ID NPT1_HUMAN Reviewed; 467 AA. AC Q14916; A8K418; O60761; Q13783; Q3MIP5; Q5MJP8; Q5TB83; Q96KL8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 2. DT 27-NOV-2024, entry version 182. DE RecName: Full=Sodium-dependent phosphate transport protein 1; DE AltName: Full=Na(+)/PI cotransporter 1; DE AltName: Full=Na/Pi-4; DE AltName: Full=Renal Na(+)-dependent phosphate cotransporter 1; DE AltName: Full=Renal sodium-dependent phosphate transport protein 1; DE Short=Renal sodium-phosphate transport protein 1; DE AltName: Full=Sodium/phosphate cotransporter 1; DE AltName: Full=Solute carrier family 17 member 1; GN Name=SLC17A1; Synonyms=NPT1; 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] (ISOFORM 1), AND VARIANT ILE-269. RC TISSUE=Kidney; RX PubMed=8288239; DOI=10.1006/geno.1993.1476; RA Chong S.S., Kristjansson K., Zoghbi H.Y., Hughes M.R.; RT "Molecular cloning of the cDNA encoding a human renal sodium phosphate RT transport protein and its assignment to chromosome 6p21.3-p23."; RL Genomics 18:355-359(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Zhou G., Nong W., Li H., Ke R., Zhong G., Shen C., Lin L., Yang S.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [4] 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., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., 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., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA 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 GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Liver; 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 [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-113. RX PubMed=11704559; DOI=10.1152/ajprenal.0092.2001; RA Soumounou Y., Gauthier C., Tenenhouse H.S.; RT "Murine and human type I Na-phosphate cotransporter genes: structure and RT promoter activity."; RL Am. J. Physiol. 281:F1082-F1091(2001). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11. RX PubMed=9545579; DOI=10.1016/s0167-4781(97)00231-5; RA Taketani Y., Miyamoto K., Chikamori M., Tanaka K., Yamamoto H., Tatsumi S., RA Morita K., Takeda E.; RT "Characterization of the 5' flanking region of the human NPT-1 RT Na+/phosphate cotransporter gene."; RL Biochim. Biophys. Acta 1396:267-272(1998). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-467 (ISOFORM 1), VARIANT ILE-269, FUNCTION, RP TRANSPORTER ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE RP SPECIFICITY. RC TISSUE=Kidney cortex; RX PubMed=7826357; DOI=10.1042/bj3050081; RA Miyamoto K., Tatsumi S., Sonoda T., Yamamoto H., Minami H., Taketani Y., RA Takeda E.; RT "Cloning and functional expression of a Na(+)-dependent phosphate co- RT transporter from human kidney: cDNA cloning and functional expression."; RL Biochem. J. 305:81-85(1995). RN [10] RP VARIANT ILE-269, CHARACTERIZATION OF VARIANT ILE-269, FUNCTION, TRANSPORTER RP ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=25252215; DOI=10.1002/art.38884; RA Chiba T., Matsuo H., Kawamura Y., Nagamori S., Nishiyama T., Wei L., RA Nakayama A., Nakamura T., Sakiyama M., Takada T., Taketani Y., Suma S., RA Naito M., Oda T., Kumagai H., Moriyama Y., Ichida K., Shimizu T., Kanai Y., RA Shinomiya N.; RT "NPT1/SLC17A1 is a renal urate exporter in humans and its common gain-of- RT function variant decreases the risk of renal underexcretion gout."; RL Arthritis Rheum. 67:281-287(2015). RN [11] RP VARIANT ILE-269, CHARACTERIZATION OF VARIANT ILE-269, SUBCELLULAR LOCATION, RP FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=27906618; DOI=10.1080/15257770.2016.1149192; RA Sakiyama M., Matsuo H., Nagamori S., Ling W., Kawamura Y., Nakayama A., RA Higashino T., Chiba T., Ichida K., Kanai Y., Shinomiya N.; RT "Expression of a human NPT1/SLC17A1 missense variant which increases urate RT export."; RL Nucleosides Nucleotides Nucleic Acids 35:536-542(2016). CC -!