ID HMP_ECOLI STANDARD; PRT; 396 AA. AC P24232; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 1. DT 02-MAY-2006, entry version 70. DE Flavohemoprotein (Hemoglobin-like protein) (Flavohemoglobin) (HMP) DE (Nitric oxide dioxygenase) (EC 1.14.12.17) (NO oxygenase) (NOD). GN Name=hmp; Synonyms=fsrB, hmpA; OrderedLocusNames=b2552; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-20. RC STRAIN=K12; RX MEDLINE=91238719; PubMed=2034230; DOI=10.1007/BF00273586; RA Vasudevan S.G., Armarego W.L.F., Shaw D.C., Lilley P.E., Dixon N.E., RA Poole R.K.; RT "Isolation and nucleotide sequence of the hmp gene that encodes a RT haemoglobin-like protein in Escherichia coli K-12."; RL Mol. Gen. Genet. 226:49-58(1991). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110; RX MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., RA Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli- RT K12 genome corresponding to 50.0-68.8 min on the linkage map and RT analysis of its sequence features."; RL DNA Res. 4:91-113(1997). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10. RX MEDLINE=83235562; PubMed=6190704; DOI=10.1016/0378-1119(83)90059-8; RA Plamann M.D., Stauffer G.V.; RT "Characterization of the Escherichia coli gene for serine RT hydroxymethyltransferase."; RL Gene 22:9-18(1983). RN [5] RP PARTIAL PROTEIN SEQUENCE, AND FERRISIDEROPHORE REDUCTASE ACTIVITY. RC STRAIN=K12; RX MEDLINE=92290008; PubMed=1601132; DOI=10.1016/0014-5793(92)80452-M; RA Andrews S.C., Shipley D., Keen J.N., Findlay J.B.C., Harrison P.M., RA Guest J.R.; RT "The haemoglobin-like protein (HMP) of Escherichia coli has RT ferrisiderophore reductase activity and its C-terminal domain shares RT homology with ferredoxin NADP+ reductases."; RL FEBS Lett. 302:247-252(1992). RN [6] RP PROTEIN SEQUENCE OF 1-12. RC STRAIN=K12 / EMG2; RX MEDLINE=97443975; PubMed=9298646; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded RT in the genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [7] RP PROTEIN SEQUENCE OF 1-20, AND CHARACTERIZATION. RX MEDLINE=98393652; PubMed=9724711; DOI=10.1073/pnas.95.18.10378; RA Gardner P.R., Gardner A.M., Martin L.A., Salzman A.L.; RT "Nitric oxide dioxygenase: an enzymic function for flavohemoglobin."; RL Proc. Natl. Acad. Sci. U.S.A. 95:10378-10383(1998). RN [8] RP RAPID-SCAN AND FLASH PHOTOLYSIS SPECTROSCOPY. RX MEDLINE=92392388; PubMed=1325799; RA Orii Y., Ioannidis N., Poole R.K.; RT "The oxygenated flavohaemoglobin from Escherichia coli: evidence from RT photodissociation and rapid-scan studies for two kinetic and spectral RT forms."; RL Biochem. Biophys. Res. Commun. 187:94-100(1992). RN [9] RP FERRIC CITRATE REDUCTASE ACTIVITY. RX MEDLINE=94121620; PubMed=8292013; RA Eschenbrenner M., Coves J., Fontecave M.; RT "Ferric reductases in Escherichia coli: the contribution of the RT haemoglobin-like protein."; RL Biochem. Biophys. Res. Commun. 198:127-131(1994). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=7875569; DOI=10.1016/0378-1097(94)00501-H; RA Vasudevan S.G., Tang P., Dixon N.E., Poole R.K.; RT "Distribution of the flavohaemoglobin, HMP, between periplasm and RT cytoplasm in Escherichia coli."; RL FEMS Microbiol. Lett. 125:219-224(1995). RN [11] RP NADH OXIDASE ACTIVITY, AND ROLE IN OXIDATIVE STRESS. RX PubMed=8612736; DOI=10.1016/0014-5793(96)00154-8; RA Membrillo-Hernandez J., Ioannidis N., Poole R.K.; RT "The flavohaemoglobin (HMP) of Escherichia coli generates superoxide RT in vitro and causes oxidative stress in vivo."; RL FEBS Lett. 382:141-144(1996). RN [12] RP TRANSCRIPTIONAL REGULATION. RC STRAIN=K12; RX MEDLINE=96404799; PubMed=8808940; RA Poole R.K., Anjum M.F., Membrillo-Hernandez J., Kim S.O., Hughes M.N., RA Stewart V.; RT "Nitric oxide, nitrite, and Fnr regulation of hmp (flavohemoglobin) RT gene expression in Escherichia coli K-12."; RL J. Bacteriol. 