F:peptide antigen binding; IDA:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0048002; P:antigen processing and presentation of peptide antigen; IDA:MGI. DR GO; GO:0002455; P:humoral immune response mediated by circulating immunoglobulin; ISO:MGI. DR GO; GO:0006955; P:immune response; IMP:MGI. DR GO; GO:0002381; P:immunoglobulin production involved in immunoglobulin mediated immune response; ISO:MGI. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome; Disulfide bond; Glycoprotein; Immunity; Membrane; KW MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT SIGNAL 1 27 FT CHAIN 28 263 H-2 class II histocompatibility antigen, FT A-S beta chain. FT /FTId=PRO_0000018998. FT TOPO_DOM 28 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 263 Cytoplasmic. {ECO:0000255}. FT DOMAIN 123 211 Ig-like C1-type. FT REGION 28 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 104 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 143 199 {ECO:0000255|PROSITE-ProRule:PRU00114}. SQ SEQUENCE 263 AA; 29788 MW; F87F0CCFCF6DD587 CRC64; MALQIPSLLL SAAVVVLMVL SSPGTEGGDS ERHFVFQFKG ECYFTNGTQR IRSVDRYIYN REEYLRFDSD VGEYRAVTEL GRPDAEYYNK QYLEQTRAEL DTVCRHNYEG VETHTSLRRL EQPNVVISLS RTEALNHHNT LVCSVTDFYP AKIKVRWFRN GQEETVGVSS TQLISNGDWT FQVLVMLEMT PRRGEVYTCH VEHPSLKSPI TVEWRAQSES ARSKMLSGIG GCVLGVIFLG LGLFIRHRSQ KGPRGPPPAG LLQ // ID HB2U_MOUSE Reviewed; 263 AA. AC P06344; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 12-SEP-2018, entry version 127. DE RecName: Full=H-2 class II histocompatibility antigen, A-U beta chain; DE Flags: Precursor; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=3086866; DOI=10.1073/pnas.83.11.3594; RA Estess P., Begovich A.B., Koo M., Jones P.P., McDevitt H.O.; RT "Sequence analysis and structure-function correlations of murine q, k, RT u, s, and f haplotype I-A beta cDNA clones."; RL Proc. Natl. Acad. Sci. U.S.A. 83:3594-3598(1986). RN [2] RP NUCLEOTIDE SEQUENCE OF 174-263. RX PubMed=3500915; DOI=10.3109/08820138709087096; RA Sharma S., King L.B., Corley R.B., Maki R.; RT "Comparative sequence analysis of cDNA clones encoding I-A molecules RT of the CH12 B cell lymphoma: nucleotide differences do not account for RT their 'defective' function in B cell stimulation."; RL Immunol. Invest. 16:425-436(1987). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MHC class II family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR PIR; A02239; HLMSBU. DR UniGene; Mm.254067; -. DR PDB; 1K2D; X-ray; 2.20 A; B=28-216. DR PDB; 1U3H; X-ray; 2.42 A; D/H=28-215. DR PDB; 2P24; X-ray; 2.15 A; B=28-224. DR PDB; 2PXY; X-ray; 2.23 A; D=29-217. DR PDB; 2Z31; X-ray; 2.70 A; D=28-216. DR PDBsum; 1K2D; -. DR PDBsum; 1U3H; -. DR PDBsum; 2P24; -. DR PDBsum; 2PXY; -. DR PDBsum; 2Z31; -. DR ProteinModelPortal; P06344; -. DR SMR; P06344; -. DR MINT; P06344; -. DR MaxQB; P06344; -. DR PRIDE; P06344; -. DR HOVERGEN; HBG012730; -. DR EvolutionaryTrace; P06344; -. DR Proteomes; UP000000589; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disulfide bond; Glycoprotein; KW Immunity; Membrane; MHC II; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 27 FT CHAIN 28 263 H-2 class II histocompatibility antigen, FT A-U beta chain. FT /FTId=PRO_0000018999. FT TOPO_DOM 28 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 263 Cytoplasmic. {ECO:0000255}. FT DOMAIN 123 211 Ig-like C1-type. FT REGION 28 120 Beta-1. FT REGION 121 214 Beta-2. FT REGION 215 224 Connecting peptide. FT CARBOHYD 46 46 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 42 104 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT DISULFID 143 199 {ECO:0000255|PROSITE-ProRule:PRU00114}. FT STRAND 34 45 {ECO:0000244|PDB:2P24}. FT TURN 46 49 {ECO:0000244|PDB:2P24}. FT STRAND 50 59 {ECO:0000244|PDB:2P24}. FT STRAND 62 68 {ECO:0000244|PDB:2P24}. FT TURN 69 71 {ECO:0000244|PDB:2P24}. FT STRAND 73 78 {ECO:0000244|PDB:2P24}. FT HELIX 79 81 {ECO:0000244|PDB:2P24}. FT TURN 82 84 {ECO:0000244|PDB:2P24}. FT HELIX 85 91 {ECO:0000244|PDB:2P24}. FT HELIX 93 102 {ECO:0000244|PDB:2P24}. FT HELIX 104 111 {ECO:0000244|PDB:2P24}. FT TURN 112 118 {ECO:0000244|PDB:2P24}. FT STRAND 124 129 {ECO:0000244|PDB:2P24}. FT STRAND 135 137 {ECO:0000244|PDB:1K2D}. FT STRAND 140 151 {ECO:0000244|PDB:2P24}. FT STRAND 154 159 {ECO:0000244|PDB:2P24}. FT STRAND 162 164 {ECO:0000244|PDB:2P24}. FT STRAND 168 170 {ECO:0000244|PDB:2P24}. FT STRAND 177 179 {ECO:0000244|PDB:2P24}. FT STRAND 181 188 {ECO:0000244|PDB:2P24}. FT STRAND 196 202 {ECO:0000244|PDB:2P24}. FT STRAND 210 215 {ECO:0000244|PDB:2P24}. FT TURN 216 218 {ECO:0000244|PDB:2P24}. SQ SEQUENCE 263 AA; 30041 MW; 1ECEF8669CF91389 CRC64; MALQIPSLLL LAAVVVLMVL SSPGTEGGDS ERHFVVQFQP FCYFTNGTQR IRYVTRYIYN REEYLRFDSD VGEYRAVTEL GRPDAEYYNK QYLERTRAEL DTVCRYNYEE TEVPTSLRRL EQPNVVISLS RTEALNHHNT LVCSVTDFYP AKIKVRWFRN GQEETVGVSS TQLIRNGDWT FQVLVMLEMT PRRGEVYTCH VEHPSLKSPI TVEWRAQSES ARSKMLSGIG GCVLGVIFLG LGLFIRHRSQ KGPRGPPPAG LLQ // ID I3J7S6_ORENI Unreviewed; 247 AA. AC I3J7S6; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000004916}; GN Name=LOC100701975 {ECO:0000313|Ensembl:ENSONIP00000004916}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000004916, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000004916} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01065987; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01065988; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005465962.1; XM_005465905.3. DR ProteinModelPortal; I3J7S6; -. DR STRING; 8128.ENSONIP00000004916; -. DR Ensembl; ENSONIT00000004919; ENSONIP00000004916; ENSONIG00000003902. DR GeneID; 100701975; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3J7S6; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 247 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003672350. FT TRANSMEM 213 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 110 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 247 AA; 28535 MW; 8B11AABCCE9B4423 CRC64; MASSFLCLLF ISLSTADGFK MYVLSRCDFN STELKDMKYI RSYYYNKIEV TRFDSDVRKF VGYTEYGVKK AETWNNDQAH MAAFRVEKER YCYTNIGIWY RNILSKSAKP YVKLHSTTPD YSHHPAMLVC SVYDFFPSKI KVSWLRDGQE VTSDVTSTEE MADGDWYYQT HSHLEYTPRS GEKISCKVEH ASLEKPLITD WDSSMPESER NKLAIGASGL ILGLILSLAG FIYYRRKAQG RILVPTN // ID I3J9N8_ORENI Unreviewed; 135 AA. AC I3J9N8; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000005578}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005578, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000005578} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01019647; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3J9N8; -. DR Ensembl; ENSONIT00000005582; ENSONIP00000005578; ENSONIG00000004432. DR eggNOG; ENOG410KH5C; Eukaryota. DR eggNOG; ENOG4110RMF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3J9N8; -. DR OrthoDB; EOG091G0GI5; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}. FT DOMAIN 95 135 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 135 AA; 15529 MW; 963E73CEDFFE0F4B CRC64; EDGYFMFADF CCVMHSRDPK TVEYLIDWYF NKEFTMQYNS TVGKWTGLTP AGLITASQFN EDKFDVDQRK AEKQLTCVNN VDAVFNGVQE NIAAPSMTLQ EGDHTSTHDT ILVCSVYDFY PKHILVTWYL NGQEV // ID I3J9P0_ORENI Unreviewed; 223 AA. AC I3J9P0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000005580}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005580, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000005580} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01019647; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01019648; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3J9P0; -. DR Ensembl; ENSONIT00000005584; ENSONIP00000005580; ENSONIG00000004434. DR eggNOG; ENOG410KH5C; Eukaryota. DR eggNOG; ENOG4110RMF; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3J9P0; -. DR OMA; NITVENM; -. DR OrthoDB; EOG091G0H2N; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 223 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003671976. FT TRANSMEM 190 212 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 28 103 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT DOMAIN 127 174 IGc1. {ECO:0000259|SMART:SM00407}. SQ SEQUENCE 223 AA; 25528 MW; 4740F7A7138CC75E CRC64; RCQFLINLFF SFLDCSINGD GYFMFADFWC AVHSRDREEV EYLIDWYFNK EFTMQYNSTV GKWTGLTPAG LITASRFNED SADILQRKVE KQLICVNNVD AVFNITVENM AAPSMTLQEG DHTSSHDTIL VCSVYDFYPK HILVTWYLNG QEVTEXIPKD RVTCTVEHVS LKEPKSSYWD SSLKQSDRSF LTGGLCALLL GALILSLGLI YYRRKTSDPT FSN // ID I3JEZ1_ORENI Unreviewed; 251 AA. AC I3JEZ1; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 20-JUN-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000007432}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007432, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000007432} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01071490; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01071491; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JEZ1; -. DR STRING; 8128.ENSONIP00000007432; -. DR Ensembl; ENSONIT00000007437; ENSONIP00000007432; ENSONIG00000005905. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3JEZ1; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 251 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003672655. FT TRANSMEM 217 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 110 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 251 AA; 28643 MW; 89AEC56B33B76C87 CRC64; MASSFLCLLF ISLSTVDGFM TYRLSRCDFN STELKDIQFT DSYYYNMIEI IRFDSNVGKF VGFTDFGVKT AETWNNIPAR LASMRAQKGT YCKSNIDVRY HKLTSKSAQP TVKLHSTTPL SSHHPAMLVC SVYDFFPSKI KVSWHRDGQE VTSDVTSTEE MEDGDWYYQT HCYLEYTPRS GEKISCVVEH ASLEKPLITN WDPSSSSFMP KIERYKLAIG ASGLILCLIL SLAGFIYYRQ RARGRILVPT N // ID I3JFR5_ORENI Unreviewed; 265 AA. AC I3JFR5; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 20-JUN-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000007706}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007706, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000007706} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01025173; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JFR5; -. DR STRING; 8128.ENSONIP00000007706; -. DR Ensembl; ENSONIT00000007711; ENSONIP00000007706; ENSONIG00000006116. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3JFR5; -. DR OMA; QIRVTWL; -. DR OrthoDB; EOG091G0GI5; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 219 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 29970 MW; B87383DA78ACC1FA CRC64; SLCEKIRLIA TFIRDFVFVT MHTHNFLILP HVLLIFSTAD AYFGYGVVRC LFTSKDDVVY LAQVYLNKML LGQYNSSLGK YVGYTEKTKE IADNLNKNKG FLEHEKKNKE KCRTNIPLVL DILSRPVKPS VRLRLVESAD SKHPGLFMCS AYNFYPKQIK LTWLRDGKEA TSNVTSTDEL PNGNWLYQIH SYIEISSKPG EKISCVVEHA SLTEPKVIDW VPITEAGKNK IAVGAAGLLL GLVFPIIGVI FYKRKTTDEM IVTTN // ID I3JGI7_ORENI Unreviewed; 252 AA. AC I3JGI7; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000007978}; GN Name=LOC100708205 {ECO:0000313|Ensembl:ENSONIP00000007978}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000007978, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000007978} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01036178; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005459602.1; XM_005459545.3. DR ProteinModelPortal; I3JGI7; -. DR STRING; 8128.ENSONIP00000007978; -. DR Ensembl; ENSONIT00000007983; ENSONIP00000007978; ENSONIG00000006327. DR GeneID; 100708205; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3JGI7; -. DR OMA; RIPEAHC; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 252 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003672874. FT TRANSMEM 217 239 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 252 AA; 28758 MW; 1E1B2C6250F02AA6 CRC64; MASSFLCFTL LFISIHNADG FLEYIVDRCD FNSTELENME YIYSHYYNKM EYIRFSSNVG QYVGFTDFGV RLAEVWNNDT ADLNLMRLKI ATYCHHNIDI NDRAILTKSV QPSVRIKSMT PPSGQHPAML VCSVYDFFPS KIKVSWLRDG QAVSSDITST EEMPNGDWYY QTHSQLEYTP RSGEKISCVV EHASLKEPLI TDWDPSSDKS TSESTTLIAI GASILTLGLI LLLAGFIFYR WRARDPTLFS NE // ID I3JKG2_ORENI Unreviewed; 252 AA. AC I3JKG2; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 20-JUN-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000009356}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000009356, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000009356} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01025503; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JKG2; -. DR STRING; 8128.ENSONIP00000009356; -. DR Ensembl; ENSONIT00000009362; ENSONIP00000009356; ENSONIG00000007425. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3JKG2; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 252 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003672900. FT TRANSMEM 217 239 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 252 AA; 28876 MW; FA3EE4EB9022C597 CRC64; MASSFVCFTL LLISIHTADG FLEYMVERCK FNSTELKDME YIYSHYYNKI EYIRFSSSVG KYVGVTEFGE NLAKHWNNDT EELNSTRSKI VTYCLNNIDI HDRAILAKSV QPRVRIKSKT PLSGQHPAML VCSVYDFFPT KIKVSWLRDG QEVYSDVTST EVMPNGDWYY QTHSHLEYKP RSGEKISCVV EHVSLSEPLI TDWDPSSDKS TSESTPLTAI GASILTLGLI LLLVGYIFYR WKARGQTRTH TH // ID I3JKI8_ORENI Unreviewed; 222 AA. AC I3JKI8; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000009382}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000009382, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000009382} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01025628; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JKI8; -. DR STRING; 8128.ENSONIP00000009382; -. DR Ensembl; ENSONIT00000009388; ENSONIP00000009382; ENSONIG00000007445. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3JKI8; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 197 219 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 92 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 222 AA; 25698 MW; B34FA2683BED85B7 CRC64; FLEYIVDRCE FNSTELKDME YIYSHYYNKI EYIRFSSSVE QYVGFTEYGV MLAEILNNNT ALLNSSRQMI TEYCYHNIDV HDQAIIAKSV RPRVRIKSKT PLSGQHPAML VCSVYDFFPN KIKVRWLRDE QEVTSDVTST EVMPNGDWYY QTHSYLEYTP RSGEKISCVV EHVSLSEPLI TDWESSSDKS TSESTPLTAI GASILTLGLV LLLAGFIFYR WK // ID I3JKJ2_ORENI Unreviewed; 255 AA. AC I3JKJ2; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000009386}; GN Name=LOC100690666 {ECO:0000313|Ensembl:ENSONIP00000009386}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000009386, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000009386} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01025637; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JKJ2; -. DR STRING; 8128.ENSONIP00000009386; -. DR Ensembl; ENSONIT00000009392; ENSONIP00000009386; ENSONIG00000007449. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3JKJ2; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 255 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003672674. FT TRANSMEM 220 242 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 255 AA; 28951 MW; ACAF12BEE36D7D80 CRC64; MASSFLRFTF LFISIHIADG FLEYIVDRCE FNSTELKEME YIYSHYYNKI EYIRFSSSVG KYVGVTDFGV NLAKRWNNNT ALLNSTRSKI ATYCLSNIGI HDRAIIAKSV RPSVRIKSKT PLSGQHPAML VCSVYNFFPR KIKVSWLRDG QKVTSDVTST QEMPNGDWYY QTHSHLEYTP RSGENISCVV EHASLKEPLI TDWAHSDPPS DKSTPESTTL IAIGASILTL GLILLLAGFF LYRWKARARL VVKTA // ID I3JKJ3_ORENI Unreviewed; 252 AA. AC I3JKJ3; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000009387}; GN Name=LOC100690666 {ECO:0000313|Ensembl:ENSONIP00000009387}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000009387, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000009387} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01025637; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_019209823.1; XM_019354278.1. DR Ensembl; ENSONIT00000009393; ENSONIP00000009387; ENSONIG00000007449. DR GeneID; 100690666; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 252 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003673207. FT TRANSMEM 217 239 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 252 AA; 28761 MW; 4567BCE583839E5F CRC64; MASSFLRFTF LFISIHIADG FLEYIVDRCE FNSTELKEME YIYSHYYNKI EYIRFSSSVG KYVGVTDFGV NLAKRWNNNT ALLNSTRSKI ATYCLSNIGI HDRAIIAKSV RPSVRIKSKT PLSGQHPAML VCSVYNFFPR KIKVSWLRDG QKVTSDVTST QEMPNGDWYY QTHSHLEYTP RSGENISCVV EHASLKEPLI TDWDPPSDKS TPESTTLIAI GASILTLGLI LLLAGFFLYR WKARDHTLFS NE // ID I3JNP0_ORENI Unreviewed; 182 AA. AC I3JNP0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000010484}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000010484, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000010484} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01073278; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JNP0; -. DR STRING; 8128.ENSONIP00000010484; -. DR Ensembl; ENSONIT00000010493; ENSONIP00000010484; ENSONIG00000008338. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3JNP0; -. DR OMA; GETISCM; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 182 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003672810. FT DOMAIN 28 103 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT DOMAIN 128 182 IGc1. {ECO:0000259|SMART:SM00407}. SQ SEQUENCE 182 AA; 21793 MW; D4B5E5EA4F25038A CRC64; NMDSSFLCFS LFFIILCRAD GYEYYTSSRC LFNSSELRDI EYVRSYYYNR IEYVRFSSSV GMFVGYTEYG VREADQWNKD QGQLAVMRAQ KETYCTPNID LWYRSVLTKY VKPFVRLHWT KPPVDHHPAI LACSIYDFYP KYIKVTWLRN GQRVTSNTTT TEELPDADWF YQTHSYLEYT PK // ID I3JRI4_ORENI Unreviewed; 253 AA. AC I3JRI4; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000011478}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000011478, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000011478} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01045716; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01045717; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3JRI4; -. DR STRING; 8128.ENSONIP00000011478; -. DR Ensembl; ENSONIT00000011487; ENSONIP00000011478; ENSONIG00000009129. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3JRI4; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 253 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003672748. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 202 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 253 AA; 28763 MW; 4B2B7982E5642A05 CRC64; RNMASKFLCF TLLFINICTA DGYECYSSTR CLFNSTELKD IEFITSYYYN KIEYVRFSSD VGKFVGYTEY GVKNAEYWNK NQALLAQMRA QKETYCQPNI GIWYADVLSK SVTPSVRLHS TMAPGCHHPA MLVCSVYDFY PKLIKVSWLR NGQEITSDIT STEEFANGDW LYQVHSHLEY MPRSGEKISC VVEHASLEKP LIINWVPPMP ETERLIIVGV VGLILGLILF LAGVIYRRRS GVCAPGLMLV PSS // ID I3K3H6_ORENI Unreviewed; 255 AA. AC I3K3H6; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 34. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000015671}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000015671, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000015671} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01038925; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3K3H6; -. DR STRING; 8128.ENSONIP00000015671; -. DR Ensembl; ENSONIT00000015685; ENSONIP00000015671; ENSONIG00000012441. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3K3H6; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G0N6U; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 255 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003674039. FT TRANSMEM 220 241 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 120 208 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 255 AA; 29549 MW; 0101E694EF43C8EE CRC64; MDSFYFCFSL FFIILCRADG YEYYTSSRCL FNSTELRDIE YIRSYYYNKT EYVRFSSSVG KFVGYTEYGV READQWNKDQ GQGSWTRKGQ LAAMRAQKET YCKPKIDFWY QSVLTKAVKP SVRLHSIPPV YLNPAILVCS VYNFYPKEIK VSWLRNGQQV SPDITSTVEF ANADWLYQTH SYMEYTPRSG EKISCMVEHA SLKEPLVTDW VPSMSESKKL MIVGAFGLIL GLLFFLAGVI YTRMCSRGQS STHTK // ID I3KS32_ORENI Unreviewed; 255 AA. AC I3KS32; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000023928}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000023928, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000023928} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01068237; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 8128.ENSONIP00000023928; -. DR Ensembl; ENSONIT00000023949; ENSONIP00000023928; ENSONIG00000019004. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3KS32; -. DR OMA; NGTERRY; -. DR OrthoDB; EOG091G0N6U; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 255 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003674880. FT TRANSMEM 220 242 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 120 208 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 255 AA; 29451 MW; 40034332EE5D0C77 CRC64; MDSSFLCFSL FFIILCRADG YEYYTSSRCL FNSTELRDIE YIRSYYYNKT EYVRFSSSVG KFVGYTEYGV READQWNKDQ GQGSWTRKGQ LAAMRAQKET YCKPKIDFWY QSVLTKAVKP SVRLHSIPPV YLNPAILVCS VYNFYPKEIK VSWLRNGQQV SPDITSTVEF ANADWLYQTH SYMEYTPRSG EKISCMVEHA SLKEPLVTDW VPSMSESKKL MIVGAFGLIL GLLFFLAGVI YIRMCSRGQS STHTK // ID I3KSG3_ORENI Unreviewed; 252 AA. AC I3KSG3; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 20-JUN-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000024059}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000024059, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000024059} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01022072; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3KSG3; -. DR Ensembl; ENSONIT00000024080; ENSONIP00000024059; ENSONIG00000019113. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3KSG3; -. DR OrthoDB; EOG091G1GUG; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 252 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003674901. FT TRANSMEM 218 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 113 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 252 AA; 28708 MW; D27992A246980D03 CRC64; AVCSLLLLLL LLRSKGVAED EKYFHILKTC QFIEKSSQSD VHYQVQYWYN GLLQAFYNSS TEKVVGFTHY GKVFADEVNK SPDYLKVRRN DLNYFCKVLG AVLYKDIQVK AVPPVSRLKS VTSNSSEDSE VLVCSAYNFY PQQIRLSWLR DGVVIPDPPG MMITEMPGGE WRYQIHSYLQ HKLNSGQNIT CMIEHRGLQE PQLLKLERSE VQSNSVTLAW EGAILATGLF VLLASVVFHC RKTHCIIFVG SF // ID I3KVG0_ORENI Unreviewed; 249 AA. AC I3KVG0; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000025106}; GN Name=LOC100701969 {ECO:0000313|Ensembl:ENSONIP00000025106}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000025106, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000025106} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01056955; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01056956; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01056957; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003459301.2; XM_003459253.4. DR ProteinModelPortal; I3KVG0; -. DR STRING; 8128.ENSONIP00000025106; -. DR Ensembl; ENSONIT00000025127; ENSONIP00000025106; ENSONIG00000019932. DR GeneID; 100701969; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3KVG0; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003675232. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 107 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28313 MW; 54B8F7A0F308CAE1 CRC64; MASSFLCLSL LFISLSTAGG FMHYSVDRCN FNSSEPQDIE YIRSYYFRKV EFTRFDSSVG KYVGYTEYGV KNAEEWNKDK GNLAAMNAQK EVYCQKKIDN RYNAILPKSA KPYVKLHSTM PLSSHHPAML VCSVYDFFPS EIKVSWQRDG QEVTSDVTST EEMADGDWYY QTHSHLEYTP RSGEKISCVV EHASLEKPLI TDWDPSMPES ERNKLAIGAS GLILGVILSL AGFIYYKRKA RGRILVPTN // ID I3KVG5_ORENI Unreviewed; 249 AA. AC I3KVG5; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 36. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000025111}; GN Name=LOC100701242 {ECO:0000313|Ensembl:ENSONIP00000025111}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000025111, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000025111} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01057007; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005464761.1; XM_005464704.3. DR ProteinModelPortal; I3KVG5; -. DR STRING; 8128.ENSONIP00000025111; -. DR Ensembl; ENSONIT00000025132; ENSONIP00000025111; ENSONIG00000019937. DR GeneID; 100701242; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3KVG5; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0K7A; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 249 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003675053. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 249 AA; 28371 MW; 5B4B39825C4024BF CRC64; MASSFLCLSI LFISFSTADG FMEYHVDRCN FNSTDLKDIE YIYSCYYNKI EYARFSSSVG KFVGFTKHGV YNADKWNNDP AELNNRRAQK ERYCHNNIGV DYQVALTKSA KPYVKLHSMT PASSHHPAML VCSVYDFFPS KIKVSWLRDG QEVSSDVTST EEMADGDWYY QTHSHLEYTP RSGEKISCKV EHASLEKPLI TDWDSSMPES ERNKLAIGAS GLILGLILSL AGFIYYRRKA RGRILVPTN // ID I3KVH3_ORENI Unreviewed; 247 AA. AC I3KVH3; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 1. DT 23-MAY-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSONIP00000025119}; OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids; OC Pseudocrenilabrinae; Oreochromini; Oreochromis. OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000025119, ECO:0000313|Proteomes:UP000005207}; RN [1] {ECO:0000313|Ensembl:ENSONIP00000025119} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. RN [2] {ECO:0000313|Proteomes:UP000005207} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=25186727; DOI=10.1038/nature13726; RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S., RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., RA Johnson J., Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., RA Amemiya C., Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., RA Bloomquist R., Carleton K.L., Conte M.A., D'Cotta H., Eshel O., RA Gaffney L., Galibert F., Gante H.F., Gnerre S., Greuter L., Guyon R., RA Haddad N.S., Haerty W., Harris R.M., Hofmann H.A., Hourlier T., RA Hulata G., Jaffe D.B., Lara M., Lee A.P., MacCallum I., Mwaiko S., RA Nikaido M., Nishihara H., Ozouf-Costaz C., Penman D.J., Przybylski D., RA Rakotomanga M., Renn S.C., Ribeiro F.J., Ron M., Salzburger W., RA Sanchez-Pulido L., Santos M.E., Searle S., Sharpe T., Swofford R., RA Tan F.J., Williams L., Young S., Yin S., Okada N., Kocher T.D., RA Miska E.A., Lander E.S., Venkatesh B., Fernald R.D., Meyer A., RA Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O., RA Di Palma F.; RT "The genomic substrate for adaptive radiation in African cichlid RT fish."; RL Nature 513:375-381(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AERX01057023; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AERX01057024; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3KVH3; -. DR STRING; 8128.ENSONIP00000025119; -. DR Ensembl; ENSONIT00000025140; ENSONIP00000025119; ENSONIG00000019944. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3KVH3; -. DR OMA; GENCAVT; -. DR OrthoDB; EOG091G1WIE; -. DR TreeFam; TF333780; -. DR Proteomes; UP000005207; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000005207}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000005207}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 247 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003674307. FT TRANSMEM 213 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 28 103 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 247 AA; 28220 MW; FF489EB9A0EC3606 CRC64; LRNMASSFIC LLFISLSTAD GFKMYVVSRC DFNSTELKDI KYIRSYYYNK IEVTRFDSDV RKFVGFTGFG VKQAKHFNSQ PGRLATLKAE KERYCQHNIG IWYSNVLPKS DSDFQSLCSS FTPANIYRSG HLLSGSDIRA DFLCISQPAH FDLTGEEHRE EADGDWYYQI HSHLEYTPRS GEKISCKVEH ASLEKPLITD WDSSMPESER NKLAIGASGL ILGLILSLAG FIYYRRKARG RILVPQH // ID I3M278_ICTTR Unreviewed; 282 AA. AC I3M278; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 28-MAR-2018, entry version 36. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSSTOP00000003042}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSSTOP00000003042}; OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) OS (Spermophilus tridecemlineatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; OC Sciuridae; Xerinae; Marmotini; Ictidomys. OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000003042, ECO:0000313|Proteomes:UP000005215}; RN [1] {ECO:0000313|Ensembl:ENSSTOP00000003042} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Assembly & Analysis Group; RG Computational R&D Group; RG and Sequencing Platform; RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.; RT "The Draft Genome of Spermophilus tridecemlineatus."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSTOP00000003042} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTP01011077; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3M278; -. DR STRING; 43179.ENSSTOP00000003042; -. DR Ensembl; ENSSTOT00000003399; ENSSTOP00000003042; ENSSTOG00000003405. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3M278; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000005215; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005215}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005215}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. SQ SEQUENCE 282 AA; 31907 MW; 13F9D30D494F2B96 CRC64; MSSAWAPWVT VLLVNLIRLN FSMTQDRDSP EDFVIQAKAD CYFTNGTEKV QFVVRFIFNL EEYARFDSDL GVFVALTELG LPDAEQWNNR PDILERSRAS VDMLCRHNYN LGAPFTVGRK VQPEVTVYPE KTPLLHQHNL LLCSVTGFYP GDIKIRWFWN GQEERAGVLS TGLIRNGDWT FQTMVMLEVT PSPGDVYSCL VEHPSLPGPV SVEWRAQREY SWKKILSGVG AFLLGLTFLL VGIIIHLRAR KGNEPSSLFP QISRAILQKP NSGPNQSFSP ET // ID I3M2H9_ICTTR Unreviewed; 288 AA. AC I3M2H9; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 28-MAR-2018, entry version 38. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSSTOP00000003186}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSSTOP00000003186}; OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) OS (Spermophilus tridecemlineatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; OC Sciuridae; Xerinae; Marmotini; Ictidomys. OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000003186, ECO:0000313|Proteomes:UP000005215}; RN [1] {ECO:0000313|Ensembl:ENSSTOP00000003186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Assembly & Analysis Group; RG Computational R&D Group; RG and Sequencing Platform; RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.; RT "The Draft Genome of Spermophilus tridecemlineatus."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSTOP00000003186} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTP01011071; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3M2H9; -. DR STRING; 43179.ENSSTOP00000003186; -. DR Ensembl; ENSSTOT00000003557; ENSSTOP00000003186; ENSSTOG00000003567. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3M2H9; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000005215; Unassembled WGS sequence. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005215}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005215}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 257 277 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 155 243 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 288 AA; 32752 MW; 0295770A8BAE9D5D CRC64; MVSDISPRIS IQQVLPSLTA TVFSSPAFSS SAMVLQVSEA SWAPALMVSL MVLFNPVVQG MATPENYIFQ ARQDCYASHG TQRFVERYIY NREEYARFDS DVGEYRAVTE LGRPQAEYWN SQKDLLEDER ARVDTLCRHN YEGIERYTEQ RRVQPKVHVS PTKKGTLQHH NMLVCHVTDF YPGNIKVRWF LNGQEETAGV VATELIRNGD WTFQIMVMLE MTPKQGDVYT CHVEHPSLNS PVTVEWRAQS DSARNKTLTG VGGFVLGLIF LVVGVFMHKR SKKAQRGP // ID I3MDW1_ICTTR Unreviewed; 269 AA. AC I3MDW1; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 28-MAR-2018, entry version 42. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSTOP00000008626}; GN Name=LOC101968779 {ECO:0000313|Ensembl:ENSSTOP00000008626}; OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) OS (Spermophilus tridecemlineatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; OC Sciuridae; Xerinae; Marmotini; Ictidomys. OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000008626, ECO:0000313|Proteomes:UP000005215}; RN [1] {ECO:0000313|Ensembl:ENSSTOP00000008626} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Assembly & Analysis Group; RG Computational R&D Group; RG and Sequencing Platform; RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.; RT "The Draft Genome of Spermophilus tridecemlineatus."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSTOP00000008626} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTP01099908; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_013220096.1; XM_013364642.1. DR ProteinModelPortal; I3MDW1; -. DR STRING; 43179.ENSSTOP00000008626; -. DR Ensembl; ENSSTOT00000009616; ENSSTOP00000008626; ENSSTOG00000020276. DR GeneID; 101968779; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3MDW1; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Proteomes; UP000005215; Unassembled WGS sequence. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl. DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl. DR GO; GO:0008134; F:transcription factor binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0002344; P:B cell affinity maturation; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl. DR GO; GO:0046635; P:positive regulation of alpha-beta T cell activation; IEA:Ensembl. DR GO; GO:0002579; P:positive regulation of antigen processing and presentation; IEA:Ensembl. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005215}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005215}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5011780408. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 269 AA; 30829 MW; A9FAD6FBE16ADB3E CRC64; MLGKMALQIL RGFCTAAMMV MLMMLTSPVA NCRDSPQDFV YQFKFSCYFT NGTERVRVIT RDVYNLEEFV RFDSDVGEYR AVTELGRRTA EYWNSQKDIL ERRQAEVDTV CRHNYKNELR TSLQRRVEPK VTISPSRTVA LNHHNLLVCS VTDFYPSQIK VRWFQNNQEE IAGVVSTPLI RNGDWTFQIL VMLEVTPQRG DVYTCHVEHP SLQSPITVEW RAQSESSKSK MLSGIGGFVL GLIFFGLGLL IRHRSQKGTR GLPATGLLH // ID I3MDX8_ICTTR Unreviewed; 266 AA. AC I3MDX8; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 28-MAR-2018, entry version 39. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSTOP00000008646}; GN Name=LOC101968188 {ECO:0000313|Ensembl:ENSSTOP00000008646}; OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) OS (Spermophilus tridecemlineatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; OC Sciuridae; Xerinae; Marmotini; Ictidomys. OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000008646, ECO:0000313|Proteomes:UP000005215}; RN [1] {ECO:0000313|Ensembl:ENSSTOP00000008646} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Assembly & Analysis Group; RG Computational R&D Group; RG and Sequencing Platform; RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.; RT "The Draft Genome of Spermophilus tridecemlineatus."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSTOP00000008646} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTP01099909; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGTP01099910; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGTP01099911; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005338990.1; XM_005338933.2. DR ProteinModelPortal; I3MDX8; -. DR STRING; 43179.ENSSTOP00000008646; -. DR Ensembl; ENSSTOT00000009637; ENSSTOP00000008646; ENSSTOG00000019974. DR GeneID; 101968188; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3MDX8; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000005215; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005215}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005215}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5011454481. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30330 MW; 42AB41C67E5C27CB CRC64; MVSLWLRGSS CMARLTMMLM ALSLPLALTR DTRPRFLEQR FSECHFSNGT ERVRFLERYF HNRQEFVRFD SDVGEYRAVT ELGRPDAEYW NSQKDLLEQK RGQVDNYCRH NYGVGESFTV ERRVKPKVTV YPTKTQSLQH HNLLVCAVSG FYPGQIEVRW FRNGQEEQAG VVSTGLIQNG DWTFQMLVML ETVPQSGEVY TCQVEHPSLT SPVTVEWRAQ SGSAQSKMLS GVGGFVLGSL FLGLGMFIYY KNQKGRSGLQ PTGLLS // ID I3NB97_ICTTR Unreviewed; 272 AA. AC I3NB97; DT 11-JUL-2012, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 2. DT 28-MAR-2018, entry version 41. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSSTOP00000021644}; GN Name=LOC101959667 {ECO:0000313|Ensembl:ENSSTOP00000021644}; OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) OS (Spermophilus tridecemlineatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; OC Sciuridae; Xerinae; Marmotini; Ictidomys. OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000021644, ECO:0000313|Proteomes:UP000005215}; RN [1] {ECO:0000313|Ensembl:ENSSTOP00000021644} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG The Broad Institute Genome Assembly & Analysis Group; RG Computational R&D Group; RG and Sequencing Platform; RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.; RT "The Draft Genome of Spermophilus tridecemlineatus."; RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSSTOP00000021644} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAY-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTP01011073; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; I3NB97; -. DR STRING; 43179.ENSSTOP00000021644; -. DR Ensembl; ENSSTOT00000023969; ENSSTOP00000021644; ENSSTOG00000019821. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; I3NB97; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Proteomes; UP000005215; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005215}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005215}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 272 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5012858950. FT DOMAIN 114 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 272 AA; 29752 MW; 267599088609BA1E CRC64; MTTLLPLLLG LSLGCTGAGG FVAHVESTCL LDDDRNPKDF TYCISFNKDL LACWNPEEGK IAPCEFGTLY PLAQQISQYL NQNDNLLQRL RNGLQDCATH TQPFWKSLTN RTRPPSVQVA QATPFNTREP VMLACYVWGF YPAEVTITWM KNGQLINPNN SAQKTSQPNG DWTYQTVSHL PLTPSYGDIY TCVVEHFGNP GPIFQDWTPG LSPVQTVKVS VSAVTLGLGL IIFSLGCISW RNSASSSYIP LPGSNYPEGN LLICVPSVGG EG // ID J9PAY3_CANLF Unreviewed; 263 AA. AC J9PAY3; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 12-SEP-2018, entry version 37. DE SubName: Full=Major histocompatibility complex, class II, DM beta precursor {ECO:0000313|Ensembl:ENSCAFP00000042961}; GN Name=DLA-DMB {ECO:0000313|Ensembl:ENSCAFP00000042961}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000042961, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000042961, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000042961, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000042961} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000042961}; RG Ensembl; RL Submitted (SEP-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAEX03008236; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; J9PAY3; -. DR STRING; 9615.ENSCAFP00000042961; -. DR PaxDb; J9PAY3; -. DR PRIDE; J9PAY3; -. DR Ensembl; ENSCAFT00000043628; ENSCAFP00000042961; ENSCAFG00000032102. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; J9PAY3; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Reactome; R-CFA-2132295; MHC class II antigen presentation. DR Proteomes; UP000002254; Chromosome 12. DR Bgee; ENSCAFG00000032102; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003825762. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28892 MW; DE372A2236740595 CRC64; MTTLLPLLLG LSLGSTGEGG FIAHVESSCL LDDDGTPKDF TYCVSFNKDL LTCWDPDEAK MVPYEFGTLN VLANYLSDYL NQQEYLHQRL SNGLQDCATH TQSFWGSLTH RTRPPTVQVA KSTPFNTKES VMLACYVWGF YPADVTISWR KNGQPVPSHS SALNMAQPNG DWTYQTVSHL ATTPSYEDTY TCVVEHIGAP EPVCEDWTPG LSPMQTVKVS VSGVTLGLGF IIFSLGLLSW RRAGSSGYVF LPGTSYPEGQ HVS // ID J9PB59_CANLF Unreviewed; 237 AA. AC J9PB59; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 12-SEP-2018, entry version 32. