ID PDGFB_HUMAN Reviewed; 241 AA. AC P01127; G3XAG8; P78431; Q15354; Q6FHE7; Q9UF23; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 28-JAN-2026, entry version 261. DE RecName: Full=Platelet-derived growth factor subunit B; DE Short=PDGF subunit B; DE AltName: Full=PDGF-2; DE AltName: Full=Platelet-derived growth factor B chain; DE AltName: Full=Platelet-derived growth factor beta polypeptide; DE AltName: Full=Proto-oncogene c-Sis; DE AltName: INN=Becaplermin; DE Flags: Precursor; GN Name=PDGFB; Synonyms=PDGF2, SIS; 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 [GENOMIC DNA]. RX PubMed=6740330; DOI=10.1126/science.6740330; RA Josephs S.F., Ratner L., Clarke M.F., Westin E.H., Reitz M.S., RA Wong-Staal F.; RT "Transforming potential of human c-sis nucleotide sequences encoding RT platelet-derived growth factor."; RL Science 225:636-639(1984). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=4033772; DOI=10.1038/316748a0; RA Collins T., Ginsburg D., Boss J.M., Orkin S.H., Pober J.S.; RT "Cultured human endothelial cells express platelet-derived growth factor B RT chain: cDNA cloning and structural analysis."; RL Nature 316:748-750(1985). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2991848; DOI=10.1093/nar/13.14.5007; RA Ratner L., Josephs S.F., Jarrett R., Reitz M.S., Wong-Staal F.; RT "Nucleotide sequence of transforming human c-sis cDNA clones with homology RT to platelet-derived growth factor."; RL Nucleic Acids Res. 13:5007-5018(1985). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3472769; DOI=10.1101/sqb.1986.051.01.109; RA Rao C.D., Igarashi H., Pech M.W., Robbins K.C., Aaronson S.A.; RT "Oncogenic potential of the human platelet-derived growth factor RT transcriptional unit."; RL Cold Spring Harb. Symp. Quant. Biol. 51:959-966(1986). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3517869; DOI=10.1073/pnas.83.8.2392; RA Rao C.D., Igarashi H., Chiu I.-M., Robbins K.C., Aaronson S.A.; RT "Structure and sequence of the human c-sis/platelet-derived growth factor 2 RT (SIS/PDGF2) transcriptional unit."; RL Proc. Natl. Acad. Sci. U.S.A. 83:2392-2396(1986). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [9] 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Lung, Pancreas, 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-185 (ISOFORM 2). RC TISSUE=Choriocarcinoma; RX PubMed=7659502; DOI=10.1093/nar/23.15.2815; RA Dirks R.P.H., Onnekink C., Jansen H.J., de Jong A., Bloemers H.P.J.; RT "A novel human c-sis mRNA species is transcribed from a promoter in c-sis RT intron 1 and contains the code for an alternative PDGF B-like protein."; RL Nucleic Acids Res. 23:2815-2822(1995). RN [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53, AND CHROMOSOMAL TRANSLOCATION RP WITH COL1A1. RX PubMed=8988177; DOI=10.1038/ng0197-95; RA Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F., RA Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D., Blin N., RA Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I., Guilbaud C., RA Dumanski J.P.; RT "Deregulation of the platelet-derived growth factor B-chain gene via fusion RT with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell RT fibroblastoma."; RL Nat. Genet. 15:95-98(1997). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-241. RX PubMed=6327048; DOI=10.1016/0092-8674(84)90307-6; RA Chiu I.