178:5487-5492(1996). RN [13] RP AEROBIC NADH OXIDASE AND ANAEROBIC FAD REDUCTASE ACTIVITIES. RX MEDLINE=96254006; PubMed=8704956; RA Poole R.K., Ioannidis N., Orii Y.; RT "Reactions of the Escherichia coli flavohaemoglobin (Hmp) with NADH RT and near-micromolar oxygen: oxygen affinity of NADH oxidase RT activity."; RL Microbiology 142:1141-1148(1996). RN [14] RP TRANSCRIPTIONAL REGULATION. RC STRAIN=K12; RX MEDLINE=97294454; PubMed=9150210; RA Membrillo-Hernandez J., Kim S.O., Cook G.M., Poole R.K.; RT "Paraquat regulation of hmp (flavohemoglobin) gene expression in RT Escherichia coli K-12 is SoxRS independent but modulated by sigma S."; RL J. Bacteriol. 179:3164-3170(1997). RN [15] RP CYTOCHROME C REDUCTASE AND FERRISIDEROPHORE REDUCTASE ACTIVITIES. RX MEDLINE=97311995; PubMed=9168606; RA Poole R.K., Rogers N.J., D'mello R.A.M., Hughes M.N., Orii Y.; RT "Escherichia coli flavohaemoglobin (Hmp) reduces cytochrome c and RT Fe(III)-hydroxamate K by electron transfer from NADH via FAD: RT sensitivity of oxidoreductase activity to haem-bound dioxygen."; RL Microbiology 143:1557-1565(1997). RN [16] RP NADH AND NADPH OXIDASE ACTIVITIES. RX MEDLINE=98442413; PubMed=9770277; RA Anjum M.F., Ioannidis N., Poole R.K.; RT "Response of the NAD(P)H-oxidising flavohaemoglobin (Hmp) to prolonged RT oxidative stress and implications for its physiological role in RT Escherichia coli."; RL FEMS Microbiol. Lett. 166:219-223(1998). RN [17] RP ROLE IN NITRIC OXIDE DETOXIFICATION. RX PubMed=9756889; DOI=10.1074/jbc.273.41.26528; RA Gardner P.R., Costantino G., Salzman A.L.; RT "Constitutive and adaptive detoxification of nitric oxide in RT Escherichia coli. Role of nitric-oxide dioxygenase in the protection RT of aconitase."; RL J. Biol. Chem. 273:26528-26533(1998). RN [18] RP TRANSCRIPTIONAL REGULATION BY NITRIC OXIDE DONORS. RC STRAIN=K12; RX MEDLINE=99000516; PubMed=9767577; RA Membrillo-Hernandez J., Coopamah M.D., Channa A., Hughes M.N., RA Poole R.K.; RT "A novel mechanism for upregulation of the Escherichia coli K-12 hmp RT (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: RT nitrosation of homocysteine and modulation of MetR binding to the RT glyA-hmp intergenic region."; RL Mol. Microbiol. 29:1101-1112(1998). RN [19] RP NITRIC OXIDE DIOXYGENASE ACTIVITY. RX PubMed=9826660; DOI=10.1073/pnas.95.24.14100; RA Hausladen A., Gow A., Stamler J.S.; RT "Nitrosative stress: metabolic pathway involving the RT flavohemoglobin."; RL Proc. Natl. Acad. Sci. U.S.A. 95:14100-14105(1998). RN [20] RP ANAEROBIC NITRIC OXIDE REDUCTASE ACTIVITY. RX PubMed=10094495; DOI=10.1016/S0014-5793(99)00157-X; RA Kim S.O., Orii Y., Lloyd D., Hughes M.N., Poole R.K.; RT "Anoxic function for the Escherichia coli flavohaemoglobin (Hmp): RT reversible binding of nitric oxide and reduction to nitrous oxide."; RL FEBS Lett. 445:389-394(1999). RN [21] RP ROLE IN RESISTANCE TO NITRIC OXIDE AND PARAQUAT. RX PubMed=9873011; DOI=10.1074/jbc.274.2.748; RA Membrillo-Hernandez J., Coopamah M.D., Anjum M.F., Stevanin T.M., RA Kelly A., Hughes M.N., Poole R.K.; RT "The flavohemoglobin of Escherichia coli confers resistance to a RT nitrosating agent, a 'nitric oxide releaser', and paraquat and is RT