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain precursor {ECO:0000313|Ensembl:ENSCAFP00000043037}; GN Name=HLA-DRB1 {ECO:0000313|Ensembl:ENSCAFP00000043037}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000043037, ECO:0000313|Proteomes:UP000002254}; RN [1] {ECO:0000313|Ensembl:ENSCAFP00000043037, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000043037, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000043037} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000043037}; RG Ensembl; RL Submitted (SEP-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAEX03008234; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAEX03008235; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; J9PB59; -. DR PRIDE; J9PB59; -. DR Ensembl; ENSCAFT00000047689; ENSCAFP00000043037; ENSCAFG00000000806. DR GeneTree; ENSGT00900000140849; -. DR Reactome; R-CFA-2132295; MHC class II antigen presentation. DR Proteomes; UP000002254; Chromosome 12. DR Bgee; ENSCAFG00000000806; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 100 188 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 237 AA; 27150 MW; FD5B05C3698077E5 CRC64; PDPPVPTAHF VYQFKPECHF TNGTERVRFV ERHIHNREEF VRFDSDVGEY RAVTELGRPD AESWNGQKEL LEQERATVDT YCRHNYGVIE SFTVQRRVEP TVTVYPTKTQ TLQHHNLLVC SVNGFYPGHI EVRWLRNGQE EEAGVVSTGL IRNGDWTFQI LVMLEIVPQS GEVYTCQVEH PSLTSPVTVE WSEKLPDISS STTKEGICLF LSVRVLSPYT IFSFPPYSLL FSTGPWG // ID K7E2Z6_MONDO Unreviewed; 278 AA. AC K7E2Z6; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 12-SEP-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMODP00000040147}; GN Name=MODO-DAB1 {ECO:0000313|Ensembl:ENSMODP00000040147}; OS Monodelphis domestica (Gray short-tailed opossum). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Metatheria; Didelphimorphia; Didelphidae; Monodelphis. OX NCBI_TaxID=13616 {ECO:0000313|Ensembl:ENSMODP00000040147, ECO:0000313|Proteomes:UP000002280}; RN [1] {ECO:0000313|Ensembl:ENSMODP00000040147, ECO:0000313|Proteomes:UP000002280} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17495919; DOI=10.1038/nature05805; RA Mikkelsen T.S., Wakefield M.J., Aken B., Amemiya C.T., Chang J.L., RA Duke S., Garber M., Gentles A.J., Goodstadt L., Heger A., Jurka J., RA Kamal M., Mauceli E., Searle S.M., Sharpe T., Baker M.L., Batzer M.A., RA Benos P.V., Belov K., Clamp M., Cook A., Cuff J., Das R., Davidow L., RA Deakin J.E., Fazzari M.J., Glass J.L., Grabherr M., Greally J.M., RA Gu W., Hore T.A., Huttley G.A., Kleber M., Jirtle R.L., Koina E., RA Lee J.T., Mahony S., Marra M.A., Miller R.D., Nicholls R.D., Oda M., RA Papenfuss A.T., Parra Z.E., Pollock D.D., Ray D.A., Schein J.E., RA Speed T.P., Thompson K., VandeBerg J.L., Wade C.M., Walker J.A., RA Waters P.D., Webber C., Weidman J.R., Xie X., Zody M.C., Baldwin J., RA Abdouelleil A., Abdulkadir J., Abebe A., Abera B., Abreu J., RA Acer S.C., Aftuck L., Alexander A., An P., Anderson E., Anderson S., RA Arachi H., Azer M., Bachantsang P., Barry A., Bayul T., Berlin A., RA Bessette D., Bloom T., Bloom T., Boguslavskiy L., Bonnet C., RA Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S., RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., RA Costello M., D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., RA Dhargay N., Dooley K., Dooley E., Doricent M., Dorje P., Dorjee K., RA Dupes A., Elong R., Falk J., Farina A., Faro S., Ferguson D., RA Fisher S., Foley C.D., Franke A., Friedrich D., Gadbois L., Gearin G., RA Gearin C.R., Giannoukos G., Goode T., Graham J., Grandbois E., RA Grewal S., Gyaltsen K., Hafez N., Hagos B., Hall J., Henson C., RA Hollinger A., Honan T., Huard M.D., Hughes L., Hurhula B., Husby M.E., RA Kamat A., Kanga B., Kashin S., Khazanovich D., Kisner P., Lance K., RA Lara M., Lee W., Lennon N., Letendre F., LeVine R., Lipovsky A., RA Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y., Lubonja R., RA Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C., RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O., RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., RA Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., RA Nicol R., Norbu C., Norbu N., Novod N., O'Neill B., Osman S., RA Markiewicz E., Oyono O.L., Patti C., Phunkhang P., Pierre F., RA Priest M., Raghuraman S., Rege F., Reyes R., Rise C., Rogov P., RA Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L., Shih D., RA Sparrow T., Spaulding J., Stalker J., Stange-Thomann N., RA Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T., RA Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T., RA Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., RA Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A., RA Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C., RA Gnerre S., MacCallum I., Graves J.A., Ponting C.P., Breen M., RA Samollow P.B., Lander E.S., Lindblad-Toh K.; RT "Genome of the marsupial Monodelphis domestica reveals innovation in RT non-coding sequences."; RL Nature 447:167-177(2007). RN [2] {ECO:0000313|Ensembl:ENSMODP00000040147} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; K7E2Z6; -. DR STRING; 13616.ENSMODP00000040147; -. DR Ensembl; ENSMODT00000043249; ENSMODP00000040147; ENSMODG00000012706. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; K7E2Z6; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Proteomes; UP000002280; Chromosome 2. DR Bgee; ENSMODG00000012706; Expressed in 8 organ(s), highest expression level in liver. DR ExpressionAtlas; K7E2Z6; baseline. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002280}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002280}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 240 260 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 138 242 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 278 AA; 30529 MW; 14755F2157CC9599 CRC64; MKSACCSGVD ILISPSHCGL GAGLEKEVEQ PGRIFVCGRA SEGAREHFTE YFISECYFIN GTEQVWLVQR YITNGEETVR FDSNVGVFEA VTESGRPDAE HWNSQKEFLE NLRAAVDTAC RHNYKISEPF LVRRRVEPEV LVYPSKTAPV GHHNLLVCSV SGFYPGAVAV TWSVNGQEQR AGVVSTGLMR NGDWTFQTLV MLEVTPQRGD VYTCHVEHSS LQKPVLVAWS AQSESAQSKM LSGVGGFVLG LIFFGVGLIV HMRSQKANRG SQPAGLLS // ID K7EU97_PONAB Unreviewed; 258 AA. AC K7EU97; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 28-MAR-2018, entry version 30. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSPPYP00000024121}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSPPYP00000024121}; OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000024121, ECO:0000313|Proteomes:UP000001595}; RN [1] {ECO:0000313|Ensembl:ENSPPYP00000024121, ECO:0000313|Proteomes:UP000001595} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wilson R.K., Mardis E.; RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome."; RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSPPYP00000024121} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ABGA01207495; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01278362; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ABGA01278363; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9601.ENSPPYP00000024121; -. DR Ensembl; ENSPPYT00000033384; ENSPPYP00000024121; ENSPPYG00000029571. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; K7EU97; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR TreeFam; TF336626; -. DR Proteomes; UP000001595; Chromosome 6. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl. DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001595}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001595}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003904269. FT TRANSMEM 227 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29238 MW; 67E2C8EB730CF862 CRC64; MMVLQVSASP RTVALTALLM VLLTSVVQGR ATPENYVYQA RHECYAFNGT QRLLERHIYN REEYVRFDSD VGEFRAVTEL GRPAAEYWNS QKDLLEEKRA EPDRVCRHNY ELDEAVTLQR RVQPKVNVSP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYIC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID K7F7N0_PELSI Unreviewed; 280 AA. AC K7F7N0; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 28-MAR-2018, entry version 33. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPSIP00000004040}; OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Trionychia; Trionychidae; OC Pelodiscus. OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000004040, ECO:0000313|Proteomes:UP000007267}; RN [1] {ECO:0000313|Ensembl:ENSPSIP00000004040} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17381049; DOI=10.1080/10425170600760091; RA Jung S.-O., Lee Y.-M., Kartavtsev Y., Park I.-S., Kim D.S., Lee J.-S.; RT "The complete mitochondrial genome of the Korean soft-shelled turtle RT Pelodiscus sinensis (Testudines, Trionychidae)."; RL DNA Seq. 17:471-483(2006). RN [2] {ECO:0000313|Proteomes:UP000007267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267}; RG Soft-shell Turtle Genome Consortium; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPSIP00000004040} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGCU01145890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; K7F7N0; -. DR STRING; 13735.ENSPSIP00000004040; -. DR Ensembl; ENSPSIT00000004063; ENSPSIP00000004040; ENSPSIG00000003812. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0F53; -. DR TreeFam; TF336626; -. DR Proteomes; UP000007267; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007267}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007267}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 280 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003901378. FT TRANSMEM 225 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 280 AA; 32142 MW; D58F755335D5AD68 CRC64; MAPGVNGNCW TAALIMAIGL RIHRAHCTDP PEYFLLQQKS ECYYTNGTQQ VRYVKRIIWG QQEICYYDSD LGFSVARTEL GRPFAEHWNS LELLSYLWAS VEKFCSYTYR RFKNITVDRR VKPRVKISTL TAEPSHRPSS LVCSATGFYP SKIETKWFKN GQEETAGIVS RQLLQNGDWT FQSHVMLETK PRWGDVYTCQ VEHISLQTPI SIQWATQSDS AKTKMFTGIV GFILGLSLMV LGLLIYQKNK RGTSLSSRVH HPNRELLGPQ VTQLEPVLWR // ID K7F7N5_PELSI Unreviewed; 253 AA. AC K7F7N5; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 28-MAR-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPSIP00000004045}; OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Trionychia; Trionychidae; OC Pelodiscus. OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000004045, ECO:0000313|Proteomes:UP000007267}; RN [1] {ECO:0000313|Ensembl:ENSPSIP00000004045} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17381049; DOI=10.1080/10425170600760091; RA Jung S.-O., Lee Y.-M., Kartavtsev Y., Park I.-S., Kim D.S., Lee J.-S.; RT "The complete mitochondrial genome of the Korean soft-shelled turtle RT Pelodiscus sinensis (Testudines, Trionychidae)."; RL DNA Seq. 17:471-483(2006). RN [2] {ECO:0000313|Proteomes:UP000007267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267}; RG Soft-shell Turtle Genome Consortium; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPSIP00000004045} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGCU01145890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_014433461.1; XM_014577975.1. DR Ensembl; ENSPSIT00000004068; ENSPSIP00000004045; ENSPSIG00000003812. DR GeneID; 102458068; -. DR KEGG; pss:102458068; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR Proteomes; UP000007267; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007267}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007267}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 253 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003901297. FT TRANSMEM 225 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 253 AA; 29038 MW; CAE09DE3FC7C2C11 CRC64; MAPGVNGNCW TAALIMAIGL RIHRAHCTDP PEYFLLQQKS ECYYTNGTQQ VRYVKRIIWG QQEICYYDSD LGFSVARTEL GRPFAEHWNS LELLSYLWAS VEKFCSYTYR RFKNITVDRR VKPRVKISTL TAEPSHRPSS LVCSATGFYP SKIETKWFKN GQEETAGIVS RQLLQNGDWT FQSHVMLETK PRWGDVYTCQ VEHISLQTPI SIQWATQSDS AKTKMFTGIV GFILGLSLMV LGLLIYQKNK RGE // ID K7FHZ3_PELSI Unreviewed; 185 AA. AC K7FHZ3; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 28-MAR-2018, entry version 27. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPSIP00000007653}; OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Trionychia; Trionychidae; OC Pelodiscus. OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000007653, ECO:0000313|Proteomes:UP000007267}; RN [1] {ECO:0000313|Ensembl:ENSPSIP00000007653} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17381049; DOI=10.1080/10425170600760091; RA Jung S.-O., Lee Y.-M., Kartavtsev Y., Park I.-S., Kim D.S., Lee J.-S.; RT "The complete mitochondrial genome of the Korean soft-shelled turtle RT Pelodiscus sinensis (Testudines, Trionychidae)."; RL DNA Seq. 17:471-483(2006). RN [2] {ECO:0000313|Proteomes:UP000007267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267}; RG Soft-shell Turtle Genome Consortium; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPSIP00000007653} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGCU01110602; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; K7FHZ3; -. DR Ensembl; ENSPSIT00000007694; ENSPSIP00000007653; ENSPSIG00000007000. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G0NF1; -. DR Proteomes; UP000007267; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007267}; KW Reference proteome {ECO:0000313|Proteomes:UP000007267}. FT DOMAIN 92 184 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 185 AA; 20863 MW; 5467E834325C241E CRC64; PPEPYYMQIL KICEVDDAAS NIRAVTRYAL NGEEVLRYQS DQNRWFSVHP SAWPLAERWN QAKETFAEIT PQRCMFFIEQ SAQFITGKTA QPTARVALIP GTQALPRRLI CHVTGFYPHH IEVTWERGGQ VAQGEQLSSG IRPNADPTFQ TQVSIELGQE GTSPAEHVCV VRHSSLGNTT LRVTW // ID K7FJC0_PELSI Unreviewed; 241 AA. AC K7FJC0; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 28-MAR-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPSIP00000008130}; OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Trionychia; Trionychidae; OC Pelodiscus. OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000008130, ECO:0000313|Proteomes:UP000007267}; RN [1] {ECO:0000313|Ensembl:ENSPSIP00000008130} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17381049; DOI=10.1080/10425170600760091; RA Jung S.-O., Lee Y.-M., Kartavtsev Y., Park I.-S., Kim D.S., Lee J.-S.; RT "The complete mitochondrial genome of the Korean soft-shelled turtle RT Pelodiscus sinensis (Testudines, Trionychidae)."; RL DNA Seq. 17:471-483(2006). RN [2] {ECO:0000313|Proteomes:UP000007267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267}; RG Soft-shell Turtle Genome Consortium; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPSIP00000008130} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGCU01110604; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; K7FJC0; -. DR Ensembl; ENSPSIT00000008173; ENSPSIP00000008130; ENSPSIG00000007434. DR GeneTree; ENSGT00900000140849; -. DR OMA; YEILEPF; -. DR OrthoDB; EOG091G0NF1; -. DR Proteomes; UP000007267; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007267}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000007267}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 200 220 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 90 187 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 241 AA; 26605 MW; 93A81E4C2491F708 CRC64; PAEPYYMQVL KTCELDDDTD AVRAVTRYSL NGEDVVWYDA EQNRWFTVHP AASHVAELWN REAKTFGELK VHTEQHCRFV MKITEAFITE KTAQPTARVA LVPGTQARPG RLVCHVTGFY PRDIEVTWER GGQVAQGEQL TRGIRPNGDT TFQIQVSIEL GKEGTGPPEH VCVVRHSSLG NTTLRVSWDS QPPGLAGVPW IVAGCILAVL GVGALGLLLW KRPAGQKGPY HLAQMQPGTL N // ID K7G587_PELSI Unreviewed; 197 AA. AC K7G587; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 28-MAR-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSPSIP00000015448}; OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Trionychia; Trionychidae; OC Pelodiscus. OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000015448, ECO:0000313|Proteomes:UP000007267}; RN [1] {ECO:0000313|Ensembl:ENSPSIP00000015448} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=17381049; DOI=10.1080/10425170600760091; RA Jung S.-O., Lee Y.-M., Kartavtsev Y., Park I.-S., Kim D.S., Lee J.-S.; RT "The complete mitochondrial genome of the Korean soft-shelled turtle RT Pelodiscus sinensis (Testudines, Trionychidae)."; RL DNA Seq. 17:471-483(2006). RN [2] {ECO:0000313|Proteomes:UP000007267} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267}; RG Soft-shell Turtle Genome Consortium; RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSPSIP00000015448} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2012) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGCU01110602; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; K7G587; -. DR Ensembl; ENSPSIT00000015520; ENSPSIP00000015448; ENSPSIG00000013783. DR GeneTree; ENSGT00900000140849; -. DR Proteomes; UP000007267; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000007267}; KW Reference proteome {ECO:0000313|Proteomes:UP000007267}. FT DOMAIN 133 197 IGc1. {ECO:0000259|SMART:SM00407}. SQ SEQUENCE 197 AA; 22335 MW; 9F3FDC2B5D25F3D9 CRC64; HAQSWSPWQV TLGGSGQLDQ SVEFVRTSPE PFYMQILKNC ELDDATGAVQ IVTRYSLNGE DVLRYQSDQN HWFSVHPVAR SLAEHWNRTR ETFAGLTPQR CKFLIEESRE FITGKTAQPK VRVIPVPAAL DQPHRLICHV TDFYPRNIEV TLERGEQLSS GIRPNGDSTF QIQVSIKLGQ ERAGPTEHVC VVRHSSL // ID L5KZ13_PTEAL Unreviewed; 630 AA. AC L5KZ13; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 23. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:ELK16647.1}; GN ORFNames=PAL_GLEAN10007119 {ECO:0000313|EMBL:ELK16647.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK16647.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|RuleBase:RU004238, ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB030441; ELK16647.1; -; Genomic_DNA. DR InParanoid; L5KZ13; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 2. DR Gene3D; 3.10.320.10; -; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR001003; MHC_II_a_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 2. DR Pfam; PF00993; MHC_II_alpha; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 2. DR SMART; SM00920; MHC_II_alpha; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 2. DR SUPFAM; SSF54452; SSF54452; 2. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS00290; IG_MHC; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 630 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003969693. FT TRANSMEM 234 254 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 121 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 402 484 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 630 AA; 69634 MW; 059669AA84E2C986 CRC64; MDYELSQGAA LLWLLPFLWL LPHSWTAPQA PTPRWQDDLQ NHTFLHTMYC QNASPSVALS ESYDEDQLFS FDFSQNIRVP RLPEFADWAQ KSEDISTIFF DKGFCQAMIH EIGPRLEGQI PVSRGIPVAE VFTLKPLEFG KPNTLVCFVS NLFPPALTVN WQHHSAPVEG VGPTYVSAID GLSFQAFSYL NFTPVPSDIF SCIVTHEIDS HTAIAYWVPQ NALPSDLLEN VLCGVAFGLG VLGIIVGLVL IIYFRKPCSG GLKIIYPDWG FWSRQGFKAP GGAGPGDRIA CVFPQQTMTI LLQLLLGLGL GCTGADGFVA HVESTCLLDD DGTPQEFTYC ISFNKDLLTC WDPEEHRMAP CEFGALNVLA TYLSSYLNPQ ENLLQRLTEG PFWGSLTRRT RPPSVQVAKT TPFNTREPVM LACYVWGFYP MDVTITWRKN GKLVLPHGSA HKTAQPNGDW TYQTISYLAT TPSFGDVYTC VVEHIGAPDP ILQDWTPGLS PVQTLKVSVS AVTLGLGLII FSLGLLSWRR AGSSGYTSLP GSNYPEGNIC VGLFANWSFG RCEVGRGSQH WAQLTVIIVG VRFHQDRVKS LCKQPLLRLG AGKKRPFSSN HGVSLGKRLK VVPEFSISLY // ID L5KZ18_PTEAL Unreviewed; 225 AA. AC L5KZ18; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain {ECO:0000313|EMBL:ELK16652.1}; GN ORFNames=PAL_GLEAN10007124 {ECO:0000313|EMBL:ELK16652.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK16652.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB030441; ELK16652.1; -; Genomic_DNA. DR ProteinModelPortal; L5KZ18; -. DR InParanoid; L5KZ18; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 24 {ECO:0000256|SAM:SignalP}. FT CHAIN 25 225 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003969696. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 225 AA; 25522 MW; 2523EC33DBE7B3A9 CRC64; MGSGWVPWVV GLLVNLIRLN SSMTQGRDSL EDFVIQAKAD CYFTNGTERV QFVVRFIFNL EEYAHFDSDV GMFVALTELG QPDVELWNNR PDILERSRAS VDALCRHNYK LGAPFTVGRK VQPEVTVYLE KLPTLQHHNV LLCSVTDFYP GDIKIRWFRN GQEERAGVMS TGLIRNGDWT FQITVMLEMT PEFGDVYTCL VDHASLLSPV SVEWSENQLL VLSGA // ID L5L081_PTEAL Unreviewed; 105 AA. AC L5L081; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 05-OCT-2016, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DRB1-1 beta chain {ECO:0000313|EMBL:ELK16681.1}; GN ORFNames=PAL_GLEAN10015914 {ECO:0000313|EMBL:ELK16681.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK16681.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB030438; ELK16681.1; -; Genomic_DNA. DR InParanoid; L5L081; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}. FT DOMAIN 2 67 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 105 AA; 12193 MW; B27077E89176EF75 CRC64; MEQVQLVTRC IYNREELVRF DNDVGEYRAV TELRRPEAEY WNSQEDILEQ TRADAGRRRP RRTGCADTTT RWTPPLPGNA TSGVHSPMEE MDKQTNSFSM VTEVL // ID L5L0S0_PTEAL Unreviewed; 188 AA. AC L5L0S0; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=HLA class II histocompatibility antigen, SB beta chain {ECO:0000313|EMBL:ELK16643.1}; GN ORFNames=PAL_GLEAN10007114 {ECO:0000313|EMBL:ELK16643.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK16643.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB030441; ELK16643.1; -; Genomic_DNA. DR ProteinModelPortal; L5L0S0; -. DR InParanoid; L5L0S0; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 54 142 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 188 AA; 21576 MW; DE4C97BFAA412A01 CRC64; MGVFVAVTEL RRITAKNWNI QREFLELRKS AVDTVCRHNY ELDKGFALKC RVQPKVNVFP SKKGLLQHHN LFVCHVTDFY PGNVQVHWFL NGQEETTGVV STNLIYNGDW TFHLLVMLEM TPQQENVYTC QVEHPSLDSP VTVEWNESLL DDPLGSRVWS LLTTHWGHTP MDSLDIPQLG QSCHCGVE // ID L5L0T1_PTEAL Unreviewed; 609 AA. AC L5L0T1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=BOLA class II histocompatibility antigen, DQB*0101 beta chain {ECO:0000313|EMBL:ELK16653.1}; GN ORFNames=PAL_GLEAN10007125 {ECO:0000313|EMBL:ELK16653.1}; OS Pteropus alecto (Black flying fox). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; OC Pteropodidae; Pteropodinae; Pteropus. OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK16653.1, ECO:0000313|Proteomes:UP000010552}; RN [1] {ECO:0000313|Proteomes:UP000010552} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB030441; ELK16653.1; -; Genomic_DNA. DR ProteinModelPortal; L5L0T1; -. DR InParanoid; L5L0T1; -. DR Proteomes; UP000010552; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 2. DR Gene3D; 3.10.320.10; -; 3. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 2. DR Pfam; PF00969; MHC_II_beta; 2. DR ProDom; PD000328; MHC_II_b_N; 3. DR SMART; SM00407; IGc1; 2. DR SMART; SM00921; MHC_II_beta; 3. DR SUPFAM; SSF48726; SSF48726; 2. DR SUPFAM; SSF54452; SSF54452; 3. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS00290; IG_MHC; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010552}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010552}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 258 278 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 550 570 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 127 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 448 538 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 609 AA; 69858 MW; B5EC2A7427E26D08 CRC64; MTVTILRNPW TVAGIVMVIL MVLRTPMAHC RGVPKDFVYQ FKGMCYFTNG TERVRLVARQ IYNKEEIVRF DSDVGMFVAV TELGRSNAQS WNSQKDLLAQ YRAQVDTLCR HNYKETAQFT VQRREEPTVT ISPARTEFLN HHNLLVCMVT NFYPRQIKVR WFRNKLEEKA GVVSTPLIQN GDWTYQILVM LEIVPQRGDV YICHVDHSSL QRPITVEWRK GRFTDTMDSD NTTGREDSAS GAQSESAQSK MLSGIEGFVL GLISFGLGFI IHLWNMKVMS GMMALQIPRG LWTAAVMVTL VVLSTPVAEG RDSPQDFVYQ FKSYCYFTNG TERVRLLNRY VYNLEEYVGF DSDVGEFRAV TELGRHTAEY WNSQADILEV ARYVYNLEEF VRFDSDVWEY RAVTELGRPD AEYWNSDFVE QTRAVVDTVC RHNYQLETHM SLKRRVIPTV TVSPSKTEAL NHHNLLVCSV TDFYPGQIKV RWFRNDQEET AGIVSTPLIR NGDWTFQIIV MLEMTPQQGD VYTCHVEHPS LQSPTTVEWR AQSESAQSKM LSGVGGFVLG LIFLVLGLFI RHRKQKGIRK VTTHCGSLHM DPILKAGLHL NLWVMKMGG // ID L5LIG2_MYODS Unreviewed; 236 AA. AC L5LIG2; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 30. DE SubName: Full=HLA class II histocompatibility antigen, DRB1-4 beta chain {ECO:0000313|EMBL:ELK26104.1}; GN ORFNames=MDA_GLEAN10006832 {ECO:0000313|EMBL:ELK26104.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26104.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB111258; ELK26104.1; -; Genomic_DNA. DR RefSeq; XP_006769195.1; XM_006769132.2. DR ProteinModelPortal; L5LIG2; -. DR GeneID; 102753992; -. DR KEGG; myd:102753992; -. DR KO; K06752; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 236 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003970220. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 236 AA; 27041 MW; C68BD1CF55862F04 CRC64; MVCLRFPGGT LMATLMVMLM ALSPPMTQAR DTPPNFLVQH KGECHFSNGT ERVQYLDRYF YNGEEYARFD SDVGEFHAVT ELGRPDNEYW NSQEDLLEEK RAEVDRYCRH NYWLCEGSLV QRQTEPTVTM YPAKTQRLQH HNLLVCSVSG FYPGHIEVRW LRNGQEEEAG VVSTGLILNG DWTFQTLVML ETVPLRGEVY TCQVRHPSST SSVTVEWSET PSDLTHLQPR GAFACP // ID L5LIR9_MYODS Unreviewed; 240 AA. AC L5LIR9; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:ELK26102.1}; GN ORFNames=MDA_GLEAN10006830 {ECO:0000313|EMBL:ELK26102.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26102.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB111258; ELK26102.1; -; Genomic_DNA. DR ProteinModelPortal; L5LIR9; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 202 224 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 100 188 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 240 AA; 26876 MW; 2937338BCBCEBAC3 CRC64; MAILSHQAHF LGQAKSECHF SNGTERVRFL DRYIYNGQEG VRFDSDVGEY RALTELGRPD AEYWNSQEDI LEDARAQVDK LCMYNYEVSD KYLMQWQTEP TVTGYPAKTQ RLQHHNLLVC SVNGFSPGHI EVRWLRNGQE QEAGVVSTGL IRNGDWTFQI LVMLETVPRS GEVYTCQVQH PSSPSPVTVE WRAQSGSAQS KMLSGAGGFM LGLLFLGAGL LIYFRAQKGH SGLQPTGNAL // ID L5LJC5_MYODS Unreviewed; 173 AA. AC L5LJC5; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 18. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:ELK26100.1}; GN ORFNames=MDA_GLEAN10006828 {ECO:0000313|EMBL:ELK26100.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26100.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB111258; ELK26100.1; -; Genomic_DNA. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 135 157 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 17 91 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 173 AA; 19509 MW; 83F56DB240DA1967 CRC64; MMVLTVPSAH FLEQLKSECH FSNGTERVRY LQRYIHNGQE DVRFDSDVGE YHAVTELGRP DAEAWNSQKD SLEQKRAEVD TFCREAYRVL DGFLVHRQTE PTVTVYPSKT QRLQHHNLLV CSVNGFYPGH IESKVLSGAS GFVLGLLFLG AGLLIYFRAQ KGHSGLQPTG NTL // ID L5LJF5_MYODS Unreviewed; 259 AA. AC L5LJF5; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 24. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:ELK26135.1}; GN ORFNames=MDA_GLEAN10006863 {ECO:0000313|EMBL:ELK26135.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26135.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB111258; ELK26135.1; -; Genomic_DNA. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 259 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003970240. FT TRANSMEM 227 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 122 228 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 259 AA; 28470 MW; D9CE593AB65B69D8 CRC64; MPRLPRQIMG ALLRLLLGLS LGCTGTGGFV AHVVSTCLLD DNGIPQDFTY CISFNKDLLT CWDPEERAMV PVEFGVLNPL AANFANYLNK QEILIQRLSA GLQDCATRTQ PFWESLTQRT RPPSVQVAKA TPVNTREPVM LACYVWGFYP ADVTITWRKN GQLVPPHGSA HKVIQSNGDW TYQTLSHLAT TPSFGDTYTC VVEHFGALEP ILQDWTPGLS PEQTVKVSVS VVTLGLGLII FSLGLLSWRR AGSSGRHIS // ID L5LJG1_MYODS Unreviewed; 282 AA. AC L5LJG1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 24. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|EMBL:ELK26140.1}; GN ORFNames=MDA_GLEAN10006868 {ECO:0000313|EMBL:ELK26140.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26140.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB111258; ELK26140.1; -; Genomic_DNA. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 282 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003970361. FT TRANSMEM 228 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 282 AA; 31948 MW; 8611AFEC7B9F5269 CRC64; MTRTPRSPWA AAGIVTVVLT VLRTPLAHRR GTPADFVYQF KGTCYFTNGT QRVRLVATQI YNRQEIVRFD SDVGVFVAVT ELGRPHAESW NSQEDLLLVY RAQVDVLCRH NYKETAPFTV QRRVEPTVTI SPSRTEALNH HNMLVCSVTD FYPAHIKVRW FRNDQEETAG VVSTPLIRNG DWTYQVLVML EMSPQRGDVY TCRVEHPSLQ SPITVEWRAQ SESAQSKMLS GIGGFVLGLA FLGLGLVVHL WKKKESSSKE DSEKDCSLSL MHRHTISSTI QQ // ID L5LJN2_MYODS Unreviewed; 300 AA. AC L5LJN2; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 24. DE SubName: Full=HLA class II histocompatibility antigen, DR beta 5 chain {ECO:0000313|EMBL:ELK26101.1}; GN ORFNames=MDA_GLEAN10006829 {ECO:0000313|EMBL:ELK26101.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26101.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB111258; ELK26101.1; -; Genomic_DNA. DR ProteinModelPortal; L5LJN2; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 163 251 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 300 AA; 33038 MW; 49689ACC14B4CCB0 CRC64; MAQVLAQPGA RSPTGQPSGS QWLRVPGVSL PCGLPATAEG TRALAAGVPG PVSPPPGSPT LGDVAIFSHQ PNFLYQRKCE CHFANGTERV QFLYRDIYNG QENVRFDSDV GECRALTELG RPDAEYWNSQ KDKLERARAY VDTFCRHNYG VFEGFSVQQK TEPTVTVYPA KTQRLQHHNL LVCSVNGFYP GHIEVRWLRN GQEEEAGVVS TGLILNGDWT FQILVMLETV PLRGEVYTCQ VRHPSRTSPV TVEWSEMPSD LTCLPQQGPL LVSEGQGPLS PQPVFLCACL SFTTGHRVAL // ID L5LJQ1_MYODS Unreviewed; 305 AA. AC L5LJQ1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|EMBL:ELK26131.1}; GN ORFNames=MDA_GLEAN10006859 {ECO:0000313|EMBL:ELK26131.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK26131.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB111258; ELK26131.1; -; Genomic_DNA. DR ProteinModelPortal; L5LJQ1; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 305 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003970366. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 305 AA; 34287 MW; 89C6E01F614FCB77 CRC64; MVAPQAPGAP CMAALLMPLV MLSSPWAQGR DTTAVHVYQR RSDCYESNGT HRFLERYVYN RDVFVQFDST VGVFVAVTEL GRTTARNWNI QGEFLELRRG AVDAVCRHNY ELDRAFTLER RVQPKVNVSP SKKGPLQHPD LLVCHVTDFY PGHVQVRWFL NGQEETAGVV STNLIHNGDW TFQILVMLEM TPQQGDVYTC HVEHPSLDSA VTVEWKAQSD SARSKMLTGV GGFVLGLLAL VVSATVHFRG QQGKNPWKVV DIALPLSHSV MTLRQKSKMT ERMRPLKSDS GPAMTDDRRA DRKRP // ID L5LZW8_MYODS Unreviewed; 131 AA. AC L5LZW8; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 05-OCT-2016, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DRB1-4 beta chain {ECO:0000313|EMBL:ELK31612.1}; GN ORFNames=MDA_GLEAN10001158 {ECO:0000313|EMBL:ELK31612.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31612.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB105970; ELK31612.1; -; Genomic_DNA. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}. FT DOMAIN 21 95 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 131 AA; 15194 MW; 5E6DC05BF4EFD195 CRC64; MTIKKFLKAK VAGGTELTPK AECHFYNGTE QVRYLERYFY NRQEYVHFDS DLGEYRALTE LGWPDEKDWN SQEDLMEQKR AALNKFCRHN YWVSEGFSVQ RKSERGVGEE GQVACVPVCV CVCVGRTHTG L // ID L5M013_MYODS Unreviewed; 288 AA. AC L5M013; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 24. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:ELK31610.1}; GN ORFNames=MDA_GLEAN10001156 {ECO:0000313|EMBL:ELK31610.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31610.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB105970; ELK31610.1; -; Genomic_DNA. DR ProteinModelPortal; L5M013; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 2. DR ProDom; PD000328; MHC_II_b_N; 2. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 2. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 2. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 144 232 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 288 AA; 33759 MW; 1132D4989C531835 CRC64; MGEFRAETEL RRPIAEFFNS LEVLLQRERA QVDRFCRDNY RFSEGFLVQR QTHFLYQPKS ECHFSNGTEQ VRFLERHIYN GQEFMCFDTD MGEFRAETEL RRPIAEFFNS LEVLLQRERA QVDRFCRDNY RFSEGFLVQR QTEPTVTVYP AKTQRLQHHN LLVCCVSDFY PGHIEVHWLR NGQEEEAVVV TMGLIQNGDW TFQTLVMLET VPRSGELYTC QVRHPSSTSP VTVEWSETPS DLTHFPLRGL CLSLRVRVPS SHTPFSCARV FPSAQATGEP CDRFCEHP // ID L5M0Y8_MYODS Unreviewed; 318 AA. AC L5M0Y8; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=BoLa class II histocompatibility antigen, DQB*0101 beta chain {ECO:0000313|EMBL:ELK31996.1}; GN ORFNames=MDA_GLEAN10000540 {ECO:0000313|EMBL:ELK31996.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31996.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB105889; ELK31996.1; -; Genomic_DNA. DR ProteinModelPortal; L5M0Y8; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 318 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003970763. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 227 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 318 AA; 35205 MW; E73DD38AADABB76C CRC64; MSGKPALWGP GGPWTAAVMV WLVALSFPVA EGGDSPCPLL LHQRDGTQRV RLLTSYIYNL EEYARFDSEV GEYRALTPLG RPTVEYFNSQ KDILEEARAE VDTVCRPNYQ NEARTTLQRR VEPTVTISPA KTEALNHHNM LVCSVTDFYP AHIKVRWFRN NQEETAGVVS TPLIRNGDWT YQILVMLEMT PQRGDIYTCR VEHPSLQSPI AVEWRAQSGS AQSKMLSGIG GFVLGLIFLG LGLVIRHRKQ KGKQLGKRED GLCPGPSVES TGVTVASILG LRSHHCLPGP FPEAASLRSG LWLPFLLVTG PFIWGIVA // ID L5M1N0_MYODS Unreviewed; 278 AA. AC L5M1N0; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:ELK31613.1}; GN ORFNames=MDA_GLEAN10001159 {ECO:0000313|EMBL:ELK31613.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK31613.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB105970; ELK31613.1; -; Genomic_DNA. DR ProteinModelPortal; L5M1N0; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 218 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 96 182 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 278 AA; 31219 MW; 62F9981B635DEFE0 CRC64; MTAVHFLYQP KSECHFSNGT ERVRFLYRDI YNGQEDVRFD SDVGELRELT ELGRPDAEAW NSQKDYLERE RAYVNTLCRE SYRVAEGFLV QRQTEPTVTV YPAKTQRLQH HNLLVCFVNG FYPGNIEVRS SGEEEEAGVV STGLIRNGDW TFQTLVMLET VPRSGEVYTC QVRHPSRTSP VTVKWRAQSG SAQRKVLSGV GGFVLGLLFL GAGLLIYFRA QKGKEPAGSR GPKAVGGPGP LLGELWVWQC SRNFSYPVGP TFPGNAEITS SRLFRVET // ID L5M4X1_MYODS Unreviewed; 221 AA. AC L5M4X1; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 20. DE SubName: Full=BoLa class II histocompatibility antigen, DQB*0101 beta chain {ECO:0000313|EMBL:ELK32758.1}; GN ORFNames=MDA_GLEAN10000673 {ECO:0000313|EMBL:ELK32758.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK32758.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB105157; ELK32758.1; -; Genomic_DNA. DR ProteinModelPortal; L5M4X1; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 221 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003970870. FT DOMAIN 129 169 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 221 AA; 25394 MW; B03F39B9CDBAC991 CRC64; MSGKLALWPP RGPWTAAVMV WLVALSVPVA EGGDSPRDFV YQIKYLCYFT NGTQRVRAVE SYIYNLEELV RMDTDVGEYR AVTELGRPDA EYWNSQKDLL EQKRAQVDTV CRHNYQNEAR TTFQRRVEPT VTISPARTED MNHKNMLVCS VTDFYPAHIK VRWFRNDQEE TAVRRVHPPY QERGLDLPDP CDAGNDPPAR RRLHLPCGAP QPPEPHRSGV A // ID L5M6V3_MYODS Unreviewed; 196 AA. AC L5M6V3; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 25. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:ELK34047.1}; GN ORFNames=MDA_GLEAN10000117 {ECO:0000313|EMBL:ELK34047.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK34047.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB103403; ELK34047.1; -; Genomic_DNA. DR ProteinModelPortal; L5M6V3; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 100 180 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 196 AA; 22636 MW; 16C8911DA04706D5 CRC64; MAQVLAQPGG RSLPKSECHF SNGTEQVRFL ERHIYNGQED LRFDSDLGEF RAVTELGRPI AEFFNSLEVL LQRERAQVDR FCRDNYRFSE GFLVQRQTEP TVTVYPAKTQ RLQHHNLLVC SVNGFYPGHI EVRWLRNGQK EEAGVVSTGL IRNGDWTFQT LVMLETVPRS GEDYTCQVRH PSRTHCPDQP CHRGME // ID L5MBL8_MYODS Unreviewed; 99 AA. AC L5MBL8; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 05-OCT-2016, entry version 13. DE SubName: Full=HLA class II histocompatibility antigen, DRB1-15 beta chain {ECO:0000313|EMBL:ELK35128.1}; GN ORFNames=MDA_GLEAN10000737 {ECO:0000313|EMBL:ELK35128.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK35128.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB102551; ELK35128.1; -; Genomic_DNA. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}. FT DOMAIN 2 67 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 99 AA; 11617 MW; 5867CEB115F8B2D0 CRC64; MERVRYLETY IYNGQEDIRF DSDVGEYRAL TELRRPEEKL WSSQKDILER KRGAVDTFCR YNYRVSEGFL VPRQSERRGG VGGIGPMCRG ERGKVYTGL // ID L5MK76_MYODS Unreviewed; 294 AA. AC L5MK76; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 25-OCT-2017, entry version 24. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|EMBL:ELK38722.1}; GN ORFNames=MDA_GLEAN10000460 {ECO:0000313|EMBL:ELK38722.1}; OS Myotis davidii (David's myotis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK38722.1, ECO:0000313|Proteomes:UP000010556}; RN [1] {ECO:0000313|Proteomes:UP000010556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23258410; DOI=10.1126/science.1230835; RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X., RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., RA Zhou P., Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., RA Sun X., Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., RA Wang L.F., Wang J.; RT "Comparative analysis of bat genomes provides insight into the RT evolution of flight and immunity."; RL Science 339:456-460(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB098307; ELK38722.1; -; Genomic_DNA. DR ProteinModelPortal; L5MK76; -. DR Proteomes; UP000010556; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000010556}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000010556}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT DOMAIN 134 237 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 294 AA; 32670 MW; B7A743CD62F7255F CRC64; MVQRPVHLNP TCNHTKPHDP SQCQAQAGSR LLGVLETLSP LSPPFSRADP KAIAERGRAA GLSPAKGSRH AGQACQGQRP EGRLPAGDFL FQFKGLCYYT NGTQHVRLVT SYIYNREEFA RFDSYVGEFR AVTPQGRLDA EAWNSQKDFL EETRAYVDTV CRHNYPLDEA KALHQRAHIK VRWFRNDQEE TAGVVSTPLI RNGDWTYQIL VMLEMTPQRG DIYTCRVEHP SLQSPIAVEW RKGQFVSCTL GPTDRGQTAA PVCSIAALPL MSLLNGHHRT LEPSGAMAGA SEDS // ID L7N1E8_MYOLU Unreviewed; 266 AA. AC L7N1E8; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 28-MAR-2018, entry version 35. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000007083}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000007083, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000007083} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The genome sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000007083} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02060444; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006108279.1; XM_006108217.2. DR ProteinModelPortal; L7N1E8; -. DR STRING; 59463.ENSMLUP00000007083; -. DR Ensembl; ENSMLUT00000007757; ENSMLUP00000007083; ENSMLUG00000007755. DR GeneID; 102431574; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; L7N1E8; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003982256. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29739 MW; 3F230AA7FD4C6402 CRC64; MVCLRLPGGS WMAALKVMLM ALSPPLAQAR DTPPHFLHQQ KGECQFSNGT ERVRLLYRYI YNGQEYVRFD SDVGEHRAVT ELGRPAEEDF NSQENLLERM RAAVDRFCRH NYGVFGGFLV LQQTEPTVTV YPAKTQRLQH HNLLVCSVND FYPGHIEVRW LRNGQEEEAG VVSTGLIRNG DWTFQTLVML ETVPRSGEVY TCQVRHPSST SPVTVEWRAQ TGSAQSKVLS GAGGFVLGLL FLGAGLLIYF RAQKGHSGLQ PTGLLS // ID L7N1Q8_MYOLU Unreviewed; 269 AA. AC L7N1Q8; DT 06-MAR-2013, integrated into UniProtKB/TrEMBL. DT 06-MAR-2013, sequence version 1. DT 28-MAR-2018, entry version 32. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMLUP00000013135}; OS Myotis lucifugus (Little brown bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000013135, ECO:0000313|Proteomes:UP000001074}; RN [1] {ECO:0000313|Ensembl:ENSMLUP00000013135} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., RA Lindblad-Toh K.; RT "The genome sequence of Myotis lucifugus (Bat)."; RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Proteomes:UP000001074} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [3] {ECO:0000313|Ensembl:ENSMLUP00000013135} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAPE02049614; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02049615; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02049616; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAPE02049617; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; L7N1Q8; -. DR STRING; 59463.ENSMLUP00000013135; -. DR Ensembl; ENSMLUT00000014443; ENSMLUP00000013135; ENSMLUG00000014440. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; L7N1Q8; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000001074; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001074}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001074}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003982271. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 269 AA; 30162 MW; 37ED9EED7E4BA499 CRC64; MSGKPALWAP GGPWTAAVMV WLVALSVPVA EGGDSPGDFV YQGKALCYFT NGTEQVRLVA RYIYNREELV RFDSDVGEFR ALTPLGRPTA KYFNSQKDLL EEYRAYVDTL CRHNYPMVEA MALHQRVEPT VTISPARTEA LNHHNMLVCS VTDFYPAHIK VRWFRNDQEE TAGVVSTPLI RNGDWTYQIL VMLEMTPQRG DVYTCRVEHP SLQSPISVEW RAQSGSAQSK MLSGVGGFVL GLIFLGLGLV IRHRKQKGSH GPPPRYCLC // ID L7RZ36_CHLSB Unreviewed; 81 AA. AC L7RZ36; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 31-JAN-2018, entry version 25. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AGC12002.1}; DE Flags: Fragment; GN Name=Chsa-DRB {ECO:0000313|EMBL:AGC12002.1}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|EMBL:AGC12002.1}; RN [1] {ECO:0000313|EMBL:AGC12002.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24676686; DOI=10.1007/s00251-014-0770-9; RA Aarnink A., Jacquelin B., Dauba A., Hebrard S., Moureaux E., RA Muller-Trutwin M., Blancher A.; RT "MHC polymorphism in Caribbean African green monkeys."; RL Immunogenetics 66:353-360(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JX312685; AGC12002.1; -; Genomic_DNA. DR OrthoDB; EOG091G15IU; -. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; FT DOMAIN 7 81 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:AGC12002.1}. FT NON_TER 81 81 {ECO:0000313|EMBL:AGC12002.1}. SQ SEQUENCE 81 AA; 9771 MW; D39A8C4183D16A7E CRC64; FLWQAKAKCH FFNGTERVRY LERHFYNQEE LVRFDSDVGE YRAVSELGRP DAEYWNSLKD YLEQARAAVD NYCRHNYGVV E // ID L7RZP8_CHLSB Unreviewed; 81 AA. AC L7RZP8; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 05-JUL-2017, entry version 24. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AGC11999.1}; DE Flags: Fragment; GN Name=Chsa-DRB {ECO:0000313|EMBL:AGC11999.1}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|EMBL:AGC11999.1}; RN [1] {ECO:0000313|EMBL:AGC11999.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24676686; DOI=10.1007/s00251-014-0770-9; RA Aarnink A., Jacquelin B., Dauba A., Hebrard S., Moureaux E., RA Muller-Trutwin M., Blancher A.; RT "MHC polymorphism in Caribbean African green monkeys."; RL Immunogenetics 66:353-360(2014). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; JX312682; AGC11999.1; -; Genomic_DNA. DR OrthoDB; EOG091G15IU; -. DR ExpressionAtlas; L7RZP8; baseline. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; FT DOMAIN 7 81 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:AGC11999.1}. FT NON_TER 81 81 {ECO:0000313|EMBL:AGC11999.1}. SQ SEQUENCE 81 AA; 9881 MW; C7D31648ADE645B4 CRC64; FLEQVKSECH FFNGTERVRF LDRYFYNQEE YVRFDSDVGE FRAVSELGRH SAEYWNSRKD LLEDERASVD NYCRYNYGVV E // ID L8Y0J3_TUPCH Unreviewed; 272 AA. AC L8Y0J3; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 25-OCT-2017, entry version 24. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|EMBL:ELV09848.1}; GN ORFNames=TREES_T100010374 {ECO:0000313|EMBL:ELV09848.1}; OS Tupaia chinensis (Chinese tree shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia. OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV09848.1, ECO:0000313|Proteomes:UP000011518}; RN [1] {ECO:0000313|Proteomes:UP000011518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhang G., Fan Y., Yao Y., Huang Z.; RT "Genome of the Chinese tree shrew, a rising model animal genetically RT related to primates."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB369523; ELV09848.1; -; Genomic_DNA. DR ProteinModelPortal; L8Y0J3; -. DR InParanoid; L8Y0J3; -. DR Proteomes; UP000011518; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011518}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011518}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 272 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003997970. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 272 AA; 31263 MW; E0858B4780AC0A29 CRC64; MVLQVIGATW MAARMVSLVM LSSALAQGRD TPEMYVYQRR SDCFEFNGTH RFLERYVYNR EVYVQFDSAV GSFTAETQLG EITAQKWNRW KGFLELRRSA VDTVCRHNYE LDEGFTLKRR VQPRVNVSPS KKRPLQHHNL LVCHVTDFYP GDIRVRWFLN GKEETDGVVS TNLIRNGDWT YQILVVLETI PQQGDVYTCH VEHPSLDRPV TVEWKAQSDS ARTKMLTGVG GFVLGLTSLV ASFVLHLRNQ RGKKTSGKHW YHLPTVLSSL LL // ID L8Y201_TUPCH Unreviewed; 264 AA. AC L8Y201; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 25-OCT-2017, entry version 23. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|EMBL:ELV10297.1}; GN ORFNames=TREES_T100021334 {ECO:0000313|EMBL:ELV10297.1}; OS Tupaia chinensis (Chinese tree shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia. OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV10297.1, ECO:0000313|Proteomes:UP000011518}; RN [1] {ECO:0000313|Proteomes:UP000011518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhang G., Fan Y., Yao Y., Huang Z.; RT "Genome of the Chinese tree shrew, a rising model animal genetically RT related to primates."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB368061; ELV10297.1; -; Genomic_DNA. DR ProteinModelPortal; L8Y201; -. DR InParanoid; L8Y201; -. DR Proteomes; UP000011518; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011518}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011518}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003998156. FT DOMAIN 125 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 30436 MW; CD767E090BDAC317 CRC64; MMVLQVAEGP WTVALMMTLL VLLNPMVQVK ATPGKYVWQG LQECYTVNGT QRYVERHVYN REEYARFDSH LGKFQAVTEL GRPSVNHWND RKDILEQKQG RVDTMCRHIY EQYEGFPPQR LVARPDVNVF LSKKRPLQHH NMLICHVTDF YPGDIRVRWF LNGKEETDGV VSTKVIRNGD WTYQILVVLE MIPQQGDVYT PMSVDFMDRP GGQPLVEVTR TKTQNLGAFH IYLPTLGPGL ASWSPSDPVR LQDVRQGPGP SRQR // ID L8Y8U7_TUPCH Unreviewed; 221 AA. AC L8Y8U7; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 25-OCT-2017, entry version 24. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|EMBL:ELV12863.1}; GN ORFNames=TREES_T100003536 {ECO:0000313|EMBL:ELV12863.1}; OS Tupaia chinensis (Chinese tree shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia. OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV12863.1, ECO:0000313|Proteomes:UP000011518}; RN [1] {ECO:0000313|Proteomes:UP000011518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhang G., Fan Y., Yao Y., Huang Z.; RT "Genome of the Chinese tree shrew, a rising model animal genetically RT related to primates."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB364355; ELV12863.1; -; Genomic_DNA. DR ProteinModelPortal; L8Y8U7; -. DR InParanoid; L8Y8U7; -. DR Proteomes; UP000011518; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011518}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011518}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 221 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003998436. FT DOMAIN 107 195 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 221 AA; 25533 MW; 20751DA8AFE7E96F CRC64; MSWKMAQQLS RGLWTAAVTV MLMVLSTRPA EGRDSPQDFV FQFKFQCYFT NGTQRVRLVT RYIYNLEEFA GFDSDLWEYR AVTELGRRDA KYWNEQQDVL EGTLEKPTVT ISPSRTEALN HHNLLVCSVT DFYPGQIKVR WFRNNQEETA GIVSTPLIRN GDWTFQIMVM LEMAPQRGDV YTCQVEHPSL QSPITVEWRK RKFVSFTVGP TRQGKASSGL A // ID L8Y9Y0_TUPCH Unreviewed; 274 AA. AC L8Y9Y0; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 25-OCT-2017, entry version 23. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:ELV11889.1}; DE Flags: Fragment; GN ORFNames=TREES_T100006953 {ECO:0000313|EMBL:ELV11889.1}; OS Tupaia chinensis (Chinese tree shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia. OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV11889.1, ECO:0000313|Proteomes:UP000011518}; RN [1] {ECO:0000313|Proteomes:UP000011518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhang G., Fan Y., Yao Y., Huang Z.; RT "Genome of the Chinese tree shrew, a rising model animal genetically RT related to primates."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB364864; ELV11889.1; -; Genomic_DNA. DR ProteinModelPortal; L8Y9Y0; -. DR InParanoid; L8Y9Y0; -. DR Proteomes; UP000011518; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011518}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011518}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 218 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:ELV11889.1}. SQ SEQUENCE 274 AA; 30766 MW; 803D8E048F954B69 CRC64; HGVSVVSWRL LDGSSGSDTD GAEPSPDFSQ GHQTLEWVPK GSGSKGFYCQ SGVLLQFLDR YFYNREEYLR FDSDVGEYRA VTELGRPDAE YWNRLTDRLD YLRGAVDTYC RHNYGVGESF TVQRRAQPKV TVYPTRTQPL QHHSLLVCSV NGFYPGNIEV RWFRNGQEEK AGVVSTGLIR NGDWTFQILV MLETVPQSGE VYTCQVEHPS LTDPVRMEWR AQSESVQGKM LSGIGGSVLG LLFLGVGLFI HKRNQKGHSG LQPTGMTFTS LLET // ID L8YBX5_TUPCH Unreviewed; 281 AA. AC L8YBX5; DT 03-APR-2013, integrated into UniProtKB/TrEMBL. DT 03-APR-2013, sequence version 1. DT 25-OCT-2017, entry version 24. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:ELV12569.1}; GN ORFNames=TREES_T100016443 {ECO:0000313|EMBL:ELV12569.1}; OS Tupaia chinensis (Chinese tree shrew). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia. OX NCBI_TaxID=246437 {ECO:0000313|EMBL:ELV12569.1, ECO:0000313|Proteomes:UP000011518}; RN [1] {ECO:0000313|Proteomes:UP000011518} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Zhang G., Fan Y., Yao Y., Huang Z.; RT "Genome of the Chinese tree shrew, a rising model animal genetically RT related to primates."; RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB364440; ELV12569.1; -; Genomic_DNA. DR ProteinModelPortal; L8YBX5; -. DR InParanoid; L8YBX5; -. DR Proteomes; UP000011518; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011518}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011518}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 281 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003998448. FT TRANSMEM 219 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 205 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 281 AA; 30542 MW; F851FF0E17CE5A4B CRC64; MTTLLPLLLG LSLGCSGAGG FVAHVERNCL LDDDGNPKDF TYCVSFNKDL LTCWDKEEDK MVPLEFGFLQ HLAGYIADIL NQEETLLQRL RSGLQDCSTH TQPFWGPLTH RTRPPLVQVA QTTPFNTRES VMLACYVWGF YPADVTITWM KNGQLVAPHN SGQKTAQPNG DWTYQTVSYL ASTPSYGDTY SCIVEHIGTP EPTIQNWTSG LSPIQTVKIS VSVAILGLGL IIFFLGLVSC RRAAPSSYTS LPGSNYPEGN LSVGLFAYGS FAGVQAGGGL C // ID M3VWH3_FELCA Unreviewed; 266 AA. AC M3VWH3; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 41. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain precursor {ECO:0000313|Ensembl:ENSFCAP00000001253}; GN Name=LOC102899262 {ECO:0000313|Ensembl:ENSFCAP00000001253}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000001253, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000001253, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001253, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000001253} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001253}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000001253} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000001253}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY152834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY152836; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSFCAT00000001348; ENSFCAP00000001253; ENSFCAG00000001348. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3VWH3; -. DR Proteomes; UP000011712; Chromosome B2. DR Bgee; ENSFCAG00000001348; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. SQ SEQUENCE 266 AA; 30491 MW; 1ADDA5B4B60D8DCF CRC64; MVCLCFMGGS WMTALMLILM MLSPPLAWAR DTSPHFLTMW KFECHYPNGT ERVRYLVRYF YNREELARFD SEVGEYRAVT ELGRPDAKYW NGQKEVLERK HAEVDTVCRH NYGVFDSFLV QRRVEPTVTV FPSKTQPLQH HNLLVCSVNG FYPGHIEVKW FRNGQEEETG VVSTGLIRNG DWTFQTLVML ETVPQSGEVY TCHVEHPSRT SPLTVEWRAQ SESAQSKMLS GIGGFVLGLL FLVVGLFIYF RNQKGHSGLQ PTGLLS // ID M3WAZ6_FELCA Unreviewed; 266 AA. AC M3WAZ6; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFCAP00000008528}; GN Name=LOC111556169 {ECO:0000313|Ensembl:ENSFCAP00000008528}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000008528, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000008528, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008528, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000008528} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008528}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000008528} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008528}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY152833; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003986036.2; XM_003985987.4. DR ProteinModelPortal; M3WAZ6; -. DR STRING; 9685.ENSFCAP00000008528; -. DR Ensembl; ENSFCAT00000009204; ENSFCAP00000008528; ENSFCAG00000009202. DR GeneID; 111556169; -. DR KEGG; fca:111556169; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3WAZ6; -. DR KO; K06752; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000011712; Chromosome B2. DR Bgee; ENSFCAG00000009202; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014166025. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30213 MW; 9C8CAF8852721487 CRC64; MACLWFPRGF LMAALMVMLM VLSPPLAWAR DTPPHFLNML KAECHFTNGT EQVRFLVRCF YNGEEYVRFD SEVGEFRAVT ELGRPDAKYW NEQKDHLEQA RTAVDRICRH NYGVGESFTV QRRVEPTVTV FPSKTQPLQH HNLLVCSVNG FYPGHIEVKW FRNGQEEETG VVSTGLIRNG DWTFQTLVML ETVPQSGEVY TCHVEHPSRT SPITVEWRVQ SDSAQSKMLS GIGGFVLGLL FLALGLFIYF RNQKGHSGLP PTGLLS // ID M3WBW8_FELCA Unreviewed; 263 AA. AC M3WBW8; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 38. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFCAP00000008987}; GN Name=LOC111556173 {ECO:0000313|Ensembl:ENSFCAP00000008987}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000008987, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000008987, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008987, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000008987} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008987}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000008987} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000008987}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY152830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_006931668.1; XM_006931606.3. DR ProteinModelPortal; M3WBW8; -. DR STRING; 9685.ENSFCAP00000008987; -. DR Ensembl; ENSFCAT00000009695; ENSFCAP00000008987; ENSFCAG00000009694. DR GeneID; 111556173; -. DR KEGG; fca:111556173; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3WBW8; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR Proteomes; UP000011712; Chromosome B2. DR Bgee; ENSFCAG00000009694; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014123041. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 28855 MW; F9DDD7B575EA0396 CRC64; MNTLLPLLLG LSLGSTRAGG FLAHVESTCL LDDDGTPKDF TYCVSFNKDL LTCWDPQTSQ MAPCEFGVLS VLANYLSDYL NQQESLLQRL SNGLQDCATH TQSFWGSLTH RTRPPTVQVA KTTPFNTKER VMLACYVWGF YPADVNISWR KNGQPVLPHR SAPKMAQPNG DWTYQTVSHL ATTPSFGDTY TCVVDHIGAL EPICEDWTPG LSPMQTLKVS VAAVTLGLGL IIFSLGLLSW RKASSSGYIF LPGSSYPEGQ HIS // ID M3WK10_FELCA Unreviewed; 282 AA. AC M3WK10; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 38. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSFCAP00000013051}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSFCAP00000013051}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000013051, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000013051, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013051, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000013051} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013051}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000013051} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000013051}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY152831; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_003986037.2; XM_003985988.4. DR ProteinModelPortal; M3WK10; -. DR STRING; 9685.ENSFCAP00000013051; -. DR Ensembl; ENSFCAT00000014077; ENSFCAP00000013051; ENSFCAG00000014072. DR GeneID; 101082906; -. DR KEGG; fca:101082906; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3WK10; -. DR KO; K06752; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000011712; Chromosome B2. DR Bgee; ENSFCAG00000014072; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 259 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 135 223 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 282 AA; 31898 MW; 13BB5F0BE8172F03 CRC64; MILLSHLFFP SRMRSGWVSW MVVLQVSVIR LDSSMTQGRD SPEDFVIQAK ADCYFTNGTE KVQFVVRFIF NLEEYARFDS DVGMFVALTE LGKPDAELWN NRPDILERSK ASVDALCRHN YKLGAPFTVG RKVQPEVAVY PERTPSLQHH NLLLCSVTGF YPGDIKIMWF RNGQQERVGV MSTGLIRNGD WTFQTMVMLE MTPELGDVYT CLVNHPSLLS PISVEWRAQS AYSWRKMLSG IAAFLLGLIF LLVGTVICLR AQKGYVETQL SGDEVSRAVP SP // ID M3X7T5_FELCA Unreviewed; 253 AA. AC M3X7T5; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 39. DE SubName: Full=Major histocompatibility complex, class II, DP beta 1 {ECO:0000313|Ensembl:ENSFCAP00000022687}; GN Name=HLA-DPB1 {ECO:0000313|Ensembl:ENSFCAP00000022687}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000022687, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000022687, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022687, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000022687} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022687}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000022687} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000022687}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY152826; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY152828; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; M3X7T5; -. DR STRING; 9685.ENSFCAP00000022687; -. DR Ensembl; ENSFCAT00000022536; ENSFCAP00000022687; ENSFCAG00000023854. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3X7T5; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G0W5S; -. DR Proteomes; UP000011712; Chromosome B2. DR Bgee; ENSFCAG00000023854; Expressed in 2 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 253 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014163285. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 253 AA; 28563 MW; 2899A8BEF17230E3 CRC64; MVVLRVPGAP GMAALMMSLM TLSSPLVQSR DTPELYLYQK WSVCYELNGT HRFLEQYVYN RELFVQFDSD SAAGVFVAES ELGRETAKNW NIQKVFLELR RSAVDTVCKH NFELDEGFTL QHRVQPNVNV SPSKKGHLQH HNLLVCHVSD FYPGHIQVRW FLNGQEETAG VLSTNPIHNG DWTFQMLVML EMTPQQGDVY TCRVEHPSLD SPVTVEWKAQ SDAARSKMLA GVGGFVLGLV ALGVSLLLHF RSR // ID M3XET4_FELCA Unreviewed; 266 AA. AC M3XET4; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 2. DT 12-SEP-2018, entry version 40. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain precursor {ECO:0000313|Ensembl:ENSFCAP00000025143}; GN Name=LOC102899262 {ECO:0000313|Ensembl:ENSFCAP00000025143}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000025143, ECO:0000313|Proteomes:UP000011712}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000025143, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025143, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|Ensembl:ENSFCAP00000025143, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025143, RC ECO:0000313|Proteomes:UP000011712}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000025143} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025143}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. RN [4] {ECO:0000313|Ensembl:ENSFCAP00000032351} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000032351}; RG Ensembl; RL Submitted (JAN-2018) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY152834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY152836; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_019685992.1; XM_019830433.1. DR SMR; M3XET4; -. DR STRING; 9685.ENSFCAP00000025143; -. DR Ensembl; ENSFCAT00000031150; ENSFCAP00000025143; ENSFCAG00000001348. DR Ensembl; ENSFCAT00000032972; ENSFCAP00000033056; ENSFCAG00000001348. DR Ensembl; ENSFCAT00000043905; ENSFCAP00000038554; ENSFCAG00000001348. DR Ensembl; ENSFCAT00000044487; ENSFCAP00000032351; ENSFCAG00000001348. DR GeneID; 102899262; -. DR KEGG; fca:102899262; -. DR CTD; 102899262; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR Proteomes; UP000011712; Chromosome B2. DR Bgee; ENSFCAG00000001348; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015096482. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30344 MW; 49ED0C1E97189BEB CRC64; MVCLCFMGGS WMTALMLILM MLSPPLAWAR DTSPHFLLLW KGECHFTNGT EQVRFLERHF YNGEEFVRFD SEVGEYRAVT ELGRPAAKYR NEQKDFMERK HAEVDTVCRH NYGVFDSFTV QRRVEPTVTV FPSKTQPLQH HNLLVCSVNG FYPGHIEVKW FRNGQEEETG VVSTGLIRNG DWTFQTLVML ETVPQSGEVY TCHVEHPSRT SPITVEWRAQ SESAQSKMLS GIGGFVLGLL FLVVGLFIYF RNQKGHSGLQ PTGLLS // ID C6ZK78_FELCA Unreviewed; 266 AA. AC C6ZK78; M3XF95; DT 22-SEP-2009, integrated into UniProtKB/TrEMBL. DT 22-SEP-2009, sequence version 1. DT 12-SEP-2018, entry version 50. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain precursor {ECO:0000313|Ensembl:ENSFCAP00000025304}; DE SubName: Full=MHC class II antigen beta chain {ECO:0000313|EMBL:ACK99050.1}; GN Name=Feca-DRB {ECO:0000313|EMBL:ACK99050.1}; GN Synonyms=LOC102899262 {ECO:0000313|Ensembl:ENSFCAP00000025304}; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685 {ECO:0000313|EMBL:ACK99050.1}; RN [1] {ECO:0000313|Ensembl:ENSFCAP00000025304, ECO:0000313|Proteomes:UP000011712} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025304, RC ECO:0000313|Proteomes:UP000011712}; RX PubMed=17975172; DOI=10.1101/gr.6380007; RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S., RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., RA Schaffer A.A., Agarwala R., Narfstrom K., Murphy W.J., Giger U., RA Roca A.L., Antunes A., Menotti-Raymond M., Yuhki N., RA Pecon-Slattery J., Johnson W.E., Bourque G., Tesler G., O'Brien S.J.; RT "Initial sequence and comparative analysis of the cat genome."; RL Genome Res. 17:1675-1689(2007). RN [2] {ECO:0000313|EMBL:ACK99050.1} RP NUCLEOTIDE SEQUENCE. RA Sato E., Yamamoto J.K.; RT "Adoptive-transfer studies with semi-inbred cats demonstrate RT lentivirus-specific CD4+CTL and CD8+CTL are essential for a broadly RT effective FIV AIDS vaccine."; RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSFCAP00000025304} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025304}; RA Hillier L.W., Warren W., Obrien S., Wilson R.K.; RT "Sequence assembly of the Felis catus genome version 6.2."; RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSFCAP00000025304} RP IDENTIFICATION. RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000025304}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AY152834; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY152836; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; EU916195; ACK99050.1; -; mRNA. DR RefSeq; NP_001291959.1; NM_001305030.1. DR Ensembl; ENSFCAT00000027696; ENSFCAP00000025304; ENSFCAG00000001348. DR GeneID; 101098301; -. DR KEGG; fca:101098301; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000011712; Chromosome B2. DR Bgee; ENSFCAG00000001348; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000011712}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000011712}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015088026. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30451 MW; 2FCFB350B33E80BA CRC64; MVCLCFLGGS WMTALMLILM VLSPPLAWAR DTPPHFLTMW KFECHYPNGT ERVRYLVRYF YNREELARFD SEVGEYRAVT ELGRPDAKYW NGQKEVLERK HAEVDTVCRH NYGVFDSFLV QRRVEPTVTV FPSKTQPLQH HNLLVCSVNG FYPGHIEVKW FRNGQEEETG VVSTGLIRNG DWTFQTLVML ETVPQSGEVY TCHVEHPSRT SPLTVEWRAQ SESAQSKMLS GIGGFVLGLL FLVVGLFIYF RNQKGHSGLQ PTGLLS // ID M3XS58_MUSPF Unreviewed; 171 AA. AC M3XS58; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 28-MAR-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMPUP00000001908}; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000001908, ECO:0000313|Proteomes:UP000000715}; RN [1] {ECO:0000313|Ensembl:ENSMPUP00000001908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000001908}; RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S., RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., RA Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J., RA Walker B.J., Young S., Birren B., Lindblad-Toh K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMPUP00000001908} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEYP01075262; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; M3XS58; -. DR STRING; 9669.ENSMPUP00000001908; -. DR Ensembl; ENSMPUT00000001946; ENSMPUP00000001908; ENSMPUG00000001924. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3XS58; -. DR OMA; MPHECAT; -. DR Proteomes; UP000000715; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000715}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000000715}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 141 163 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 39 127 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 171 AA; 19267 MW; C150FEC047FD7505 CRC64; XLWNHRPDIL ERSRASVDAL CRHNYKLGAP FTVGRKVQPE VTVHPERTPS LQHRSLLLCS VTGFYPGDIK IRWFRNGQEE RVGVLSTGLV RNGDWTFQTM VMLEMTPALG DVYTCLVNHA SLLSPVSVEW RAQLAYSWRK MLSGIAAFLL GLIFVLVGTV ICLRAQKGVS Y // ID M3XS76_MUSPF Unreviewed; 263 AA. AC M3XS76; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 28-MAR-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMPUP00000001926}; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000001926, ECO:0000313|Proteomes:UP000000715}; RN [1] {ECO:0000313|Ensembl:ENSMPUP00000001926} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000001926}; RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S., RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., RA Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J., RA Walker B.J., Young S., Birren B., Lindblad-Toh K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMPUP00000001926} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEYP01075280; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_012900293.1; XM_013044839.1. DR ProteinModelPortal; M3XS76; -. DR STRING; 9669.ENSMPUP00000001926; -. DR Ensembl; ENSMPUT00000001965; ENSMPUP00000001926; ENSMPUG00000001943. DR GeneID; 101674777; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3XS76; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR Proteomes; UP000000715; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000715}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000000715}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 16 {ECO:0000256|SAM:SignalP}. FT CHAIN 17 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004043863. FT TRANSMEM 219 240 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 29077 MW; 5C833B3F8F4EFA3F CRC64; MTTFLPLLLG LSLGSAGEGG FIAHVESTCL LDDDGTAKDF TYCVSFNKDL LTCWDRDKSK MVPLEFGALN PLAKYLSEFL NHQESVLSRL SNGLQDCATH TQSFWGSLTH RTRPPTVQVA KTTPFNTKES VMLACYVWGF YPADVTIWWR KNGQPVPPHS SDPKMAQPNG DWTYQTVSYF ATTPSYGDTY TCVVEHIGAP EPVFQDWTPG LSPMQTLKVS VSAVTLGLGF IIFSLGLLSW RRVRSSGYIF LPGASYPEGQ HVS // ID M3Y779_MUSPF Unreviewed; 269 AA. AC M3Y779; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 28-MAR-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMPUP00000007186}; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000007186, ECO:0000313|Proteomes:UP000000715}; RN [1] {ECO:0000313|Ensembl:ENSMPUP00000007186} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000007186}; RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S., RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., RA Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J., RA Walker B.J., Young S., Birren B., Lindblad-Toh K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMPUP00000007186} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEYP01108921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; M3Y779; -. DR STRING; 9669.ENSMPUP00000007186; -. DR Ensembl; ENSMPUT00000007305; ENSMPUP00000007186; ENSMPUG00000007244. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3Y779; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000000715; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000715}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000000715}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004044763. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 269 AA; 30427 MW; 496CC8F22890B103 CRC64; MPGKMALWVP KGLWTAAVMM ILVVLSVPVA EGRDSPQDFV VQFKGECYFT NGTERVRLLA RYIYNREEYA RFDSDVGEYL AVTELGRPDA EYWNSQKDVV EQTQAEVDTV CRHNYKNEER TTLQRQVEPA VTISPSTMEV LNHHNMLLCS VTDFYPGQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RTQSESAQNK TLSGIGGFVL GLIFLGLGLI IRHRSQKGPR GSPPTGTSS // ID M3YE13_MUSPF Unreviewed; 233 AA. AC M3YE13; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 28-MAR-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMPUP00000009570}; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000009570, ECO:0000313|Proteomes:UP000000715}; RN [1] {ECO:0000313|Ensembl:ENSMPUP00000009570} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000009570}; RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S., RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., RA Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J., RA Walker B.J., Young S., Birren B., Lindblad-Toh K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMPUP00000009570} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEYP01104753; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104754; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104755; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104756; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104757; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104758; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104759; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104760; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104761; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEYP01104762; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 9669.ENSMPUP00000009570; -. DR Ensembl; ENSMPUT00000009726; ENSMPUP00000009570; ENSMPUG00000009646. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3YE13; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000000715; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000715}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000000715}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 195 217 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 93 181 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 233 AA; 26383 MW; BD77D66BDDDC669C CRC64; AHFLYLRTAE CYFTNGTERV RFLDRYFYNG EEFVRFDSDV GEYRPVTELG RPSAQSWNSQ KDFLEDARAS VDTYCRHNYG VGESFTVQRR VEPTVTVYPV KTQPLKHHNL LVCSVNGFYP GHIEVRWFRN GQEEESGVVS TGLIRNGDWT FQTLVMLETV PQSGEVYTCQ VEHPSLTSPV TVEWRAQSGS AQSKILSGTG GFVLGLLFLV VGLFIYFRNQ KGHSGLQSTG LLS // ID M3YH07_MUSPF Unreviewed; 265 AA. AC M3YH07; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 28-MAR-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSMPUP00000010614}; OS Mustela putorius furo (European domestic ferret) (Mustela furo). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Mustelidae; OC Mustelinae; Mustela. OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000010614, ECO:0000313|Proteomes:UP000000715}; RN [1] {ECO:0000313|Ensembl:ENSMPUP00000010614} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ID#1420 {ECO:0000313|Ensembl:ENSMPUP00000010614}; RA Di Palma F., Alfoldi J., Johnson J., Jaffe D., Berlin A., Gnerre S., RA Grabherr M., Hall G., Lara M., MacCallum I., Mauceli E., RA Przyblyski D., Ribeiro F., Russell P., Sharpe T., Turner-Maier J., RA Walker B.J., Young S., Birren B., Lindblad-Toh K.; RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMPUP00000010614} RP IDENTIFICATION. RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEYP01107996; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_004782453.1; XM_004782396.2. DR ProteinModelPortal; M3YH07; -. DR STRING; 9669.ENSMPUP00000010614; -. DR Ensembl; ENSMPUT00000010788; ENSMPUP00000010614; ENSMPUG00000010697. DR GeneID; 101683501; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M3YH07; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000000715; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000715}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000000715}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 265 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004044866. FT TRANSMEM 227 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 30309 MW; 1E672281CA85AF8F CRC64; MGLWIPRGLW TAAVMMTLVV LSIPVAEGRD SPQDFVFQFK GECYFTNGTE RVRLLARHIY NREEYARFDS DVGEYRALTE LGRPSAQYWN SQKDIVEQRR AEVDTVCRHN YEIDNRIILH QRVEPTVTIS PSRTEVLNHH NMLVCSVTDF YPGQIKVRWF RNDQEETAGV VSTPLIRNGD WTFQILVMLE VTPQRGDVYT CHVEHPSLQN PITVEWRARS ESAQSKMLSG IGGFVLGLIF LGLGLIIRHR SQKGPRGSPP AGLLR // ID M4AFX7_XIPMA Unreviewed; 241 AA. AC M4AFX7; DT 01-MAY-2013, integrated into UniProtKB/TrEMBL. DT 01-MAY-2013, sequence version 1. DT 28-MAR-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSXMAP00000013371}; OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Xiphophorus. OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000013371, ECO:0000313|Proteomes:UP000002852}; RN [1] {ECO:0000313|Ensembl:ENSXMAP00000013371} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000013371}; RA Walter R., Schartl M., Warren W.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSXMAP00000013371} RP IDENTIFICATION. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000013371}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGAJ01045802; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01045803; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01045804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01045805; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AGAJ01045806; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; M4AFX7; -. DR STRING; 8083.ENSXMAP00000013371; -. DR Ensembl; ENSXMAT00000013387; ENSXMAP00000013371; ENSXMAG00000013332. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M4AFX7; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G0K7A; -. DR Proteomes; UP000002852; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002852}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002852}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 241 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004047582. FT TRANSMEM 209 228 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 110 188 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 241 AA; 26879 MW; 5574E5D7E5BC7751 CRC64; MGPSLLLILL VLVQTADGFQ SHSVSRCLFN STELKDSRYI YSCIYNKVEF LSFDSNIGLY AGYTSFGMRQ ANKLNNNPVA LSRRRAQKEA FCHHNSGVLY RNVLNRSVAP SVALSSVAPP AGGHPAMLTC SVYGFFPKQI RVTWRRDGQE VTSDVTSTAE LPDGAWLYQI HSSLEFRPSE SMEALPCRDP LPAATNPNLR FWDESVNELV LQPVILGLIL SLAGFIYYKR KVKDLVPVPT F // ID M7CA65_CHEMY Unreviewed; 282 AA. AC M7CA65; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 25-OCT-2017, entry version 26. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EMP41543.1}; GN ORFNames=UY3_01208 {ECO:0000313|EMBL:EMP41543.1}; OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Testudines; Cryptodira; Durocryptodira; Americhelydia; OC Chelonioidea; Cheloniidae; Chelonia. OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP41543.1, ECO:0000313|Proteomes:UP000031443}; RN [1] {ECO:0000313|Proteomes:UP000031443} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23624526; DOI=10.1038/ng.2615; RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., RA Li C., White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., RA Zheng Y., Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., RA Li Q., Wang J., Zhang H., Yu L., Shigenobu S., Wang J., Liu J., RA Flicek P., Searle S., Wang J., Kuratani S., Yin Y., Aken B., Zhang G., RA Irie N.; RT "The draft genomes of soft-shell turtle and green sea turtle yield RT insights into the development and evolution of the turtle-specific RT body plan."; RL Nat. Genet. 45:701-706(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB489404; EMP41543.1; -; Genomic_DNA. DR ProteinModelPortal; M7CA65; -. DR Proteomes; UP000031443; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000031443}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000031443}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 31 {ECO:0000256|SAM:SignalP}. FT CHAIN 32 282 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004080619. FT TRANSMEM 229 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 127 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 282 AA; 32033 MW; 68B2A9BAE490CA0C CRC64; MAPGGIPGVA RNCWAGALIV AIALRTHRAH CTDPPEHFLL QQKSECHYTN STQRVRYLKR LIWGQQEICY YDSDLGFSVA RTELGRPIAE YWNRLEWLSY LWASVEKFCS YNRRRFKNIT VDRRVKPRVK ISTLKAESSH RPSLLVCSAT GFYPSEIVTK WFKNGQEETA GVVSRELLHN GDWTFQIQVT LEMKPRWGDV YTCQVEHISL QTPITMQWVA QSDSAKSKMF IGIGGFVLGL SLMVVGLLIY QKNKKGYLCL DTGESRAAGS DRGSSTNLLL CD // ID M9MMA1_DANRE Unreviewed; 251 AA. AC M9MMA1; DT 29-MAY-2013, integrated into UniProtKB/TrEMBL. DT 29-MAY-2013, sequence version 1. DT 12-SEP-2018, entry version 29. DE SubName: Full=Major histocompatibility complex class II DBB gene {ECO:0000313|Ensembl:ENSDARP00000090055}; GN Name=mhc2dbb {ECO:0000313|Ensembl:ENSDARP00000090055, GN ECO:0000313|ZFIN:ZDB-GENE-010112-2}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|Ensembl:ENSDARP00000090055, ECO:0000313|Proteomes:UP000000437}; RN [1] {ECO:0000313|Ensembl:ENSDARP00000090055, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000090055, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [2] {ECO:0000313|Ensembl:ENSDARP00000090055} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000090055}; RG Ensembl; RL Submitted (APR-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; BX908800; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CT573202; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 7955.ENSDARP00000090055; -. DR PaxDb; M9MMA1; -. DR Ensembl; ENSDART00000099281; ENSDARP00000090055; ENSDARG00000056330. DR ZFIN; ZDB-GENE-010112-2; mhc2dbb. DR GeneTree; ENSGT00900000140849; -. DR InParanoid; M9MMA1; -. DR OMA; AMKWAND; -. DR OrthoDB; EOG091G0G84; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 18. DR Bgee; ENSDARG00000056330; Expressed in 6 organ(s), highest expression level in pharyngeal gill. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 251 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004100953. FT TRANSMEM 215 236 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 112 200 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 251 AA; 28844 MW; 8FBD13B3771B7D11 CRC64; MFNVLVIRLA LLLPFLLETA HGHYGFVQFT CHMLGSLQNV EVTYSIYFDT TELLRFNSTE NKAVAYTEYA MKWANDLNKQ PKWLHEQVEK NIADCKLFGE TYFPLVAKTV KPEVFVRSLR EASGKRPALL SCSAYNFYPK HIKLTWMRDD KVVTADVMST KVMADGDWYY QIHSHLEYFP QPGEKISCVV EHASSHKPMI YYWDSFLTES NKNKIITGAA GIVLGAIMAA GGLIYYKRKH TVKSHVHVLI Y // ID O35424_MOUSE Unreviewed; 271 AA. AC O35424; DT 01-JAN-1998, integrated into UniProtKB/TrEMBL. DT 01-JAN-1998, sequence version 1. DT 12-SEP-2018, entry version 158. DE SubName: Full=Histocompatibility 2, O region beta locus {ECO:0000313|Ensembl:ENSMUSP00000092985}; DE SubName: Full=IAbeta2 subunit {ECO:0000313|EMBL:AAB81530.1}; GN Name=H2-Ob {ECO:0000313|Ensembl:ENSMUSP00000092985, GN ECO:0000313|MGI:MGI:95925}; GN Synonyms=H2-IAbeta2 {ECO:0000313|EMBL:AAB81530.