ID S20A1_HUMAN Reviewed; 679 AA. AC Q8WUM9; Q08344; Q6DHX8; Q9UQ82; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2002, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Sodium-dependent phosphate transporter 1; DE AltName: Full=Gibbon ape leukemia virus receptor 1; DE Short=GLVR-1; DE AltName: Full=Leukemia virus receptor 1 homolog; DE AltName: Full=Phosphate transporter 1; DE Short=PiT-1; DE AltName: Full=Solute carrier family 20 member 1; GN Name=SLC20A1; Synonyms=GLVR1, PIT1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION (MICROBIAL INFECTION), AND TISSUE RP SPECIFICITY. RX PubMed=2078500; RA O'Hara B., Johann S.V., Klinger H.P., Blair D.G., Rubinson H., Dunn K.J., RA Sass P., Vitek S.M., Robins T.; RT "Characterization of a human gene conferring sensitivity to infection by RT gibbon ape leukemia virus."; RL Cell Growth Differ. 1:119-127(1990). RN [2] 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., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., 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., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., 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., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney, and Skin; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-646. RX PubMed=9889306; DOI=10.1016/s0378-1119(98)00572-1; RA Palmer G., Manen D., Bonjour J.-P., Caverzasio J.; RT "Characterization of the human Glvr-1 phosphate transporter/retrovirus RT receptor gene and promoter region."; RL Gene 226:25-33(1999). RN [5] RP FUNCTION (MICROBIAL INFECTION). RX PubMed=1309898; DOI=10.1128/jvi.66.2.1219-1222.1992; RA Takeuchi Y., Vile R.G., Simpson G., O'Hara B., Collins M.K., Weiss R.A.; RT "Feline leukemia virus subgroup B uses the same cell surface receptor as RT gibbon ape leukemia virus."; RL J. Virol. 66:1219-1222(1992). RN [6] RP IDENTIFICATION. RX PubMed=1531369; DOI=10.1128/jvi.66.3.1635-1640.1992; RA Johann S.V., Gibbons J.J., O'Hara B.; RT "GLVR1, a receptor for gibbon ape leukemia virus, is homologous to a RT phosphate permease of Neurospora crassa and is expressed at high levels in RT the brain and thymus."; RL J. Virol. 66:1635-1640(1992). RN [7] RP MUTAGENESIS OF 550-ASP--VAL-558 AND ASP-550, AND REGION. RX PubMed=8411375; DOI=10.1128/jvi.67.11.6733-6736.1993; RA Johann S.V., van Zeijl M., Cekleniak J., O'Hara B.; RT "Definition of a domain of GLVR1 which is necessary for infection by gibbon RT ape leukemia virus and which is highly polymorphic between species."; RL J. Virol. 67:6733-6736(1993). RN [8] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TRANSPORTER ACTIVITY. RX PubMed=7929240; DOI=10.1016/s0021-9258(18)47267-5; RA Olah Z., Lehel C., Anderson W.B., Eiden M.V., Wilson C.A.; RT "The cellular receptor for gibbon ape leukemia virus is a novel high RT affinity sodium-dependent phosphate transporter."; RL J. Biol. Chem. 269:25426-25431(1994). RN [9] RP FUNCTION (MICROBIAL FUNCTION). RX PubMed=7966619; DOI=10.1128/jvi.68.12.8270-8276.1994; RA Miller D.G., Miller A.D.; RT "A family of retroviruses that utilize related phosphate transporters for RT cell entry."; RL J. Virol. 68:8270-8276(1994). RN [10] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND TRANSPORTER RP ACTIVITY. RX PubMed=8041748; DOI=10.1073/pnas.91.15.7071; RA Kavanaugh M.P., Miller D.G., Zhang W., Law W., Kozak S.L., Kabat D., RA Miller A.D.; RT "Cell-surface receptors for gibbon ape leukemia virus and amphotropic RT murine retrovirus are inducible sodium-dependent phosphate symporters."; RL Proc. Natl. Acad. Sci. U.S.A. 91:7071-7075(1994). RN [11] RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=11009570; DOI=10.1161/01.res.87.7.e10; RA Jono S., McKee M.D., Murry C.E., Shioi A., Nishizawa Y., Mori K., Morii H., RA Giachelli C.M.; RT "Phosphate regulation of vascular smooth muscle cell calcification."; RL Circ. Res. 87:E10-E17(2000). RN [12] RP FUNCTION (MICROBIAL INFECTION), MUTAGENESIS OF ASP-550, AND REGION. RX PubMed=12097582; DOI=10.1128/jvi.76.15.7683-7693.2002; RA Farrell K.B., Russ J.L., Murthy R.K., Eiden M.V.; RT "Reassessing the role of region A in Pit1-mediated viral entry."; RL J. Virol. 