essential for transcriptional responses to oxidative stress."; RL J. Biol. Chem. 274:748-754(1999). RN [22] RP KINETIC STUDIES, AND MUTAGENESIS OF TYR-29. RX PubMed=10777548; DOI=10.1074/jbc.275.17.12581; RA Gardner A.M., Martin L.A., Gardner P.R., Dou Y., Olson J.S.; RT "Steady-state and transient kinetics of Escherichia coli nitric-oxide RT dioxygenase (flavohemoglobin). The B10 tyrosine hydroxyl is essential RT for dioxygen binding and catalysis."; RL J. Biol. Chem. 275:12581-12589(2000). RN [23] RP CHARACTERIZATION. RX PubMed=10922365; DOI=10.1074/jbc.M004141200; RA Gardner P.R., Gardner A.M., Martin L.A., Dou Y., Li T., Olson J.S., RA Zhu H., Riggs A.F.; RT "Nitric-oxide dioxygenase activity and function of flavohemoglobins. RT Sensitivity to nitric oxide and carbon monoxide inhibition."; RL J. Biol. Chem. 275:31581-31587(2000). RN [24] RP ROLE IN NITRIC OXIDE DETOXIFICATION. RX PubMed=10915782; DOI=10.1074/jbc.M002471200; RA Stevanin T.M., Ioannidis N., Mills C.E., Kim S.O., Hughes M.N., RA Poole R.K.; RT "Flavohemoglobin Hmp affords inducible protection for Escherichia coli RT respiration, catalyzed by cytochromes bo' or bd, from nitric oxide."; RL J. Biol. Chem. 275:35868-35875(2000). RN [25] RP CHARACTERIZATION. RX PubMed=11139382; DOI=10.1042/0264-6021:3530207; RA Mills C.E., Sedelnikova S., Soeballe B., Hughes M.N., Poole R.K.; RT "Escherichia coli flavohaemoglobin (Hmp) with equistoichiometric FAD RT and haem contents has a low affinity for dioxygen in the absence or RT presence of nitric oxide."; RL Biochem. J. 353:207-213(2001). RN [26] RP INFRARED SPECTROSCOPY. RX PubMed=11690654; DOI=10.1016/S0167-4838(01)00256-4; RA Bonamore A., Chiancone E., Boffi A.; RT "The distal heme pocket of Escherichia coli flavohemoglobin probed by RT infrared spectroscopy."; RL Biochim. Biophys. Acta 1549:174-178(2001). RN [27] RP ACTIVE SITE, AND RESONANCE RAMAN SPECTROSCOPY. RX PubMed=11092893; DOI=10.1074/jbc.M009280200; RA Mukai M., Mills C.E., Poole R.K., Yeh S.-R.; RT "Flavohemoglobin, a globin with a peroxidase-like catalytic site."; RL J. Biol. Chem. 276:7272-7277(2001). RN [28] RP DENITROSYLASE ACTIVITY. RX PubMed=11517313; DOI=10.1073/pnas.181199698; RA Hausladen A., Gow A., Stamler J.S.; RT "Flavohemoglobin denitrosylase catalyzes the reaction of a nitroxyl RT equivalent with molecular oxygen."; RL Proc. Natl. Acad. Sci. U.S.A. 98:10108-10112(2001). RN [29] RP ENZYMATIC ACTIVITY, AND ROLE IN AEROBIC NITRIC OXIDE DETOXIFICATION. RX PubMed=11751864; DOI=10.1074/jbc.M110470200; RA Gardner A.M., Gardner P.R.; RT "Flavohemoglobin detoxifies nitric oxide in aerobic, but not RT anaerobic, Escherichia coli. Evidence for a novel inducible anaerobic RT nitric oxide-scavenging activity."; RL J. Biol. Chem. 277:8166-8171(2002). RN [30] RP INTERACTION WITH LIPIDS. RX PubMed=12741837; DOI=10.1021/bi0206311; RA Bonamore A., Farina A., Gattoni M., Schinina M.E., Bellelli A., RA Boffi A.; RT "Interaction with membrane lipids and heme ligand binding properties RT of Escherichia coli flavohemoglobin."; RL Biochemistry 42:5792-5801(2003). RN [31] RP ALKYLHYDROPEROXIDE REDUCTASE ACTIVITY. RX PubMed=12663656; DOI=10.1074/jbc.M301285200; RA Bonamore A., Gentili P., Ilari A., Schinina M.E., Boffi A.; RT "Escherichia coli flavohemoglobin is an efficient alkylhydroperoxide RT reductase."; RL J. Biol. Chem. 278:22272-22277(2003). RN [32] RP ROLE IN NITRIC OXIDE FORMATION. RX PubMed=12783887; DOI=10.1074/jbc.M303282200; RA Corker H., Poole R.K.; RT "Nitric oxide formation by Escherichia