-M., Reddy E.P., Givol D., Robbins K.C., Tronick S.R., RA Aaronson S.A.; RT "Nucleotide sequence analysis identifies the human c-sis proto-oncogene as RT a structural gene for platelet-derived growth factor."; RL Cell 37:123-129(1984). RN [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-241 (ISOFORM 1). RX PubMed=3456904; DOI=10.1016/0014-5793(86)80433-1; RA Weich H.A., Sebald W., Schairer H.U., Hoppe J.; RT "The human osteosarcoma cell line U-2 OS expresses a 3.8 kilobase mRNA RT which codes for the sequence of the PDGF-B chain."; RL FEBS Lett. 198:344-348(1986). RN [15] RP PROTEIN SEQUENCE OF 82-112. RX PubMed=6306471; DOI=10.1038/304035a0; RA Waterfield M.D., Scrace G.T., Whittle N., Stroobant P., Johnsson A., RA Wasteson A., Westermark B., Heldin C.H., Huang J.S., Deuel T.F.; RT "Platelet-derived growth factor is structurally related to the putative RT transforming protein p28sis of simian sarcoma virus."; RL Nature 304:35-39(1983). RN [16] RP PROTEIN SEQUENCE OF 82-110. RX PubMed=6844921; DOI=10.1126/science.6844921; RA Antoniades H.N., Hunkapiller M.W.; RT "Human platelet-derived growth factor (PDGF): amino-terminal amino acid RT sequence."; RL Science 220:963-965(1983). RN [17] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 153-200, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=6329745; DOI=10.1002/j.1460-2075.1984.tb01908.x; RA Johnsson A., Heldin C.H., Wasteson A., Westermark B., Deuel T.F., RA Huang J.S., Seeburg P.H., Gray A., Ullrich A., Scrace G., Stroobant P., RA Waterfield M.D.; RT "The c-sis gene encodes a precursor of the B chain of platelet-derived RT growth factor."; RL EMBO J. 3:921-928(1984). RN [18] RP MUTAGENESIS, AND IMPORTANCE OF ARG-108 AND ILE-111 FOR RECEPTOR BINDING. RX PubMed=1661670; DOI=10.1002/j.1460-2075.1991.tb04988.x; RA Clements J.M., Bawden L.J., Bloxidge R.E., Catlin G., Cook A.L., Craig S., RA Drummond A.H., Edwards R.M., Fallon A., Green D.R., Hellewell P.G., RA Kirwin P.M., Nayee P.D., Richardson S.J., Brown D., Chahwala S.B., RA Snarey M., Winslow D.; RT "Two PDGF-B chain residues, arginine 27 and isoleucine 30, mediate receptor RT binding and activation."; RL EMBO J. 10:4113-4120(1991). RN [19] RP INTERCHAIN DISULFIDE BONDS. RX PubMed=1317862; DOI=10.1016/s0021-9258(19)49905-5; RA Andersson M., Oestman A., Baeckstroem G., Hellman U., George-Nascimento C., RA Westermark B., Heldin C.-H.; RT "Assignment of interchain disulfide bonds in platelet-derived growth factor RT (PDGF) and evidence for agonist activity of monomeric PDGF."; RL J. Biol. Chem. 267:11260-11266(1992). RN [20] RP TISSUE SPECIFICITY. RX PubMed=11331882; DOI=10.1038/35074593; RA LaRochelle W.J., Jeffers M., McDonald W.F., Chillakuru R.A., Giese N.A., RA Lokker N.A., Sullivan C., Boldog F.L., Yang M., Vernet C., Burgess C.E., RA Fernandez E., Deegler L.L., Rittman B., Shimkets J., Shimkets R.A., RA Rothberg J.M., Lichenstein H.S.; RT "PDGF D, a novel protease-activated growth factor."; RL Nat. Cell Biol. 3:517-521(2001). RN [21] RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH COL1A1. RX PubMed=12660034; DOI=10.1016/s0165-4608(02)00844-0; RA Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.; RT "Dermatofibrosarcoma protuberans of breast."; RL Cancer Genet. Cytogenet. 142:56-59(2003). RN [22] RP INTERACTION WITH LRP1 AND SORL1. RX PubMed=15053742; DOI=10.1042/bj20040149; RA Gliemann J., Hermey G., Nykjaer A., Petersen C.M., Jacobsen C., RA Andreasen P.A.; RT "The mosaic receptor sorLA/LR11 binds components of the plasminogen- RT activating system and platelet-derived growth factor-BB similarly to LRP1 RT (low-density lipoprotein receptor-related protein), but mediates slow RT internalization of bound ligand."; RL Biochem. J. 381:203-212(2004). RN [23] RP INTERACTION WITH SORL1. RX PubMed=16393139; DOI=10.1042/bj20051364; RA Hermey G., Sjoegaard S.S., Petersen C.M., Nykjaer A., Gliemann J.; RT "Tumour necrosis factor alpha-converting enzyme mediates ectodomain RT shedding of Vps10p-domain