76:7683-7693(2002). RN [13] RP INDUCTION. RX PubMed=15641067; DOI=10.1002/art.20748; RA Cecil D.L., Rose D.M., Terkeltaub R., Liu-Bryan R.; RT "Role of interleukin-8 in PiT-1 expression and CXCR1-mediated inorganic RT phosphate uptake in chondrocytes."; RL Arthritis Rheum. 52:144-154(2005). RN [14] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TRANSPORTER ACTIVITY. RX PubMed=16790504; DOI=10.1152/ajpcell.00015.2006; RA Boettger P., Hede S.E., Grunnet M., Hoyer B., Klaerke D.A., Pedersen L.; RT "Characterization of transport mechanisms and determinants critical for RT Na+-dependent Pi symport of the PiT family paralogs human PiT1 and PiT2."; RL Am. J. Physiol. 291:C1377-C1387(2006). RN [15] RP FUNCTION, TRANSPORTER ACTIVITY, AND STOICHIOMETRY. RX PubMed=17494632; DOI=10.1152/ajpcell.00064.2007; RA Ravera S., Virkki L.V., Murer H., Forster I.C.; RT "Deciphering PiT transport kinetics and substrate specificity using RT electrophysiology and flux measurements."; RL Am. J. Physiol. 293:C606-C620(2007). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND IDENTIFICATION BY RP 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 [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [18] RP FUNCTION, TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP SER-128. RX PubMed=19726692; DOI=10.1074/jbc.m109.053132; RA Beck L., Leroy C., Salauen C., Margall-Ducos G., Desdouets C., RA Friedlander G.; RT "Identification of a novel function of PiT1 critical for cell proliferation RT and independent of its phosphate transport activity."; RL J. Biol. Chem. 284:31363-31374(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 AND SER-269, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). CC -!- FUNCTION: Sodium-phosphate symporter which preferentially transports CC the monovalent form of phosphate with a stoichiometry of two sodium CC ions per phosphate ion (PubMed:11009570, PubMed:7929240, CC PubMed:8041748, PubMed:19726692, PubMed:17494632, PubMed:16790504). May CC play a role in extracellular matrix and cartilage calcification as well CC as in vascular calcification (PubMed:11009570). Essential for cell CC proliferation but this function is independent of its phosphate CC transporter activity (PubMed:19726692). {ECO:0000269|PubMed:11009570, CC ECO:0000269|PubMed:16790504, ECO:0000269|PubMed:17494632, CC ECO:0000269|PubMed:19726692, ECO:0000269|PubMed:7929240, CC ECO:0000269|PubMed:8041748}. CC -!- FUNCTION: (Microbial infection) May function as a retroviral receptor CC as it confers human cells susceptibility to infection to Gibbon Ape CC Leukemia Virus (GaLV), Simian sarcoma-associated virus (SSAV) and CC Feline leukemia virus subgroup B (FeLV-B) as well as 10A1 murine CC leukemia virus (10A1 MLV). {ECO:0000269|PubMed:12097582, CC ECO:0000269|PubMed:1309898, ECO:0000269|PubMed:2078500, CC ECO:0000269|PubMed:7966619}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 Na(+)(out) + phosphate(out) = 2 Na(+)(in) + phosphate(in); CC Xref=Rhea:RHEA:71259, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; CC Evidence={ECO:0000269|PubMed:11009570, ECO:0000269|PubMed:16790504, CC ECO:0000269|PubMed:17494632, ECO:0000269|PubMed:19726692, CC ECO:0000269|PubMed:7929240, ECO:0000269|PubMed:8041748}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=24.1 uM for phosphate {ECO:0000269|PubMed:7929240, CC ECO:0000269|PubMed:8041748}; CC KM=322.5 uM for phosphate {ECO:0000269|PubMed:16790504}; CC Vmax=1.9 nmol/min/mg enzyme (in the presence of 0.05-2 mM phosphate) CC {ECO:0000269|PubMed:7929240, ECO:0000269|PubMed:8041748}; CC Note=With an increase in pH, a decrease in phosphate uptake is CC observed.; CC pH dependence: CC Optimum pH is 6.5 and 7.5. {ECO:0000269|PubMed:7929240, CC ECO:0000269|PubMed:8041748}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19726692}; CC Multi-pass membrane protein {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:2078500}. CC -!