coli. Dependence on nitrite RT reductase, the NO-sensing regulator Fnr, and flavohemoglobin Hmp."; RL J. Biol. Chem. 278:31584-31592(2003). RN [33] RP CHARACTERIZATION OF SEPARATE FUNCTIONAL DOMAINS. RX PubMed=12826671; DOI=10.1074/jbc.M303629200; RA Hernandez-Urzua E., Mills C.E., White G.P., Contreras-Zentella M.L., RA Escamilla E., Vasudevan S.G., Membrillo-Hernandez J., Poole R.K.; RT "Flavohemoglobin Hmp, but not its individual domains, confers RT protection from respiratory inhibition by nitric oxide in Escherichia RT coli."; RL J. Biol. Chem. 278:34975-34982(2003). RN [34] RP X-RAY CRYSTALLOGRAPHY (2.19 ANGSTROMS). RX PubMed=11964402; DOI=10.1074/jbc.M202228200; RA Ilari A., Bonamore A., Farina A., Johnson K.A., Boffi A.; RT "The X-ray structure of ferric Escherichia coli flavohemoglobin RT reveals an unexpected geometry of the distal heme pocket."; RL J. Biol. Chem. 277:23725-23732(2002). RN [35] RP REVIEW. RX MEDLINE=20305024; PubMed=10844666; RA Poole R.K., Hughes M.N.; RT "New functions for the ancient globin family: bacterial responses to RT nitric oxide and nitrosative stress."; RL Mol. Microbiol. 36:775-783(2000). RN [36] RP REVIEW. RX PubMed=14550944; DOI=10.1016/S0168-6445(03)00056-1; RA Frey A.D., Kallio P.T.; RT "Bacterial hemoglobins and flavohemoglobins: versatile proteins and RT their impact on microbiology and biotechnology."; RL FEMS Microbiol. Rev. 27:525-545(2003). CC -!- FUNCTION: Is involved in NO detoxification in an aerobic process, CC termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) CC and NAD(P)H to convert NO to nitrate, which protects the bacterium CC from various noxious nitrogen compounds. Therefore, plays a CC central role in the inducible response to nitrosative stress. CC -!- FUNCTION: In the presence of oxygen and NADH, HMP has NADH oxidase CC activity, which leads to the generation of superoxide and CC H(2)O(2), both in vitro and in vivo, and it has been suggested CC that HMP might act as an amplifier of superoxide stress. Under CC anaerobic conditions, HMP also exhibits nitric oxide reductase and CC FAD reductase activities. However, all these reactions are much CC lower than NOD activity. CC -!- FUNCTION: Various electron acceptors are also reduced by HMP in CC vitro, including dihydropterine, ferrisiderophores, ferric CC citrate, cytochrome c, nitrite, S-nitrosoglutathione, and CC alkylhydroperoxides. However, it is unknown if these reactions are CC of any biological significance in vivo. CC -!- CATALYTIC ACTIVITY: 2 NO + 2 O(2) + NAD(P)H = 2 NO(3)(-) + CC NAD(P)(+). CC -!- COFACTOR: Binds 1 FAD per subunit. CC -!- COFACTOR: Binds 1 heme B per subunit. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.28 uM for NO; CC KM=90 uM for O(2); CC KM=1.8 uM for NADH; CC KM=19.6 uM for NADPH; CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Has also been found to localize CC into the periplasm, but spectral analysis revealed that CC biochemically active HMP is exclusively found in the cytoplasmic CC fraction. CC -!- INDUCTION: By nitric oxyde NO (under aerobic conditions), nitrite, CC nitrate (under anaerobic conditions), nitroso compounds, and CC paraquat. CC -!- DOMAIN: Consists of two distinct domains; an N-terminal heme- CC containing oxygen-binding domain and a C-terminal reductase domain CC with binding sites for FAD and NAD(P)H. CC -!- MISCELLANEOUS: No protein-heme interactions have been detected at CC the distal side of the heme molecule. CC -!