receptor family members."; RL Biochem. J. 395:285-293(2006). RN [24] RP CHARACTERIZATION OF VARIANTS IBGC5 ARG-9 AND PRO-119, AND FUNCTION. RX PubMed=26599395; DOI=10.1371/journal.pone.0143407; RA Vanlandewijck M., Lebouvier T., Andaloussi Maee M., Nahar K., Hornemann S., RA Kenkel D., Cunha S.I., Lennartsson J., Boss A., Heldin C.H., Keller A., RA Betsholtz C.; RT "Functional characterization of germline mutations in PDGFB and PDGFRB in RT primary familial brain calcification."; RL PLoS ONE 10:E0143407-E0143407(2015). RN [25] RP INTERACTION WITH CD82. RX PubMed=34530889; DOI=10.1186/s13045-021-01147-6; RA Lee J.W., Hur J., Kwon Y.W., Chae C.W., Choi J.I., Hwang I., Yun J.Y., RA Kang J.A., Choi Y.E., Kim Y.H., Lee S.E., Lee C., Jo D.H., Seok H., RA Cho B.S., Baek S.H., Kim H.S.; RT "KAI1(CD82) is a key molecule to control angiogenesis and switch angiogenic RT milieu to quiescent state."; RL J. Hematol. Oncol. 14:148-148(2021). RN [26] RP REVIEW ON FUNCTION IN DEVELOPMENT AND DISEASE. RX PubMed=18483217; DOI=10.1101/gad.1653708; RA Andrae J., Gallini R., Betsholtz C.; RT "Role of platelet-derived growth factors in physiology and medicine."; RL Genes Dev. 22:1276-1312(2008). RN [27] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=1396586; DOI=10.1002/j.1460-2075.1992.tb05485.x; RA Oefner C., D'Arcy A., Winkler F.K., Eggimann B., Hosang M.; RT "Crystal structure of human platelet-derived growth factor BB."; RL EMBO J. 11:3921-3926(1992). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-185 IN COMPLEX WITH PDGFRB, RP SUBUNIT, AND DISULFIDE BONDS. RX PubMed=20534510; DOI=10.1073/pnas.1000806107; RA Shim A.H., Liu H., Focia P.J., Chen X., Lin P.C., He X.; RT "Structures of a platelet-derived growth factor/propeptide complex and a RT platelet-derived growth factor/receptor complex."; RL Proc. Natl. Acad. Sci. U.S.A. 107:11307-11312(2010). RN [29] RP VARIANTS IBGC5 ARG-9 AND PRO-119. RX PubMed=23913003; DOI=10.1038/ng.2723; RA Keller A., Westenberger A., Sobrido M.J., Garcia-Murias M., Domingo A., RA Sears R.L., Lemos R.R., Ordonez-Ugalde A., Nicolas G., da Cunha J.E., RA Rushing E.J., Hugelshofer M., Wurnig M.C., Kaech A., Reimann R., RA Lohmann K., Dobricic V., Carracedo A., Petrovic I., Miyasaki J.M., RA Abakumova I., Mae M.A., Raschperger E., Zatz M., Zschiedrich K., RA Klepper J., Spiteri E., Prieto J.M., Navas I., Preuss M., Dering C., RA Jankovic M., Paucar M., Svenningsson P., Saliminejad K., Khorshid H.R., RA Novakovic I., Aguzzi A., Boss A., Le Ber I., Defer G., Hannequin D., RA Kostic V.S., Campion D., Geschwind D.H., Coppola G., Betsholtz C., RA Klein C., Oliveira J.R.; RT "Mutations in the gene encoding PDGF-B cause brain calcifications in humans RT and mice."; RL Nat. Genet. 45:1077-1082(2013). CC -!- FUNCTION: Growth factor that plays an essential role in the regulation CC of embryonic development, cell proliferation, cell migration, survival CC and chemotaxis. Potent mitogen for cells of mesenchymal origin CC (PubMed:26599395). Required for normal proliferation and recruitment of CC pericytes and vascular smooth muscle cells in the central nervous CC system, skin, lung, heart and placenta. Required for normal blood CC vessel development, and for normal development of kidney glomeruli. CC Plays an important role in wound healing. Signaling is modulated by the CC formation of heterodimers with PDGFA (By similarity). CC {ECO:0000250|UniProtKB:P31240, ECO:0000269|PubMed:26599395}. CC -!