ID   MBOA2_HUMAN             Reviewed;         520 AA.
AC   Q6ZWT7; A9EDR2; Q8NCE7; Q96KY4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   19-FEB-2014, entry version 71.
DE   RecName: Full=Lysophospholipid acyltransferase 2;
DE            Short=LPLAT 2;
DE            EC=2.3.1.-;
DE   AltName: Full=1-acylglycerophosphate O-acyltransferase;
DE            EC=2.3.1.51;
DE   AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase;
DE            EC=2.3.1.n7;
DE   AltName: Full=Lysophosphatidic acid acyltransferase;
DE            Short=LPAAT;
DE            Short=Lyso-PA acyltransferase;
DE   AltName: Full=Lysophosphatidylethanolamine acyltransferase;
DE            Short=LPEAT;
DE            Short=Lyso-PE acyltransferase;
DE   AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 2;
DE            Short=O-acyltransferase domain-containing protein 2;
GN   Name=MBOAT2; Synonyms=OACT2;
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].
RX   PubMed=17890783; DOI=10.1074/jbc.M704509200;
RA   Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
RA   Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
RT   "LPT1 encodes a membrane-bound O-acyltransferase involved in the
RT   acylation of lysophospholipids in the yeast Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 282:34288-34298(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Lung, and Testis;
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 [LARGE SCALE MRNA] OF 349-520.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-
RT   length human cDNAs encoding secretion or membrane proteins from oligo-
RT   capped cDNA libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=18772128; DOI=10.1074/jbc.M806194200;
RA   Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.;
RT   "Lysophospholipid acyltransferases and arachidonate recycling in human
RT   neutrophils.";
RL   J. Biol. Chem. 283:30235-30245(2008).
CC   -!- FUNCTION: Acyltransferase which mediates the conversion of
CC       lysophosphatidylethanolamine (1-acyl-sn-glycero-3-
CC       phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-
CC       diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity).
CC       Catalyzes also the acylation of lysophosphatidic acid (LPA) into
CC       phosphatidic acid (PA) (LPAAT activity). Has also a very weak
CC       lysophosphatidylcholine acyltransferase (LPCAT activity). Prefers
CC       oleoyl-CoA as the acyl donor. Lysophospholipid acyltransferases
CC       (LPLATs) catalyze the reacylation step of the phospholipid
CC       remodeling pathway also known as the Lands cycle.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
CC       phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-
CC       phosphoethanolamine.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC   -!- ENZYME REGULATION: Partially inhibited by thimerosal.
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in neutrophils.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC11204.1; Type=Erroneous initiation;
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DR   EMBL; AB305044; BAF93900.1; -; mRNA.
DR   EMBL; AK027321; BAC85105.1; -; mRNA.
DR   EMBL; AC012495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC112723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016005; AAH16005.1; -; mRNA.
DR   EMBL; BC146871; AAI46872.1; -; mRNA.
DR   EMBL; BC157827; AAI57828.1; -; mRNA.
DR   EMBL; AK074779; BAC11204.1; ALT_INIT; mRNA.
DR   RefSeq; NP_620154.2; NM_138799.2.
DR   UniGene; Hs.467634; -.
DR   UniGene; Hs.593538; -.
DR   ProteinModelPortal; Q6ZWT7; -.
DR   STRING; 9606.ENSP00000302177; -.
DR   PhosphoSite; Q6ZWT7; -.
DR   DMDM; 143811417; -.
DR   PaxDb; Q6ZWT7; -.
DR   PRIDE; Q6ZWT7; -.
DR   Ensembl; ENST00000305997; ENSP00000302177; ENSG00000143797.
DR   GeneID; 129642; -.
DR   KEGG; hsa:129642; -.
DR   UCSC; uc002qzg.1; human.
DR   CTD; 129642; -.
DR   GeneCards; GC02M008910; -.
DR   H-InvDB; HIX0001805; -.
DR   HGNC; HGNC:25193; MBOAT2.
DR   HPA; HPA014836; -.
DR   MIM; 611949; gene.
DR   neXtProt; NX_Q6ZWT7; -.
DR   PharmGKB; PA134987740; -.
DR   eggNOG; COG5202; -.
DR   HOGENOM; HOG000015994; -.
DR   HOVERGEN; HBG058823; -.
DR   InParanoid; Q6ZWT7; -.
DR   KO; K13517; -.
DR   OMA; IVTQVAI; -.
DR   OrthoDB; EOG73Z2SW; -.
DR   PhylomeDB; Q6ZWT7; -.
DR   TreeFam; TF314906; -.
DR   Reactome; REACT_111217; Metabolism.
DR   UniPathway; UPA00085; -.
DR   ChiTaRS; MBOAT2; human.
DR   GenomeRNAi; 129642; -.
DR   NextBio; 82616; -.
DR   PRO; PR:Q6ZWT7; -.
DR   ArrayExpress; Q6ZWT7; -.
DR   Bgee; Q6ZWT7; -.
DR   CleanEx; HS_MBOAT2; -.
DR   Genevestigator; Q6ZWT7; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR   GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; TAS:Reactome.
DR   GO; GO:0036152; P:phosphatidylethanolamine acyl-chain remodeling; TAS:Reactome.
DR   InterPro; IPR004299; MBOAT_fam.
DR   Pfam; PF03062; MBOAT; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Complete proteome; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Polymorphism; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    520       Lysophospholipid acyltransferase 2.
FT                                /FTId=PRO_0000273020.
FT   TRANSMEM     22     42       Helical; (Potential).
FT   TRANSMEM     61     81       Helical; (Potential).
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TRANSMEM    184    204       Helical; (Potential).
FT   TRANSMEM    237    257       Helical; (Potential).
FT   TRANSMEM    264    284       Helical; (Potential).
FT   TRANSMEM    366    386       Helical; (Potential).
FT   TRANSMEM    416    436       Helical; (Potential).
FT   TRANSMEM    444    464       Helical; (Potential).
FT   ACT_SITE    342    342       By similarity.
FT   ACT_SITE    373    373       By similarity.
FT   VARIANT     501    501       T -> A (in dbSNP:rs16866827).
FT                                /FTId=VAR_030068.
FT   CONFLICT    402    402       H -> R (in Ref. 5; BAC11204).
FT   CONFLICT    484    484       K -> R (in Ref. 2; BAC85105).
SQ   SEQUENCE   520 AA;  59527 MW;  27FFC44815B21288 CRC64;
     MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAI WFRTYLHSSK TSSFIRHVVA
     TLLGLYLALF CFGWYALHFL VQSGISYCIM IIIGVENMHN YCFVFALGYL TVCQVTRVYI
     FDYGQYSADF SGPMMIITQK ITSLACEIHD GMFRKDEELT SSQRDLAVRR MPSLLEYLSY
     NCNFMGILAG PLCSYKDYIT FIEGRSYHIT QSGENGKEET QYERTEPSPN TAVVQKLLVC
     GLSLLFHLTI CTTLPVEYNI DEHFQATASW PTKIIYLYIS LLAARPKYYF AWTLADAINN
     AAGFGFRGYD ENGAARWDLI SNLRIQQIEM STSFKMFLDN WNIQTALWLK RVCYERTSFS
     PTIQTFILSA IWHGVYPGYY LTFLTGVLMT LAARAMRNNF RHYFIEPSQL KLFYDVITWI
     VTQVAISYTV VPFVLLSIKP SLTFYSSWYY CLHILGILVL LLLPVKKTQR RKNTHENIQL
     SQSKKFDEGE NSLGQNSFST TNNVCNQNQE IASRHSSLKQ
//