- MISCELLANEOUS: HMP is able to bind specifically unsaturated and/or CC cyclopropanated fatty acids with high affinity. CC -!- SIMILARITY: Belongs to the globin family. Two-domain CC flavohemoproteins subfamily. CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein CC pyridine nucleotide cytochrome reductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X58872; CAA41682.1; -; Genomic_DNA. DR EMBL; U00096; AAC75605.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16460.1; -; Genomic_DNA. DR EMBL; J01620; AAA23911.1; -; Genomic_DNA. DR PIR; S15992; S15992. DR PDB; 1GVH; X-ray; A=1-396. DR GenomeReviews; U00096_GR; b2552. DR EchoBASE; EB0451; -. DR EcoGene; EG10456; hmp. DR BioCyc; EcoCyc:EG10456-MONOMER; -. DR HAMAP; MF_01252; -; 1. DR InterPro; IPR001709; FPN_cyt_redctse. DR InterPro; IPR000971; Globin. DR InterPro; IPR009050; Globin_like. DR InterPro; IPR012292; Globin_related. DR InterPro; IPR008333; Oxred_FAD_bd. DR InterPro; IPR001433; Oxred_FAD_NAD_bd. DR InterPro; IPR001221; Phe_hydroxylase. DR Pfam; PF00970; FAD_binding_6; 1. DR Pfam; PF00042; Globin; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PRINTS; PR00371; FPNCR. DR PRINTS; PR00410; PHEHYDRXLASE. DR PROSITE; PS01033; GLOBIN; 1. KW 3D-structure; Complete proteome; Detoxification; KW Direct protein sequencing; FAD; Flavoprotein; Heme; Iron; KW Metal-binding; NAD; NADP; Oxidoreductase; Oxygen transport; Transport. FT CHAIN 1 396 Flavohemoprotein. FT /FTId=PRO_0000052431. FT DOMAIN 151 251 FAD-binding. FT NP_BIND 204 207 FAD. FT NP_BIND 268 273 NADP; ribose group (By similarity). FT NP_BIND 389 392 FAD. FT REGION 1 138 Globin. FT REGION 147 396 Reductase. FT REGION 259 396 NAD or NADP-binding. FT ACT_SITE 95 95 Charge relay system. FT ACT_SITE 135 135 Charge relay system. FT METAL 85 85 Iron (heme proximal ligand). FT BINDING 188 188 FAD. FT SITE 29 29 Involved in heme-bound ligand FT stabilization and O-O bond activation. FT SITE 84 84 Influences the redox potential of the FT prosthetic heme and FAD groups. FT SITE 388 388 Influences the redox potential of the FT prosthetic heme and FAD groups. FT MUTAGEN 29 29 Y->E,H: 15 to 35-fold reduction in NO FT dioxygenase activity. FT MUTAGEN 29 29 Y->F: 30-fold reduction in NO dioxygenase FT activity, and 80-fold increase in the FT O(2) dissociation rate constant. FT HELIX 4 18 FT TURN 19 20 FT HELIX 21 35 FT HELIX 37 41 FT TURN 42 42 FT TURN 47 48 FT HELIX 52 65 FT TURN 66 67 FT HELIX 68 74 FT HELIX 75 87 FT TURN 88 89 FT HELIX 92 110 FT HELIX 114 144 FT TURN 146 147 FT STRAND 152 162 FT STRAND 167 174 FT TURN 175 176 FT TURN 185 186 FT STRAND 188 193 FT TURN 196 197 FT STRAND 202 207 FT STRAND 217 222 FT TURN 225 226 FT HELIX 228 235 FT TURN 236 236 FT TURN 239 240 FT STRAND 242 249 FT TURN 258 259 FT STRAND 262 267 FT HELIX 268 271 FT HELIX 272 284 FT TURN 285 285 FT STRAND 290 296 FT TURN 299 301 FT HELIX 305 313 FT TURN 314 314 FT STRAND 318 324 FT HELIX 329 334 FT TURN 335 335 FT STRAND 339 340 FT HELIX 345 347 FT TURN 355 356 FT STRAND 358 362 FT HELIX 365 377 FT TURN 378 379 FT HELIX 382 384 FT STRAND 385 388 SQ SEQUENCE 396 AA; 43868 MW; 49961BDE1444BD6B CRC64; MLDAQTIATV KATIPLLVET GPKLTAHFYD RMFTHNPELK EIFNMSNQRN GDQREALFNA IAAYASNIEN LPALLPAVEK IAQKHTSFQI KPEQYNIVGE HLLATLDEMF SPGQEVLDAW GKAYGVLANV FINREAEIYN ENASKAGGWE GTRDFRIVAK TPRSALITSF ELEPVDGGAV AEYRPGQYLG VWLKPEGFPH QEIRQYSLTR KPDGKGYRIA VKREEGGQVS NWLHNHANVG DVVKLVAPAG DFFMAVADDT PVTLISAGVG QTPMLAMLDT LAKAGHTAQV NWFHAAENGD VHAFADEVKE LGQSLPRFTA HTWYRQPSEA DRAKGQFDSE GLMDLSKLEG AFSDPTMQFY LCGPVGFMQF TAKQLVDLGV KQENIHYECF GPHKVL //