- SUBUNIT: Antiparallel homodimer; disulfide-linked. Antiparallel CC heterodimer with PDGFA; disulfide-linked. The PDGFB homodimer interacts CC with PDGFRA and PDGFRB homodimers, and with heterodimers formed by CC PDGFRA and PDGFRB. The heterodimer composed of PDGFA and PDGFB CC interacts with PDGFRB homodimers, and with heterodimers formed by CC PDGFRA and PDGFRB. Interacts with XLKD1 (By similarity). Interacts with CC LRP1 (PubMed:15053742). Interacts with SORL1 (via the N-terminal CC ectodomain) (PubMed:15053742, PubMed:16393139). Interacts with CD82; CC this interaction inhibits PDGFB-mediated signaling pathway CC (PubMed:34530889). {ECO:0000250, ECO:0000269|PubMed:15053742, CC ECO:0000269|PubMed:16393139, ECO:0000269|PubMed:34530889}. CC -!- INTERACTION: CC P01127; Q9P287: BCCIP; NbExp=3; IntAct=EBI-1554925, EBI-711154; CC P01127; P01127: PDGFB; NbExp=3; IntAct=EBI-1554925, EBI-1554925; CC P01127; P16234: PDGFRA; NbExp=11; IntAct=EBI-1554925, EBI-2861522; CC P01127; P09619: PDGFRB; NbExp=16; IntAct=EBI-1554925, EBI-641237; CC -!- SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon CC wounding. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage; Named isoforms=2; CC Name=1; CC IsoId=P01127-1; Sequence=Displayed; CC Name=2; CC IsoId=P01127-2; Sequence=VSP_044913; CC -!- TISSUE SPECIFICITY: Expressed at high levels in the heart, brain CC (sustantia nigra), placenta and fetal kidney. Expressed at moderate CC levels in the brain (hippocampus), skeletal muscle, kidney and lung. CC {ECO:0000269|PubMed:11331882}. CC -!- DISEASE: Basal ganglia calcification, idiopathic, 5 (IBGC5) CC [MIM:615483]: A form of basal ganglia calcification, an autosomal CC dominant condition characterized by symmetric calcification in the CC basal ganglia and other brain regions. Affected individuals can either CC be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, CC including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, CC seizures, and chronic headache. Serum levels of calcium, phosphate, CC alkaline phosphatase and parathyroid hormone are normal. The CC neuropathological hallmark of the disease is vascular and pericapillary CC calcification, mainly of calcium phosphate, in the affected brain CC areas. {ECO:0000269|PubMed:23913003, ECO:0000269|PubMed:26599395}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving PDGFB is found in CC dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with CC PDGFB. {ECO:0000269|PubMed:12660034}. CC -!- PHARMACEUTICAL: Available under the name Regranex (Ortho-McNeil). Used CC to promote healing in diabetic neuropathic foot ulcers. CC -!- SIMILARITY: Belongs to the PDGF/VEGF growth factor family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/155/PDGFB"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K01401; AAA60552.1; -; Genomic_DNA. DR EMBL; K01918; AAA60552.1; JOINED; Genomic_DNA. DR EMBL; J00121; AAA60552.1; JOINED; Genomic_DNA. DR EMBL; K01398; AAA60552.1; JOINED; Genomic_DNA. DR EMBL; K01399; AAA60552.1; JOINED; Genomic_DNA. DR EMBL; K01400; AAA60552.1; JOINED; Genomic_DNA. DR EMBL; X02811; CAA26579.1; -; mRNA. DR EMBL; X02744; CAA26524.1; -; mRNA. DR EMBL; M12783; AAA60553.1; -; mRNA. DR EMBL; CR456538; CAG30424.1; -; mRNA. DR EMBL; Z81010; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR541807; CAG46606.1; -; mRNA. DR EMBL; CH471095; EAW60306.1; -; Genomic_DNA. DR EMBL; CH471095; EAW60307.1; -; Genomic_DNA. DR EMBL; BC029822; AAH29822.1; -; mRNA. DR EMBL; BC077725; AAH77725.1; -; mRNA. DR EMBL; X83705; CAA58679.1; -; mRNA. DR EMBL; X98706; CAA67262.1; -; Genomic_DNA. DR EMBL; K01917; AAA98793.1; -; Genomic_DNA. DR EMBL; K01913; AAA98793.1; JOINED; Genomic_DNA. DR EMBL; K01914; AAA98793.1; JOINED; Genomic_DNA. DR EMBL; K01915; AAA98793.1; JOINED; Genomic_DNA. DR EMBL; K01916; AAA98793.1; JOINED; Genomic_DNA. DR EMBL; X03702; CAA27333.1; -; mRNA. DR