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAB81530.1}; RN [1] {ECO:0000313|EMBL:AAB81530.1} RP NUCLEOTIDE SEQUENCE. RA Rowen L., Qin S., Ahearn M.E., Loretz C., Faust J., Lasky S., RA Mahairas G., Hood L.; RT "Sequence of the mouse major histocompatibility locus class II RT region."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSMUSP00000092985, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000092985, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [3] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [4] {ECO:0000313|Ensembl:ENSMUSP00000092985} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000092985}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR974422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF027865; AAB81530.1; -; Genomic_DNA. DR PIR; A23884; A23884. DR RefSeq; NP_034519.2; NM_010389.3. DR UniGene; Mm.327358; -. DR STRING; 10090.ENSMUSP00000092985; -. DR Ensembl; ENSMUST00000095342; ENSMUSP00000092985; ENSMUSG00000041538. DR GeneID; 15002; -. DR KEGG; mmu:15002; -. DR UCSC; uc008cca.1; mouse. DR CTD; 15002; -. DR MGI; MGI:95925; H2-Ob. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000041538; Expressed in 74 organ(s), highest expression level in lymph node. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IDA:MGI. DR GO; GO:0005764; C:lysosome; ISO:MGI. DR GO; GO:0042613; C:MHC class II protein complex; ISO:MGI. DR GO; GO:0023026; F:MHC class II protein complex binding; ISO:MGI. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; ISO:MGI. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|EPD:O35424, KW ECO:0000213|MaxQB:O35424}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 271 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015096771. FT TRANSMEM 225 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 271 AA; 30464 MW; A0F324D82564A4AA CRC64; MGAGRAPWVV ALLVNLMRLD SFMIEGRDSP ENFVIQAKAD CYFTNGTEKV HLLVRFIFNL EEYLHFDSDL GMFVALTELG EPDADQWNKR LDLLETSRAA VNMVCRQKYK LGAPFTVERN VPPEVTVYPE RTPLLQQHNL LLCSVTGFYP GDISVKWFRN GQEERSGVMS TGLVRNGDWT FQTTVMLEMI PELGDIYSCL VEHPGLLRPV SVAWMAQSEY SWKKILSGAA VFLLGLIVFL VGVVIHLKAQ KASVETQPGN EASRESLHSQ P // ID O62938_XIPMA Unreviewed; 256 AA. AC O62938; DT 01-AUG-1998, integrated into UniProtKB/TrEMBL. DT 01-AUG-1998, sequence version 1. DT 28-MAR-2018, entry version 114. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain-like precursor {ECO:0000313|Ensembl:ENSXMAP00000013078}; DE SubName: Full=MHC class II beta chain {ECO:0000313|EMBL:AAC05654.1}; GN Name=Xima-DXB {ECO:0000313|EMBL:AAC05654.1}; OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; OC Poeciliinae; Xiphophorus. OX NCBI_TaxID=8083 {ECO:0000313|EMBL:AAC05654.1}; RN [1] {ECO:0000313|EMBL:AAC05653.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Jp 163 A {ECO:0000313|EMBL:AAC05653.1}; RA McConnell T.J., Godwin U.B., Norton S.F., Nairn R.S., Kazianis S., RA Morizot D.C.; RT "Identification and mapping of two divergent, unlinked major RT histocompatibility complex class II B genes in Xiphophorus fishes."; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAC05654.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Jp 163 A {ECO:0000313|EMBL:AAC05654.1}; RC TISSUE=Whole fish {ECO:0000313|EMBL:AAC05654.1}; RX PubMed=9691047; RA McConnell T.J., Godwin U.B., Norton S.F., Nairn R.S., Kazianis S., RA Morizot D.C.; RT "Identification and mapping of two divergent, unlinked major RT histocompatibility complex class II B genes in Xiphophorus fishes."; RL Genetics 149:1921-1934(1998). RN [3] {ECO:0000313|Ensembl:ENSXMAP00000013078} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000013078}; RA Walter R., Schartl M., Warren W.; RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSXMAP00000013078} RP IDENTIFICATION. RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000013078}; RG Ensembl; RL Submitted (MAR-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGAJ01029216; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF040761; AAC05653.1; -; mRNA. DR EMBL; AF040762; AAC05654.1; -; Genomic_DNA. DR RefSeq; NP_001273222.1; NM_001286293.1. DR STRING; 8083.ENSXMAP00000013078; -. DR Ensembl; ENSXMAT00000013094; ENSXMAP00000013078; ENSXMAG00000013052. DR GeneID; 102219346; -. DR KEGG; xma:102219346; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; QIRVTWL; -. DR OrthoDB; EOG091G0W5S; -. DR Proteomes; UP000002852; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002852}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000002852}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 256 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014102048. FT TRANSMEM 213 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 111 193 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 256 AA; 28947 MW; CD00B36BEE918364 CRC64; MAQAQGCSVF LVFFLAFSPG GAFYLTVLER CQFSSTDGHD AVLLDQIYFN KILEGQYNST VGKAIGYTEK VEALVIFLNN NTGFITHEIW KTNLCKRNTP LAQKLLTPVE PYVQLRLEKA EYSQHQQMLI CSAYDFYPKQ IRVTWLRDGK EATSDVTSTD ELPNGNWLYQ IHTYLEFTPK PGEKITCMVE HASLKKPNLY DWEPEPDSKW SKIVVGSAGL LLGLVFSIAG FIYYKTTSNG RVVVPTTEDV CPEETL // ID O78196_MOUSE Unreviewed; 264 AA. AC O78196; F6VX29; DT 01-NOV-1998, integrated into UniProtKB/TrEMBL. DT 01-NOV-1998, sequence version 1. DT 12-SEP-2018, entry version 171. DE SubName: Full=H-2 class II histocompatibility antigen, I-A beta chain {ECO:0000313|Ensembl:ENSMUSP00000074143}; DE SubName: Full=Major histocompatibility protein class II beta chain {ECO:0000313|EMBL:AAC05286.1}; GN Name=H2-Eb1 {ECO:0000313|Ensembl:ENSMUSP00000074143, GN ECO:0000313|MGI:MGI:95901}; GN Synonyms=Btnl2 {ECO:0000313|MGI:MGI:95901}, GN IEbeta {ECO:0000313|EMBL:AAC05286.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAC05286.1}; RN [1] {ECO:0000313|EMBL:AAC05286.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=129 {ECO:0000313|EMBL:AAC05286.1}; RA Rowen L., Qin S., Loretz C., Mix L., Lasky S., Madan A., Hood L.; RT "Sequence of the mouse major histocompatibility class II region."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAE35816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35816.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAE35816.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [3] {ECO:0000313|EMBL:BAE35816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35816.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAE35816.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [4] {ECO:0000313|EMBL:BAE35816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35816.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAE35816.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [5] {ECO:0000313|EMBL:BAE35816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35816.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAE35816.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [6] {ECO:0000313|EMBL:BAE35816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35816.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAE35816.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [7] {ECO:0000313|EMBL:BAE35816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35816.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAE35816.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., RA Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., RA Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N., RA Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D., RA Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A., RA Muramatsu M., Hayashizaki Y.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:BAE35816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35816.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAE35816.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [9] {ECO:0000313|EMBL:BAE35816.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE35816.1}; RC TISSUE=Stomach {ECO:0000313|EMBL:BAE35816.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [10] {ECO:0000313|Ensembl:ENSMUSP00000074143, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000074143, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [11] {ECO:0000313|Ensembl:ENSMUSP00000074143} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000074143}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR974422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF050157; AAC05286.1; -; Genomic_DNA. DR EMBL; AK160485; BAE35816.1; -; mRNA. DR RefSeq; NP_034512.2; NM_010382.2. DR UniGene; Mm.22564; -. DR IntAct; O78196; 2. DR Ensembl; ENSMUST00000074557; ENSMUSP00000074143; ENSMUSG00000060586. DR GeneID; 14969; -. DR KEGG; mmu:14969; -. DR UCSC; uc008cch.1; mouse. DR CTD; 14969; -. DR MGI; MGI:95901; H2-Eb1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-MMU-202424; Downstream TCR signaling. DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-MMU-202433; Generation of second messenger molecules. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-389948; PD-1 signaling. DR ChiTaRS; H2-Eb1; mouse. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000060586; Expressed in 155 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|EPD:O78196, KW ECO:0000213|MaxQB:O78196, ECO:0000213|PeptideAtlas:O78196}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015096816. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 30153 MW; 25B9632404172BCF CRC64; MVWLPRVPCV AAVILLLTVL SPPVALVRDS RPWFLEYCKS ECHFYNGTQR VRLLERYFYN LEENLRFDSD VGEFRAVTEL GRPDAENWNS QPEFLEQKRA EVDTVCRHNY EISDKFLVRR RVEPTVTVYP TKTQPLEHHN LLVCSVSDFY PGNIEVRWFR NGKEEKTGIV STGLVRNGDW TFQTLVMLET VPQSGEVYTC QVEHPSLTDP VTVEWKAQST SAQNKMLSGV GGFVLGLLFL GAGLFIYFRN QKGQSGLQPT GLLS // ID Q1MTC8_DANRE Unreviewed; 250 AA. AC Q1MTC8; DT 30-MAY-2006, integrated into UniProtKB/TrEMBL. DT 30-MAY-2006, sequence version 1. DT 12-SEP-2018, entry version 109. DE SubName: Full=Major histocompatibility complex class II DAB gene {ECO:0000313|Ensembl:ENSDARP00000100252}; DE SubName: Full=Novel protein similar to vertebrate major histocompatibility complex class II DAB gene (Mhc2dab) {ECO:0000313|EMBL:CAK11370.1}; GN Name=mhc2dab {ECO:0000313|Ensembl:ENSDARP00000100252, GN ECO:0000313|ZFIN:ZDB-GENE-980526-200}; GN ORFNames=DKEYP-2H4.1-001 {ECO:0000313|EMBL:CAK11370.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:CAK11370.1}; RN [1] {ECO:0000313|EMBL:CAK11370.1} RP NUCLEOTIDE SEQUENCE. RA Barker D.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSDARP00000100252} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000100252}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSDARP00000100252, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000100252, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CU694380; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL928944; CAK11370.1; -; Genomic_DNA. DR UniGene; Dr.132799; -. DR STRING; 7955.ENSDARP00000100252; -. DR Ensembl; ENSDART00000111240; ENSDARP00000100252; ENSDARG00000079105. DR ZFIN; ZDB-GENE-980526-200; mhc2dab. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR TreeFam; TF333780; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000079105; Expressed in 20 organ(s), highest expression level in pharyngeal gill. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 250 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015097101. FT TRANSMEM 217 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 202 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 250 AA; 28442 MW; CBD23B23C7FCF3D8 CRC64; MYLLKPFLVI LMLSTFTGTA DGYYDYIKQQ CFYSTSDYSD MVYLASYSFN KVVDTQFNSS VGKFVGYTEQ GLIFAENFNK DQAYLHQLKA QVDTFCRHNA QIWDSAVRDK AVLPEVTIKS VRQAEGRHPA VLLCSAYEFY PKKIKMSWLR DGKEVTSDVT STMEMADGDW YYQIHSHLEY TPKSGEKIQC LVEHASLTQP LTKDWNPHIS ESDRNKFAIG ASGLVLGIII AIAGLIYYKK KSTGRILVPN // ID Q29967_HUMAN Unreviewed; 224 AA. AC Q29967; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 18-JUL-2018, entry version 142. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000393979}; DE SubName: Full=Lymphocyte antigen {ECO:0000313|EMBL:AAA36236.1}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSP00000393979}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAA36236.1}; RN [1] {ECO:0000313|EMBL:AAA36236.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=2464826; DOI=10.1073/pnas.86.3.1003; RA Briata P., Radka S.F., Sartoris S., Lee J.S.; RT "Alternative splicing of HLA-DQB transcripts and secretion of HLA-DQ RT beta-chain proteins: allelic polymorphism in splicing and RT polyadenylylation sites."; RL Proc. Natl. Acad. Sci. U.S.A. 86:1003-1007(1989). RN [2] {ECO:0000313|Ensembl:ENSP00000393979, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [3] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [4] {ECO:0000313|Ensembl:ENSP00000393979} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M24364; AAA36236.1; -; mRNA. DR PIR; A31459; A31459. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR SMR; Q29967; -. DR MaxQB; Q29967; -. DR PRIDE; Q29967; -. DR Ensembl; ENST00000434886; ENSP00000393979; ENSG00000233209. DR UCSC; uc011gkd.3; human. DR HGNC; HGNC:4944; HLA-DQB1. DR HOVERGEN; HBG012730; -. DR ChiTaRS; HLA-DQB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:Q29967, KW ECO:0000213|PeptideAtlas:Q29967}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 224 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014586089. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 224 AA; 26081 MW; 2F96FFAEF7F5DE5A CRC64; MSWKKALRIP GGLRVATVTL MLAMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVT RYIYNREEYA RFDSDVGVYR AVTPLGPPDA EYWNSQKEVL ERTRAELDTV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQNPIIVEW RLLH // ID Q31072_PIG Unreviewed; 266 AA. AC Q31072; F6PX54; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 12-SEP-2018, entry version 153. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AAN35100.1}; DE SubName: Full=MHC class II histocompatibility antigen SLA-DRB1 precursor {ECO:0000313|Ensembl:ENSSSCP00000001570}; DE SubName: Full=SLA-DR-beta class II light chain {ECO:0000313|EMBL:AAA31124.1}; GN Name=LA-DRB-d {ECO:0000313|EMBL:AAA31124.1}; GN Synonyms=SLA-DRB {ECO:0000313|EMBL:AAN35100.1}, GN SLA-DRB1 {ECO:0000313|EMBL:AAO63766.1, GN ECO:0000313|Ensembl:ENSSSCP00000001570}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAA31124.1}; RN [1] {ECO:0000313|EMBL:AAA31124.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Spleen and blood {ECO:0000313|EMBL:AAA31124.1}; RX PubMed=2124703; DOI=10.1073/pnas.87.24.9798; RA Gustafsson K., Germana S., Hirsch F., Pratt K., LeGuern C., RA Sachs D.H.; RT "Structure of miniature swine class II DRB genes: conservation of RT hypervariable amino acid residues between distantly related mammalian RT species."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9798-9802(1990). RN [2] {ECO:0000313|EMBL:AAO63766.1} RP NUCLEOTIDE SEQUENCE. RA Lee J.H., Simond D., Walters S., Patel T., Smith D.M., O'Connell P.J., RA Moran C.; RT "Characterization of the swine major histocompatibility complex RT alleles at eight loci in westran pigs."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:AAN35100.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15713212; DOI=10.1111/j.1399-0039.2005.00337.x; RA Smith D.M., Lunney J.K., Martens G.W., Ando A., Lee J.H., Ho C.S., RA Schook L., Renard C., Chardon P.; RT "Nomenclature for factors of the SLA class-I system, 2004."; RL Tissue Antigens 65:136-149(2005). RN [4] {ECO:0000313|EMBL:AAX63485.1} RP NUCLEOTIDE SEQUENCE. RA Ho C.-S., Smith D.M.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:BAD99124.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Trachea {ECO:0000313|EMBL:BAD99124.1}; RA Uenishi H., Tanaka M., Eguchi-Ogawa T., Domukai M., Awata T.; RT "SLABLAST: a database of SLA sequences with nomenclature and for RT discrimination of newly cloned SLA sequences against known SLA RT alleles."; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:ACA21791.1} RP NUCLEOTIDE SEQUENCE. RA Ho C.-S., Lee Y.-J., Franzo-Romain M.H., Smith D.M.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:ACE07021.1} RP NUCLEOTIDE SEQUENCE. RA Yeom S.C., Park C.G., Lee B.C., Lee W.J.; RT "Sequence base SLA typing in CMS miniature pig."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:ACA21791.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19508353; DOI=10.1111/j.1744-313X.2009.00853.x; RA Ho C.S., Franzo-Romain M.H., Lee Y.J., Lee J.H., Smith D.M.; RT "Sequence-based characterization of swine leucocyte antigen alleles in RT commercially available porcine cell lines."; RL Int. J. Immunogenet. 36:231-234(2009). RN [9] {ECO:0000313|Ensembl:ENSSSCP00000001570, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000001570, RC ECO:0000313|Proteomes:UP000008227}; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|Ensembl:ENSSSCP00000001570} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [11] {ECO:0000313|EMBL:AOP12359.1} RP NUCLEOTIDE SEQUENCE. RA Gao C., Quan J., Jiang X., He X., Li C., Chen H.; RT "Swine leukocyte antigen (SLA) diversity in Large White and Landrace RT pigs."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|Ensembl:ENSSSCP00000054557} RP IDENTIFICATION. RG Ensembl; RL Submitted (OCT-2017) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEMK02000055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; M55166; AAA31124.1; -; mRNA. DR EMBL; AY135582; AAN35100.1; -; mRNA. DR EMBL; AY135583; AAN35101.1; -; mRNA. DR EMBL; AY247784; AAO63766.1; -; mRNA. DR EMBL; AY247785; AAO63767.1; -; mRNA. DR EMBL; AY962314; AAX63485.1; -; mRNA. DR EMBL; EU432078; ACA21791.1; -; mRNA. DR EMBL; EU722919; ACE07021.1; -; mRNA. DR EMBL; KU754592; AOP12359.1; -; mRNA. DR EMBL; AB215121; BAD99124.1; -; mRNA. DR PIR; B39260; B39260. DR UniGene; Ssc.94333; -. DR UniGene; Ssc.95910; -. DR SMR; Q31072; -. DR STRING; 9823.ENSSSCP00000001570; -. DR PRIDE; Q31072; -. DR Ensembl; ENSSSCT00000001612; ENSSSCP00000001570; ENSSSCG00000001455. DR Ensembl; ENSSSCT00000041968; ENSSSCP00000054557; ENSSSCG00000001455. DR Ensembl; ENSSSCT00000052939; ENSSSCP00000054687; ENSSSCG00000001455. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-SSC-202424; Downstream TCR signaling. DR Reactome; R-SSC-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-SSC-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-SSC-202433; Generation of second messenger molecules. DR Reactome; R-SSC-2132295; MHC class II antigen presentation. DR Reactome; R-SSC-389948; PD-1 signaling. DR Proteomes; UP000008227; Chromosome 7. DR Bgee; ENSSSCG00000001455; Expressed in 6 organ(s), highest expression level in lung. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q31072}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015097380. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30282 MW; 497B8AD887948099 CRC64; MLHLCFSRGF WMAALTVMLV VLSPPLALAR DTPPHFLHLL KFECHFFNGT ERVRLLERQY YNGEEFLRFD SDVGEYRAVT ELGRPDAKDW NSQKDLLEQR RAEVDTYCRH NYRILDTFLV PRRAEPTVTV YPAKTQPLQH HNLLVCSVTG FYPGHVEVRW FRNGQEEAAG VVSTGLIPNG DWTFQTMVML ETVPQSGEVY SCRVEHPSLT SPVTVEWRAR SESAQGKMMS GIGGFVLGLL FVAVGLFIYF KNQKGRPALQ PTGLLS // ID Q31094_MOUSE Unreviewed; 261 AA. AC Q31094; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-AUG-1999, sequence version 2. DT 12-SEP-2018, entry version 175. DE SubName: Full=Class II histocompatibility antigen, M beta 1 chain {ECO:0000313|Ensembl:ENSMUSP00000109870}; DE SubName: Full=H2-M beta1 {ECO:0000313|EMBL:AAC69909.1}; DE SubName: Full=Histocompatibility 2, class II, locus Mb1 {ECO:0000313|EMBL:AAH03718.1}; DE SubName: Full=MHC class II antigen Mb1 {ECO:0000313|EMBL:AIC84013.1}; GN Name=H2-DMb1 {ECO:0000313|EMBL:AAH03718.1, GN ECO:0000313|Ensembl:ENSMUSP00000109870, ECO:0000313|MGI:MGI:95922}; GN Synonyms=H2-DMb2 {ECO:0000313|MGI:MGI:95922}, GN H2-M beta1 {ECO:0000313|EMBL:AAC69909.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAC69909.1}; RN [1] {ECO:0000313|EMBL:AAC69909.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=129svj {ECO:0000313|EMBL:AAC69909.1}; RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., RA Hall J., Lasky S., Hood L.; RT "Sequence of the mouse major histocomaptibility locus class II RT region."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:BAC28006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC28006.1}; RC TISSUE=Wolffian duct includes surrounding region RC {ECO:0000313|EMBL:BAC28006.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [3] {ECO:0000313|EMBL:BAC28006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC28006.1}; RC TISSUE=Wolffian duct includes surrounding region RC {ECO:0000313|EMBL:BAC28006.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [4] {ECO:0000313|EMBL:BAC28006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC28006.1}; RC TISSUE=Wolffian duct includes surrounding region RC {ECO:0000313|EMBL:BAC28006.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [5] {ECO:0000313|EMBL:BAC28006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC28006.1}; RC TISSUE=Wolffian duct includes surrounding region RC {ECO:0000313|EMBL:BAC28006.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [6] {ECO:0000313|EMBL:BAC28006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC28006.1}; RC TISSUE=Wolffian duct includes surrounding region RC {ECO:0000313|EMBL:BAC28006.1}; RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., RA Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., RA Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T., RA Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S., RA Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M., RA Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y., RA Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H., RA Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M., RA Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T., RA Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAC28006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC28006.1}; RC TISSUE=Wolffian duct includes surrounding region RC {ECO:0000313|EMBL:BAC28006.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [8] {ECO:0000313|EMBL:AAH03718.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Mix FVB/N {ECO:0000313|EMBL:AAH03718.1}; RC TISSUE=Mammary tumor. WAP-TGF alpha model. 7 months old RC {ECO:0000313|EMBL:AAH03718.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., RA Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., RA Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., RA Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., RA Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., RA Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., RA Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., RA Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., RA Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., RA Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., RA Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., RA Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., RA Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., RA Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., RA Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., RA Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., RA Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., RA Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., RA Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] {ECO:0000313|EMBL:BAC28006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC28006.1}; RC TISSUE=Wolffian duct includes surrounding region RC {ECO:0000313|EMBL:BAC28006.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [10] {ECO:0000313|EMBL:BAC28006.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC28006.1}; RC TISSUE=Wolffian duct includes surrounding region RC {ECO:0000313|EMBL:BAC28006.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [11] {ECO:0000313|Ensembl:ENSMUSP00000109870, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000109870, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [12] {ECO:0000313|Ensembl:ENSMUSP00000109870} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000109870}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [13] {ECO:0000313|EMBL:AIC84013.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=I/StSnEgYCit {ECO:0000313|EMBL:AIC84013.1}; RC TISSUE=Spleen {ECO:0000313|EMBL:AIC84013.1}; RA Harrison E.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|EMBL:AIC84013.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=I/StSnEgYCit {ECO:0000313|EMBL:AIC84013.1}; RC TISSUE=Spleen {ECO:0000313|EMBL:AIC84013.1}; RX PubMed=26618355; RA Logunova N., Korotetskaya M., Polshakov V., Apt A.; RT "The QTL within the H2 Complex Involved in the Control of Tuberculosis RT Infection in Mice Is the Classical Class II H2-Ab1 Gene."; RL PLoS Genet. 11:E1005672-E1005672(2015). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR974422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF100956; AAC69909.1; -; Genomic_DNA. DR EMBL; BC003718; AAH03718.1; -; mRNA. DR EMBL; KJ650225; AIC84013.1; -; mRNA. DR EMBL; AK032745; BAC28006.1; -; mRNA. DR RefSeq; NP_034517.2; NM_010387.3. DR UniGene; Mm.460938; -. DR Ensembl; ENSMUST00000114232; ENSMUSP00000109870; ENSMUSG00000079547. DR GeneID; 14999; -. DR KEGG; mmu:14999; -. DR UCSC; uc008cbq.1; mouse. DR CTD; 14999; -. DR MGI; MGI:95922; H2-DMb1. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG007327; -. DR KO; K06752; -. DR OMA; NCASHTK; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR ChiTaRS; Hbb-b1; mouse. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000079547; Expressed in 141 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|EPD:Q31094, KW ECO:0000213|MaxQB:Q31094}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015097375. FT TRANSMEM 219 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 115 204 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 28914 MW; 50203DECC9E1888A CRC64; MAALWLLLLV LSLDCMGAGG FVAHVESTCV LDDAGTPQDF TYCVSFNKDL LACWDPDVGK IVPCEFGVLY PWAENFSRIL NKEESLLQRL QNGLLDCASH TQPFWNALTH RTRAPSVRVA QTTPFNTREP VMLACYVWGF YPADVTITWM KNGQLVPSHS NKEKTAQPNG DWTYQTVSYL ALTPSYGDVY TCVVQHSGTS EPIRGDWTPG LSPIQTVKVS VSAATLGLGF IIFCVGFFRW RKSHSSSYTP LSGSTYPEGQ H // ID Q31099_MOUSE Unreviewed; 261 AA. AC Q31099; Q31609; Q60975; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-AUG-1999, sequence version 2. DT 12-SEP-2018, entry version 179. DE SubName: Full=H2-M beta 2 {ECO:0000313|EMBL:AAC69908.1}; DE SubName: Full=H2-M beta 2 chain {ECO:0000313|EMBL:AAA98930.1}; DE SubName: Full=Histocompatibility 2, class II, locus Mb2 {ECO:0000313|Ensembl:ENSMUSP00000043526}; DE SubName: Full=MCG132703, isoform CRA_a {ECO:0000313|EMBL:EDL10254.1}; DE SubName: Full=MHC class II H2-M beta 2 chain {ECO:0000313|EMBL:AAA91144.1}; DE SubName: Full=MHC class II antigen Mb2 {ECO:0000313|EMBL:AIC84012.1}; GN Name=H2-DMb2 {ECO:0000313|EMBL:AIC84012.1, GN ECO:0000313|Ensembl:ENSMUSP00000043526, ECO:0000313|MGI:MGI:95923}; GN Synonyms=H2-M beta2 {ECO:0000313|EMBL:AAC69908.1}, GN H2-Mb2 {ECO:0000313|EMBL:AAA91144.1}; GN ORFNames=mCG_132703 {ECO:0000313|EMBL:EDL10254.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAC69908.1}; RN [1] {ECO:0000313|EMBL:AAA91144.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=B10.M {ECO:0000313|EMBL:AAA91145.1}, RC BALB/c {ECO:0000313|EMBL:AAA98930.1}, and RC C57BL/6 {ECO:0000313|EMBL:AAA91144.1}; RC TISSUE=Spleen {ECO:0000313|EMBL:AAA91144.1}; RX PubMed=8575819; DOI=10.1007/s002510050047; RA Peleraux A., Karlsson L., Chambers J., Peterson P.A.; RT "Genomic organization of a mouse MHC class II region including the H2- RT M and Lmp2 loci."; RL Immunogenetics 43:204-214(1996). RN [2] {ECO:0000213|PDB:1K8I} RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 20-210, AND DISULFIDE BONDS. RX PubMed=9768758; DOI=10.1016/S1074-7613(00)80621-4; RA Fremont D.H., Crawford F., Marrack P., Hendrickson W.A., Kappler J.; RT "Crystal structure of mouse H2-M."; RL Immunity 9:385-393(1998). RN [3] {ECO:0000313|EMBL:AAC69908.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=129svj {ECO:0000313|EMBL:AAC69908.1}; RA Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L., RA Hall J., Lasky S., Hood L.; RT "Sequence of the mouse major histocomaptibility locus class II RT region."; RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:BAE32928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE32928.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [5] {ECO:0000313|EMBL:BAE32928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE32928.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [6] {ECO:0000313|EMBL:BAE32928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE32928.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [7] {ECO:0000313|EMBL:BAE32928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE32928.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [8] {ECO:0000313|EMBL:BAE32928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE32928.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [9] {ECO:0000313|EMBL:EDL10254.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mixed {ECO:0000313|EMBL:EDL10254.1}; RX PubMed=12040188; DOI=10.1126/science.1069193; RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R., RA Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A., RA Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W., RA Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K., RA Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J., RA Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R., RA Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H., RA Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A., RA Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A., RA Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C., RA Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C., RA Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B., RA Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E., RA Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R., RA Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C., RA Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L., RA Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S., RA Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L., RA Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R., RA Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R., RA Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J., RA Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L., RA Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C., RA Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A., RA Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H., RA Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L., RA Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M., RA Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K., RA Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S., RA Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J., RA Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G., RA Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.; RT "A comparison of whole-genome shotgun-derived mouse chromosome 16 and RT the human genome."; RL Science 296:1661-1671(2002). RN [10] {ECO:0000313|EMBL:BAE32928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE32928.1}; RA Chen C.-T., Hsu E.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:BAE32928.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD {ECO:0000313|EMBL:BAE32928.1}; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [12] {ECO:0000313|EMBL:BAE32928.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE32928.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [13] {ECO:0000313|EMBL:EDL10254.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Mixed {ECO:0000313|EMBL:EDL10254.1}; RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [14] {ECO:0000313|Ensembl:ENSMUSP00000043526} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000043526}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [15] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [16] {ECO:0000313|EMBL:AIC84012.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=I/StSnEgYCit {ECO:0000313|EMBL:AIC84012.1}; RC TISSUE=Spleen {ECO:0000313|EMBL:AIC84012.1}; RA Harrison E.; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [17] {ECO:0000313|EMBL:AIC84012.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=I/StSnEgYCit {ECO:0000313|EMBL:AIC84012.1}; RC TISSUE=Spleen {ECO:0000313|EMBL:AIC84012.1}; RX PubMed=26618355; RA Logunova N., Korotetskaya M., Polshakov V., Apt A.; RT "The QTL within the H2 Complex Involved in the Control of Tuberculosis RT Infection in Mice Is the Classical Class II H2-Ab1 Gene."; RL PLoS Genet. 11:E1005672-E1005672(2015). RN [18] {ECO:0000313|Ensembl:ENSMUSP00000043526} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000043526}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR974422; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; U35334; AAA91144.1; -; mRNA. DR EMBL; U35335; AAA91145.1; -; mRNA. DR EMBL; U35323; AAA98930.1; -; Genomic_DNA. DR EMBL; AF100956; AAC69908.1; -; Genomic_DNA. DR EMBL; KJ650224; AIC84012.1; -; mRNA. DR EMBL; AK154923; BAE32928.1; -; mRNA. DR EMBL; CH466660; EDL10254.1; -; Genomic_DNA. DR PIR; A55242; A55242. DR RefSeq; NP_034518.1; NM_010388.4. DR UniGene; Mm.195060; -. DR PDB; 1K8I; X-ray; 3.10 A; B=20-210. DR PDBsum; 1K8I; -. DR IntAct; Q31099; 1. DR STRING; 10090.ENSMUSP00000043526; -. DR Ensembl; ENSMUST00000041982; ENSMUSP00000043526; ENSMUSG00000037548. DR GeneID; 15000; -. DR KEGG; mmu:15000; -. DR UCSC; uc008cbn.1; mouse. DR CTD; 15000; -. DR MGI; MGI:95923; H2-DMb2. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG007327; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000037548; Expressed in 166 organ(s), highest expression level in blood. DR GO; GO:0010008; C:endosome membrane; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IDA:MGI. DR GO; GO:0005770; C:late endosome; IDA:MGI. DR GO; GO:0005765; C:lysosomal membrane; IDA:MGI. DR GO; GO:0005764; C:lysosome; IDA:MGI. DR GO; GO:0042613; C:MHC class II protein complex; ISO:MGI. DR GO; GO:0005771; C:multivesicular body; IDA:MGI. DR GO; GO:0023026; F:MHC class II protein complex binding; ISO:MGI. DR GO; GO:0019882; P:antigen processing and presentation; IDA:MGI. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IDA:MGI. DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IDA:MGI. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:1K8I}; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|EPD:Q31099, KW ECO:0000213|MaxQB:Q31099}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015097373. FT TRANSMEM 219 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 115 204 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DISULFID 29 97 {ECO:0000213|PDB:1K8I}. FT DISULFID 43 53 {ECO:0000213|PDB:1K8I}. FT DISULFID 135 192 {ECO:0000213|PDB:1K8I}. SQ SEQUENCE 261 AA; 28873 MW; 0CC0E08B8BE47218 CRC64; MAALWLLLLV LSLHCMGAGG FVAHVESTCV LNDAGTPQDF TYCVSFNKDL LACWDPDVGK IVPCEFGVLS RLAEIISNIL NEQESLIHRL QNGLQDCATH TQPFWDVLTH RTRAPSVRVA QTTPFNTREP VMLACYVWGF YPADVTITWM KNGQLVPSHS NKEKTAQPNG DWTYQTVSYL ALTPSYGDVY TCVVQHSGTS EPIRGDWTPG LSPIQTVKVS VSAATLGLGF IIFCVGFFRW RKSHSSSYTP LPGSTYPEGR H // ID Q3UUV9_MOUSE Unreviewed; 287 AA. AC Q3UUV9; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 12-SEP-2018, entry version 116. DE SubName: Full=Histocompatibility 2, class II antigen E beta2 {ECO:0000313|EMBL:CAO77744.1, ECO:0000313|Ensembl:ENSMUSP00000056814}; GN Name=H2-Eb2 {ECO:0000313|EMBL:CAO77744.1, GN ECO:0000313|Ensembl:ENSMUSP00000056814, ECO:0000313|MGI:MGI:95902}; GN ORFNames=CR974457.1-001 {ECO:0000313|EMBL:CAO77744.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAE23514.1}; RN [1] {ECO:0000313|EMBL:BAE23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23514.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAE23514.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [2] {ECO:0000313|EMBL:BAE23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23514.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAE23514.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [3] {ECO:0000313|EMBL:BAE23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23514.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAE23514.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [4] {ECO:0000313|EMBL:BAE23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23514.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAE23514.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [5] {ECO:0000313|EMBL:BAE23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23514.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAE23514.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [6] {ECO:0000313|EMBL:BAE23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23514.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAE23514.1}; RA Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., RA Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., RA Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N., RA Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D., RA Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A., RA Muramatsu M., Hayashizaki Y.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:BAE23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23514.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAE23514.1}; RG The FANTOM Consortium; RG Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group); RT "The Transcriptional Landscape of the Mammalian Genome."; RL Science 309:1559-1563(2005). RN [8] {ECO:0000313|EMBL:BAE23514.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23514.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:BAE23514.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [9] {ECO:0000313|Ensembl:ENSMUSP00000056814, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000056814, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [10] {ECO:0000313|EMBL:CAO77744.1} RP NUCLEOTIDE SEQUENCE. RA Pelan S.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [12] {ECO:0000313|Ensembl:ENSMUSP00000056814} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000056814}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AK137912; BAE23514.1; -; mRNA. DR EMBL; CR974457; CAO77744.1; -; Genomic_DNA. DR RefSeq; NP_001029150.1; NM_001033978.3. DR UniGene; Mm.139204; -. DR STRING; 10090.ENSMUSP00000056814; -. DR Ensembl; ENSMUST00000050325; ENSMUSP00000056814; ENSMUSG00000067341. DR GeneID; 381091; -. DR KEGG; mmu:381091; -. DR UCSC; uc012apx.1; mouse. DR CTD; 381091; -. DR MGI; MGI:95902; H2-Eb2. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-MMU-202424; Downstream TCR signaling. DR Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-MMU-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-MMU-202433; Generation of second messenger molecules. DR Reactome; R-MMU-2132295; MHC class II antigen presentation. DR Reactome; R-MMU-389948; PD-1 signaling. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000067341; Expressed in 32 organ(s), highest expression level in mesenteric lymph node. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 6 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 227 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 287 AA; 32381 MW; 00275715A5D9AE3D CRC64; MVSLWLPRGL CVAAVILSLM MLTPPVILVR DPRPRFLEQL KAECHYFNGK ERVWSVTRFI YNQEEFARFN SDFGKFLAVT ELGRPIVEYL NTQKDMLDNY RASVDRCRNN YDLVDIFMLN LKAEPKVTVY PAKTQPLEHH NLLVCSVIDF YPGSIEVRWF RNGEEEKTGV VSTGLIQNRD WTYQTLVMLE MVPRGGEVYT CQVEHPSLTS PVTVEWRARS TSAQNKLLSG VMGMALGLFI LAVGLFFYLR NLRAGSVSHG AGEGAESFTS RLTGSGSECH MGPGLSI // ID Q58DW7_BOVIN Unreviewed; 262 AA. AC Q58DW7; DT 26-APR-2005, integrated into UniProtKB/TrEMBL. DT 26-APR-2005, sequence version 1. DT 12-SEP-2018, entry version 134. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AAY34701.1}; DE SubName: Full=Major histocompatibility complex, class II, DM beta-chain, expressed {ECO:0000313|EMBL:AAI18362.1}; GN Name=HLA-DMB {ECO:0000313|EMBL:AAX46327.1}; GN Synonyms=BOLA-DMB {ECO:0000313|EMBL:AAI18362.1, GN ECO:0000313|Ensembl:ENSBTAP00000016520}, GN DMB {ECO:0000313|EMBL:AAY34701.1}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAX46327.1}; RN [1] {ECO:0000313|EMBL:AAX46327.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Pooled {ECO:0000313|EMBL:AAX46327.1}; RX PubMed=12140684; DOI=10.1007/s00335-001-2145-4; RA Sonstegard T.S., Capuco A.V., White J., Van Tassell C.P., Connor E.E., RA Cho J., Sultana R., Shade L., Wray J.E., Wells K.D., Quackenbush J.; RT "Analysis of bovine mammary gland EST and functional annotation of the RT Bos taurus gene index."; RL Mamm. Genome 13:373-379(2002). RN [2] {ECO:0000313|EMBL:AAX46327.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Pooled {ECO:0000313|EMBL:AAX46327.1}; RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [3] {ECO:0000313|EMBL:AAY34701.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16573526; DOI=10.1111/j.1365-2052.2005.01395.x; RA Childers C.P., Newkirk H.L., Honeycutt D.A., Ramlachan N., RA Muzney D.M., Sodergren E., Gibbs R.A., Weinstock G.M., Womack J.E., RA Skow L.C.; RT "Comparative analysis of the bovine MHC class IIb sequence identifies RT inversion breakpoints and three unexpected genes."; RL Anim. Genet. 37:121-129(2006). RN [4] {ECO:0000313|EMBL:AAI18362.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Hereford {ECO:0000313|EMBL:AAI18362.1}; RC TISSUE=Fetal liver {ECO:0000313|EMBL:AAI18362.1}; RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y., RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C., RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J., RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J., RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., RA Siddiqui A., Holt R., Jones S.J., Marra M.A.; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|Ensembl:ENSBTAP00000016520, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000016520, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [6] {ECO:0000313|Ensembl:ENSBTAP00000016520} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000016520}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; DAAA02054879; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC118361; AAI18362.1; -; mRNA. DR EMBL; BT021480; AAX46327.1; -; mRNA. DR EMBL; AY957499; AAY34701.1; -; Genomic_DNA. DR RefSeq; NP_001035571.1; NM_001040481.3. DR UniGene; Bt.1007; -. DR STRING; 9913.ENSBTAP00000016520; -. DR Ensembl; ENSBTAT00000016520; ENSBTAP00000016520; ENSBTAG00000012451. DR GeneID; 282491; -. DR KEGG; bta:282491; -. DR CTD; 282491; -. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000231198; -. DR HOVERGEN; HBG007327; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Reactome; R-BTA-2132295; MHC class II antigen presentation. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000012451; Expressed in 10 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 262 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014105495. FT TRANSMEM 219 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 114 196 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 262 AA; 29070 MW; 6CF09454AC73EE56 CRC64; MTVLLSLLLG FSLGCTAAGG FVAHVESTCV LDDDGDPKDF SYCISFNKDL LTCWDPLQAS MIPREFGVLN GLARYLSQFL NNNSYLIQRL SNGLQNCAAH TQPFWSSLTH RTRPPTVQVA KTTPFNTRES VMLACYVWGF YPADVAITWR RNGQEVLPHG RAWRIIQPNG DWTYQTVSHL ATTPSFGDTY TCVVEHIGAP ELILQDWTPG LLPAQTVKVS VALVTLVLGL IIFVFGLHSW RRATSSGYIF LPGSTYPEGQ HN // ID Q5EP54_HUMAN Unreviewed; 258 AA. AC Q5EP54; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 12-SEP-2018, entry version 132. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|Ensembl:ENSP00000399298}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AAW78739.1}; GN Name=HLA-DPB1 {ECO:0000313|EMBL:AAW78739.1, GN ECO:0000313|Ensembl:ENSP00000399298}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAW78739.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000399298, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|EMBL:AAW78739.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16189666; DOI=10.1007/s00251-005-0043-8; RA Reinders J., Rozemuller E.H., van Gent R., Arts-Hilkes Y.H., RA van den Tweel J.G., Tilanus M.G.J.; RT "Extended HLA-DPB1 polymorphism: an RNA approach for HLA-DPB1 RT typing."; RL Immunogenetics 57:790-794(2005). RN [3] {ECO:0000313|EMBL:ABC66207.1} RP NUCLEOTIDE SEQUENCE. RA Song C.-H., Lee J.-K., Koh I., Lee J.-Y., Lim Y.-H., Kang J., RA Cha Y.-Y., Yun H.-S., Lee E.-J., Kwack K.; RT "Identification of HLA-DPB1*020102 allele variant, in the Korean RT population."; RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:BAN59793.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23714642; DOI=10.1186/1471-2164-14-355; RA Hosomichi K., Jinam T.A., Mitsunaga S., Nakaoka H., Inoue I.; RT "Phase-defined complete sequencing of the HLA genes by next-generation RT sequencing."; RL BMC Genomics 14:355-355(2013). RN [5] {ECO:0000313|EMBL:AMT81697.1} RP NUCLEOTIDE SEQUENCE. RA Marino S.R., Brown N.K., West T.A., Issangya B.M., Upchurch R.L.; RT "Novel HLA alleles identified and characterized by an NGS-based typing RT assay."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|Ensembl:ENSP00000399298} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2016) to UniProtKB. RN [7] {ECO:0000313|EMBL:SIT60286.1} RP NUCLEOTIDE SEQUENCE. RA Song W.-J., Kurnit D.M.; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:SMY43988.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28547825; DOI=.1111/tan.13057; RA Albrecht V., Zweiniger C., Surendranath V., Lang K., Schofl G., RA Dahl A., Winkler S., Lange V., Bohme I., Schmidt A.H.; RT "Dual redundant sequencing strategy: Full-length gene characterisation RT of 1056 novel and confirmatory HLA alleles."; RL HLA. 90:79-87(2017). RN [9] {ECO:0000313|EMBL:SIT60286.1} RP NUCLEOTIDE SEQUENCE. RA Lang K., Schoefl G., Schmidt A., Lange V.; RT "Complementing the HLA-DPB1 Database: Full-Length Gene RT Characterization of all Common and Well-Documented Alleles."; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:SJK83216.1} RP NUCLEOTIDE SEQUENCE. RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.; RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:AVI26629.1} RP NUCLEOTIDE SEQUENCE. RA Balz V., Krause S., Enzcmann J., Fischer J.; RT "Determination of full gene HLA-DPB1 sequences and variations RT thereof."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:SMZ62531.1} RP NUCLEOTIDE SEQUENCE. RA Albrecht V., Zweiniger C., Boehme I., Schmidt A.H.; RT "Characterisation and Confirmation of new HLA alleles found by DKMS RT Life Science Lab."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. RN [13] {ECO:0000313|EMBL:SPT23801.1} RP NUCLEOTIDE SEQUENCE. RA Zhirakovskaya E.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR847849; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY804134; AAW78739.1; -; mRNA. DR EMBL; DQ284441; ABC66207.1; -; mRNA. DR EMBL; KU745858; AMT81697.1; -; Genomic_DNA. DR EMBL; KY801329; AVI26629.1; -; Genomic_DNA. DR EMBL; KY801330; AVI26630.1; -; Genomic_DNA. DR EMBL; KY801331; AVI26631.1; -; Genomic_DNA. DR EMBL; KY801332; AVI26632.1; -; Genomic_DNA. DR EMBL; KY801333; AVI26633.1; -; Genomic_DNA. DR EMBL; AB774947; BAN59793.1; -; Genomic_DNA. DR EMBL; LT707787; SIT60286.1; -; Genomic_DNA. DR EMBL; LT707788; SIT60287.1; -; Genomic_DNA. DR EMBL; LT707800; SIT60299.1; -; Genomic_DNA. DR EMBL; LT707801; SIT60300.1; -; Genomic_DNA. DR EMBL; LT707854; SIT60353.1; -; Genomic_DNA. DR EMBL; LT707855; SIT60354.1; -; Genomic_DNA. DR EMBL; LT707856; SIT60355.1; -; Genomic_DNA. DR EMBL; LT707857; SIT60356.1; -; Genomic_DNA. DR EMBL; LT707858; SIT60357.1; -; Genomic_DNA. DR EMBL; LT707859; SIT60358.1; -; Genomic_DNA. DR EMBL; LT707860; SIT60359.1; -; Genomic_DNA. DR EMBL; LT707861; SIT60360.1; -; Genomic_DNA. DR EMBL; LT707862; SIT60361.1; -; Genomic_DNA. DR EMBL; LT707863; SIT60362.1; -; Genomic_DNA. DR EMBL; LT707864; SIT60363.1; -; Genomic_DNA. DR EMBL; LT707865; SIT60364.1; -; Genomic_DNA. DR EMBL; LT707866; SIT60365.1; -; Genomic_DNA. DR EMBL; LT707867; SIT60366.1; -; Genomic_DNA. DR EMBL; LT707868; SIT60367.1; -; Genomic_DNA. DR EMBL; LT707869; SIT60368.1; -; Genomic_DNA. DR EMBL; LT707870; SIT60369.1; -; Genomic_DNA. DR EMBL; LT707871; SIT60370.1; -; Genomic_DNA. DR EMBL; LT707872; SIT60371.1; -; Genomic_DNA. DR EMBL; LT707873; SIT60372.1; -; Genomic_DNA. DR EMBL; LT718901; SJK83216.1; -; Genomic_DNA. DR EMBL; LT718902; SJK83217.1; -; Genomic_DNA. DR EMBL; LT718903; SJK83218.1; -; Genomic_DNA. DR EMBL; LT718904; SJK83219.1; -; Genomic_DNA. DR EMBL; LT718905; SJK83220.1; -; Genomic_DNA. DR EMBL; LT718906; SJK83221.1; -; Genomic_DNA. DR EMBL; LT718907; SJK83222.1; -; Genomic_DNA. DR EMBL; LT718908; SJK83223.1; -; Genomic_DNA. DR EMBL; LT718909; SJK83224.1; -; Genomic_DNA. DR EMBL; LT718910; SJK83225.1; -; Genomic_DNA. DR EMBL; LT718912; SJK83227.1; -; Genomic_DNA. DR EMBL; LT718913; SJK83228.1; -; Genomic_DNA. DR EMBL; LT718914; SJK83229.1; -; Genomic_DNA. DR EMBL; LT718915; SJK83230.1; -; Genomic_DNA. DR EMBL; LT718916; SJK83231.1; -; Genomic_DNA. DR EMBL; LT718917; SJK83232.1; -; Genomic_DNA. DR EMBL; LT718918; SJK83233.1; -; Genomic_DNA. DR EMBL; LT718919; SJK83234.1; -; Genomic_DNA. DR EMBL; LT718920; SJK83235.1; -; Genomic_DNA. DR EMBL; LT718921; SJK83236.1; -; Genomic_DNA. DR EMBL; LT718922; SJK83237.1; -; Genomic_DNA. DR EMBL; LT718923; SJK83238.1; -; Genomic_DNA. DR EMBL; LT719017; SJK83332.1; -; Genomic_DNA. DR EMBL; LT882732; SMY43988.1; -; Genomic_DNA. DR EMBL; LT882733; SMY43989.1; -; Genomic_DNA. DR EMBL; LT882771; SMY44028.1; -; Genomic_DNA. DR EMBL; LT883489; SMZ62531.1; -; Genomic_DNA. DR EMBL; LT883490; SMZ62532.1; -; Genomic_DNA. DR EMBL; LT883497; SMZ62539.1; -; Genomic_DNA. DR EMBL; LT883498; SMZ62540.1; -; Genomic_DNA. DR EMBL; LT883504; SMZ62546.1; -; Genomic_DNA. DR EMBL; LS480665; SPT23801.1; -; Genomic_DNA. DR EMBL; LS480666; SPT23802.1; -; Genomic_DNA. DR UniGene; Hs.485130; -. DR Ensembl; ENST00000415996; ENSP00000399298; ENSG00000229295. DR UCSC; uc011hgd.3; human. DR H-InvDB; HIX0078608; -. DR H-InvDB; HIX0165957; -. DR H-InvDB; HIX0166647; -. DR H-InvDB; HIX0166960; -. DR HGNC; HGNC:4940; HLA-DPB1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR OrthoDB; EOG091G0W5S; -. DR ChiTaRS; HLA-DPB1; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:Q5EP54, KW ECO:0000213|PeptideAtlas:Q5EP54}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 258 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015097870. FT TRANSMEM 227 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 258 AA; 29290 MW; BD74758796CA4B5B CRC64; MMVLQVSAAP RTVALTALLM VLLTSVVQGR ATPENYLFQG RQECYAFNGT QRFLERYIYN REEFVRFDSD VGEFRAVTEL GRPDEEYWNS QKDILEEERA VPDRMCRHNY ELGGPMTLQR RVQPRVNVSP SKKGPLQHHN LLVCHVTDFY PGSIQVRWFL NGQEETAGVV STNLIRNGDW TFQILVMLEM TPQQGDVYTC QVEHTSLDSP VTVEWKAQSD SARSKTLTGA GGFVLGLIIC GVGIFMHRRS KKVQRGSA // ID Q5KTP6_BOVIN Unreviewed; 271 AA. AC Q5KTP6; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 12-SEP-2018, entry version 116. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain precursor {ECO:0000313|Ensembl:ENSBTAP00000055511}; DE SubName: Full=MHC class II DO-beta chain {ECO:0000313|EMBL:BAD83671.1}; GN Name=BoLA-DOB {ECO:0000313|EMBL:BAD83671.1}; GN Synonyms=BOLA-DOB {ECO:0000313|Ensembl:ENSBTAP00000055511}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:BAD83671.1}; RN [1] {ECO:0000313|EMBL:BAD83671.1} RP NUCLEOTIDE SEQUENCE. RA Takeshima S., Aida Y.; RT "Complete coding region of the BoLA-DOB mRNA."; RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSBTAP00000055511, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000055511, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [3] {ECO:0000313|Ensembl:ENSBTAP00000055511} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000055511}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; DAAA02054876; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DAAA02054877; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AB117945; BAD83671.1; -; mRNA. DR UniGene; Bt.89681; -. DR STRING; 9913.ENSBTAP00000055511; -. DR Ensembl; ENSBTAT00000065976; ENSBTAP00000055511; ENSBTAG00000047707. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-BTA-2132295; MHC class II antigen presentation. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000047707; Expressed in 10 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 271 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015097926. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 271 AA; 30708 MW; 24240FE91850CA2B CRC64; MSPSWVPWVV TFLSTALRLD ASVTQGRDSP EDFVTQAKAD CYFTNGTEKV RFVVRFIFNL EEYARFDSDL GMFVALTELG KPDAERWNNR PDILARSRAS VDMLCRRNYY LGAPFTVGRR VQPEVTVYPE KTPALQHRNL LLCLVTGFYP GDIKVTWFRN GQEQREGIMS TGLIRNGDWT FQMTVMLAMT PELGEVYTCL VDHPSLLSPV SVEWRAQSEY SWRKILSGAA AFLVGLVFFL VGIVVHIRAW KGRVETPLPG NEVPRAVLPP P // ID Q5M8Y9_XENTR Unreviewed; 262 AA. AC Q5M8Y9; DT 01-FEB-2005, integrated into UniProtKB/TrEMBL. DT 01-FEB-2005, sequence version 1. DT 12-SEP-2018, entry version 134. DE SubName: Full=Major histocompatibility complex, class II, DR beta 1 {ECO:0000313|Ensembl:ENSXETP00000027810}; GN Name=hla-drb1 {ECO:0000313|Ensembl:ENSXETP00000027810, GN ECO:0000313|Xenbase:XB-GENE-945971}; GN Synonyms=MGC108235 {ECO:0000313|EMBL:AAH87775.1}; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364 {ECO:0000313|EMBL:AAH87775.1}; RN [1] {ECO:0000313|EMBL:AAH87775.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Whole body {ECO:0000313|EMBL:AAH87775.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSXETP00000027810} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nigerian {ECO:0000313|Ensembl:ENSXETP00000027810}; RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [3] {ECO:0000313|Ensembl:ENSXETP00000027810} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2011) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAMC01083582; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083583; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083584; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083585; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083586; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083587; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01083588; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC087775; AAH87775.1; -; mRNA. DR RefSeq; NP_001039259.1; NM_001045794.1. DR UniGene; Str.51033; -. DR Ensembl; ENSXETT00000027810; ENSXETP00000027810; ENSXETG00000025586. DR GeneID; 734125; -. DR KEGG; xtr:734125; -. DR CTD; 3123; -. DR Xenbase; XB-GENE-945971; hla-drb1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR Reactome; R-XTR-2132295; MHC class II antigen presentation. DR Proteomes; UP000008143; Unassembled WGS sequence. DR Bgee; ENSXETG00000025586; Expressed in 18 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000008143}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000008143}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 262 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015298100. FT TRANSMEM 221 243 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 109 206 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 262 AA; 29986 MW; D6CD253409C04917 CRC64; MCGISVRVLS VLLTLGVCLC SSPPEDFVYQ YKGQCCFRNG TENVRGLDRY IYNQEEIAYF DSDVGFFIAK TELGKKHFAD YWNSQKDLLE QKRAETDTVC RYNYQFDKPD VIDRKSQPNV KIVNSKTLDL EHENLITCFV DGFFPPMIKV TWLKNGIEEG EQVTSSELLP NGDWTFEIHV MLETTIKHGD TFTCRVEHSS LQQPISVNWE PDVSESARNK MLTGIVGFVL GSIFIIVGLV VYLRSKKTMT RFSVVQNENL MS // ID Q5SQ91_HUMAN Unreviewed; 231 AA. AC Q5SQ91; Q8MGQ8; DT 21-DEC-2004, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 2. DT 18-JUL-2018, entry version 133. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000400295}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000400295}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000400295, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000400295, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000400295} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSP00000382566} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL773543; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR753846; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759848; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR788227; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; Q5SQ91; -. DR STRING; 9606.ENSP00000390431; -. DR PRIDE; Q5SQ91; -. DR Ensembl; ENST00000399658; ENSP00000382566; ENSG00000196610. DR Ensembl; ENST00000417780; ENSP00000394016; ENSG00000228813. DR Ensembl; ENST00000428972; ENSP00000407691; ENSG00000228254. DR Ensembl; ENST00000433114; ENSP00000400295; ENSG00000229493. DR UCSC; uc063vwq.1; human. DR HGNC; HGNC:4945; HLA-DQB2. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR HOVERGEN; HBG012730; -. DR ChiTaRS; HLA-DQB2; human. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q5SQ91}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 231 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014586881. FT DOMAIN 128 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 231 AA; 26536 MW; ABC5BE72C1C4E8AE CRC64; MSWKMALQIP GGFWAAAVTV MLVMLSTPVA EARDFPKDFL VQFKGMCYFT NGTERVRGVA RYIYNREEYG RFDSDVGEFQ AVTELGRSIE DWNNYKDFLE QERAAVDKVC RHNYEAELRT TLQRQVEPTV TISPSRTEAL NHHNLLVCSV TDFYPAQIKV QWFRNDQEET AGVVSTSLIR NGDWTFQILV MLEITPQRGD IYTCQVEHPS LQSPITVEWR PRGPPPAGLL H // ID Q5SR05_HUMAN Unreviewed; 264 AA. AC Q5SR05; DT 21-DEC-2004, integrated into UniProtKB/TrEMBL. DT 21-DEC-2004, sequence version 1. DT 12-SEP-2018, entry version 140. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 2 chain {ECO:0000313|Ensembl:ENSP00000396330}; GN Name=HLA-DQB2 {ECO:0000313|Ensembl:ENSP00000396330}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000396330, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000396330, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|Ensembl:ENSP00000396330} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSP00000388849} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL671681; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL672104; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL713890; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX296564; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936921; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_001287719.1; NM_001300790.1. DR UniGene; Hs.731563; -. DR PRIDE; Q5SR05; -. DR Ensembl; ENST00000419685; ENSP00000416466; ENSG00000230675. DR Ensembl; ENST00000429783; ENSP00000388849; ENSG00000224305. DR Ensembl; ENST00000430668; ENSP00000392299; ENSG00000226165. DR Ensembl; ENST00000437316; ENSP00000396330; ENSG00000232629. DR GeneID; 3120; -. DR UCSC; uc063nrq.1; human. DR CTD; 3120; -. DR EuPathDB; HostDB:ENSG00000232629.8; -. DR HGNC; HGNC:4945; HLA-DQB2. DR OpenTargets; ENSG00000232629; -. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR ChiTaRS; HLA-DQB2; human. DR GenomeRNAi; 3120; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000232629; Expressed in 120 organ(s), highest expression level in skin of abdomen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q5SR05}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 28 {ECO:0000256|SAM:SignalP}. FT CHAIN 29 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014586897. FT TRANSMEM 226 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 29854 MW; 26E9B8B769A9D55A CRC64; MALQIPGGFW AAAVTVMLVM LSTPVAEARD FPKDFLVQFK GMCYFTNGTE RVRGVARYIY NREEYGRFDS DVGEFQAVTE LGRSIEDWNN YKDFLEQERA AVDKVCRHNY EAELRTTLQR QVEPTVTISP SRTEALNHHN LLVCSVTDFY PAQIKVRWFR NDQEETAGVV STSLIRNGDW TFQILVMLEI TPQRGDIYTC QVEHPSLQSP ITVEWRAQSE SAQSKMLSGI GGFVLGLIFL GLGLIIRHRG QKGPRGPPPA GLLH // ID Q5SU54_HUMAN Unreviewed; 269 AA. AC Q5SU54; DT 20-FEB-2007, integrated into UniProtKB/TrEMBL. DT 20-FEB-2007, sequence version 1. DT 12-SEP-2018, entry version 105. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000364080}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:CRL52706.1}; GN Name=HLA-DQB1 {ECO:0000313|EMBL:CRL52706.1, GN ECO:0000313|Ensembl:ENSP00000364080}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000364080, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000364080, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [3] {ECO:0000313|Ensembl:ENSP00000364080} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [4] {ECO:0000313|EMBL:CRL52706.1} RP NUCLEOTIDE SEQUENCE. RA Albrecht V., Boehme I., Schmidt A.H.; RT "Characterisation and Confirmation of new HLA-Alleles found by DKMS RT Life Science Lab."; RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; LN854610; CRL52706.1; -; Genomic_DNA. DR RefSeq; NP_001230890.1; NM_001243961.1. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR SMR; Q5SU54; -. DR EPD; Q5SU54; -. DR MaxQB; Q5SU54; -. DR PRIDE; Q5SU54; -. DR DNASU; 3119; -. DR Ensembl; ENST00000374943; ENSP00000364080; ENSG00000179344. DR GeneID; 3119; -. DR UCSC; uc063nrg.1; human. DR CTD; 3119; -. DR EuPathDB; HostDB:ENSG00000179344.16; -. DR HGNC; HGNC:4944; HLA-DQB1. DR OpenTargets; ENSG00000179344; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR ChiTaRS; HLA-DQB1; human. DR GenomeRNAi; 3119; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000179344; Expressed in 206 organ(s), highest expression level in right lung. DR Genevisible; Q5SU54; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:Q5SU54, KW ECO:0000213|PeptideAtlas:Q5SU54}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 269 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014586887. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 269 AA; 30493 MW; 8406DCC525CF48CA CRC64; MSWKKALRIP GDLRVATVTL MLAMLSSLLA EGRDSPEDFV FQFKGMCYFT NGTERVRLVT RYIYNREEYA RFDSDVGVYR AVTPQGRPDA EYWNSQKEVL EGTRAELDTV CRHNYEVAFR GILQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI IRQRSQKGPQ GPPPAGLLH // ID Q5W418_CANLF Unreviewed; 270 AA. AC Q5W418; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 07-DEC-2004, sequence version 1. DT 12-SEP-2018, entry version 119. DE SubName: Full=MHC class II DO beta {ECO:0000313|EMBL:CAH63450.1}; DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSCAFP00000031388}; GN Name=DLA-DOB {ECO:0000313|EMBL:CAH63450.1, GN ECO:0000313|Ensembl:ENSCAFP00000031388}; GN ORFNames=DLA-DOB-001 {ECO:0000313|EMBL:CAH63450.1}; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615 {ECO:0000313|EMBL:CAH63450.1}; RN [1] {ECO:0000313|EMBL:CAH63450.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15607421; DOI=10.1016/j.ygeno.2004.09.009; RA Debenham S.L., Hart E.A., Ashurst J.L., Howe K.L., Quail M.A., RA Ollier W.E.R., Binns M.M.; RT "Genomic sequence of the class II region of the canine MHC: comparison RT with the MHC of other mammalian species."; RL Genomics 85:48-59(2005). RN [2] {ECO:0000313|Ensembl:ENSCAFP00000031388, ECO:0000313|Proteomes:UP000002254} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000031388, RC ECO:0000313|Proteomes:UP000002254}; RX PubMed=16341006; DOI=10.1038/nature04338; RG Broad Sequencing Platform; RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., RA Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., RA Ponting C.P., Galibert F., Smith D.R., deJong P.J., Kirkness E.F., RA Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., RA Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., RA Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., RA Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., RA Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., RA Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., RA Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., RA Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., RA Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., RA Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., RA Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., RA Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., RA Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., RA Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., RA Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., RA Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., RA Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., RA Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., RA Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., RA Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., RA Marabella R., Maru K., Matthews C., McDonough S., Mehta T., RA Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., RA Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., RA Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., RA Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., RA Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., RA Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., RA Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., RA Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., RA Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., RA Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., RA Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., RA Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., RA Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.; RT "Genome sequence, comparative analysis and haplotype structure of the RT domestic dog."; RL Nature 438:803-819(2005). RN [3] {ECO:0000313|Ensembl:ENSCAFP00000031388} RP IDENTIFICATION. RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000031388}; RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAEX03008236; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AJ630364; CAH63450.1; -; Genomic_DNA. DR RefSeq; NP_001041592.1; NM_001048127.1. DR UniGene; Cfa.26688; -. DR STRING; 9615.ENSCAFP00000031388; -. DR Ensembl; ENSCAFT00000036056; ENSCAFP00000031388; ENSCAFG00000000819. DR GeneID; 607786; -. DR KEGG; cfa:607786; -. DR CTD; 607786; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-CFA-2132295; MHC class II antigen presentation. DR Proteomes; UP000002254; Chromosome 12. DR Bgee; ENSCAFG00000000819; Expressed in 3 organ(s), highest expression level in liver. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002254}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002254}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 270 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015298229. FT TRANSMEM 225 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 270 AA; 30355 MW; B3CAE6F8EAE7CF7C CRC64; MGSGWVPWML ALLVNVTGLD SSMTQGRDSP EDFVIQAKAD CYFINGTEKV QFVVRFIFNL EEYARFDSHV GMFVALTELG KPDAELWNSQ PGILERSRAS VDLLCRHNYE LGAPFTVGRK VQPEVTVYPE RTPSMQHHNL LLCSVTGFYP GDIKIKWFRN GQEERVGVMS TGLIRNGDWT FQTMVMLEMT PELGDVYTCL VNHPSLLSPV SVEWRAQSTY SWRKMLSGIA AFLLGLIFLL VGTVICLRAQ KGYVETQFSG DEISRAVPSP // ID Q5Y7D3_HUMAN Unreviewed; 261 AA. AC Q5Y7D3; U3Q031; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 18-JUL-2018, entry version 146. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000372602}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AAU88012.1}; GN Name=HLA-DQB1 {ECO:0000313|EMBL:AAU88012.1, GN ECO:0000313|Ensembl:ENSP00000372602}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAU88012.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000372602, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|EMBL:AAU88012.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [3] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [4] {ECO:0000213|PDB:4D8P} RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 33-230, AND DISULFIDE BONDS. RX PubMed=22362761; DOI=10.1074/jbc.M111.320374; RA Tollefsen S., Hotta K., Chen X., Simonsen B., Swaminathan K., RA Mathews I.I., Sollid L.M., Kim C.Y.; RT "Structural and functional studies of trans-encoded HLA-DQ2.3 RT (DQA1*03:01/DQB1*02:01) protein molecule."; RL J. Biol. Chem. 287:13611-13619(2012). RN [5] {ECO:0000313|EMBL:AGW82920.2} RP NUCLEOTIDE SEQUENCE. RA Li J.; RT "44 novel HLA-DQB1 alleles found by BGI in 2011 year."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000213|PDB:4OZF, ECO:0000213|PDB:4OZG, ECO:0000213|PDB:4OZH} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 33-224 IN COMPLEX WITH RP CALCIUM, AND DISULFIDE BONDS. RX PubMed=24777060; DOI=10.1038/nsmb.2817; RA Petersen J., Montserrat V., Mujico J.R., Loh K.L., Beringer D.X., RA van Lummel M., Thompson A., Mearin M.L., Schweizer J., RA Kooy-Winkelaar Y., van Bergen J., Drijfhout J.W., Kan W.T., RA La Gruta N.L., Anderson R.P., Reid H.H., Koning F., Rossjohn J.; RT "T-cell receptor recognition of HLA-DQ2-gliadin complexes associated RT with celiac disease."; RL Nat. Struct. Mol. Biol. 21:480-488(2014). RN [7] {ECO:0000313|Ensembl:ENSP00000372602} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2016) to UniProtKB. RN [8] {ECO:0000213|PDB:5KSU, ECO:0000213|PDB:5KSV} RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS) OF 33-230, AND DISULFIDE BONDS. RX PubMed=28364043; DOI=10.1074/jbc.M117.785139; RA Nguyen T.B., Jayaraman P., Bergseng E., Madhusudhan M.S., Kim C.Y., RA Sollid L.M.; RT "Unraveling the structural basis for the unusually rich association of RT human leukocyte antigen DQ2.5 with class-II-associated invariant chain RT peptides."; RL J. Biol. Chem. 292:9218-9228(2017). RN [9] {ECO:0000313|EMBL:AVN68382.1} RP NUCLEOTIDE SEQUENCE. RA Balz V., Krause S., Enczmann J., Fischer J.; RT "New variants of HLA-DQB1."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL731683; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL935026; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY663399; AAU87991.1; -; Genomic_DNA. DR EMBL; AY663407; AAU88012.1; -; Genomic_DNA. DR EMBL; KF270524; AGW82920.2; -; Genomic_DNA. DR EMBL; KY856761; AVN68382.1; -; Genomic_DNA. DR RefSeq; NP_001230891.1; NM_001243962.1. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR PDB; 4D8P; X-ray; 3.05 A; B/D=33-230. DR PDB; 4OZF; X-ray; 2.70 A; B=33-224. DR PDB; 4OZG; X-ray; 3.00 A; B/D=33-224. DR PDB; 4OZH; X-ray; 2.80 A; B/D=33-224. DR PDB; 4OZI; X-ray; 3.20 A; B/D=33-224. DR PDB; 5KSU; X-ray; 2.73 A; B/E=33-230. DR PDB; 5KSV; X-ray; 2.19 A; B=33-230. DR PDBsum; 4D8P; -. DR PDBsum; 4OZF; -. DR PDBsum; 4OZG; -. DR PDBsum; 4OZH; -. DR PDBsum; 4OZI; -. DR PDBsum; 5KSU; -. DR PDBsum; 5KSV; -. DR SMR; Q5Y7D3; -. DR PRIDE; Q5Y7D3; -. DR DNASU; 3119; -. DR Ensembl; ENST00000383121; ENSP00000372602; ENSG00000206237. DR Ensembl; ENST00000383247; ENSP00000372734; ENSG00000206302. DR GeneID; 3119; -. DR KEGG; hsa:3119; -. DR UCSC; uc011fnt.3; human. DR CTD; 3119; -. DR H-InvDB; HIX0166158; -. DR H-InvDB; HIX0167206; -. DR HGNC; HGNC:4944; HLA-DQB1. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OrthoDB; EOG09370O5R; -. DR ChiTaRS; HLA-DQB1; human. DR GenomeRNAi; 3119; -. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4D8P, ECO:0000213|PDB:4OZF, KW ECO:0000213|PDB:4OZG, ECO:0000213|PDB:4OZH}; KW Calcium {ECO:0000213|PDB:4OZI}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000213|PDB:4OZI}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:Q5Y7D3, KW ECO:0000213|PeptideAtlas:Q5Y7D3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015098086. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT METAL 128 128 Calcium. {ECO:0000213|PDB:4OZI}. FT METAL 211 211 Calcium; via carbonyl oxygen. FT {ECO:0000213|PDB:4OZI}. FT METAL 213 213 Calcium. {ECO:0000213|PDB:4OZI}. FT DISULFID 47 111 {ECO:0000213|PDB:4D8P, FT ECO:0000213|PDB:4OZF, FT ECO:0000213|PDB:4OZG}. FT DISULFID 149 205 {ECO:0000213|PDB:4D8P, FT ECO:0000213|PDB:4OZF, FT ECO:0000213|PDB:4OZG}. SQ SEQUENCE 261 AA; 29733 MW; 8957ACD3E93DD105 CRC64; MSWKKALRIP GGLRAATVTL MLSMLSTPVA EGRDSPEDFV YQFKGMCYFT NGTERVRLVS RSIYNREEIV RFDSDVGEFR AVTLLGLPAA EYWNSQKDIL ERKRAAVDRV CRHNYQLELR TTLQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPAQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGIGGFVL GLIFLGLGLI IHHRSQKGLL H // ID Q5Y7D6_HUMAN Unreviewed; 261 AA. AC Q5Y7D6; DT 10-MAY-2005, integrated into UniProtKB/TrEMBL. DT 10-MAY-2005, sequence version 1. DT 12-SEP-2018, entry version 141. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|Ensembl:ENSP00000382034}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AAU88009.1}; DE SubName: Full=cDNA, FLJ79232, highly similar to HLA class II histocompatibility antigen, DQB1*0602 beta chain {ECO:0000313|EMBL:BAH14704.1}; GN Name=HLA-DQB1 {ECO:0000313|EMBL:AAU88009.1, GN ECO:0000313|Ensembl:ENSP00000382034}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AAU88009.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000382034, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|EMBL:AAU88009.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16140993; DOI=10.1101/gr.3554305; RA Raymond C.K., Kas A., Paddock M., Qiu R., Zhou Y., Subramanian S., RA Chang J., Palmieri A., Haugen E., Kaul R., Olson M.V.; RT "Ancient haplotypes of the HLA Class II region."; RL Genome Res. 15:1250-1257(2005). RN [3] {ECO:0000313|EMBL:BAH14704.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Spleen {ECO:0000313|EMBL:BAH14704.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., RA Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., RA Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., RA Kisu Y., Nishikawa T., Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000213|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Burckstummer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [5] {ECO:0000313|Ensembl:ENSP00000382034} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [6] {ECO:0000313|EMBL:BAN59788.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23714642; DOI=10.1186/1471-2164-14-355; RA Hosomichi K., Jinam T.A., Mitsunaga S., Nakaoka H., Inoue I.; RT "Phase-defined complete sequencing of the HLA genes by next-generation RT sequencing."; RL BMC Genomics 14:355-355(2013). RN [7] {ECO:0000313|EMBL:AGW82949.2} RP NUCLEOTIDE SEQUENCE. RA Li J.; RT "44 novel HLA-DQB1 alleles found by BGI in 2011 year."; RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|EMBL:CUX91065.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28547825; DOI=.1111/tan.13057; RA Albrecht V., Zweiniger C., Surendranath V., Lang K., Schofl G., RA Dahl A., Winkler S., Lange V., Bohme I., Schmidt A.H.; RT "Dual redundant sequencing strategy: Full-length gene characterisation RT of 1056 novel and confirmatory HLA alleles."; RL HLA. 90:79-87(2017). RN [9] {ECO:0000313|EMBL:AVN68388.1} RP NUCLEOTIDE SEQUENCE. RA Balz V., Krause S., Enczmann J., Fischer J.; RT "New variants of HLA-DQB1."; RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases. RN [10] {ECO:0000313|EMBL:AST16107.1} RP NUCLEOTIDE SEQUENCE. RA Hurley C.K., Hou L., Lazaro A., Gerfen J., Enriquez E., Galarza P., RA Rodriguez Cardozo M.B., Halagan M., Maiers M., Behm D., Ng J.; RT "Next generation sequencing characterizes the extent of HLA diversity RT in an Argentinian registry population."; RL HLA. 91:175-186(2018). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL662789; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY663395; AAU87980.1; -; Genomic_DNA. DR EMBL; AY663406; AAU88009.1; -; Genomic_DNA. DR EMBL; AY663411; AAU88024.1; -; Genomic_DNA. DR EMBL; KF270555; AGW82949.2; -; Genomic_DNA. DR EMBL; MF417566; AST16107.1; -; Genomic_DNA. DR EMBL; KY856767; AVN68388.1; -; Genomic_DNA. DR EMBL; KY856768; AVN68389.1; -; Genomic_DNA. DR EMBL; AK316333; BAH14704.1; -; mRNA. DR EMBL; AB774942; BAN59788.1; -; Genomic_DNA. DR EMBL; AB774978; BAN59824.1; -; Genomic_DNA. DR EMBL; LN999672; CUX91065.1; -; Genomic_DNA. DR EMBL; LN999677; CUX91070.1; -; Genomic_DNA. DR EMBL; LN999709; CUX91102.1; -; Genomic_DNA. DR EMBL; LN999710; CUX91103.1; -; Genomic_DNA. DR EMBL; LN999767; CUX91160.1; -; Genomic_DNA. DR EMBL; LN999771; CUX91164.1; -; Genomic_DNA. DR EMBL; LT578429; SBO45770.1; -; Genomic_DNA. DR RefSeq; NP_002114.3; NM_002123.4. DR UniGene; Hs.409934; -. DR UniGene; Hs.534322; -. DR STRING; 9606.ENSP00000382034; -. DR MaxQB; Q5Y7D6; -. DR PRIDE; Q5Y7D6; -. DR DNASU; 3119; -. DR Ensembl; ENST00000399084; ENSP00000382034; ENSG00000179344. DR Ensembl; ENST00000434651; ENSP00000407332; ENSG00000179344. DR GeneID; 3119; -. DR UCSC; uc003obw.4; human. DR CTD; 3119; -. DR EuPathDB; HostDB:ENSG00000179344.16; -. DR HGNC; HGNC:4944; HLA-DQB1. DR OpenTargets; ENSG00000179344; -. DR PharmGKB; PA35068; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR TreeFam; TF336626; -. DR ChiTaRS; HLA-DQB1; human. DR GenomeRNAi; 3119; -. DR Proteomes; UP000005640; Chromosome 6. DR Bgee; ENSG00000179344; Expressed in 206 organ(s), highest expression level in right lung. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|MaxQB:Q5Y7D6, KW ECO:0000213|PeptideAtlas:Q5Y7D6}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014587155. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29791 MW; 955BF0E22AA4BD79 CRC64; MSWKKALRIP GDLRVATVTL MLAMLSSLLA EGRDSPEDFV FQFKGMCYFT NGTERVRLVT RYIYNREEYA RFDSDVGVYR AVTPQGRPDA EYWNSQKEVL EGTRAELDTV CRHNYEVAFR GILQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TAGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQSPITVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI IRQRSQKGLL H // ID Q6AYB1_RAT Unreviewed; 263 AA. AC Q6AYB1; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 12-SEP-2018, entry version 141. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AAV40616.1}; DE SubName: Full=RT1 class II, locus Bb {ECO:0000313|EMBL:AAH79121.1}; DE SubName: Full=RT1-Bb {ECO:0000313|EMBL:AGV39037.1}; DE SubName: Full=Rano class II histocompatibility antigen, B-1 beta chain {ECO:0000313|Ensembl:ENSRNOP00000000525}; GN Name=RT1-Bb {ECO:0000313|EMBL:AAH79121.1, GN ECO:0000313|Ensembl:ENSRNOP00000000525, ECO:0000313|RGD:3469}; GN Synonyms=Bb {ECO:0000313|EMBL:AGV39037.1}, GN LOC688090 {ECO:0000313|RGD:3469}; GN ORFNames=rCG_60913 {ECO:0000313|EMBL:EDL96803.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH79121.1}; RN [1] {ECO:0000313|EMBL:AAH79121.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney {ECO:0000313|EMBL:AAH79121.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., RA Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., RA Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., RA Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., RA Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., RA Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., RA Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., RA Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., RA Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., RA Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., RA Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., RA Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., RA Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., RA Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., RA Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., RA Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., RA Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., RA Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., RA Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [2] {ECO:0000313|EMBL:AAV40616.