- FUNCTION: Important for the resorption of phosphate by the kidney CC (PubMed:7826357). May be involved in actively transporting phosphate CC into cells via Na(+) cotransport in the renal brush border membrane CC (PubMed:7826357). Plays a role in urate transport in the kidney CC (PubMed:25252215, PubMed:27906618). {ECO:0000269|PubMed:25252215, CC ECO:0000269|PubMed:27906618, ECO:0000269|PubMed:7826357}. CC -!- CATALYTIC ACTIVITY: CC Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); CC Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; CC Evidence={ECO:0000269|PubMed:7826357}; CC -!- CATALYTIC ACTIVITY: CC Reaction=urate(out) = urate(in); Xref=Rhea:RHEA:60368, CC ChEBI:CHEBI:17775; Evidence={ECO:0000269|PubMed:25252215, CC ECO:0000269|PubMed:27906618}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.29 mM for phosphate {ECO:0000269|PubMed:7826357}; CC -!- SUBUNIT: Interacts with PDZK1. {ECO:0000250|UniProtKB:Q61983}. CC -!- SUBCELLULAR LOCATION: Apical cell membrane CC {ECO:0000269|PubMed:25252215, ECO:0000269|PubMed:27906618}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14916-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14916-2; Sequence=VSP_035012; CC -!- TISSUE SPECIFICITY: Expressed in kidney cortex, liver and brain but not CC in other tissues. {ECO:0000269|PubMed:7826357}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion CC cotransporter family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA05888.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; X71355; CAA50490.1; -; mRNA. DR EMBL; AY780791; AAV98361.1; -; mRNA. DR EMBL; AK290783; BAF83472.1; -; mRNA. DR EMBL; AL138726; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471087; EAW55494.1; -; Genomic_DNA. DR EMBL; BC101745; AAI01746.1; -; mRNA. DR EMBL; BC101747; AAI01748.1; -; mRNA. DR EMBL; AF362494; AAL04478.1; -; Genomic_DNA. DR EMBL; AF362490; AAL04478.1; JOINED; Genomic_DNA. DR EMBL; AF362492; AAL04478.1; JOINED; Genomic_DNA. DR EMBL; D83236; BAA25645.1; -; Genomic_DNA. DR EMBL; D28532; BAA05888.1; ALT_INIT; mRNA. DR CCDS; CCDS4565.1; -. [Q14916-1] DR PIR; A48916; A48916. DR PIR; I39473; I39473. DR RefSeq; NP_005065.2; NM_005074.3. [Q14916-1] DR RefSeq; XP_016866688.1; XM_017011199.1. [Q14916-1] DR RefSeq; XP_016866690.1; XM_017011201.1. [Q14916-1] DR AlphaFoldDB; Q14916; -. DR SMR; Q14916; -. DR BioGRID; 112456; 2. DR STRING; 9606.ENSP00000244527; -. DR ChEMBL; CHEMBL3769298; -. DR TCDB; 2.A.1.14.27; the major facilitator superfamily (mfs). DR GlyCosmos; Q14916; 3 sites, No reported glycans. DR GlyGen; Q14916; 3 sites. DR iPTMnet; Q14916; -. DR PhosphoSitePlus; Q14916; -. DR BioMuta; SLC17A1; -. DR DMDM; 205371809; -. DR MassIVE; Q14916; -. DR PaxDb; 9606-ENSP00000244527; -. DR PeptideAtlas; Q14916; -. DR Antibodypedia; 25435; 67 antibodies from 20 providers. DR DNASU; 6568; -. DR Ensembl; ENST00000244527.10; ENSP00000244527.4; ENSG00000124568.12. [Q14916-1] DR Ensembl; ENST00000468082.1; ENSP00000420546.1; ENSG00000124568.12. [Q14916-2] DR Ensembl; ENST00000476801.5; ENSP00000420614.1; ENSG00000124568.12. [Q14916-1] DR GeneID; 6568; -. DR KEGG; hsa:6568; -. DR MANE-Select; ENST00000244527.10; ENSP00000244527.4; NM_005074.5; NP_005065.2. DR UCSC; uc003nfh.5; human. [Q14916-1] DR AGR; HGNC:10929; -. DR CTD; 6568; -. DR DisGeNET; 6568; -. DR GeneCards; SLC17A1; -. DR HGNC; HGNC:10929; SLC17A1. DR HPA; ENSG00000124568; Group enriched (kidney, liver). DR MIM; 182308; gene. DR neXtProt; NX_Q14916; -. DR OpenTargets; ENSG00000124568; -. DR PharmGKB; PA35820; -. DR VEuPathDB; HostDB:ENSG00000124568; -. DR eggNOG; KOG2532; Eukaryota. DR GeneTree; ENSGT00940000162346; -. DR HOGENOM; CLU_001265_5_0_1; -. DR InParanoid; Q14916; -. DR OMA; RRTTWGM; -. DR OrthoDB; 2685946at2759; -. DR PhylomeDB; Q14916; -. DR TreeFam; TF313535; -. DR PathwayCommons; Q14916; -. DR Reactome; R-HSA-428643; Organic anion transporters. DR SignaLink; Q14916; -. DR BioGRID-ORCS; 6568; 7 hits in 1135 CRISPR screens. DR ChiTaRS; SLC17A1; human. DR GeneWiki; SLC17A1; -. DR GenomeRNAi; 6568; -. DR Pharos; Q14916; Tbio. DR PRO; PR:Q14916; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q14916; protein. DR Bgee; ENSG00000124568; Expressed in adult mammalian kidney and 43 other cell types or tissues. DR ExpressionAtlas; Q14916; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005436; F:sodium:phosphate symporter activity; TAS:Reactome. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006820; P:monoatomic anion transport; IBA:GO_Central. DR GO; GO:0006811; P:monoatomic ion transport; TAS:Reactome. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IEA:InterPro. DR GO; GO:0006817; P:phosphate ion transport; TAS:ProtInc. DR GO; GO:0044341; P:sodium-dependent phosphate transport; IDA:UniProtKB. DR GO; GO:0046415; P:urate metabolic process; IMP:BHF-UCL. DR GO; GO:0015747; P:urate transport; IMP:UniProtKB. DR CDD; cd17318; MFS_SLC17; 1. DR FunFam; 1.20.1250.20:FF:000003; Solute carrier family 17 member 3; 1. DR FunFam; 1.20.1250.20:FF:000060; Solute carrier family 17 member 3; 1. DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR050382; MFS_Na/Anion_cotransporter. DR InterPro; IPR036259; MFS_trans_sf. DR InterPro; IPR004745; Pi_cotranspt. DR NCBIfam; TIGR00894; 2A0114euk; 1. DR PANTHER; PTHR11662:SF26; SODIUM-DEPENDENT PHOSPHATE TRANSPORT PROTEIN 1; 1. DR PANTHER; PTHR11662; SOLUTE CARRIER FAMILY 17; 1. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; MFS general substrate transporter; 1. DR PROSITE; PS50850; MFS; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Glycoprotein; Ion transport; Membrane; KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..467 FT /note="Sodium-dependent phosphate transport protein 1" FT /id="PRO_0000220936" FT TRANSMEM 81..101 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 119..139 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 178..198 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 200..220 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 257..277 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 301..321 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 339..359 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 365..385 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 401..421 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 433..453 FT /note="Helical" FT /evidence="ECO:0000255" FT CARBOHYD 41 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 49 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 58 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 246..299 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_035012" FT VARIANT 76 FT /note="S -> N (in dbSNP:rs6933573)" FT /id="VAR_050060" FT VARIANT 269 FT /note="T -> I (increased urate transport; dbSNP:rs1165196)" FT /evidence="ECO:0000269|PubMed:25252215, FT ECO:0000269|PubMed:27906618, ECO:0000269|PubMed:7826357, FT ECO:0000269|PubMed:8288239" FT /id="VAR_050061" FT CONFLICT 37..38 FT /note="RA -> LM (in Ref. 9; BAA05888)" FT /evidence="ECO:0000305" FT CONFLICT 79 FT /note="I -> V (in Ref. 9; BAA05888)" FT /evidence="ECO:0000305" FT CONFLICT 100 FT /note="Y -> H (in Ref. 2; AAV98361)" FT /evidence="ECO:0000305" FT CONFLICT 117 FT /note="L -> P (in Ref. 3; BAF83472)" FT /evidence="ECO:0000305" FT CONFLICT 209 FT /note="G -> C (in Ref. 9; BAA05888)" FT /evidence="ECO:0000305" FT CONFLICT 215 FT /note="L -> F (in Ref. 2; AAV98361)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="S -> G (in Ref. 9; BAA05888)" FT /evidence="ECO:0000305" SQ SEQUENCE 467 AA; 51132 MW; 10FE6C7E202BCFF7 CRC64; MQMDNRLPPK KVPGFCSFRY GLSFLVHCCN VIITAQRACL NLTMVVMVNS TDPHGLPNTS TKKLLDNIKN PMYNWSPDIQ GIILSSTSYG VIIIQVPVGY FSGIYSTKKM IGFALCLSSV LSLLIPPAAG IGVAWVVVCR AVQGAAQGIV ATAQFEIYVK WAPPLERGRL TSMSTSGFLL GPFIVLLVTG VICESLGWPM VFYIFGACGC AVCLLWFVLF YDDPKDHPCI SISEKEYITS SLVQQVSSSR QSLPIKAILK SLPVWAISTG SFTFFWSHNI MTLYTPMFIN SMLHVNIKEN GFLSSLPYLF AWICGNLAGQ LSDFFLTRNI LSVIAVRKLF TAAGFLLPAI FGVCLPYLSS TFYSIVIFLI LAGATGSFCL GGVFINGLDI APRYFGFIKA CSTLTGMIGG LIASTLTGLI LKQDPESAWF KTFILMAAIN VTGLIFYLIV ATAEIQDWAK EKQHTRL //