EMBL; X00561; CAA25228.1; -; Genomic_DNA. DR EMBL; X00561; CAA25229.1; -; Genomic_DNA. DR CCDS; CCDS13987.1; -. [P01127-1] DR CCDS; CCDS33650.1; -. [P01127-2] DR PIR; A94276; PFHUG2. DR RefSeq; NP_002599.1; NM_002608.4. [P01127-1] DR RefSeq; NP_148937.1; NM_033016.3. [P01127-2] DR PDB; 1PDG; X-ray; 3.00 A; A/B/C=82-190. DR PDB; 3MJG; X-ray; 2.30 A; A/B=21-185. DR PDB; 4HQU; X-ray; 2.20 A; A=82-190. DR PDB; 4HQX; X-ray; 2.30 A; A=82-183. DR PDB; 4QCI; X-ray; 2.30 A; C/D=82-190. DR PDB; 6T9E; X-ray; 2.99 A; CCC/DDD=82-190. DR PDBsum; 1PDG; -. DR PDBsum; 3MJG; -. DR PDBsum; 4HQU; -. DR PDBsum; 4HQX; -. DR PDBsum; 4QCI; -. DR PDBsum; 6T9E; -. DR AlphaFoldDB; P01127; -. DR EMDB; EMD-6426; -. DR SMR; P01127; -. DR BioGRID; 111181; 93. DR ComplexPortal; CPX-1875; Platelet-derived growth factor AB complex. DR ComplexPortal; CPX-1876; Platelet-derived growth factor BB complex. DR ComplexPortal; CPX-2882; PDGF receptor beta - PDGF-BB complex. DR ComplexPortal; CPX-2883; PDGF receptor alpha-beta - PDGF-BB complex. DR ComplexPortal; CPX-2884; PDGF receptor alpha - PDGF-BB complex. DR ComplexPortal; CPX-2885; PDGF receptor alpha - PDGF-AB complex. DR ComplexPortal; CPX-2886; PDGF receptor beta - PDGF-AB complex. DR ComplexPortal; CPX-2892; PDGF receptor alpha-beta - PDGF-AB complex. DR CORUM; P01127; -. DR DIP; DIP-5737N; -. DR FunCoup; P01127; 1104. DR IntAct; P01127; 69. DR STRING; 9606.ENSP00000330382; -. DR BindingDB; P01127; -. DR ChEMBL; CHEMBL3108633; -. DR DrugBank; DB06325; Pegpleranib. DR GlyConnect; 754; 4 N-Linked glycans (1 site). DR GlyCosmos; P01127; 1 site, 5 glycans. DR GlyGen; P01127; 3 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (2 sites). DR iPTMnet; P01127; -. DR PhosphoSitePlus; P01127; -. DR BioMuta; PDGFB; -. DR DMDM; 129724; -. DR MassIVE; P01127; -. DR PaxDb; 9606-ENSP00000330382; -. DR PeptideAtlas; P01127; -. DR ProteomicsDB; 33745; -. DR ProteomicsDB; 51325; -. [P01127-1] DR TopDownProteomics; P01127-2; -. [P01127-2] DR ABCD; P01127; 9 sequenced antibodies. DR Antibodypedia; 293; 734 antibodies from 42 providers. DR DNASU; 5155; -. DR Ensembl; ENST00000331163.11; ENSP00000330382.6; ENSG00000100311.18. [P01127-1] DR Ensembl; ENST00000381551.8; ENSP00000370963.4; ENSG00000100311.18. [P01127-2] DR GeneID; 5155; -. DR KEGG; hsa:5155; -. DR MANE-Select; ENST00000331163.11; ENSP00000330382.6; NM_002608.4; NP_002599.1. DR UCSC; uc003axe.4; human. [P01127-1] DR AGR; HGNC:8800; -. DR CIViC; 5155; 3 evidence items across 1 molecular profile. DR ClinPGx; PA33145; -. DR CTD; 5155; -. DR DisGeNET; 5155; -. DR GeneCards; PDGFB; -. DR GeneReviews; PDGFB; -. DR HGNC; HGNC:8800; PDGFB. DR HPA; ENSG00000100311; Low tissue specificity. DR MalaCards; PDGFB; -. DR MIM; 190040; gene. DR MIM; 607907; phenotype. DR MIM; 615483; phenotype. DR OpenTargets; ENSG00000100311; -. DR Orphanet; 1980; Bilateral striopallidodentate calcinosis. DR Orphanet; 31112; Dermatofibrosarcoma protuberans. DR Orphanet; 263662; Familial multiple meningioma. DR Orphanet; 2495; Meningioma. DR VEuPathDB; HostDB:ENSG00000100311; -. DR eggNOG; ENOG502S2VW; Eukaryota. DR GeneTree; ENSGT00940000157367; -. DR HOGENOM; CLU_094438_0_0_1; -. DR InParanoid; P01127; -. DR OMA; KHTHDKE; -. DR OrthoDB; 8878063at2759; -. DR PAN-GO; P01127; 9 GO annotations based on evolutionary models. DR PhylomeDB; P01127; -. DR PathwayCommons; P01127; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling. DR Reactome; R-HSA-186763; Downstream signal transduction. DR Reactome; R-HSA-186797; Signaling by PDGF. DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer. DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions. DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade. DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. DR