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN/CrlBR {ECO:0000313|EMBL:AAV40616.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:AAV40616.1}; RX PubMed=15517241; DOI=10.1007/s00251-004-0725-7; RA Ettinger R.A., Moustakas A.K., Lobaton S.D.; RT "Open reading frame sequencing and structure-based alignment of RT polypeptides encoded by RT1-Bb, RT1-Ba, RT1-Db, and RT1-Da alleles."; RL Immunogenetics 56:585-596(2004). RN [3] {ECO:0000313|Ensembl:ENSRNOP00000000525, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000525, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [4] {ECO:0000313|EMBL:EDL96803.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL96803.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [5] {ECO:0000313|EMBL:EDL96803.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL96803.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., RA Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., RA Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|Ensembl:ENSRNOP00000000525} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000525}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [7] {ECO:0000313|EMBL:AGV39037.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DA.1H {ECO:0000313|EMBL:AGV39037.1}; RX PubMed=24586191; DOI=10.1371/journal.pgen.1004151; RG EURATRANS; RA Tuncel J., Haag S., Yau A.C.Y., Norin U., Baud A., Lonnblom E., RA Maratou K., Ytterberg A.J., Ekman D., Thordardottir S., RA Johannesson M., Gillett A., Stridh P., Jagodic M., Olsson T., RA Fernandez-Teruel A., Zubarev R.A., Mott R., Aitman T.J., Flint J., RA Holmdahl R.; RT "Natural polymorphisms in Tap2 influence negative selection and RT CD4?CD8 lineage commitment in the rat."; RL PLoS Genet. 10:e1004151-e1004151(2014). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC098547; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC079121; AAH79121.1; -; mRNA. DR EMBL; AY626187; AAV40616.1; -; mRNA. DR EMBL; KC222940; AGV39037.1; -; mRNA. DR EMBL; CH473988; EDL96803.1; -; Genomic_DNA. DR RefSeq; NP_001004084.1; NM_001004084.2. DR UniGene; Rn.202964; -. DR SMR; Q6AYB1; -. DR PRIDE; Q6AYB1; -. DR Ensembl; ENSRNOT00000000525; ENSRNOP00000000525; ENSRNOG00000032708. DR GeneID; 309622; -. DR KEGG; rno:309622; -. DR CTD; 309622; -. DR RGD; 3469; RT1-Bb. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-RNO-202424; Downstream TCR signaling. DR Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-RNO-202433; Generation of second messenger molecules. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Reactome; R-RNO-389948; PD-1 signaling. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000032708; Expressed in 9 organ(s), highest expression level in spleen. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl. DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl. DR GO; GO:0008134; F:transcription factor binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0002344; P:B cell affinity maturation; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl. DR GO; GO:0046635; P:positive regulation of alpha-beta T cell activation; IEA:Ensembl. DR GO; GO:0002579; P:positive regulation of antigen processing and presentation; IEA:Ensembl. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 263 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015298383. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 263 AA; 29970 MW; A7CE8A478C8126C1 CRC64; MALQTPSFLL PAAVVVLMVL SSPGTEGRDS PRDFVFQFKG LCYYTNGTQR IRLVIRYIYN REEYVRFDSD VGEFRALTEL GRPSAEYYNK QYLERTRAEL DTVCRHNYEE TEVPTSLRRL EQPNVAISLS RTEALNHHNL LVCSVTDFYP AQIKVRWFRN GQEETAGVVS TQLIRNGDWT FQILVMLEMT PQRGEVYICH VDHPSLESPV TVEWRAQSES AQSKMLSGIG GFVLGVIFLG LGLFIRHKRQ KGPRGPPPAG LLQ // ID Q6MGA2_RAT Unreviewed; 272 AA. AC Q6MGA2; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 12-SEP-2018, entry version 125. DE SubName: Full=RCG60952 {ECO:0000313|EMBL:EDL96804.1}; DE SubName: Full=RT1 class II, DO beta {ECO:0000313|EMBL:CAE83944.1}; DE SubName: Full=RT1 class II, locus DOb {ECO:0000313|Ensembl:ENSRNOP00000000526}; DE SubName: Full=RT1-DOb {ECO:0000313|EMBL:AGV39012.1}; GN Name=RT1-DOb {ECO:0000313|EMBL:CAE83944.1, GN ECO:0000313|Ensembl:ENSRNOP00000000526, ECO:0000313|RGD:1595814}; GN Synonyms=Arrb2-ps {ECO:0000313|RGD:1595814}, GN DOb {ECO:0000313|EMBL:AGV39012.1}, Hla-dma {ECO:0000313|RGD:1595814}, GN Hla-dmb {ECO:0000313|RGD:1595814}, Psmb9 {ECO:0000313|RGD:1595814}, GN RT1-Ba {ECO:0000313|RGD:1595814}, RT1-Bb {ECO:0000313|RGD:1595814}, GN RT1-Da {ECO:0000313|RGD:1595814}, RT1-Db1 {ECO:0000313|RGD:1595814}, GN RT1-Db2 {ECO:0000313|RGD:1595814}, Tap1 {ECO:0000313|RGD:1595814}, GN Tap2 {ECO:0000313|RGD:1595814}, Tesb {ECO:0000313|RGD:1595814}; GN ORFNames=rCG_60952 {ECO:0000313|EMBL:EDL96804.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:CAE83944.1}; RN [1] {ECO:0000313|EMBL:CAE83944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83944.1}; RA Boehm S., Borzym K., Gelling S., Gimmel V., Heitmann K., Kosiura A., RA Lang N., Lehrack S., Thiel J., Sontag M., Hurt P., Himmelbauer H., RA Sudbrak R., Reinhardt R.; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAE83944.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83944.1}; RX PubMed=15060004; DOI=10.1101/gr.1987704; RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., RA Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.; RT "The genomic sequence and comparative analysis of the rat major RT histocompatibility complex."; RL Genome Res. 14:631-639(2004). RN [3] {ECO:0000313|Ensembl:ENSRNOP00000000526, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000526, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [4] {ECO:0000313|EMBL:EDL96804.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL96804.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [5] {ECO:0000313|EMBL:EDL96804.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL96804.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., RA Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., RA Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|Ensembl:ENSRNOP00000000526} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000526}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [7] {ECO:0000313|EMBL:AGV39012.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DA.1H {ECO:0000313|EMBL:AGV39012.1}; RX PubMed=24586191; DOI=10.1371/journal.pgen.1004151; RG EURATRANS; RA Tuncel J., Haag S., Yau A.C.Y., Norin U., Baud A., Lonnblom E., RA Maratou K., Ytterberg A.J., Ekman D., Thordardottir S., RA Johannesson M., Gillett A., Stridh P., Jagodic M., Olsson T., RA Fernandez-Teruel A., Zubarev R.A., Mott R., Aitman T.J., Flint J., RA Holmdahl R.; RT "Natural polymorphisms in Tap2 influence negative selection and RT CD4?CD8 lineage commitment in the rat."; RL PLoS Genet. 10:e1004151-e1004151(2014). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC098547; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC222915; AGV39012.1; -; mRNA. DR EMBL; BX883043; CAE83944.1; -; Genomic_DNA. DR EMBL; CH473988; EDL96804.1; -; Genomic_DNA. DR RefSeq; NP_001008846.1; NM_001008846.1. DR UniGene; Rn.215279; -. DR STRING; 10116.ENSRNOP00000000526; -. DR PRIDE; Q6MGA2; -. DR Ensembl; ENSRNOT00000000526; ENSRNOP00000000526; ENSRNOG00000000454. DR GeneID; 365542; -. DR KEGG; rno:365542; -. DR UCSC; RGD:1595814; rat. DR CTD; 365542; -. DR RGD; 1595814; RT1-DOb. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000000454; Expressed in 8 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 225 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 272 AA; 30604 MW; 162F9B6BAEBC861B CRC64; MGAGRAPWVV ALLVNLMRPD SFMVEGRDSP EDFVIQAKAE CYFTNGTEKV RFLVRFIFNL EEYLHFDSDL GFFVALTELG EVDADQWNKR LDLLETSRAA VNMVCRQEYK LGAPFTVERN VPPEVTVYPE RTPLLQQHNL LLCSVTDFYP GDISVRWFRN GQEERSGVMS TGLVRNGDWT FQTTVMLEMI PELGDVYSCL VEHPGLLRPV SVAWVAQSEY SWEKILSGAA AFLLGLTVFL VGAVIHLKAQ KASVETQPGN EASRALLPPH PY // ID Q6MGA7_RAT Unreviewed; 261 AA. AC Q6MGA7; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 12-SEP-2018, entry version 143. DE SubName: Full=Hla-dmb protein {ECO:0000313|EMBL:AAH91108.1}; DE SubName: Full=Major histocompatibility complex, class II, DM beta, isoform CRA_a {ECO:0000313|EMBL:EDL96812.1}; DE SubName: Full=RT1 class II, DM beta {ECO:0000313|EMBL:CAE83939.1}; DE SubName: Full=RT1 class II, locus DMb {ECO:0000313|Ensembl:ENSRNOP00000065741}; DE SubName: Full=RT1-DMb {ECO:0000313|EMBL:AGV38996.1}; GN Name=RT1-DMb {ECO:0000313|EMBL:CAE83939.1, GN ECO:0000313|Ensembl:ENSRNOP00000065741, ECO:0000313|RGD:735096}; GN Synonyms=DMb {ECO:0000313|EMBL:AGV38996.1}, GN Hla-dmb {ECO:0000313|EMBL:AAH91108.1}, GN LOC100909630 {ECO:0000313|RGD:735096}, GN LOC108348139 {ECO:0000313|RGD:11469141}; GN ORFNames=rCG_60904 {ECO:0000313|EMBL:EDL96812.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:CAE83939.1}; RN [1] {ECO:0000313|EMBL:CAE83939.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83939.1}; RA Boehm S., Borzym K., Gelling S., Gimmel V., Heitmann K., Kosiura A., RA Lang N., Lehrack S., Thiel J., Sontag M., Hurt P., Himmelbauer H., RA Sudbrak R., Reinhardt R.; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAE83939.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83939.1}; RX PubMed=15060004; DOI=10.1101/gr.1987704; RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., RA Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.; RT "The genomic sequence and comparative analysis of the rat major RT histocompatibility complex."; RL Genome Res. 14:631-639(2004). RN [3] {ECO:0000313|EMBL:AAH91108.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Thymus {ECO:0000313|EMBL:AAH91108.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., RA Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., RA Feolo M., Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., RA Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., RA Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., RA Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., RA Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., RA Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., RA Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., RA Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., RA Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., RA Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., RA Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., RA Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., RA Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., RA Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., RA Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., RA Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., RA Makowski K.A., Bosak S., Malek J.; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] {ECO:0000313|Ensembl:ENSRNOP00000065741, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000065741, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [5] {ECO:0000313|EMBL:EDL96812.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL96812.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [6] {ECO:0000313|EMBL:EDL96812.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL96812.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., RA Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., RA Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|Ensembl:ENSRNOP00000065741} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000065741}; RG Ensembl; RL Submitted (FEB-2013) to UniProtKB. RN [8] {ECO:0000313|EMBL:AGV38996.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DA.1H {ECO:0000313|EMBL:AGV38997.1}, RC DA.1I {ECO:0000313|EMBL:AGV38996.1}, and RC DA.1U {ECO:0000313|EMBL:AGV38998.1}; RX PubMed=24586191; DOI=10.1371/journal.pgen.1004151; RG EURATRANS; RA Tuncel J., Haag S., Yau A.C.Y., Norin U., Baud A., Lonnblom E., RA Maratou K., Ytterberg A.J., Ekman D., Thordardottir S., RA Johannesson M., Gillett A., Stridh P., Jagodic M., Olsson T., RA Fernandez-Teruel A., Zubarev R.A., Mott R., Aitman T.J., Flint J., RA Holmdahl R.; RT "Natural polymorphisms in Tap2 influence negative selection and RT CD4?CD8 lineage commitment in the rat."; RL PLoS Genet. 10:e1004151-e1004151(2014). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AABR07044415; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC098547; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC091108; AAH91108.1; -; mRNA. DR EMBL; KC222899; AGV38996.1; -; mRNA. DR EMBL; KC222900; AGV38997.1; -; mRNA. DR EMBL; KC222901; AGV38998.1; -; mRNA. DR EMBL; BX883043; CAE83939.1; -; Genomic_DNA. DR EMBL; CH473988; EDL96812.1; -; Genomic_DNA. DR RefSeq; NP_942035.2; NM_198740.2. DR RefSeq; XP_017443521.1; XM_017588032.1. DR RefSeq; XP_017457348.1; XM_017601859.1. DR UniGene; Rn.5892; -. DR STRING; 10116.ENSRNOP00000066169; -. DR PRIDE; Q6MGA7; -. DR Ensembl; ENSRNOT00000073474; ENSRNOP00000065741; ENSRNOG00000051002. DR Ensembl; ENSRNOT00000075342; ENSRNOP00000066169; ENSRNOG00000049491. DR GeneID; 108348139; -. DR GeneID; 294273; -. DR KEGG; rno:108348139; -. DR KEGG; rno:294273; -. DR CTD; 294273; -. DR RGD; 11469141; LOC108348139. DR RGD; 735096; RT1-DMb. DR eggNOG; ENOG410IFNH; Eukaryota. DR eggNOG; ENOG410YU9X; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000231198; -. DR HOVERGEN; HBG007327; -. DR KO; K06752; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR TreeFam; TF335727; -. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000049491; Expressed in 9 organ(s), highest expression level in colon. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015298569. FT TRANSMEM 219 238 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 115 208 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 28995 MW; 66FE048AB738D99A CRC64; MAALWPLLLA LSLGCIGAGG FVAHVESTCL LDDEGTPMDF TYCISFNKDL LACWDPEEGQ IVPCEYGVLF KLAEFISNIL NKEEGLIQRL KNGLQDCSTH TQPFWNALTH RTRTPSVQVA QTAPFNTREP VMLACYVWGF YPADVTVVWM KNGQLVTSHS NKEKTAQPNG DWTYQTVSYL ALTPSYWDIY TCVVQHSGTP EPIRANWTPG LSPIQTVKVS VSAATLGLGF IIFCLGFFRW RKSHSSSYTP LPGSTYPEGR P // ID Q70IB5_BOVIN Unreviewed; 259 AA. AC Q70IB5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 12-SEP-2018, entry version 127. DE SubName: Full=Putative MHC class II antigen {ECO:0000313|EMBL:CAE45176.1}; GN Name=BoLA-DIB {ECO:0000313|EMBL:CAE45176.1}; GN Synonyms=BOLA-DYB {ECO:0000313|Ensembl:ENSBTAP00000054535}, GN BoLA-DYB {ECO:0000313|EMBL:CAE45176.1}, GN DYB {ECO:0000313|EMBL:AAY34694.1}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913 {ECO:0000313|EMBL:CAE45176.1}; RN [1] {ECO:0000313|EMBL:CAE45176.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Afferent lymph {ECO:0000313|EMBL:CAE45176.1}; RX PubMed=14745522; DOI=10.1007/s00251-004-0641-x; RA Ballingall K.T., Ellis S.A., MacHugh N.D., Archibald S.D., RA McKeever D.J.; RT "The DY genes of the cattle MHC: expression and comparative analysis RT of an unusual class II MHC gene pair."; RL Immunogenetics 55:748-755(2004). RN [2] {ECO:0000313|EMBL:AAY34694.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=16573526; DOI=10.1111/j.1365-2052.2005.01395.x; RA Childers C.P., Newkirk H.L., Honeycutt D.A., Ramlachan N., RA Muzney D.M., Sodergren E., Gibbs R.A., Weinstock G.M., Womack J.E., RA Skow L.C.; RT "Comparative analysis of the bovine MHC class IIb sequence identifies RT inversion breakpoints and three unexpected genes."; RL Anim. Genet. 37:121-129(2006). RN [3] {ECO:0000313|Ensembl:ENSBTAP00000054535, ECO:0000313|Proteomes:UP000009136} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000054535, RC ECO:0000313|Proteomes:UP000009136}; RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42; RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., RA Puiu D., Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., RA Marcais G., Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.; RT "A whole-genome assembly of the domestic cow, Bos taurus."; RL Genome Biol. 10:R42.01-R42.10(2009). RN [4] {ECO:0000313|Ensembl:ENSBTAP00000054535} RP IDENTIFICATION. RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000054535}; RG Ensembl; RL Submitted (MAR-2016) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; DAAA02054876; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AY957499; AAY34694.1; -; Genomic_DNA. DR EMBL; AJ580584; CAE45176.1; -; mRNA. DR RefSeq; NP_001012697.1; NM_001012679.1. DR UniGene; Bt.29870; -. DR Ensembl; ENSBTAT00000063954; ENSBTAP00000054535; ENSBTAG00000045923. DR GeneID; 282498; -. DR KEGG; bta:282498; -. DR CTD; 282498; -. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR Proteomes; UP000009136; Chromosome 23. DR Bgee; ENSBTAG00000045923; Expressed in 3 organ(s), highest expression level in spleen. DR ExpressionAtlas; Q70IB5; baseline and differential. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000009136}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000009136}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 259 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014106743. FT TRANSMEM 232 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 127 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 259 AA; 29440 MW; 2F6EF4936A7218CB CRC64; MRVTIPRNPG TVAGMVMAVF LVLRIPEAHC RDAPKNFVYQ FKGMCYFTNG TEHVRLVARQ IYNKEEILHF DSDLGEFVAV TELGRVCAEI WNTQKDLLAE FRAYVDTLCR HNYKETAGFT VQRRVEPTVT VSPASTEALN HHNLLVCSVT DFYPRQVKVK WFRNQQEQTA GVGFTPLTQN GDWTYQIHVM LETVPQLGDV YVCHVDHPSL QSPITVEWRA QSESAQSKMQ SGIGGFVLGL IFLGVGLFVH FWDKRASRS // ID Q8MGP9_PIG Unreviewed; 261 AA. AC Q8MGP9; DT 01-OCT-2002, integrated into UniProtKB/TrEMBL. DT 01-OCT-2002, sequence version 1. DT 12-SEP-2018, entry version 142. DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AAM20963.1}; DE SubName: Full=MHC class II histocompatibility antigen SLA-DQB1 {ECO:0000313|EMBL:BAD99117.1}; DE SubName: Full=SLA class II histocompatibility antigen, DQ haplotype C beta chain precursor {ECO:0000313|Ensembl:ENSSSCP00000001575}; GN Name=SLA-DQB {ECO:0000313|EMBL:AAM20963.1}; GN Synonyms=SLA-DQB1 {ECO:0000313|EMBL:AAR22514.1, GN ECO:0000313|Ensembl:ENSSSCP00000001575}; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae; OC Sus. OX NCBI_TaxID=9823 {ECO:0000313|EMBL:AAM20963.1}; RN [1] {ECO:0000313|EMBL:AAR22514.1} RP NUCLEOTIDE SEQUENCE. RA Ho C.-S., Martens G.W., Baker J.E., Smith D.M.; RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AAM20963.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15713212; DOI=10.1111/j.1399-0039.2005.00337.x; RA Smith D.M., Lunney J.K., Martens G.W., Ando A., Lee J.H., Ho C.S., RA Schook L., Renard C., Chardon P.; RT "Nomenclature for factors of the SLA class-I system, 2004."; RL Tissue Antigens 65:136-149(2005). RN [3] {ECO:0000313|EMBL:BAD99117.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Spleen {ECO:0000313|EMBL:BAD99117.1}; RA Uenishi H., Tanaka M., Eguchi-Ogawa T., Domukai M., Awata T.; RT "SLABLAST: a database of SLA sequences with nomenclature and for RT discrimination of newly cloned SLA sequences against known SLA RT alleles."; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:ABW24127.1} RP NUCLEOTIDE SEQUENCE. RA Ho C.-S., Lee Y.-J., Franzo-Romain M.H., Winfree L.E., Smith D.M.; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. RN [5] {ECO:0000313|EMBL:ACA21777.1} RP NUCLEOTIDE SEQUENCE. RA Ho C.-S., Lee Y.-J., Franzo-Romain M.H., Smith D.M.; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. RN [6] {ECO:0000313|EMBL:ACE07016.1} RP NUCLEOTIDE SEQUENCE. RA Yeom S.C., Park C.G., Lee B.C., Lee W.J.; RT "Sequence base SLA typing in CMS miniature pig."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. RN [7] {ECO:0000313|EMBL:ABW24127.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19508353; DOI=10.1111/j.1744-313X.2009.00853.x; RA Ho C.S., Franzo-Romain M.H., Lee Y.J., Lee J.H., Smith D.M.; RT "Sequence-based characterization of swine leucocyte antigen alleles in RT commercially available porcine cell lines."; RL Int. J. Immunogenet. 36:231-234(2009). RN [8] {ECO:0000313|Ensembl:ENSSSCP00000001575, ECO:0000313|Proteomes:UP000008227} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000001575}; RG Porcine genome sequencing project; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [9] {ECO:0000313|Ensembl:ENSSSCP00000001575} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [10] {ECO:0000313|EMBL:AOP12369.1} RP NUCLEOTIDE SEQUENCE. RA Gao C., Quan J., Jiang X., He X., Li C., Chen H.; RT "Swine leukocyte antigen (SLA) diversity in Large White and Landrace RT pigs."; RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AEMK02000055; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF464024; AAM20963.1; -; mRNA. DR EMBL; AF464028; AAM20967.1; -; mRNA. DR EMBL; AY135569; AAN35087.1; -; mRNA. DR EMBL; AY459300; AAR22514.1; -; mRNA. DR EMBL; EU170461; ABW24127.1; -; mRNA. DR EMBL; EU432064; ACA21777.1; -; mRNA. DR EMBL; EU722914; ACE07016.1; -; mRNA. DR EMBL; KU754584; AOP12369.1; -; mRNA. DR EMBL; AB215114; BAD99117.1; -; mRNA. DR UniGene; Ssc.11063; -. DR SMR; Q8MGP9; -. DR PRIDE; Q8MGP9; -. DR Ensembl; ENSSSCT00000001617; ENSSSCP00000001575; ENSSSCG00000001457. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR TreeFam; TF336626; -. DR Reactome; R-SSC-202424; Downstream TCR signaling. DR Reactome; R-SSC-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-SSC-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-SSC-202433; Generation of second messenger molecules. DR Reactome; R-SSC-2132295; MHC class II antigen presentation. DR Reactome; R-SSC-389948; PD-1 signaling. DR Proteomes; UP000008227; Chromosome 7. DR Bgee; ENSSSCG00000001457; Expressed in 6 organ(s), highest expression level in lung. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000008227}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q8MGP9}; KW Reference proteome {ECO:0000313|Proteomes:UP000008227}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015099291. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 233 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29595 MW; F67D59082B54EB12 CRC64; MSGMVALRLP RGLWTAALTV MLVVLGAPVA EGRDSPQDFV YQFKFECYFF NGTQRVRGVA RWVYNQEEHV RFDSDVGEFR AVTPLGRPTA DYWNGQKDVL EQKRAEVDTV CKHNYQIEEG TTLQRRVQPT VTISPSKAEA LNHHNLLVCA VTDFYPSQVK VQWFRNGQEE TAGVVSTPLI RNGDWTYQVL VMLEMNLQRG DVYTCRVEHS SLQNPILVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLF IRHRSQKGLV R // ID Q95HJ4_DANRE Unreviewed; 303 AA. AC Q95HJ4; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 12-SEP-2018, entry version 126. DE SubName: Full=Novel protein similar to parts of MHC class II beta chain and MHC class II antigen {ECO:0000313|EMBL:CAD10086.1}; DE SubName: Full=Si:busm1-228j01.6 {ECO:0000313|Ensembl:ENSDARP00000133249}; GN Name=si:busm1-228j01.6 {ECO:0000313|Ensembl:ENSDARP00000133249, GN ECO:0000313|ZFIN:ZDB-GENE-030616-396}; GN ORFNames=dZ228J01.6-001 {ECO:0000313|EMBL:CAD10086.1}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:CAD10086.1}; RN [1] {ECO:0000313|EMBL:CAD10086.1} RP NUCLEOTIDE SEQUENCE. RA Lloyd D.; RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSDARP00000133249, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000133249, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human genome."; RL Nature 496:498-503(2013). RN [3] {ECO:0000313|Ensembl:ENSDARP00000133249} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000133249}; RG Ensembl; RL Submitted (NOV-2015) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CU914776; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL591442; CAD10086.1; -; Genomic_DNA. DR RefSeq; NP_001001595.1; NM_001001595.1. DR UniGene; Dr.92213; -. DR Ensembl; ENSDART00000158784; ENSDARP00000133249; ENSDARG00000041705. DR GeneID; 368846; -. DR KEGG; dre:368846; -. DR ZFIN; ZDB-GENE-030616-396; si:busm1-228j01.6. DR GeneTree; ENSGT00900000140849; -. DR HOGENOM; HOG000100909; -. DR HOVERGEN; HBG012730; -. DR OrthoDB; EOG091G05RP; -. DR Reactome; R-DRE-2132295; MHC class II antigen presentation. DR Proteomes; UP000000437; Chromosome 8. DR Bgee; ENSDARG00000041705; Expressed in 3 organ(s), highest expression level in pharyngeal gill. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000000437}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 303 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015299605. FT TRANSMEM 231 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 303 AA; 34486 MW; 470F7C5CB5C98C51 CRC64; MNAKINYSLA AVFLSALFET VHAYYTYAQI QCHVSDSLQK IEFIFSVTYN MIELVRYNST EDTFFGYTAI GQKFAEEYNK DKVLLAQHDF VLNQCRELGD VILPNAVWLA GECLIQLLTL NIKTKVKPEV IIRSVTEAKG NRKAVLVCSA YDFYPKGIKL TWMRDDKKVT AELTSSEVMA DGHWHYQIHS YLEYFPQTGE KISCVVDHAS SLKPMIYYWD PSLPESERSK IILGAVGLLM GIFTAAAGVI YYKRKQTDLL IEDAPKLLNR VELRGEWWPH HFSFTEAPAA SNIGLLLCNS ILI // ID Q9TQA6_RAT Unreviewed; 264 AA. AC Q9TQA6; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 12-SEP-2018, entry version 148. DE SubName: Full=Class II MHC RT1.D(N) beta chain {ECO:0000313|EMBL:AAD39083.1}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AAV40636.1}; DE SubName: Full=RCG60985, isoform CRA_a {ECO:0000313|EMBL:EDL96798.1}; DE SubName: Full=RT1 class II, D beta 1 {ECO:0000313|EMBL:CAE83947.1}; DE SubName: Full=RT1-Db1 {ECO:0000313|EMBL:AGV39047.1}; DE SubName: Full=Rano class II histocompatibility antigen, D-1 beta chain {ECO:0000313|Ensembl:ENSRNOP00000000522}; GN Name=RT1-Db1 {ECO:0000313|EMBL:CAE83947.1, GN ECO:0000313|Ensembl:ENSRNOP00000000522, ECO:0000313|RGD:1593282}; GN Synonyms=Arrb2-ps {ECO:0000313|RGD:1593282}, GN Db1 {ECO:0000313|EMBL:AGV39047.1}, Hla-dma {ECO:0000313|RGD:1593282}, GN Hla-dmb {ECO:0000313|RGD:1593282}, Psmb9 {ECO:0000313|RGD:1593282}, GN RT1-Ba {ECO:0000313|RGD:1593282}, RT1-Bb {ECO:0000313|RGD:1593282}, GN RT1-Da {ECO:0000313|RGD:1593282}, GN RT1-Db {ECO:0000313|EMBL:AAV40636.1}, GN RT1-Db2 {ECO:0000313|RGD:1593282}, RT1-DOb {ECO:0000313|RGD:1593282}, GN RT1.D(n) {ECO:0000313|EMBL:AAD39083.1}, GN Tap1 {ECO:0000313|RGD:1593282}, Tap2 {ECO:0000313|RGD:1593282}, GN Tesb {ECO:0000313|RGD:1593282}; GN ORFNames=rCG_60985 {ECO:0000313|EMBL:EDL96798.1}; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116 {ECO:0000313|EMBL:AAD39083.1}; RN [1] {ECO:0000313|EMBL:AAD39083.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:AAD39083.1}; RX PubMed=10369938; DOI=10.1007/s002510050676; RA Tian L., Wang M., Yu J., Kahan B.D., Stepkowski S.M.; RT "Nucleotide sequences of three distinct complementary DNA clones RT encoding rat class II major histocompatibility complex RT1.D beta- RT chain proteins."; RL Immunogenetics 49:735-737(1999). RN [2] {ECO:0000313|EMBL:CAE83947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83947.1}; RA Boehm S., Borzym K., Gelling S., Gimmel V., Heitmann K., Kosiura A., RA Lang N., Lehrack S., Thiel J., Sontag M., Hurt P., Himmelbauer H., RA Sudbrak R., Reinhardt R.; RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:CAE83947.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Brown Norway {ECO:0000313|EMBL:CAE83947.1}; RX PubMed=15060004; DOI=10.1101/gr.1987704; RA Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., RA Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.; RT "The genomic sequence and comparative analysis of the rat major RT histocompatibility complex."; RL Genome Res. 14:631-639(2004). RN [4] {ECO:0000313|EMBL:AAV40636.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN/CrlBR {ECO:0000313|EMBL:AAV40636.1}; RC TISSUE=Thymus {ECO:0000313|EMBL:AAV40636.1}; RX PubMed=15517241; DOI=10.1007/s00251-004-0725-7; RA Ettinger R.A., Moustakas A.K., Lobaton S.D.; RT "Open reading frame sequencing and structure-based alignment of RT polypeptides encoded by RT1-Bb, RT1-Ba, RT1-Db, and RT1-Da alleles."; RL Immunogenetics 56:585-596(2004). RN [5] {ECO:0000313|Ensembl:ENSRNOP00000000522, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000522, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [6] {ECO:0000313|EMBL:EDL96798.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL96798.1}; RX PubMed=15632090; DOI=10.1101/gr.2889405; RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M., RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z., RA Istrail S., Li P., Sutton G.; RT "Gene and alternative splicing annotation with AIR."; RL Genome Res. 15:54-66(2005). RN [7] {ECO:0000313|EMBL:EDL96798.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BN {ECO:0000313|EMBL:EDL96798.1}; RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H., RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M., RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., RA Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., RA Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] {ECO:0000313|Ensembl:ENSRNOP00000000522} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000000522}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [9] {ECO:0000313|EMBL:AGV39047.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DA.1H {ECO:0000313|EMBL:AGV39047.1}; RX PubMed=24586191; DOI=10.1371/journal.pgen.1004151; RG EURATRANS; RA Tuncel J., Haag S., Yau A.C.Y., Norin U., Baud A., Lonnblom E., RA Maratou K., Ytterberg A.J., Ekman D., Thordardottir S., RA Johannesson M., Gillett A., Stridh P., Jagodic M., Olsson T., RA Fernandez-Teruel A., Zubarev R.A., Mott R., Aitman T.J., Flint J., RA Holmdahl R.; RT "Natural polymorphisms in Tap2 influence negative selection and RT CD4?CD8 lineage commitment in the rat."; RL PLoS Genet. 10:e1004151-e1004151(2014). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AABR07072809; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF084933; AAD39083.1; -; mRNA. DR EMBL; AY626207; AAV40636.1; -; mRNA. DR EMBL; KC222950; AGV39047.1; -; mRNA. DR EMBL; BX883043; CAE83947.1; -; Genomic_DNA. DR EMBL; CH473988; EDL96798.1; -; Genomic_DNA. DR RefSeq; NP_001008884.1; NM_001008884.2. DR UniGene; Rn.33311; -. DR STRING; 10116.ENSRNOP00000000522; -. DR Ensembl; ENSRNOT00000000522; ENSRNOP00000000522; ENSRNOG00000033215. DR GeneID; 294270; -. DR KEGG; rno:294270; -. DR CTD; 294270; -. DR RGD; 1593282; RT1-Db1. DR eggNOG; ENOG410IWG3; Eukaryota. DR eggNOG; ENOG410YI0S; LUCA. DR GeneTree; ENSGT00900000140849; -. DR HOVERGEN; HBG012730; -. DR KO; K06752; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G15IU; -. DR TreeFam; TF336626; -. DR Reactome; R-RNO-202424; Downstream TCR signaling. DR Reactome; R-RNO-202427; Phosphorylation of CD3 and TCR zeta chains. DR Reactome; R-RNO-202430; Translocation of ZAP-70 to Immunological synapse. DR Reactome; R-RNO-202433; Generation of second messenger molecules. DR Reactome; R-RNO-2132295; MHC class II antigen presentation. DR Reactome; R-RNO-389948; PD-1 signaling. DR Proteomes; UP000002494; Chromosome 20. DR Bgee; ENSRNOG00000033215; Expressed in 10 organ(s), highest expression level in spleen. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW Complete proteome {ECO:0000313|Proteomes:UP000002494}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Proteomics identification {ECO:0000213|PeptideAtlas:Q9TQA6}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5015300041. FT TRANSMEM 227 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 228 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 30202 MW; C57FCD5C5CBF0FB3 CRC64; MVWLARDSCV AAVILLLTVL SPPVALVRDP TPRFLEQYKS ECYFYNGTQR VRLLVRYIYN REEYTRFDSD VGEFRAVTEL GRRDTEYYNK QKEYIERERA AVDTICRHNY EISDRFLVPR TVEPKVTVYP SKTQPLKHHN LLVCSVSDFY PGSVEVRWFR NGEEEKDGLV STGLIPNGDW TFQLLVMLEM VPQGGEVYTC QVEHPSLTSP VRVEWKAQST SAQNKKMSGV GGIVLGLLFL GAGLFVYFRN QKGQSGLQPT GLLN // ID R0JJE7_ANAPL Unreviewed; 190 AA. AC R0JJE7; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=Class II histocompatibility antigen, B-L beta chain {ECO:0000313|EMBL:EOA97141.1}; DE Flags: Fragment; GN ORFNames=Anapl_17424 {ECO:0000313|EMBL:EOA97141.1}; OS Anas platyrhynchos (Mallard) (Anas boschas). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae; OC Anatinae; Anas. OX NCBI_TaxID=8839 {ECO:0000313|EMBL:EOA97141.1}; RN [1] {ECO:0000313|EMBL:EOA97141.1, ECO:0000313|Ensembl:ENSAPLP00000004513} RP NUCLEOTIDE SEQUENCE. RA Li N.; RT "The genome sequence and transcriptome of duck provide insight into RT the interaction host."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAPLP00000004513} RP NUCLEOTIDE SEQUENCE. RX PubMed=23749191; DOI=10.1038/ng.2657; RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., RA Gan S., Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., RA Fairley S., Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., RA Lee T., Kim K.W., Sheng Z., An Y., Searle S., Herrero J., RA Groenen M.A., Crooijmans R.P., Faraut T., Cai Q., Webster R.G., RA Aldridge J.R., Warren W.C., Bartschat S., Kehr S., Marz M., RA Stadler P.F., Smith J., Kraus R.H., Zhao Y., Ren L., Fei J., RA Morisson M., Kaiser P., Griffin D.K., Rao M., Pitel F., Wang J., RA Li N.; RT "The duck genome and transcriptome provide insight into an avian RT influenza virus reservoir species."; RL Nat. Genet. 45:776-783(2013). RN [3] {ECO:0000313|Ensembl:ENSAPLP00000004513} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ADON01111057; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KB743770; EOA97141.1; -; Genomic_DNA. DR Ensembl; ENSAPLT00000005129; ENSAPLP00000004513; ENSAPLG00000004981. DR GeneTree; ENSGT00900000140849; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000016666; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016666}; KW Reference proteome {ECO:0000313|Proteomes:UP000016666}. FT DOMAIN 99 187 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:EOA97141.1}. FT NON_TER 190 190 {ECO:0000313|EMBL:EOA97141.1}. SQ SEQUENCE 190 AA; 22189 MW; 3A9E1D9AB936D07E CRC64; TRPAHTGFLQ EMMVGECQYL NGTERVRYLL RYIYNGQQYA HFDSDVGHYV ADTELGKPDA DYWNSLPEEM AYRRGEVDRY CRHNYEVVTP FTVDRRVEPK VRVSPMQSSS LPQTDRLACY VTGFYPAEIQ VKWFKNGQEE TKHVVSTDVI QNGDWTYQVL VMLESTPQHG DTYECHVQHA SLKSPITHEW // ID R7VQC7_COLLI Unreviewed; 222 AA. AC R7VQC7; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 28-FEB-2018, entry version 24. DE SubName: Full=Class II histocompatibility antigen, B-L beta chain {ECO:0000313|EMBL:EMC81784.1}; DE Flags: Fragment; GN ORFNames=A306_10339 {ECO:0000313|EMBL:EMC81784.1}; OS Columba livia (Rock dove). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba. OX NCBI_TaxID=8932 {ECO:0000313|EMBL:EMC81784.1}; RN [1] {ECO:0000313|EMBL:EMC81784.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Blood {ECO:0000313|EMBL:EMC81784.1}; RX PubMed=23371554; DOI=10.1126/science.1230422; RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M., RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A., RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.; RT "Genomic diversity and evolution of the head crest in the rock RT pigeon."; RL Science 339:1063-1067(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB379702; EMC81784.1; -; Genomic_DNA. DR ProteinModelPortal; R7VQC7; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Membrane {ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 196 217 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 94 182 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:EMC81784.1}. FT NON_TER 222 222 {ECO:0000313|EMBL:EMC81784.1}. SQ SEQUENCE 222 AA; 25347 MW; D8F1152476E0CCF6 CRC64; AGYFQEQLKG DCYFTNGTEQ VRLVTRHIYN REQYVHFDSD VGLYVADTPL GEPTAKYFNS QPDILDQTRA QVDTVCRHNY GVAAPFTVDR KVQPKVRVSP MQSSSLPQTD RLVCYVTGFY PAEIEVKWLK NGQEETEHVV STDVIQNGDW TYQVLVFLET TPQRGETYTC QVEHVSLEHP LTRHWELQSD GARSKMLTGV GGFVLGLIFL ALGLFLYMRK KV // ID R7VTK2_COLLI Unreviewed; 120 AA. AC R7VTK2; DT 24-JUL-2013, integrated into UniProtKB/TrEMBL. DT 24-JUL-2013, sequence version 1. DT 28-FEB-2018, entry version 23. DE SubName: Full=BolA class II histocompatibility antigen, DQB*0101 beta chain {ECO:0000313|EMBL:EMC87810.1, ECO:0000313|EMBL:PKK16940.1}; DE Flags: Fragment; GN ORFNames=A306_00015197 {ECO:0000313|EMBL:PKK16940.1}, GN A306_03437 {ECO:0000313|EMBL:EMC87810.1}; OS Columba livia (Rock dove). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba. OX NCBI_TaxID=8932 {ECO:0000313|EMBL:EMC87810.1}; RN [1] {ECO:0000313|EMBL:EMC87810.1, ECO:0000313|Proteomes:UP000053872} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Blood {ECO:0000313|EMBL:EMC87810.1}; RX PubMed=23371554; DOI=10.1126/science.1230422; RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M., RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A., RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.; RT "Genomic diversity and evolution of the head crest in the rock RT pigeon."; RL Science 339:1063-1067(2013). RN [2] {ECO:0000313|EMBL:PKK16940.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:PKK16940.1}; RA Holt C., Campbell M., Edelman N., Keays D., Kapusta A., Domyan E., RA Suh A., Carleton J., Warren W., Yandell M., Gilbert M.T., RA Shapiro M.D.; RT "Improved genome assembly and annotation for the rock pigeon (Columba RT livia)."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB376878; EMC87810.1; -; Genomic_DNA. DR EMBL; AKCR02000581; PKK16940.1; -; Genomic_DNA. DR RefSeq; XP_005515596.1; XM_005515539.1. DR GeneID; 102098807; -. DR KEGG; clv:102098807; -. DR KO; K06752; -. DR Proteomes; UP000053872; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000053872}; KW Reference proteome {ECO:0000313|Proteomes:UP000053872}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 120 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004458556. FT DOMAIN 39 113 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 120 120 {ECO:0000313|EMBL:EMC87810.1}. SQ SEQUENCE 120 AA; 13235 MW; 0CDA09FB026F8929 CRC64; MATGRVGGAV AVLVALVVLG APPARGQQTS GYFQEQLKGD CYFTNGTEQV RLVTRYIYNR EQYVHFDSDV GLYVADTPLG EPTAKYFNSQ PDILDQTRAQ VDTVCRHNYG VAAPFTVDRK // ID S4SPY7_CHLSB Unreviewed; 261 AA. AC S4SPY7; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 28-MAR-2018, entry version 38. DE SubName: Full=MHC class II DQB protein {ECO:0000313|EMBL:AFP92191.1}; DE SubName: Full=Major histocompatibility complex, class II, DQ beta 1 {ECO:0000313|Ensembl:ENSCSAP00000005645}; GN Name=HLA-DQB1 {ECO:0000313|Ensembl:ENSCSAP00000005645}; OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Chlorocebus. OX NCBI_TaxID=60711 {ECO:0000313|EMBL:AFP92191.1}; RN [1] {ECO:0000313|EMBL:AFP92191.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:AFP92191.1}; RX PubMed=24676686; DOI=10.1007/s00251-014-0770-9; RA Aarnink A., Jacquelin B., Dauba A., Hebrard S., Moureaux E., RA Muller-Trutwin M., Blancher A.; RT "MHC polymorphism in Caribbean African green monkeys."; RL Immunogenetics 66:353-360(2014). RN [2] {ECO:0000313|Ensembl:ENSCSAP00000005645, ECO:0000313|Proteomes:UP000029965} RP NUCLEOTIDE SEQUENCE. RA Warren W., Wilson R.K.; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSCSAP00000005645} RP IDENTIFICATION. RG Ensembl; RL Submitted (APR-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AC241603; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KA650614; AFP92191.1; -; mRNA. DR RefSeq; XP_007971185.1; XM_007972994.1. DR Ensembl; ENSCSAT00000007465; ENSCSAP00000005645; ENSCSAG00000009394. DR GeneID; 103221696; -. DR KEGG; csab:103221696; -. DR CTD; 103221696; -. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000029965; Chromosome 17. DR GO; GO:0005769; C:early endosome; IEA:Ensembl. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0042605; F:peptide antigen binding; IEA:Ensembl. DR GO; GO:1990405; F:protein antigen binding; IEA:Ensembl. DR GO; GO:0015643; F:toxic substance binding; IEA:Ensembl. DR GO; GO:0008134; F:transcription factor binding; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:Ensembl. DR GO; GO:0002344; P:B cell affinity maturation; IEA:Ensembl. DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl. DR GO; GO:0046635; P:positive regulation of alpha-beta T cell activation; IEA:Ensembl. DR GO; GO:0002579; P:positive regulation of antigen processing and presentation; IEA:Ensembl. DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 2: Evidence at transcript level; KW Complete proteome {ECO:0000313|Proteomes:UP000029965}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000029965}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 261 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014108920. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 261 AA; 29861 MW; 7A00C6D154D7EC30 CRC64; MPRKKALRIP GGLWGTTVTL MLAMLSTPVA EGRDSPEDFV YQFKGLCYFT NGTERVRHVT RYIYNREEYA RFDSDVGKYL PVTPLGPPDA EYWNSQKDVL ESTRAELDTV CRHNYQLELR TILQRRVEPT VTISPSRTEA LNHHNLLVCS VTDFYPGQIK VRWFRNDQEE TTGVVSTPLI RNGDWTFQIL VMLEMTPQRG DVYTCHVEHP SLQRPITVEW RAQSESAQSK MLSGVGGFVL GLIFLGLGLI IHHRSQKGLL H // ID S7MIW5_MYOBR Unreviewed; 302 AA. AC S7MIW5; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 22-NOV-2017, entry version 24. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|EMBL:EPQ03931.1}; DE Flags: Fragment; GN ORFNames=D623_10000853 {ECO:0000313|EMBL:EPQ03931.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ03931.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE161455; EPQ03931.1; -; Genomic_DNA. DR ProteinModelPortal; S7MIW5; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR InterPro; IPR016185; PreATP-grasp_dom_sf. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 197 217 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 95 183 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT NON_TER 1 1 {ECO:0000313|EMBL:EPQ03931.1}. SQ SEQUENCE 302 AA; 34757 MW; 622E5BCE0610C906 CRC64; PAEDFLYQYK PRCYYTNGTQ RVRILESVIY NREEYARFDS DVGEYRAVTP LGQRQAEYWN SQKDFMEQKR AELDTVCRHN YPIAEAIALH QRVEPTVTIS PAKTEALNHH NMLVCLVTDF YPAHIKVRWF RNDQEETAGV VSTPLIRNGD WTYQILVMLE MTPQRGDIYT CRVEHPSLQS PLTVEWRAQS GSAQSKMLSG IGGFVLGLIF LGLGLVIRHR KQKDFTPTQI LGEVLIANNG IAAVKCMRSI RRWSYEMFRN ERAIRFVVMV TPEDLKANAD DEQPRDDFGS DKEDGPESST NL // ID S7MJP5_MYOBR Unreviewed; 98 AA. AC S7MJP5; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 05-OCT-2016, entry version 10. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|EMBL:EPQ04569.1}; GN ORFNames=D623_10001657 {ECO:0000313|EMBL:EPQ04569.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ04569.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE161569; EPQ04569.1; -; Genomic_DNA. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}. FT DOMAIN 6 80 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 98 AA; 11597 MW; 4036F9D274E1FB55 CRC64; MLQGKALCYF TNGTQRVRFL VRYIYNREEF VRFDSDVGEF RALTPLGRPD AEYFNSQKDL LERTRAAVDT VCRHNYPLHE AIALHLRVCQ TDRFYESS // ID S7MTM4_MYOBR Unreviewed; 282 AA. AC S7MTM4; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EPQ07824.1}; GN ORFNames=D623_10003256 {ECO:0000313|EMBL:EPQ07824.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07824.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162332; EPQ07824.1; -; Genomic_DNA. DR ProteinModelPortal; S7MTM4; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 282 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004554209. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 282 AA; 31821 MW; 9E012F1E1EE65843 CRC64; MVCLQFPGGS WMAALMVMLM ALSPPLAQAR DTPPHFLYQP KSECHFSNGT EQVRFLERHI YNGQEVLRFD SDVGEFRAVT ELGRPIAEFF NSLEVLLERE RAQVDRFCRD NYRLSEEFLV QRQTEPTVTM YPAKTQHLQH HNLLFCSVNG FYPGHIEVRW LRNGQEEEAG VVSTGLIRNG DWTFQTLVML ETVPRSGEVY TCQVRHPSST SPVTVEWRAQ SGSAQSKVLS GAGGFVLGLL FLGAGLLIYF RAQKGKELLA AKAPRWWGEL GLCWVPLGMA TP // ID S7MTP3_MYOBR Unreviewed; 226 AA. AC S7MTP3; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 21. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EPQ07826.1}; GN ORFNames=D623_10003259 {ECO:0000313|EMBL:EPQ07826.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07826.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162332; EPQ07826.1; -; Genomic_DNA. DR ProteinModelPortal; S7MTP3; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 226 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004543153. FT DOMAIN 115 203 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 226 AA; 25872 MW; 34A1B3768CF18A45 CRC64; MAALMVMLMA LSPPLAQARD TPRHFLEQVK FECHFSNGTE RVRFLERYFY NGQEYLRFDS DVGEYRAVTE LGRLDAEYLN SQEDLMEDER AEVDTLCIYN YVGAEGFLLP RQTEPSVTVY TAKTQRLQHH NLLVCSVNGF YPGHIEVRWL RNGQEEEAGV VSTGLIRNGD WTFQILVMLE TVPRSGEVYT CQVRHPSRTS PVTLEWSEMP SDLPRLTPPT GAFACP // ID S7MWG8_MYOBR Unreviewed; 309 AA. AC S7MWG8; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EPQ07825.1}; GN ORFNames=D623_10003258 {ECO:0000313|EMBL:EPQ07825.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07825.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162332; EPQ07825.1; -; Genomic_DNA. DR ProteinModelPortal; S7MWG8; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00437961}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 309 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004543438. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 309 AA; 34583 MW; CB2559FDC69570A7 CRC64; MVCLRLPGGS WMAALTVMLM ALSPPLARAR NTPPHFLEQV KQECHFSNGT ERVRYLLRYI YNGQDYVLFD SDLGEFQAVT ELGRPEEKGW NSKERELELR RAMVDTYCRH NYMGAEGFLV PRQTEPTVTV YPAKTQRLQH HNLLVCSVNG FYPGHIEVRW LRNGQEEEAG VVSTGLIRNG DWTFQTLVML ETVPRSGEVY TCQLQHPSST SPVTVEWRAQ SGSAQSKVLS GAGGFVLGLL FLGAGLLIYF RAQKGKELLA AEAPRWWGEL GLCWVSSGYG NALEASLSLS VSCSLEIRNN QLPVLRVET // ID S7PC41_MYOBR Unreviewed; 326 AA. AC S7PC41; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EPQ07823.1}; GN ORFNames=D623_10003253 {ECO:0000313|EMBL:EPQ07823.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07823.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162332; EPQ07823.1; -; Genomic_DNA. DR ProteinModelPortal; S7PC41; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 326 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004543575. FT TRANSMEM 248 270 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 326 AA; 35950 MW; 042E785A264BDF77 CRC64; MVCLRFPGGS WVAALTVMLM ALSPPLAQAR DTPPNFLQQV KDECHFSNGT ERVRFLLRYI YNGQEYVRFD SDVGEYRTVT ELGRPFAEYW NSLEGELERA RAAVDMLCRC NYGVSKGFLV QRRTEPTVTV YPAKTQRLQH HNLLVCSVNG FYPGNIEVRW LRNGQEEEAG VVSTGLIRNG DWTFQTLVML ETAPRSGEVY TCQVQHPSRT SPVTVEWSET PSDLTRLPPQ GPLLVPEGAQ SGSAQSKVLS GVGGFLLGLL FLGAGLLIYF RAQKGKEPAG SRGSEMVGGT GALLGELWGG DMRSHGCGGR DGLTRIKIWV QILGYT // ID S7PE57_MYOBR Unreviewed; 284 AA. AC S7PE57; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 21. DE SubName: Full=HLA class II histocompatibility antigen, DM beta chain {ECO:0000313|EMBL:EPQ08788.1}; GN ORFNames=D623_10004236 {ECO:0000313|EMBL:EPQ08788.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ08788.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162539; EPQ08788.1; -; Genomic_DNA. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 284 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004555472. FT TRANSMEM 227 246 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 122 228 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 284 AA; 31043 MW; 2A58CA9D339B4052 CRC64; MPRLPRQIMS TLLRLLLGLS LGCTGAGGFV AHVESTCLLD DDGIPQDFAY CISFNKDLLT CWDPETEAMV PLEFGMLNPL AANLANYLNS QDVLRQRLSV GRQDCATRTQ PFWESLTQRT RPPSVQVAKA TPVNTREPVM LACYVWGFYP ADVTITWRKN GQLVPPHGSA HKVIQSNGDW TYQTLSHLAT TPSFGDTYTC VVEHFGTLEP ILQDWTPGLS PEQTVKVSVS VVTLGLGLII FSLGLLSWRR AGSSGYTVLA GSTYPQGNIC VGLFAFGPFG RGEV // ID S7PEQ1_MYOBR Unreviewed; 271 AA. AC S7PEQ1; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=HLA class II histocompatibility antigen, DQ beta 1 chain {ECO:0000313|EMBL:EPQ08913.1}; GN ORFNames=D623_10001877 {ECO:0000313|EMBL:EPQ08913.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ08913.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162584; EPQ08913.1; -; Genomic_DNA. DR ProteinModelPortal; S7PEQ1; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 271 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004543929. FT TRANSMEM 231 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 271 AA; 30614 MW; 13D533A67DC5AC61 CRC64; MSGKPALWPP GGPWTAAVMV WLVALSVPVA EGGDSPWDFV HQYKFLCYYT NGTQRVRLLE RHIYNREEFA LFDSDVGEYG AVTPLGRPIA EYFNSQKDIL EQKRAELDTV CRHNYPMAEA TDLHQRVEPT VTISPAKTEA LTHHNMLVCS VTDFYPAHIK VRWFRNDQEE TAGVVSTPLI RNGDWTYQVL VMLEMTPQRG DIYTCRVEHS SLQSPLTVEW RAQSGSAQSK MLSGVGGFVL GLIFLGLGPV IRHRKQKADF TPTRILDLSF T // ID S7PFE9_MYOBR Unreviewed; 342 AA. AC S7PFE9; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EPQ06697.1}; GN ORFNames=D623_10000708 {ECO:0000313|EMBL:EPQ06697.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ06697.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162037; EPQ06697.1; -; Genomic_DNA. DR ProteinModelPortal; S7PFE9; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 261 283 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 159 247 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 342 AA; 38392 MW; 0F7B6289157778D1 CRC64; MLGQLVGCLV QPTVYRTPTP TTLGGGPRCW QWGCRGPVFP PPGFPALGRF AIVPHQRDGL FIPVPAAHFL HQVKQECHFS NGTEWVQYLE RHIYEGQETL RFDSDLGEFR ALTELSRPEE KAWNSQKDFL QRKQAKAFWV CRHNYRVSER FLVPQQSEPT VTVYPTKTQR LQHHNLLVCS VNGFYPGHIE VRWLRNGQEE EAGVVSTGLI RNGDWTFQTL VMLETVPRSG EVYTCQVRHP SSTSPVTVEW RAQSGSAQSK VLSGAGGFVL GLLFLGAGLL IYFRAQKGKE LLAAEAPRWW GELGLCWVSS GYGNALEASL SLSVSCSLEI RNNQLPVLRV ET // ID S7PI84_MYOBR Unreviewed; 302 AA. AC S7PI84; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EPQ07822.1}; GN ORFNames=D623_10003252 {ECO:0000313|EMBL:EPQ07822.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07822.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162332; EPQ07822.1; -; Genomic_DNA. DR ProteinModelPortal; S7PI84; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 213 235 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 111 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 302 AA; 33993 MW; 41DEAC7DC3837EAB CRC64; MHCPMNNQNP SQLRIQAAKV KFECHFSNGT ERVRYLARLI YNGQEFVRFD SEVGEYRAVT ELGRPIAEHL NSRKDFMEQM RAAVDRCREA YRVSEGFLVP RQRMEGGDAK PTVTVYPAKT QRLQHHNLLV CSVNGFYPGH IEVRWLHNGQ EEEAGVVSTG LIWNGDWTFQ TLVMLETVPR SGEVYTCQVR HPSRTSPVTV EWRAQSGSTQ SKVLSGAGGF VLGLLFLGTG LLTYFRAQKG KEPAGSLGPN LVGTTVALLG ELWVWQLHRS LSFPVGLTCP GNAEITSSRF LGWRHEESWL WG // ID S7PI89_MYOBR Unreviewed; 313 AA. AC S7PI89; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 20. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EPQ07827.1}; GN ORFNames=D623_10003260 {ECO:0000313|EMBL:EPQ07827.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ07827.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162332; EPQ07827.1; -; Genomic_DNA. DR ProteinModelPortal; S7PI89; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 2. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 2. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 2. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 313 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004543608. FT TRANSMEM 275 297 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 173 261 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 313 AA; 35368 MW; 5D2AF73E6E899EC0 CRC64; MVCLRVPRGS WMAALKVMLM ALSPPLAQAR DTPWHFLVQR KSECHFSNGT ERVRYLERYI YNGQEDVRFD SDVGAPPPGS SHFLHQLIQE CHFSNGTERV QYLYRFFYNG QEDVRFDSNV GEFSAVTELG RPIAEHWNSQ EGLLEEKRGY VVTLCRHNYV EFERFLVHRQ TEPTVTLYPA KTQRLQHHNL LVCSVNGFYP GHIEVHWLRN GQEEEAGVVS TGLIRRNGGT FQTLVMLETV PRSGEVYTCQ VRHPSSTSPV TVEWRAQSGS AQSKVLSGAG GFVLGLLFLG AGLLIYFRAQ KGHSGLQPTG NAL // ID S7PL01_MYOBR Unreviewed; 279 AA. AC S7PL01; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|EMBL:EPQ08792.1}; GN ORFNames=D623_10004242 {ECO:0000313|EMBL:EPQ08792.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ08792.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE162539; EPQ08792.1; -; Genomic_DNA. DR ProteinModelPortal; S7PL01; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 279 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004543626. FT TRANSMEM 226 248 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 124 212 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 279 AA; 31108 MW; 2DF8FC764BBEF2D0 CRC64; MVAPQAAGAP CMAALLMPLV MLSFPWAQGK DTPAVHVYQR RSDCYESNGT HRFLERYVYN RDVFVQFDST VGVFVAVTEL GRTTARNWNI QREFLELRRG AVDAVCRHNY ELDRAFTLER RVQPKVNVSP SKKGPLQHPD LLVCHVTDFY PGHVQVRWFL NGQEETAGVV STNLIHNGDW TFQILVMLEM TPQQGDVYTC RVEHPSLDSA VTVEWKAQSD SARSKMLTGV GGFVLGLLAL AVSVTLHFRG QRGWAESGEG SVVAKEGGFL GGRDLSRAR // ID S7QH54_MYOBR Unreviewed; 294 AA. AC S7QH54; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=BoLa class II histocompatibility antigen, DQB*0101 beta chain {ECO:0000313|EMBL:EPQ20847.1}; GN ORFNames=D623_10000754 {ECO:0000313|EMBL:EPQ20847.1}; OS Myotis brandtii (Brandt's bat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; OC Vespertilionidae; Myotis. OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ20847.1, ECO:0000313|Proteomes:UP000052978}; RN [1] {ECO:0000313|Proteomes:UP000052978} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=23962925; DOI=10.1038/ncomms3212; RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y., RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., RA Hee Yim S., Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., RA Chen G., Kulakova O.I., Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., RA Sunyaev S.R., Zhang G., Krogh A., Wang J., Gladyshev V.N.; RT "Genome analysis reveals insights into physiology and longevity of the RT Brandt's bat Myotis brandtii."; RL Nat. Commun. 4:2212-2212(2013). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KE331141; EPQ20847.1; -; Genomic_DNA. DR ProteinModelPortal; S7QH54; -. DR Proteomes; UP000052978; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000052978}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000052978}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 32 {ECO:0000256|SAM:SignalP}. FT CHAIN 33 294 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004556355. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 294 AA; 33219 MW; 87985D050AD9E8CA CRC64; MSGKPALWPP GGPWTAAVMV WLVALRAPVA EGGSSPRDFV LQYKALCYFT NGTQRVRLLT SYIYNLEEYA RFDSEVGEYR ALTPLGRPTV EYFNSQKDIL EETRAEVDTV CRPNYQSEAS TTLQRRVEPT VTISPAKTEA LNHHNMLVCL VTDFYPAHIK VRWFRNDQEE TAGVVSTPLI RNGDWTYQVL VMLEMTPQRG DVYTCRVEHP SLQSPLTVEW RKGQFLSCTL VPTDRGQTAA PGCPITSLPV MSLLSGHHRM LGLFISWQGH QKIPDIMVFP DTREVTLHHS QNPA // ID S9X155_CAMFR Unreviewed; 264 AA. AC S9X155; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 21. DE SubName: Full=HLA class II histocompatibility antigen, DP beta 1 chain {ECO:0000313|EMBL:EPY84287.1}; GN ORFNames=CB1_000487050 {ECO:0000313|EMBL:EPY84287.1}; OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda; OC Camelidae; Camelus. OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY84287.1, ECO:0000313|Proteomes:UP000030684}; RN [1] {ECO:0000313|EMBL:EPY84287.1, ECO:0000313|Proteomes:UP000030684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684}; RX PubMed=23149746; RG Bactrian Camels Genome Sequencing and Analysis Consortium; RA Jirimutu null, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., RA Wang L., Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., RA Zhang W., Batmunkh M., Ts B., Narenbatu null, Unierhu null, RA Bat-Ireedui S., Gao H., Baysgalan B., Li Q., Jia Z., RA Turigenbayila null, Subudenggerile null, Narenmanduhu null, Wang Z., RA Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt null, Erdemt null, RA Altansha null, Altansukh null, Liu T., Cao M., Aruuntsever null, RA Bayart null, Hosblig null, He F., Zha-ti A., Zheng G., Qiu F., Sun Z., RA Zhao L., Zhao W., Liu B., Li C., Chen Y., Tang X., Guo C., Liu W., RA Ming L., Temuulen null, Cui A., Li Y., Gao J., Li J., Wurentaodi null, RA Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T., Bayaer T., RA Li Y., Meng H.; RT "Genome sequences of wild and domestic bactrian camels."; RL Nat. Commun. 3:1202-1202(2012). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB016771; EPY84287.1; -; Genomic_DNA. DR ProteinModelPortal; S9X155; -. DR Proteomes; UP000030684; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030684}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000030684}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 264 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004572911. FT DOMAIN 172 260 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 30146 MW; 515892D6A51EB04D CRC64; MAVFWVTGAP GMAALMKSLA MLSFPLAQGR DTPGTRSEHI RVNTELDKGG SAVEPVSTDE RRNGDAWVLE GWKGLWAQEI AELYVYQRRS DCYEFNGTHR YLERYIYNRE VYVQFDSAVG VFVAVTELGR QTAKNWNIQR EFLELRQSAV DTVCRHNYEL DKGFTLKRTV PPKVNVSPSK KEALQPHSLL ICHVTDFYPG HIQVRWFLNG QEETAGVVAT NPIHNGDWTF QLLVMLEMSP QQGDVYTCHV EHPSLDRPVT VEWT // ID S9X159_CAMFR Unreviewed; 254 AA. AC S9X159; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=Major histocompatibility complex, class II, DM beta {ECO:0000313|EMBL:EPY84292.1}; GN ORFNames=CB1_000487055 {ECO:0000313|EMBL:EPY84292.1}; OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda; OC Camelidae; Camelus. OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY84292.1, ECO:0000313|Proteomes:UP000030684}; RN [1] {ECO:0000313|EMBL:EPY84292.1, ECO:0000313|Proteomes:UP000030684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684}; RX PubMed=23149746; RG Bactrian Camels Genome Sequencing and Analysis Consortium; RA Jirimutu null, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., RA Wang L., Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., RA Zhang W., Batmunkh M., Ts B., Narenbatu null, Unierhu null, RA Bat-Ireedui S., Gao H., Baysgalan B., Li Q., Jia Z., RA Turigenbayila null, Subudenggerile null, Narenmanduhu null, Wang Z., RA Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt null, Erdemt null, RA Altansha null, Altansukh null, Liu T., Cao M., Aruuntsever null, RA Bayart null, Hosblig null, He F., Zha-ti A., Zheng G., Qiu F., Sun Z., RA Zhao L., Zhao W., Liu B., Li C., Chen Y., Tang X., Guo C., Liu W., RA Ming L., Temuulen null, Cui A., Li Y., Gao J., Li J., Wurentaodi null, RA Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T., Bayaer T., RA Li Y., Meng H.; RT "Genome sequences of wild and domestic bactrian camels."; RL Nat. Commun. 3:1202-1202(2012). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB016771; EPY84292.1; -; Genomic_DNA. DR ProteinModelPortal; S9X159; -. DR Proteomes; UP000030684; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030684}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000030684}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 254 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004559471. FT DOMAIN 114 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 254 AA; 28259 MW; 434C2918A23C68C7 CRC64; MTSLLPLLLG LSLGCTGAGG FVAHVESSCL LDDDGTPKEF KYCISFNKDL LTCWDPLQAN MVPCEFGVLY GLAKYLSDFL NRNENLIQRL SNGLQDCATH TQPFWKSLTH RTRPPSVQVA KTTPFNTRES VMLACYVWDF YPADVIITWR KNGQPILPHS SAQNIAQPNG DWTYQTVSHL ATTPSFGDTY TCVVEHIGSP EPILQGWNSE GFCVSSDSGP GAHHLLSRFA QLAESCLLWS AHFLEVEFYS FHSM // ID S9X163_CAMFR Unreviewed; 374 AA. AC S9X163; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 22. DE SubName: Full=HLA class II histocompatibility antigen, DO beta chain-like protein {ECO:0000313|EMBL:EPY84297.1}; GN ORFNames=CB1_000487060 {ECO:0000313|EMBL:EPY84297.1}; OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda; OC Camelidae; Camelus. OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY84297.1, ECO:0000313|Proteomes:UP000030684}; RN [1] {ECO:0000313|EMBL:EPY84297.1, ECO:0000313|Proteomes:UP000030684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684}; RX PubMed=23149746; RG Bactrian Camels Genome Sequencing and Analysis Consortium; RA Jirimutu null, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., RA Wang L., Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., RA Zhang W., Batmunkh M., Ts B., Narenbatu null, Unierhu null, RA Bat-Ireedui S., Gao H., Baysgalan B., Li Q., Jia Z., RA Turigenbayila null, Subudenggerile null, Narenmanduhu null, Wang Z., RA Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt null, Erdemt null, RA Altansha null, Altansukh null, Liu T., Cao M., Aruuntsever null, RA Bayart null, Hosblig null, He F., Zha-ti A., Zheng G., Qiu F., Sun Z., RA Zhao L., Zhao W., Liu B., Li C., Chen Y., Tang X., Guo C., Liu W., RA Ming L., Temuulen null, Cui A., Li Y., Gao J., Li J., Wurentaodi null, RA Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T., Bayaer T., RA Li Y., Meng H.; RT "Genome sequences of wild and domestic bactrian camels."; RL Nat. Commun. 3:1202-1202(2012). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB016771; EPY84297.1; -; Genomic_DNA. DR ProteinModelPortal; S9X163; -. DR Proteomes; UP000030684; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 2. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 2. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 2. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 2. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030684}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000030684}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 249 271 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 299 316 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 147 235 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 374 AA; 42560 MW; 06A34BF084D94772 CRC64; MTPSSSILIG YQCEELPILG RPERMSSRWV PWVVALSVNV IWPDSSMIRG RDSPEDFVIQ AKADCYFTNG TEKVQFVVRF IFNLEEYARF DSDVGMFVAL TELGRPDAEL WNNRSDILER SRASVDLVCR RNYELGAPFT VGRRVQPEVT VYPERTPSLQ HHSLLLCSVT GFYPGDITIR WFRNGREERE GVMPTGLIRN GDWTFQTMVM LEMIPELGDV YTCLVDHPSL LSPVSVEWRA QSEYSWGKML SGVAAFLVGL IFLLVGITVH VRARKGYVET QLSGDKGGRM RVTISRNPWT AAGIVMVVFM VLRTSMAHGR GAPKNFVYQF KSMCYFTNGT EHVKLVVRQI YNKEEILHFD SDLDEFVAVS ELGR // ID S9X7V2_CAMFR Unreviewed; 368 AA. AC S9X7V2; DT 16-OCT-2013, integrated into UniProtKB/TrEMBL. DT 16-OCT-2013, sequence version 1. DT 25-OCT-2017, entry version 21. DE SubName: Full=DLA class II histocompatibility antigen, DR-1 beta chain {ECO:0000313|EMBL:EPY84303.1}; GN ORFNames=CB1_000487067 {ECO:0000313|EMBL:EPY84303.1}; OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Tylopoda; OC Camelidae; Camelus. OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY84303.1, ECO:0000313|Proteomes:UP000030684}; RN [1] {ECO:0000313|EMBL:EPY84303.1, ECO:0000313|Proteomes:UP000030684} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684}; RX PubMed=23149746; RG Bactrian Camels Genome Sequencing and Analysis Consortium; RA Jirimutu null, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., RA Wang L., Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., RA Zhang W., Batmunkh M., Ts B., Narenbatu null, Unierhu null, RA Bat-Ireedui S., Gao H., Baysgalan B., Li Q., Jia Z., RA Turigenbayila null, Subudenggerile null, Narenmanduhu null, Wang Z., RA Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt null, Erdemt null, RA Altansha null, Altansukh null, Liu T., Cao M., Aruuntsever null, RA Bayart null, Hosblig null, He F., Zha-ti A., Zheng G., Qiu F., Sun Z., RA Zhao L., Zhao W., Liu B., Li C., Chen Y., Tang X., Guo C., Liu W., RA Ming L., Temuulen null, Cui A., Li Y., Gao J., Li J., Wurentaodi null, RA Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T., Bayaer T., RA Li Y., Meng H.; RT "Genome sequences of wild and domestic bactrian camels."; RL Nat. Commun. 3:1202-1202(2012). CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; KB016771; EPY84303.1; -; Genomic_DNA. DR ProteinModelPortal; S9X7V2; -. DR Proteomes; UP000030684; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 2. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 2. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 2. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 2. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 2. DR PROSITE; PS00290; IG_MHC; 2. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000030684}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000030684}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 368 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004573012. FT TRANSMEM 138 160 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 36 124 Ig-like. {ECO:0000259|PROSITE:PS50835}. FT DOMAIN 257 345 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 368 AA; 41828 MW; AAD51033F162AF6C CRC64; MVCLYFSGGS WMAALTVILM VLSPSLVWTK DTQLEPTVTV YPVKPQPLQH HNLLVCSVTG FYPGHIEVRW FRNGQEEEAG VVSTGLIPNG DWTFQTMVML ETVPQSGEVY TCRVEHPSWT RPVTVEWRAQ SESAQSKMLS GIGGFVLGLL FLGVGLFIYF RNQKATFMHQ FKGECRFFNG LERVQFLARY IYNTEEDVYF DSDVGEFRAV TELGQPDAKY WNQQKDFMEQ MRAKVDTLCR SNYWGIGSFM VQRRVEPTVT VYPAKPQPLQ HHSLLVCSVT GFYPGHIEVR WFRNGQEEEA GVVSTGLIPN GDWTFQTMVM LETVPQSGEV YTCRVEHPSW TGPVTVEWSE KLCDLMHSSP PEEGLASS // ID U3I327_ANAPL Unreviewed; 75 AA. AC U3I327; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 28-MAR-2018, entry version 22. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAPLP00000001647}; OS Anas platyrhynchos (Mallard) (Anas boschas). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae; OC Anatinae; Anas. OX NCBI_TaxID=8839 {ECO:0000313|Ensembl:ENSAPLP00000001647, ECO:0000313|Proteomes:UP000016666}; RN [1] {ECO:0000313|Ensembl:ENSAPLP00000001647} RP NUCLEOTIDE SEQUENCE. RA Li N.; RT "The genome sequence and transcriptome of duck provide insight into RT the interaction host."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAPLP00000001647} RP NUCLEOTIDE SEQUENCE. RX PubMed=23749191; DOI=10.1038/ng.2657; RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., RA Gan S., Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., RA Fairley S., Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., RA Lee T., Kim K.W., Sheng Z., An Y., Searle S., Herrero J., RA Groenen M.A., Crooijmans R.P., Faraut T., Cai Q., Webster R.G., RA Aldridge J.R., Warren W.C., Bartschat S., Kehr S., Marz M., RA Stadler P.F., Smith J., Kraus R.H., Zhao Y., Ren L., Fei J., RA Morisson M., Kaiser P., Griffin D.K., Rao M., Pitel F., Wang J., RA Li N.; RT "The duck genome and transcriptome provide insight into an avian RT influenza virus reservoir species."; RL Nat. Genet. 45:776-783(2013). RN [3] {ECO:0000313|Ensembl:ENSAPLP00000001647} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ADON01139191; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSAPLT00000002221; ENSAPLP00000001647; ENSAPLG00000002224. DR GeneTree; ENSGT00900000140849; -. DR OMA; WRDECHY; -. DR OrthoDB; EOG090D0AY2; -. DR Proteomes; UP000016666; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016666}; KW Reference proteome {ECO:0000313|Proteomes:UP000016666}. FT DOMAIN 5 75 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 75 AA; 9069 MW; 00281696AB37515F CRC64; YLTVDECHYL NGTERVRYLY RDIYNQQQNA HFDSNVGHFV ADMELGKPIA DDWNNQPKIM EDMRARVDTF CRYNY // ID U3IBD7_ANAPL Unreviewed; 277 AA. AC U3IBD7; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 20-JUN-2018, entry version 31. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAPLP00000004559}; GN Name=LOC101789604 {ECO:0000313|Ensembl:ENSAPLP00000004559}; OS Anas platyrhynchos (Mallard) (Anas boschas). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae; OC Anatinae; Anas. OX NCBI_TaxID=8839 {ECO:0000313|Ensembl:ENSAPLP00000004559, ECO:0000313|Proteomes:UP000016666}; RN [1] {ECO:0000313|Ensembl:ENSAPLP00000004559} RP NUCLEOTIDE SEQUENCE. RA Li N.; RT "The genome sequence and transcriptome of duck provide insight into RT the interaction host."; RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAPLP00000004559} RP NUCLEOTIDE SEQUENCE. RX PubMed=23749191; DOI=10.1038/ng.2657; RA Huang Y., Li Y., Burt D.W., Chen H., Zhang Y., Qian W., Kim H., RA Gan S., Zhao Y., Li J., Yi K., Feng H., Zhu P., Li B., Liu Q., RA Fairley S., Magor K.E., Du Z., Hu X., Goodman L., Tafer H., Vignal A., RA Lee T., Kim K.W., Sheng Z., An Y., Searle S., Herrero J., RA Groenen M.A., Crooijmans R.P., Faraut T., Cai Q., Webster R.G., RA Aldridge J.R., Warren W.C., Bartschat S., Kehr S., Marz M., RA Stadler P.F., Smith J., Kraus R.H., Zhao Y., Ren L., Fei J., RA Morisson M., Kaiser P., Griffin D.K., Rao M., Pitel F., Wang J., RA Li N.; RT "The duck genome and transcriptome provide insight into an avian RT influenza virus reservoir species."; RL Nat. Genet. 45:776-783(2013). RN [3] {ECO:0000313|Ensembl:ENSAPLP00000004559} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; ADON01111059; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; ADON01111060; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSAPLT00000005175; ENSAPLP00000004559; ENSAPLG00000005009. DR GeneTree; ENSGT00900000140849; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000016666; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016666}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000016666}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 277 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004643414. FT TRANSMEM 230 252 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 128 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 277 AA; 30875 MW; 5E4264DE59FBF7B7 CRC64; MGSGRILGAG AVLVALVVLG ARPAGGEETK GFFQFLGTCE CHYLNGTERV RYLDTYIYNR QQYAHFDSDV GHYVADTELG KPDADYWNSQ PEILEYQRGS VDRFCRHNYE VSDTYILHTF TVDRRVEPKV RVSPMQSSSL PQTDRLACYV TGFYPAEIQV KWFKNGQEET KHVVSTDVIQ NGDWTYQVLV MLESTPQHGD TYECHVQHAS LKSPIIHEWV LPADAARGKM LTGVGGLVLG LIFLALGLFL YVRRKVSGRG AGGGVGLGVR ALPPRCR // ID U3JEU4_FICAL Unreviewed; 187 AA. AC U3JEU4; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 23-MAY-2018, entry version 28. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000001298}; GN Name=LOC101818035 {ECO:0000313|Ensembl:ENSFALP00000001298}; OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; OC Ficedula. OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000001298, ECO:0000313|Proteomes:UP000016665}; RN [1] {ECO:0000313|Ensembl:ENSFALP00000001298} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTO01003426; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; U3JEU4; -. DR Ensembl; ENSFALT00000001305; ENSFALP00000001298; ENSFALG00000001248. DR GeneTree; ENSGT00900000140849; -. DR OMA; VWISAGC; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000016665; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016665}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000016665}. FT DOMAIN 88 176 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 187 AA; 21554 MW; 14E65AA8BC2F3B41 CRC64; INGTEKVRFV ERYIYNRMEH VRFDSDVGRF EGFTPFGECN ARHWNSDPEW MENRRTAVDW FCRDWYEPDA PFSGGIVTPF SVERRVPPSV SISLMPSSSQ PGPDRLLCSV MDFYPAQIQV RWLQGQQELS EHVVATDVVA NGDWTYQLLV LLETPPRRGL SYTCQVEHVS LEQPLRQRWG TGEALGG // ID U3JU63_FICAL Unreviewed; 278 AA. AC U3JU63; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 23-MAY-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000006317}; OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; OC Ficedula. OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000006317, ECO:0000313|Proteomes:UP000016665}; RN [1] {ECO:0000313|Ensembl:ENSFALP00000006317} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTO01002147; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSFALT00000006346; ENSFALP00000006317; ENSFALG00000006042. DR GeneTree; ENSGT00900000140849; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000016665; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016665}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000016665}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 27 {ECO:0000256|SAM:SignalP}. FT CHAIN 28 278 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004644908. FT TRANSMEM 227 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 278 AA; 30952 MW; 7EFBAE3E5E674F3E CRC64; LAMGRVAAAG AGLVALVVLG APRGAGAELS DTGVFQFKGW VECHFSNGTE KVRLVQKYIY NREEYLRYDA DVGRYEGFNP YGEWNARRFN SNPKWMQYIP SRVDLYCTHS YGCYTPFLVE RQVLPSVSIS LMPSSSQPGP GRLLCSVMDF YPAQIQVRWF QGQQELSEHV VATDVVANGD WTYQLLVLLE TPPRRGLSYT CQVEHVSLEQ PLRQRWEMPP DAARSKMLTG IGGFVLGSVF LALGLGFYVC KKVRVGGGAG DRVPPVPERV RSPRGPQP // ID U3JYJ4_FICAL Unreviewed; 247 AA. AC U3JYJ4; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 23-MAY-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000007848}; OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; OC Ficedula. OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000007848, ECO:0000313|Proteomes:UP000016665}; RN [1] {ECO:0000313|Ensembl:ENSFALP00000007848} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTO01022649; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSFALT00000007881; ENSFALP00000007848; ENSFALG00000007520. DR GeneTree; ENSGT00900000140849; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000016665; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016665}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000016665}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 247 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004645043. FT TRANSMEM 220 242 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 35 108 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT DOMAIN 136 204 IGc1. {ECO:0000259|SMART:SM00407}. SQ SEQUENCE 247 AA; 27652 MW; 3595B5BFA599F253 CRC64; MGRVVAAGAL LVLGAPQAGG TELSDTGLFQ EVVKSEGHFI NGTDCVRLVE RNISNREQFL HFGSDVGLYV GTRPGDKVAR YWNSDPEWME HRWAAENRHC WHNQELSSPF LVERRVPPSV SISLWPSSSQ PSPHRLCSVM DFYPGHIQLR WFQGQQELSG HVVAPDLVPN GDWFLSSSWC CWKLLPQCRV TSSCQVEHVS LEHPLSWHWE VLLDAARRKV LMGIGGSVLG LVSLALGLGF YLGKKVR // ID U3K034_FICAL Unreviewed; 182 AA. AC U3K034; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 23-MAY-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000008388}; OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; OC Ficedula. OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000008388, ECO:0000313|Proteomes:UP000016665}; RN [1] {ECO:0000313|Ensembl:ENSFALP00000008388} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTO01012867; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; U3K034; -. DR Ensembl; ENSFALT00000008426; ENSFALP00000008388; ENSFALG00000008046. DR GeneTree; ENSGT00900000140849; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000016665; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016665}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000016665}. FT DOMAIN 91 179 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 182 AA; 20941 MW; 38AEAFE0E184D4EF CRC64; MDCSLQELST SECHFLNGTE KVRLVERHIY NRVEDVRFDS DIGAHVGLGE KCARWNSDPD IMEYKRALVD TFCRHNYEIV TPFAVETRVP PSVSISLMPS SSQPGPDRLL CSVMDFYPAQ IQVRWFQGQQ ELSEHVVATD VVANGDWTYQ LLVLLETPPR RGLSYTCQVE HVSLEQPLRQ RW // ID U3K042_FICAL Unreviewed; 212 AA. AC U3K042; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 23-MAY-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000008396}; OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; OC Ficedula. OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000008396, ECO:0000313|Proteomes:UP000016665}; RN [1] {ECO:0000313|Ensembl:ENSFALP00000008396} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTO01012867; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; U3K042; -. DR Ensembl; ENSFALT00000008434; ENSFALP00000008396; ENSFALG00000008052. DR GeneTree; ENSGT00900000140849; -. DR OMA; ICQVEHT; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000016665; Unplaced. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016665}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Reference proteome {ECO:0000313|Proteomes:UP000016665}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 25 {ECO:0000256|SAM:SignalP}. FT CHAIN 26 212 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004645075. FT DOMAIN 121 209 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 212 AA; 23998 MW; ED12E9DC6E11088B CRC64; MGRGAAAGAV LVALVVLGAP PGAGAELSAV FQWMAKAECH FINGTEKVRF LERSFYNRFE YARFDSDVGR YEGFTPFGER NAGRWNSDPE FLEQRKAAVD TYCRYNYRVS TPFLVERRVP PSVSISLMPS SSQPGPDRLL CSVMDFYPAQ IQVRWLQGQQ ELSEHVVATD VVANGDWTYQ LLVLLETPPR RGLSYTCQVE HVSLEQPLRQ RW // ID U3KGX1_FICAL Unreviewed; 264 AA. AC U3KGX1; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 23-MAY-2018, entry version 30. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSFALP00000014275}; OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; OC Ficedula. OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000014275, ECO:0000313|Proteomes:UP000016665}; RN [1] {ECO:0000313|Ensembl:ENSFALP00000014275} RP IDENTIFICATION. RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AGTO01021489; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; U3KGX1; -. DR Ensembl; ENSFALT00000014334; ENSFALP00000014275; ENSFALG00000013677. DR GeneTree; ENSGT00900000140849; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000016665; Unplaced. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000016665}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000016665}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 33 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 233 255 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 131 219 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 264 AA; 30110 MW; C5729372C3941D81 CRC64; LRTCPALAME RVAAAGAVLV PLVVLGVFLA AGAELSETEV FQEMVKSECH FINGTSRVRF VKRFVYNREQ YVHFDSDVGH FVGDSPYGEK VARYWNRDPE WMEYRRDAVD RHCRHNYELS SPFLVERRVP PSVSISLVPS SSQSGPGRLL CSVMDFYPAE IQVRWFQGQQ ELSEHVVATD VVPNGDLTYQ VLVLLETPPR RRVSYTCQVE HVSLEHPLRR QWEMQLNATR SKVLMGIGGS VLGFVFFALC LGFYLHKSLL RFVP // ID U3KMS9_RABIT Unreviewed; 255 AA. AC U3KMS9; DT 13-NOV-2013, integrated into UniProtKB/TrEMBL. DT 13-NOV-2013, sequence version 1. DT 12-SEP-2018, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOCUP00000026538}; OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; OC Oryctolagus. OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000026538, ECO:0000313|Proteomes:UP000001811}; RN [1] {ECO:0000313|Ensembl:ENSOCUP00000026538, ECO:0000313|Proteomes:UP000001811} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811}; RX PubMed=21993624; DOI=10.1038/nature10530; RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., RA Washietl S., Kheradpour P., Ernst J., Jordan G., Mauceli E., RA Ward L.D., Lowe C.B., Holloway A.K., Clamp M., Gnerre S., Alfoldi J., RA Beal K., Chang J., Clawson H., Cuff J., Di Palma F., Fitzgerald S., RA Flicek P., Guttman M., Hubisz M.J., Jaffe D.B., Jungreis I., RA Kent W.J., Kostka D., Lara M., Martins A.L., Massingham T., Moltke I., RA Raney B.J., Rasmussen M.D., Robinson J., Stark A., Vilella A.J., RA Wen J., Xie X., Zody M.C., Baldwin J., Bloom T., Chin C.W., Heiman D., RA Nicol R., Nusbaum C., Young S., Wilkinson J., Worley K.C., Kovar C.L., RA Muzny D.M., Gibbs R.A., Cree A., Dihn H.H., Fowler G., Jhangiani S., RA Joshi V., Lee S., Lewis L.R., Nazareth L.V., Okwuonu G., RA Santibanez J., Warren W.C., Mardis E.R., Weinstock G.M., Wilson R.K., RA Delehaunty K., Dooling D., Fronik C., Fulton L., Fulton B., Graves T., RA Minx P., Sodergren E., Birney E., Margulies E.H., Herrero J., RA Green E.D., Haussler D., Siepel A., Goldman N., Pollard K.S., RA Pedersen J.S., Lander E.S., Kellis M.; RT "A high-resolution map of human evolutionary constraint using 29 RT mammals."; RL Nature 478:476-482(2011). RN [2] {ECO:0000313|Ensembl:ENSOCUP00000026538} RP IDENTIFICATION. RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000026538}; RG Ensembl; RL Submitted (SEP-2013) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AAGW02017726; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; U3KMS9; -. DR Ensembl; ENSOCUT00000033491; ENSOCUP00000026538; ENSOCUG00000029731. DR GeneTree; ENSGT00900000140849; -. DR OMA; GQVDNYC; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000001811; Chromosome 12. DR Bgee; ENSOCUG00000029731; Expressed in 3 organ(s), highest expression level in adult mammalian kidney. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000001811}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000001811}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 255 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004645838. FT TRANSMEM 229 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 214 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 255 AA; 29178 MW; A2B5ACCB033D7AFB CRC64; MLCLWLLRSS CLAALTVTLL VLRSPLSLAR DTRPRFMQQV KHECHFSNGM QRVRFLDGHL YNREEYVRFD SDVGEYRAVT ELGRLDAEYW NSQTDRLDYK RGQVDTYCRY NYGVVDSFLV QRRVVPKVTV YPAKTQPLQH HNLLVCAVSG FYPGHIEVRW FRNGEEEEAG VVSTGLICNG DWTFQTLVML ETVPQSGEVY TCQVEHPSVT SPITVEWRVQ SESAHSKQLS GIGGVVLGLF FLGVGLFIYC RTQKV // ID V8N0N7_OPHHA Unreviewed; 85 AA. AC V8N0N7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE55874.1}; DE Flags: Fragment; GN ORFNames=L345_18417 {ECO:0000313|EMBL:ETE55874.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE55874.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE55874.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE55874.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE55874.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01076128; ETE55874.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 1 71 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE55874.1}. FT NON_TER 85 85 {ECO:0000313|EMBL:ETE55874.1}. SQ SEQUENCE 85 AA; 10317 MW; F203A48B9BEFE644 CRC64; FLNGTQRVRF LDRSFYDRQE IDYFDSDLGK FVAVTPLAQL DVDKWNGDEQ WLQYQKAGVD RFCRRNYEIV SYEAPKREER MIGRR // ID V8N0S1_OPHHA Unreviewed; 118 AA. AC V8N0S1; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE55800.1}; DE Flags: Fragment; GN ORFNames=L345_18491 {ECO:0000313|EMBL:ETE55800.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE55800.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE55800.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE55800.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE55800.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01099705; ETE55800.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 118 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004771367. FT DOMAIN 31 105 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE55800.1}. FT NON_TER 118 118 {ECO:0000313|EMBL:ETE55800.1}. SQ SEQUENCE 118 AA; 14287 MW; 2747BD84A0EEBA44 CRC64; GRERWALESL LTAFLLLLLP LAAHFLYQAK HECLFFNGTQ WVRFLLRYIY DRQDFLRFDR DLRKFLALTA LGEASAEKLN GDEHWLQYYK ASVDHFCRYN YEVYKFKAAK REERLIGR // ID V8N171_OPHHA Unreviewed; 86 AA. AC V8N171; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56004.1}; DE Flags: Fragment; GN ORFNames=L345_18287 {ECO:0000313|EMBL:ETE56004.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56004.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56004.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56004.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56004.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01052873; ETE56004.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 25 86 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56004.1}. FT NON_TER 86 86 {ECO:0000313|EMBL:ETE56004.1}. SQ SEQUENCE 86 AA; 9759 MW; 777CC10219C77033 CRC64; MGLGVPPDGL PPPPPPAHFL FQHKAECHLL NGTQQVRFLE RQFYNRQEFA RFDSNLGKYV ALTALGEEAA DYWNGDEQLL QYQKAA // ID V8N1L7_OPHHA Unreviewed; 91 AA. AC V8N1L7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56169.1}; DE Flags: Fragment; GN ORFNames=L345_18120 {ECO:0000313|EMBL:ETE56169.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56169.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56169.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56169.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56169.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01037034; ETE56169.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 3 77 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56169.1}. FT NON_TER 91 91 {ECO:0000313|EMBL:ETE56169.1}. SQ SEQUENCE 91 AA; 11000 MW; F6D89836E40FF76A CRC64; MKQECRFLNG TQRVRFLERQ FYDRQEIVRF DSDLGKFVAV TALGEAKADD WNRNKQWLQY KKASVDRFCR CNYEALNFKA AKREERVVGR R // ID V8N2D2_OPHHA Unreviewed; 114 AA. AC V8N2D2; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56315.1}; DE Flags: Fragment; GN ORFNames=L345_17974 {ECO:0000313|EMBL:ETE56315.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56315.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56315.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56315.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56315.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01028023; ETE56315.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 26 100 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56315.1}. FT NON_TER 114 114 {ECO:0000313|EMBL:ETE56315.1}. SQ SEQUENCE 114 AA; 13600 MW; 097FE3543040DE29 CRC64; MSSLCASPYS PPPKGRETHF LFQRKAECCF VNGTQRVRFL DRNIYDQQEF LHFDSDLGKF VAVTEFGKVD ADKLNGDKQW LQIMRAQVDR FCRHNYEAFN FREAKREERI ICRR // ID V8N2G1_OPHHA Unreviewed; 103 AA. AC V8N2G1; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56449.1}; DE Flags: Fragment; GN ORFNames=L345_17840 {ECO:0000313|EMBL:ETE56449.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56449.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56449.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56449.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56449.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01021813; ETE56449.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 17 {ECO:0000256|SAM:SignalP}. FT CHAIN 18 103 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004771375. FT DOMAIN 15 89 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56449.1}. FT NON_TER 103 103 {ECO:0000313|EMBL:ETE56449.1}. SQ SEQUENCE 103 AA; 12010 MW; 5F7EDF615A9F2FBD CRC64; MALLLAAHFL IQAKTECHFL NGTQRVRFLV WYIYDRQEFV CFDSDLGKNV AVMALGEGDA DKWNGDEQIL QNQKAQVDRL CRRNYLLGSY EAAKREERLI GRR // ID V8N2P9_OPHHA Unreviewed; 101 AA. AC V8N2P9; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 12. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56171.1}; DE Flags: Fragment; GN ORFNames=L345_18118 {ECO:0000313|EMBL:ETE56171.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56171.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56171.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56171.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56171.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01036901; ETE56171.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 101 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004770449. FT DOMAIN 14 87 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56171.1}. FT NON_TER 101 101 {ECO:0000313|EMBL:ETE56171.1}. SQ SEQUENCE 101 AA; 12221 MW; 8FEF060E391D28CA CRC64; MAFLFLLLLL PAAHFLYQAK AEXVRYLERY FYDRQEILRF DSNLGKHVAV TQLGEATADY WNNDKRWLHD QKAAVDYFCR HNYEAYNYEA AKREERLIGR R // ID V8N2R1_OPHHA Unreviewed; 81 AA. AC V8N2R1; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE55847.1}; DE Flags: Fragment; GN ORFNames=L345_18444 {ECO:0000313|EMBL:ETE55847.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE55847.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE55847.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE55847.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE55847.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01082930; ETE55847.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 2 67 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE55847.1}. FT NON_TER 81 81 {ECO:0000313|EMBL:ETE55847.1}. SQ SEQUENCE 81 AA; 9847 MW; ABC7CEB00016F05A CRC64; MQRVRLLFRY FYDRQEYVRF DSDLGKFVAV TALGEASADY WNADEQLLQY MKASVDYFCR HNYERGIYEA AKREERTIGR R // ID V8N2T9_OPHHA Unreviewed; 59 AA. AC V8N2T9; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56216.1}; DE Flags: Fragment; GN ORFNames=L345_18073 {ECO:0000313|EMBL:ETE56216.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56216.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56216.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56216.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56216.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01034043; ETE56216.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 1 51 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56216.1}. FT NON_TER 59 59 {ECO:0000313|EMBL:ETE56216.1}. SQ SEQUENCE 59 AA; 6731 MW; 290A5324A134E291 CRC64; MVCFHSDLGE FMAITEFGKA VADGWNRDEL ILQHQKAEVD SFCRHNYEVS QSNSVVGQR // ID V8N3D7_OPHHA Unreviewed; 99 AA. AC V8N3D7; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56173.1}; DE Flags: Fragment; GN ORFNames=L345_18116 {ECO:0000313|EMBL:ETE56173.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56173.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56173.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56173.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56173.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01036747; ETE56173.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 11 85 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56173.1}. FT NON_TER 99 99 {ECO:0000313|EMBL:ETE56173.1}. SQ SEQUENCE 99 AA; 11794 MW; 6FF58B298AEAAD13 CRC64; MSTLCPLLHK VECRFLNGTQ RVRFLDRYFY DRQEFAHFDS DLGKYVAVTA LGEASADFWN ADEQLLQDRK ARVDSFCRHN YERLNFEAAK REERVVGRR // ID V8N3Q2_OPHHA Unreviewed; 96 AA. AC V8N3Q2; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 05-OCT-2016, entry version 11. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56486.1}; DE Flags: Fragment; GN ORFNames=L345_17803 {ECO:0000313|EMBL:ETE56486.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56486.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56486.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56486.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56486.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01020528; ETE56486.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}. FT DOMAIN 8 82 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56486.1}. FT NON_TER 96 96 {ECO:0000313|EMBL:ETE56486.1}. SQ SEQUENCE 96 AA; 11684 MW; F12DADBEF3104E90 CRC64; HCLYQEKNEC RFLNGTQRVR VLLRSFYDRQ EIDYFDSDLG KYVAVTPLGQ FDVDKWNRDK VYLQYLKAQV DSVCRRNYLL LNYEAPKREQ RVIGRR // ID V8N3W8_OPHHA Unreviewed; 109 AA. AC V8N3W8; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 31-JAN-2018, entry version 15. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56358.1}; DE Flags: Fragment; GN ORFNames=L345_17931 {ECO:0000313|EMBL:ETE56358.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56358.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56358.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56358.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56358.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01026322; ETE56358.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 15 {ECO:0000256|SAM:SignalP}. FT CHAIN 16 109 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5013198156. FT DOMAIN 18 92 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56358.1}. FT NON_TER 109 109 {ECO:0000313|EMBL:ETE56358.1}. SQ SEQUENCE 109 AA; 13270 MW; 267E79DA61C6F990 CRC64; MAFLLLPLAA HFLYQLKHEC RFLNRTQRMR FLDQYFYDRQ EYVRFDSDLG KFVAVKELGE ATVDYWNRDK QLLQLAKAQV DRFCRLAYEA LNDWPTRWPR GRSEQSARE // ID V8N4D4_OPHHA Unreviewed; 106 AA. AC V8N4D4; DT 19-FEB-2014, integrated into UniProtKB/TrEMBL. DT 19-FEB-2014, sequence version 1. DT 31-JAN-2018, entry version 14. DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ETE56970.1}; DE Flags: Fragment; GN ORFNames=L345_17318 {ECO:0000313|EMBL:ETE56970.1}; OS Ophiophagus hannah (King cobra) (Naja hannah). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; OC Toxicofera; Serpentes; Colubroidea; Elapidae; Elapinae; Ophiophagus. OX NCBI_TaxID=8665 {ECO:0000313|EMBL:ETE56970.1, ECO:0000313|Proteomes:UP000018936}; RN [1] {ECO:0000313|EMBL:ETE56970.1, ECO:0000313|Proteomes:UP000018936} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Blood {ECO:0000313|EMBL:ETE56970.1}; RX PubMed=24297900; DOI=10.1073/pnas.1314702110; RA Vonk F.J., Casewell N.R., Henkel C.V., Heimberg A.M., Jansen H.J., RA McCleary R.J., Kerkkamp H.M., Vos R.A., Guerreiro I., Calvete J.J., RA Wuster W., Woods A.E., Logan J.M., Harrison R.A., Castoe T.A., RA de Koning A.P., Pollock D.D., Yandell M., Calderon D., Renjifo C., RA Currier R.B., Salgado D., Pla D., Sanz L., Hyder A.S., Ribeiro J.M., RA Arntzen J.W., van den Thillart G.E., Boetzer M., Pirovano W., RA Dirks R.P., Spaink H.P., Duboule D., McGlinn E., Kini R.M., RA Richardson M.K.; RT "The king cobra genome reveals dynamic gene evolution and adaptation RT in the snake venom system."; RL Proc. Natl. Acad. Sci. U.S.A. 110:20651-20656(2013). CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:ETE56970.1}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AZIM01010608; ETE56970.1; -; Genomic_DNA. DR Proteomes; UP000018936; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018936}; KW Reference proteome {ECO:0000313|Proteomes:UP000018936}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 15 {ECO:0000256|SAM:SignalP}. FT CHAIN 16 106 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5012677978. FT DOMAIN 18 92 MHC_II_beta. {ECO:0000259|SMART:SM00921}. FT NON_TER 1 1 {ECO:0000313|EMBL:ETE56970.1}. FT NON_TER 106 106 {ECO:0000313|EMBL:ETE56970.1}. SQ SEQUENCE 106 AA; 12836 MW; 4DAB7AF0AFECA84C CRC64; MAFLLLLLAA HFLMQEKHEC RFLNGTQRVR FLLRYIYDRQ EFVRFDSDLG KHVAIMALGE EAVDYWNRDK QFLQYMKASV DRFCRYNYKA LNFKAAKREE CVIGRR // ID W5KCM3_ASTMX Unreviewed; 213 AA. AC W5KCM3; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMXP00000005334}; OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes; OC Characoidei; Characidae; Characidae incertae sedis; Astyanax clade; OC Astyanax. OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000005334, ECO:0000313|Proteomes:UP000018467}; RN [1] {ECO:0000313|Ensembl:ENSAMXP00000005334, ECO:0000313|Proteomes:UP000018467} RP NUCLEOTIDE SEQUENCE. RC STRAIN=female {ECO:0000313|Ensembl:ENSAMXP00000005334}; RA Jeffery W., Warren W., Wilson R.K.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAMXP00000005334} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; APWO01082485; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; W5KCM3; -. DR Ensembl; ENSAMXT00000005334; ENSAMXP00000005334; ENSAMXG00000005209. DR GeneTree; ENSGT00900000140849; -. DR OMA; RWFRNSQ; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000018467; Unassembled WGS sequence. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018467}; KW Reference proteome {ECO:0000313|Proteomes:UP000018467}. FT DOMAIN 113 202 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 213 AA; 24999 MW; D714A46DE313A409 CRC64; LLLCMLEYVS LNMLMAIKSF ADGYNEYTVY ECIFSEALTD VEFILSYYFN KDPYIRFNST VGKFVGYTEF GVKNAERWNK GPELQKWTTE LDRYCKPNIQ IDHSDILVKS VVPKIRLRLD KQGRDDHLAR LICSAYDFYP SAIDVYWLKD NKKVTGDVTA TEEMADGDWY YQFHSHLDYT PKSGEKISCV VEHASSTKPI ITEWSKNKEW DYY // ID W5KCP7_ASTMX Unreviewed; 248 AA. AC W5KCP7; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSAMXP00000005358}; OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes; OC Characoidei; Characidae; Characidae incertae sedis; Astyanax clade; OC Astyanax. OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000005358, ECO:0000313|Proteomes:UP000018467}; RN [1] {ECO:0000313|Ensembl:ENSAMXP00000005358, ECO:0000313|Proteomes:UP000018467} RP NUCLEOTIDE SEQUENCE. RC STRAIN=female {ECO:0000313|Ensembl:ENSAMXP00000005358}; RA Jeffery W., Warren W., Wilson R.K.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAMXP00000005358} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; APWO01082487; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; APWO01082488; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; APWO01082489; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; W5KCP7; -. DR Ensembl; ENSAMXT00000005358; ENSAMXP00000005358; ENSAMXG00000005227. DR GeneTree; ENSGT00900000140849; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G0K7A; -. DR Proteomes; UP000018467; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018467}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000018467}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 20 {ECO:0000256|SAM:SignalP}. FT CHAIN 21 248 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004862638. FT TRANSMEM 213 234 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 110 199 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 248 AA; 27758 MW; DFAEC5199DCD4882 CRC64; MILTLQLLIL LTLSLRTVDG YYHYTEAECV FSEALTDVEF IATWYFNKDP VVRFNSTVGK FVGYTEFGVK QAEGWNSGPQ LQQYKATRDA YCTNNIQIDQ STVLVKSVPP KIWINSEKQA SGDQPAVLIC SAFDFYPPAI DVYWLRDGEK MTGGFIATEE MADGDWYYQV HSRLEYTPKS GEKISCVVEH ASSTKPIITE WDPSLPETDR NKIAIGSSGL VLGLVLSAAG FIYYKKKSTG RILVPSTN // ID W5KEI7_ASTMX Unreviewed; 256 AA. AC W5KEI7; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 20-JUN-2018, entry version 20. DE SubName: Full=Major histocompatibility complex class II DBB gene {ECO:0000313|Ensembl:ENSAMXP00000005998}; OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes; OC Characoidei; Characidae; Characidae incertae sedis; Astyanax clade; OC Astyanax. OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000005998, ECO:0000313|Proteomes:UP000018467}; RN [1] {ECO:0000313|Ensembl:ENSAMXP00000005998, ECO:0000313|Proteomes:UP000018467} RP NUCLEOTIDE SEQUENCE. RC STRAIN=female {ECO:0000313|Ensembl:ENSAMXP00000005998}; RA Jeffery W., Warren W., Wilson R.K.; RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSAMXP00000005998} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; APWO01082607; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSAMXT00000005998; ENSAMXP00000005998; ENSAMXG00000005858. DR GeneTree; ENSGT00900000140849; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G0W5S; -. DR Proteomes; UP000018467; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018467}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000018467}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 29 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 226 247 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 122 202 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 256 AA; 29605 MW; 6E41356E7C21E639 CRC64; VIKQKQIMLK IGIRFSITLI MFFSFLFPVD SRYFFYDMDC FYRGSLENVE FTLTVMYNKK KVMTLNSTEG RLIGYNEVAE KWAKKFINDT QWLDFKINKG INACRRNSNP DQNNISPVTV KPKVKVRSLR SASGNQPAML ICSAYDFYPK PIKLTWLRNG KKVTGDVVFS EELYDGDWYY QIHSHLEYSP GPAEQITCMV EHLSFSQPAL FHWQKEPLSE AERDKVVVGV TGLLMGVIIA TTGLIYYKRK QTGQNL // ID W5LWG8_LEPOC Unreviewed; 271 AA. AC W5LWG8; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 19. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSLOCP00000000475}; OS Lepisosteus oculatus (Spotted gar). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae; OC Lepisosteus. OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000000475, ECO:0000313|Proteomes:UP000018468}; RN [1] {ECO:0000313|Ensembl:ENSLOCP00000000475, ECO:0000313|Proteomes:UP000018468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.; RT "The Draft Genome of Lepisosteus oculatus."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLOCP00000000475} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; W5LWG8; -. DR Ensembl; ENSLOCT00000000475; ENSLOCP00000000475; ENSLOCG00000000433. DR GeneTree; ENSGT00900000140849; -. DR OMA; DWNNYKD; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000018468; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018468}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000018468}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 237 258 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 133 224 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 271 AA; 30288 MW; 3A59DB2ECC0C8212 CRC64; PALGCCHSAA PLTACCTMDS PLHRLAVAVL VLGCTGSRRS VDGNMYQFVH DCEYNDHLED FLYTRRDIFN KIEILRYDSN IQTFVGYTPL GIKYAERFNQ DKEYLAGLKD DLDNYCKHNA GVYKSTMTDR KVPPSVKVSA TKLLSSKHPT MLVCHVTGFY PQRITVTWLR DGLEIKTDVT STDLLANGDW TYQVHSHLEL TPRAGETVAC RVEHSSLERP LEVTWDPSMP ESKKNKIVIG VSGLILGLII TAAGVIYYKK KSSGRILVPS D // ID W5MK87_LEPOC Unreviewed; 252 AA. AC W5MK87; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 20-JUN-2018, entry version 24. DE SubName: Full=Si:busm1-228j01.6 {ECO:0000313|Ensembl:ENSLOCP00000008796}; OS Lepisosteus oculatus (Spotted gar). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae; OC Lepisosteus. OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008796, ECO:0000313|Proteomes:UP000018468}; RN [1] {ECO:0000313|Ensembl:ENSLOCP00000008796, ECO:0000313|Proteomes:UP000018468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.; RT "The Draft Genome of Lepisosteus oculatus."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008796} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR RefSeq; XP_015195143.1; XM_015339657.1. DR ProteinModelPortal; W5MK87; -. DR Ensembl; ENSLOCT00000008807; ENSLOCP00000008796; ENSLOCG00000007271. DR GeneID; 107076178; -. DR GeneTree; ENSGT00900000140849; -. DR OMA; RWFRNSQ; -. DR Proteomes; UP000018468; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018468}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000018468}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 252 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004866386. FT TRANSMEM 216 237 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 113 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 252 AA; 28417 MW; 142B18B067723566 CRC64; MRLVLLCSAL VLCLTLSGAD DFVYFFRSEC HFSASDLRDL VYVRSMTFNG KERVRFNSTV GKYVGFDTWG EKQANYWNGQ KDYIARLSAD KDRFCKYNVQ LMASGMQDRK IKPEVKIYPA KTASQGHTHM LVCHAHGFYP RQIAVSWLRN GQPVSSDLTS MSFASDGDWT YQTLLYLEFT PQGGETFECA VDHVALDGTL KLRWDPAARE AKRNKVIMGA SGLVLGLVFA VIGVVYWKRK TKGHIAVPTV QS // ID W5MKA5_LEPOC Unreviewed; 253 AA. AC W5MKA5; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 20-JUN-2018, entry version 21. DE SubName: Full=Si:busm1-228j01.6 {ECO:0000313|Ensembl:ENSLOCP00000008814}; OS Lepisosteus oculatus (Spotted gar). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae; OC Lepisosteus. OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000008814, ECO:0000313|Proteomes:UP000018468}; RN [1] {ECO:0000313|Ensembl:ENSLOCP00000008814, ECO:0000313|Proteomes:UP000018468} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D., RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.; RT "The Draft Genome of Lepisosteus oculatus."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|Ensembl:ENSLOCP00000008814} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR ProteinModelPortal; W5MKA5; -. DR Ensembl; ENSLOCT00000008825; ENSLOCP00000008814; ENSLOCG00000007271. DR GeneTree; ENSGT00900000140849; -. DR OrthoDB; EOG091G0W5S; -. DR Proteomes; UP000018468; Unassembled WGS sequence. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000018468}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Reference proteome {ECO:0000313|Proteomes:UP000018468}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 218 239 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 115 205 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 253 AA; 28711 MW; 046071C17E695088 CRC64; NYFLGLTLIF VENRTLSSLV PDDFVYFFRS ECHFSASDLR DLVYVRSMTF NGKERVRFNS TVGKYVGFDT WGEKQANYWN GQKDYIARLS ADKDRFCKYN VQLMASGMQD RKTEPDVRLS STKPSSQKHP AMLMCSALGF YPKQIKVSWL RDGQTVTSDV TSTEELADGD WYYQIHSHLE YTPRAGESIV CRVEHSSFAT PKELTWDPSM PEADRNKIII GASGLVLGLV IAAAGGIYYK KKSGVRRMLV PTS // ID W5PBD4_SHEEP Unreviewed; 262 AA. AC W5PBD4; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000007745}; GN Name=LOC101108961 {ECO:0000313|Ensembl:ENSOARP00000007745}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000007745, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000007745, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000007745}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000007745} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AMGL01058166; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01058167; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01058168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; W5PBD4; -. DR Ensembl; ENSOART00000007860; ENSOARP00000007745; ENSOARG00000007221. DR GeneTree; ENSGT00900000140849; -. DR OMA; YRARTEM; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000002356; Chromosome 20. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 12 32 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 231 253 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 129 217 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 262 AA; 29892 MW; 6378F61C5A2FCC2D CRC64; FSCMVCLWYP PGSWTVILPV ILMVLSPLLA WAGNTRTLFM VQGKSECHFS NGTQQVRFLD RYIYNRDEQV RFDSLVGEYR ARTEMGQPAA ERWNRWPDPL QRARAAVHDF CASNYEFFAS LTVQRRVEPT VTVYPVKSRP LRHHNLLVCS VNGFYPGHIE VKWFQNGQEE EAGVVSTGLI PNGDWTFQIM VMLEIVPQGG EVYTCHVEHP SRTSPVTAEW RAQDESSQEK LLSGIGACVL GLLFLGMGLL FYIRRERFGL LG // ID W5PBV1_SHEEP Unreviewed; 267 AA. AC W5PBV1; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 20-JUN-2018, entry version 25. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000007912}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000007912, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000007912, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000007912}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000007912} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AMGL01058168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; W5PBV1; -. DR Ensembl; ENSOART00000008029; ENSOARP00000007912; ENSOARG00000007375. DR GeneTree; ENSGT00900000140849; -. DR OMA; RIPEAHC; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000002356; Chromosome 20. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 30 {ECO:0000256|SAM:SignalP}. FT CHAIN 31 267 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004868739. FT TRANSMEM 232 251 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 127 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 267 AA; 30350 MW; 755FEBB84E596B59 CRC64; MRVTIPRNPG TVAGMVMAVF LVLRIPEAHC REAPKNFVYQ FKGMCYFTNG TEHVRLVARQ IYNKEEILHF DSHLGEFVAV TELGRVCAEI WNTQKDLLAE FRAYVETLCR HNYKETVGVT VQRRVEPTVT VSPASTEAPN LHNLLVCSVT NFYPRQVKIK WFRNQQEQTA GVGFTPLTQN GDWTYQIHVM LETIPQLGDV YVCHVDHPSL QSPITVEWRA QSESVQSKMR SGIGGFVLGL IFLGVGLFVH FQDKRGRAPW EKKGKTG // ID W5PC43_SHEEP Unreviewed; 273 AA. AC W5PC43; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 28. DE SubName: Full=Major histocompatibility complex, class II, DO beta {ECO:0000313|Ensembl:ENSOARP00000008004}; GN Name=HLA-DOB {ECO:0000313|Ensembl:ENSOARP00000008004}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000008004, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000008004, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000008004}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000008004} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AMGL01058168; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_004018787.1; XM_004018738.3. DR ProteinModelPortal; W5PC43; -. DR Ensembl; ENSOART00000008123; ENSOARP00000008004; ENSOARG00000007458. DR GeneID; 101109219; -. DR KEGG; oas:101109219; -. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; WNNRPDI; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000002356; Chromosome 20. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0023026; F:MHC class II protein complex binding; IEA:Ensembl. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0002587; P:negative regulation of antigen processing and presentation of peptide antigen via MHC class II; IEA:Ensembl. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 21 {ECO:0000256|SAM:SignalP}. FT CHAIN 22 273 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004870794. FT TRANSMEM 225 245 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 123 211 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 273 AA; 30882 MW; EC6C95B200966000 CRC64; MSPIWVPWVV AFSSTVLRLD ASMTQGRDSP EDFVTQAKAD CYFTNGTEKV RFVVRFIFNL EEYARFDSDL GMFVALTELG KPDAELWNNR PDILARSRAS VDMLCRRNYK LGAPFTVGRR VQPEVTVYPE KTPALQHRNL LLCLVTGFYP GDIKVTWFRN GQEQREGVMS TGLIRNGDWT FQTTVMLPMT PELGEVYTCL VDHPSLPSPV SVEWRAQSEY SWRKMLSGAA AFLVGLVFFL VGIAIHIRAR KGRVETPLLG NEVPRAVLPP QPH // ID W5PDG9_SHEEP Unreviewed; 267 AA. AC W5PDG9; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 23. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000008482}; GN Name=LOC101109746 {ECO:0000313|Ensembl:ENSOARP00000008482}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000008482, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000008482, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000008482}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000008482} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AMGL01058175; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Ensembl; ENSOART00000008605; ENSOARP00000008482; ENSOARG00000007906. DR GeneTree; ENSGT00900000140849; -. DR OMA; YGDTYTC; -. DR OrthoDB; EOG091G0G84; -. DR Proteomes; UP000002356; Chromosome 20. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}. FT CHAIN 24 267 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004870584. FT TRANSMEM 224 242 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 119 201 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 267 AA; 29620 MW; A11512D40CC1B9DF CRC64; SPEQRMTVLL PLLLGLSLGR TGAGDFVAHV ESTCLLDDDG NPKEFTYCVS FNKDLLTCWD PLQARMVPRE FGALNCLAKN LSKSLNSNNV LIQRLSSGLQ DCAVHTQPFW SSLTHRTRPP TVQVARTTPF NTRESVMLAC YVWGFYPADV AITWRRNGQE VLPHGTAWRV IQPNGDWTYQ TVSHLATTPS FGDTYTCVVE HIGAPELILQ DWTPGLLPVQ AVKVSLSLVT LVLGFIVFVF GLRSWQRAAS SGYIFLPGST YPEGHHD // ID W5Q266_SHEEP Unreviewed; 167 AA. AC W5Q266; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 20. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000016804}; GN Name=LOC101119856 {ECO:0000313|Ensembl:ENSOARP00000016804}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000016804, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000016804, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000016804}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000016804} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AMGL01058976; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01058977; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01058978; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_011956261.1; XM_012100871.2. DR Ensembl; ENSOART00000017042; ENSOARP00000016804; ENSOARG00000015660. DR GeneID; 101119856; -. DR KEGG; oas:101119856; -. DR GeneTree; ENSGT00900000140849; -. DR KO; K06752; -. DR OMA; FSWARET; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000002356; Chromosome 20. DR GO; GO:0042613; C:MHC class II protein complex; IEA:InterPro. DR GO; GO:0019882; P:antigen processing and presentation; IEA:InterPro. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF54452; SSF54452; 1. PE 4: Predicted; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 18 {ECO:0000256|SAM:SignalP}. FT CHAIN 19 167 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004869741. FT DOMAIN 31 105 MHC_II_beta. {ECO:0000259|SMART:SM00921}. SQ SEQUENCE 167 AA; 19591 MW; 1133DF0C164F337B CRC64; MAALAVLLMV LSPPFSWARE TQSLFMHQFK GECRFSNGLQ RMRFFARYIY NTKEDVHFDS DVGEFTALTE LGRPDAEYWN QQKDFMEQMR AKVDTVCRSN YQGIGSFLRQ RRGERGRWVA SGRLCVCVCV RVCRSVCVRE RRREGQRQRL SPGECWIVSK FKLGKLL // ID W5Q2V1_SHEEP Unreviewed; 266 AA. AC W5Q2V1; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 24. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000017039}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000017039, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000017039, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000017039}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000017039} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AMGL01058981; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01058982; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; W5Q2V1; -. DR Ensembl; ENSOART00000017280; ENSOARP00000017039; ENSOARG00000015866. DR GeneTree; ENSGT00900000140849; -. DR OMA; NQEETAY; -. DR OrthoDB; EOG091G0SXL; -. DR Proteomes; UP000002356; Chromosome 20. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004871186. FT TRANSMEM 229 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 127 215 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 30277 MW; 5FD505E59CC3CF2A CRC64; MVALQIPRGF WTAVVMVMLV VLSTPGAESG DSPQDTVVHF MGQCYFTNGM ERVRYVTRYI YNQEETAYYD SDVGEYRAVT QLGRTLAEYW NSQKDIVLED KGIEAQTKYR YMYNVEKIFS VPPSVEPTVT ISPSRTEALN HHNLLVCSVT DFYPGQIKVR WFRNDREETA GVVSTPLIRN GDWTFQILVM LEMTPQRGDV YTCRVEHPSL QSPISVEWRA QSESAQSKML SGIGGFVLGL IFFGLGLIIR RRSQKGKELW GNGKMS // ID W5Q3J8_SHEEP Unreviewed; 244 AA. AC W5Q3J8; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 20-JUN-2018, entry version 29. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000017287}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000017287, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000017287, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000017287}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000017287} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AMGL01058986; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01058987; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AMGL01058988; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; W5Q3J8; -. DR SMR; W5Q3J8; -. DR Ensembl; ENSOART00000017532; ENSOARP00000017287; ENSOARG00000016098. DR GeneTree; ENSGT00900000140849; -. DR OMA; EMTPRRG; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000002356; Chromosome 20. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 244 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5004871396. FT TRANSMEM 206 228 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 104 192 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 244 AA; 27994 MW; ED1082EB431DEE21 CRC64; MVCLYFSRGS RMAALIVMLM VLSPPLAWAR EIQPHFLEYY RSECHFFNGT ERVRLLERYF HNGEEFARFD SDWGEFRAVT ELGRPAAHNY GVFESFAVQR RVEPIVTVYP AKTQPLQHHN LLVCSVNGFY PGHIEVRWFR NGHEEEAGVI STGLIQNGDW TFQTMVMLET VPQSGEVYTC QVEHPSRMSP ITVEWRARSD SAQSKMMSGV GGFVLGLLFL AVGLFIYFRN QKGRPTLQPT GMLF // ID W5Q4S5_SHEEP Unreviewed; 265 AA. AC W5Q4S5; DT 16-APR-2014, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 1. DT 28-MAR-2018, entry version 26. DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSOARP00000017715}; OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000017715, ECO:0000313|Proteomes:UP000002356}; RN [1] {ECO:0000313|Ensembl:ENSOARP00000017715, ECO:0000313|Proteomes:UP000002356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000017715}; RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x; RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W., RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., RA Wang J., Wang W., Xun X.; RT "The sheep genome reference sequence: a work in progress."; RL Anim. Genet. 41:449-453(2010). RN [2] {ECO:0000313|Ensembl:ENSOARP00000017715} RP IDENTIFICATION. RG Ensembl; RL Submitted (FEB-2014) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AMGL01058999; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; W5Q4S5; -. DR Ensembl; ENSOART00000017966; ENSOARP00000017715; ENSOARG00000016496. DR GeneTree; ENSGT00900000140849; -. DR OMA; KETEAHF; -. DR OrthoDB; EOG091G15IU; -. DR Proteomes; UP000002356; Chromosome 20. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000002356}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000002356}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT TRANSMEM 230 249 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 125 213 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 265 AA; 30450 MW; 0E58A2C8B6A1AB2D CRC64; LLATRFSPAQ WWALQSVISR SPPSDQIFHV FTALFMHQFK GECRFSNGLQ RMRFFARYIY NTKEDVHFDS DVGEFTALTE LGRPDAEYWN RQKDFMEQMR AKVNTVCRSN YQGIGSFLRQ RREEPTVTVY PAKTQPLQHH NLLVCSVNGF YPGHIEVRWF RNGQEEETGV ISTGLIQNGD WTFQTVVMLE TVPQSGEVYT CHVEHPSQTS PLTVEWRAQS DSAQRKLMRG IRGFVLGLLF LGVGLIIHLR SKKGHPELQP IGSAL // ID X5D2U9_HUMAN Unreviewed; 266 AA. AC X5D2U9; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 23-MAY-2018, entry version 40. DE SubName: Full=HLA class II histocompatibility antigen, DR beta 4 chain {ECO:0000313|Ensembl:ENSP00000412031}; DE SubName: Full=MHC class II antigen {ECO:0000313|EMBL:AHW47970.1}; GN Name=HLA-DRB4 {ECO:0000313|EMBL:AHW47970.1, GN ECO:0000313|Ensembl:ENSP00000412031}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:AHW47970.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000412031, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Ghori M.J., RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., RA Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [2] {ECO:0000313|EMBL:AHW47970.1} RP NUCLEOTIDE SEQUENCE. RA Pyo C.-W., Wang K., Shen S., Song Y., Wang R., Vu Q., Hall R.J., RA Eng K., Bowman B., Ranade S., Geraghty D.E.; RT "Haplotype-resolved resequencing of conserved extended haploytpes RT associated with disease using fosmid target capture and long-read SMRT RT sequencing technology."; RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|Ensembl:ENSP00000412031} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUN-2015) to UniProtKB. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|SAAS:SAAS00552561}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; CR788250; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR933859; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KJ657694; AHW47919.1; -; Genomic_DNA. DR EMBL; KJ657695; AHW47936.1; -; Genomic_DNA. DR EMBL; KJ657696; AHW47953.1; -; Genomic_DNA. DR EMBL; KJ657697; AHW47970.1; -; Genomic_DNA. DR RefSeq; NP_068818.4; NM_021983.4. DR RefSeq; XP_016885779.1; XM_017030290.1. DR UniGene; Hs.534322; -. DR UniGene; Hs.696211; -. DR UniGene; Hs.716081; -. DR UniGene; Hs.723344; -. DR SMR; X5D2U9; -. DR MaxQB; X5D2U9; -. DR Ensembl; ENST00000457451; ENSP00000412031; ENSG00000231021. DR GeneID; 3126; -. DR KEGG; hsa:3126; -. DR UCSC; uc011hzq.4; human. DR CTD; 3126; -. DR KO; K06752; -. DR OrthoDB; EOG091G0SXL; -. DR GenomeRNAi; 3126; -. DR Proteomes; UP000005640; Chromosome 6. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0002504; P:antigen processing and presentation of peptide or polysaccharide antigen via MHC class II; IEA:UniProtKB-KW. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR Gene3D; 2.60.40.10; -; 1. DR Gene3D; 3.10.320.10; -; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR ProDom; PD000328; MHC_II_b_N; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; SSF48726; 1. DR SUPFAM; SSF54452; SSF54452; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00465899}; KW Immunity {ECO:0000256|SAAS:SAAS00437896}; KW Membrane {ECO:0000256|SAAS:SAAS00437953, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|SAAS:SAAS00437896}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00437953, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 29 {ECO:0000256|SAM:SignalP}. FT CHAIN 30 266 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014316168. FT TRANSMEM 228 250 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 126 216 Ig-like. {ECO:0000259|PROSITE:PS50835}. SQ SEQUENCE 266 AA; 29941 MW; 96FF5FE572403FAE CRC64; MVCLKLPGGS CMAALTVTLT VLSSPLALAG DTQPRFLEQA KCECHFLNGT ERVWNLIRYI YNQEEYARYN SDLGEYQAVT ELGRPDAEYW NSQKDLLERR RAEVDTYCRY NYGVVESFTV QRRVQPKVTV YPSKTQPLQH HNLLVCSVNG FYPGSIEVRW FRNGQEEKAG VVSTGLIQNG DWTFQTLVML ETVPRSGEVY TCQVEHPSMM SPLTVQWSAR SESAQSKMLS GVGGFVLGLL FLGTGLFIYF RNQKGHSGLQ PTGLLS //