- INDUCTION: By phosphate deprivation as well as by IL8/interleukin-8 in CC hypertrophic chondrocytes. {ECO:0000269|PubMed:15641067, CC ECO:0000269|PubMed:8041748}. CC -!- DOMAIN: Region A confers human cells susceptibility to infection by CC Gibbon Ape Leukemia Virus (GaLV) and Feline leukemia virus subgroup B CC (FeLV-B). Substitution of Human SLC20A1 region A by region A of murine CC SLC20A1 prevents viral infection. CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) CC (TC 2.A.20) 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; L20859; AAA52572.1; -; mRNA. DR EMBL; AC079922; AAY14922.1; -; Genomic_DNA. DR EMBL; BC019944; AAH19944.1; -; mRNA. DR EMBL; BC075818; AAH75818.1; -; mRNA. DR EMBL; AH007490; AAD20286.1; -; Genomic_DNA. DR CCDS; CCDS2099.1; -. DR PIR; I52822; I52822. DR RefSeq; NP_005406.3; NM_005415.4. DR AlphaFoldDB; Q8WUM9; -. DR SMR; Q8WUM9; -. DR BioGRID; 112462; 131. DR IntAct; Q8WUM9; 27. DR MINT; Q8WUM9; -. DR STRING; 9606.ENSP00000272542; -. DR BindingDB; Q8WUM9; -. DR ChEMBL; CHEMBL4295909; -. DR DrugBank; DB11348; Calcium Phosphate. DR DrugBank; DB14481; Calcium phosphate dihydrate. DR DrugBank; DB14502; Sodium phosphate, dibasic. DR DrugBank; DB09449; Sodium phosphate, monobasic. DR DrugBank; DB14503; Sodium phosphate, monobasic, unspecified form. DR DrugBank; DB09436; Technetium Tc-99m succimer. DR TCDB; 2.A.20.2.7; the inorganic phosphate transporter (pit) family. DR GlyConnect; 2080; 1 N-Linked glycan (1 site). DR GlyCosmos; Q8WUM9; 1 site, 2 glycans. DR GlyGen; Q8WUM9; 2 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q8WUM9; -. DR PhosphoSitePlus; Q8WUM9; -. DR SwissPalm; Q8WUM9; -. DR BioMuta; SLC20A1; -. DR DMDM; 74730735; -. DR EPD; Q8WUM9; -. DR jPOST; Q8WUM9; -. DR MassIVE; Q8WUM9; -. DR MaxQB; Q8WUM9; -. DR PaxDb; 9606-ENSP00000272542; -. DR PeptideAtlas; Q8WUM9; -. DR ProteomicsDB; 74696; -. DR Pumba; Q8WUM9; -. DR Antibodypedia; 33281; 193 antibodies from 28 providers. DR DNASU; 6574; -. DR Ensembl; ENST00000272542.8; ENSP00000272542.3; ENSG00000144136.11. DR GeneID; 6574; -. DR KEGG; hsa:6574; -. DR MANE-Select; ENST00000272542.8; ENSP00000272542.3; NM_005415.5; NP_005406.3. DR UCSC; uc002tib.4; human. DR AGR; HGNC:10946; -. DR CTD; 6574; -. DR DisGeNET; 6574; -. DR GeneCards; SLC20A1; -. DR HGNC; HGNC:10946; SLC20A1. DR HPA; ENSG00000144136; Low tissue specificity. DR MIM; 137570; gene. DR neXtProt; NX_Q8WUM9; -. DR OpenTargets; ENSG00000144136; -. DR PharmGKB; PA35833; -. DR VEuPathDB; HostDB:ENSG00000144136; -. DR eggNOG; KOG2493; Eukaryota. DR GeneTree; ENSGT00390000014879; -. DR HOGENOM; CLU_015355_3_1_1; -. DR InParanoid; Q8WUM9; -. DR OMA; GDIENKH; -. DR OrthoDB; 5488632at2759; -. DR PhylomeDB; Q8WUM9; -. DR TreeFam; TF314426; -. DR BioCyc; MetaCyc:ENSG00000144136-MONOMER; -. DR BRENDA; 7.3.2.1; 2681. DR PathwayCommons; Q8WUM9; -. DR Reactome; R-HSA-427652; Sodium-coupled phosphate cotransporters. DR SignaLink; Q8WUM9; -. DR SIGNOR; Q8WUM9; -. DR BioGRID-ORCS; 6574; 108 hits in 1162 CRISPR screens. DR ChiTaRS; SLC20A1; human. DR GeneWiki; SLC20A1; -. DR GenomeRNAi; 6574; -. DR Pharos; Q8WUM9; Tbio. DR PRO; PR:Q8WUM9; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8WUM9; Protein. DR Bgee; ENSG00000144136; Expressed in mucosa of transverse colon and 202 other cell types or tissues. DR ExpressionAtlas; Q8WUM9; baseline and differential. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005316; F:high-affinity inorganic phosphate:sodium symporter activity; IEA:Ensembl. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc. DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB. DR GO; GO:0031214; P:biomineral tissue development; IEA:Ensembl. DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB. DR GO; GO:0006811; P:monoatomic ion transport; TAS:Reactome. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central. DR GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR InterPro; IPR001204; Phos_transporter. DR PANTHER; PTHR11101; PHOSPHATE TRANSPORTER; 1. DR PANTHER; PTHR11101:SF46; SODIUM-DEPENDENT PHOSPHATE TRANSPORTER 1; 1. DR Pfam; PF01384; PHO4; 1. DR Genevisible; Q8WUM9; HS. PE 1: Evidence at protein level; KW Cell membrane; Host-virus interaction; Membrane; Phosphate transport; KW Phosphoprotein; Receptor; Reference proteome; Symport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..679 FT /note="Sodium-dependent phosphate transporter 1" FT /id="PRO_0000080771" FT TRANSMEM 21..41 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 62..82 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 100..120 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 158..178 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 203..223 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 230..250 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 511..531 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 558..578 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 600..620 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 650..670 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 550..558 FT /note="A" FT MOD_RES 265 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 269 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MUTAGEN 128 FT /note="S->A: Loss of sodium-dependent phosphate transporter FT activity. Able to restore cell proliferation in FT SLC20A1-deficient HeLa cells to a level identical to that FT observed in their wild-type counterpart. No effect on its FT localization to the cell membrane." FT /evidence="ECO:0000269|PubMed:19726692" FT MUTAGEN 550..558 FT /note="DTGDVSSKV->KQEASTKA: Loss of virus infectibility." FT /evidence="ECO:0000269|PubMed:8411375" FT MUTAGEN 550 FT /note="D->K: Drastic reduction of virus infectibility, but FT conserved virus binding ability." FT /evidence="ECO:0000269|PubMed:12097582, FT ECO:0000269|PubMed:8411375" FT MUTAGEN 550 FT /note="Missing: Loss of virus infectibility." FT /evidence="ECO:0000269|PubMed:12097582, FT ECO:0000269|PubMed:8411375" FT CONFLICT 376 FT /note="Y -> S (in Ref. 1; AAA52572)" FT /evidence="ECO:0000305" FT CONFLICT 443 FT /note="E -> R (in Ref. 4; AAD20286)" FT /evidence="ECO:0000305" FT CONFLICT 487 FT /note="E -> A (in Ref. 1; AAA52572)" FT /evidence="ECO:0000305" SQ SEQUENCE 679 AA; 73700 MW; 5545F6E6DC8F5EA8 CRC64; MATLITSTTA ATAASGPLVD YLWMLILGFI IAFVLAFSVG ANDVANSFGT AVGSGVVTLK QACILASIFE TVGSVLLGAK VSETIRKGLI DVEMYNSTQG LLMAGSVSAM FGSAVWQLVA SFLKLPISGT HCIVGATIGF SLVAKGQEGV KWSELIKIVM SWFVSPLLSG IMSGILFFLV RAFILHKADP VPNGLRALPV FYACTVGINL FSIMYTGAPL LGFDKLPLWG TILISVGCAV FCALIVWFFV CPRMKRKIER EIKCSPSESP LMEKKNSLKE DHEETKLSVG DIENKHPVSE VGPATVPLQA VVEERTVSFK LGDLEEAPER ERLPSVDLKE ETSIDSTVNG AVQLPNGNLV QFSQAVSNQI NSSGHYQYHT VHKDSGLYKE LLHKLHLAKV GDCMGDSGDK PLRRNNSYTS YTMAICGMPL DSFRAKEGEQ KGEEMEKLTW PNADSKKRIR MDSYTSYCNA VSDLHSASEI DMSVKAEMGL GDRKGSNGSL EEWYDQDKPE VSLLFQFLQI LTACFGSFAH GGNDVSNAIG PLVALYLVYD TGDVSSKVAT PIWLLLYGGV GICVGLWVWG RRVIQTMGKD LTPITPSSGF SIELASALTV VIASNIGLPI STTHCKVGSV VSVGWLRSKK AVDWRLFRNI FMAWFVTVPI SGVISAAIMA IFRYVILRM //