SignaLink; P01127; -. DR SIGNOR; P01127; -. DR Agora; ENSG00000100311; -. DR BioGRID-ORCS; 5155; 8 hits in 1145 CRISPR screens. DR ChiTaRS; PDGFB; human. DR EvolutionaryTrace; P01127; -. DR GeneWiki; PDGFB; -. DR GenomeRNAi; 5155; -. DR Pharos; P01127; Tbio. DR PRO; PR:P01127; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P01127; protein. DR Bgee; ENSG00000100311; Expressed in olfactory bulb and 189 other cell types or tissues. DR ExpressionAtlas; P01127; baseline and differential. DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome. DR GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:1990265; C:platelet-derived growth factor complex; IPI:ComplexPortal. DR GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL. DR GO; GO:0005518; F:collagen binding; IDA:MGI. DR GO; GO:0008083; F:growth factor activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0048407; F:platelet-derived growth factor binding; IPI:BHF-UCL. DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:BHF-UCL. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL. DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL. DR GO; GO:0016176; F:superoxide-generating NADPH oxidase activator activity; IDA:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central. DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:BHF-UCL. DR GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB. DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:BHF-UCL. DR GO; GO:0001892; P:embryonic placenta development; ISS:UniProtKB. DR GO; GO:0010467; P:gene expression; IDA:UniProtKB. DR GO; GO:0007507; P:heart development; ISS:UniProtKB. DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:BHF-UCL. DR GO; GO:0035556; P:intracellular signal transduction; IMP:UniProtKB. DR GO; GO:0072255; P:metanephric glomerular mesangial cell development; ISS:UniProtKB. DR GO; GO:0002548; P:monocyte chemotaxis; IDA:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB. DR GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:BHF-UCL. DR GO; GO:0010512; P:negative regulation of phosphatidylinositol biosynthetic process; IDA:BHF-UCL. DR GO; GO:0010544; P:negative regulation of platelet activation; IDA:BHF-UCL. DR GO; GO:1905064; P:negative regulation of vascular associated smooth muscle cell differentiation; IDA:BHF-UCL. DR GO; GO:0038001; P:paracrine signaling; ISS:UniProtKB. DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB. DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL. DR GO; GO:0090280; P:positive regulation of calcium ion import; IDA:UniProtKB. DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW. DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:BHF-UCL. DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:UniProtKB. DR GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IDA:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL. DR GO; GO:0003104; P:positive regulation of glomerular filtration; ISS:UniProtKB. DR GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; IDA:UniProtKB. DR GO; GO:1900127; P:positive regulation of hyaluronan biosynthetic process; IDA:UniProtKB. DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB. DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:BHF-UCL. DR GO; GO:2000591; P:positive regulation of metanephric mesenchymal cell migration; IDA:UniProtKB. DR GO; GO:0035793; P:positive regulation of metanephric mesenchymal cell migration by platelet-derived growth factor receptor-beta signaling pathway; IDA:UniProtKB. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL. DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IDA:UniProtKB. DR GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB. DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:BHF-UCL. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL. DR GO; GO:1905176; P:positive regulation of vascular associated smooth muscle cell dedifferentiation; IDA:BHF-UCL. DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IDA:UniProtKB. DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IDA:UniProtKB. DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB. DR GO; GO:0072593; P:reactive oxygen species metabolic process; IMP:UniProtKB. DR GO; GO:0009611; P:response to wounding; IDA:BHF-UCL. DR GO; GO:0014805; P:smooth muscle adaptation; NAS:BHF-UCL. DR CDD; cd00135; PDGF; 1. DR DisProt; DP02770; -. DR FunFam; 2.10.90.10:FF:000023; Platelet-derived growth factor subunit B; 1. DR Gene3D; 2.10.90.10; Cystine-knot cytokines; 1. DR InterPro; IPR029034; Cystine-knot_cytokine. DR InterPro; IPR023581; PD_growth_factor_CS. DR InterPro; IPR000072; PDGF/VEGF_dom. DR InterPro; IPR006782; PDGF_N. DR PANTHER; PTHR11633; PLATELET-DERIVED GROWTH FACTOR; 1. DR PANTHER; PTHR11633:SF2; PLATELET-DERIVED GROWTH FACTOR SUBUNIT B; 1. DR Pfam; PF00341; PDGF; 1. DR Pfam; PF04692; PDGF_N; 1. DR SMART; SM00141; PDGF; 1. DR SUPFAM; SSF57501; Cystine-knot cytokines; 1. DR PROSITE; PS00249; PDGF_1; 1. DR PROSITE; PS50278; PDGF_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative promoter usage; Chromosomal rearrangement; KW Cleavage on pair of basic residues; Developmental protein; KW Direct protein sequencing; Disease variant; Disulfide bond; Glycoprotein; KW Growth factor; Mitogen; Pharmaceutical; Proteomics identification; KW Proto-oncogene; Reference proteome; Secreted; Signal. FT SIGNAL 1..20 FT PROPEP 21..81 FT /note="Removed in mature form" FT /id="PRO_0000023371" FT CHAIN 82..190 FT /note="Platelet-derived growth factor subunit B" FT /id="PRO_0000023372" FT PROPEP 191..241 FT /note="Removed in mature form" FT /id="PRO_0000023373" FT REGION 216..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 216..230 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 108 FT /note="Involved in receptor binding" FT SITE 111 FT /note="Involved in receptor binding" FT CARBOHYD 63 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 97..141 FT /evidence="ECO:0000269|PubMed:20534510" FT DISULFID 124 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:20534510" FT DISULFID 130..178 FT /evidence="ECO:0000269|PubMed:20534510" FT DISULFID 133 FT /note="Interchain" FT /evidence="ECO:0000269|PubMed:20534510" FT DISULFID 134..180 FT /evidence="ECO:0000269|PubMed:20534510" FT VAR_SEQ 1..21 FT /note="MNRCWALFLSLCCYLRLVSAE -> MFIMGL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:7659502" FT /id="VSP_044913" FT VARIANT 9 FT /note="L -> R (in IBGC5; loss of protein expression)" FT /evidence="ECO:0000269|PubMed:23913003, FT ECO:0000269|PubMed:26599395" FT /id="VAR_070870" FT VARIANT 88 FT /note="I -> V (in dbSNP:rs17565)" FT /id="VAR_014578" FT VARIANT 119 FT /note="L -> P (in IBGC5; loss of protein expression; FT dbSNP:rs397515632)" FT /evidence="ECO:0000269|PubMed:23913003, FT ECO:0000269|PubMed:26599395" FT /id="VAR_070871" FT CONFLICT 101 FT /note="T -> E (in Ref. 16; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 105 FT /note="E -> C (in Ref. 16; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 107 FT /note="S -> C (in Ref. 16; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 97..105 FT /evidence="ECO:0007829|PDB:4HQU" FT HELIX 108..111 FT /evidence="ECO:0007829|PDB:4HQU" FT STRAND 118..121 FT /evidence="ECO:0007829|PDB:4HQU" FT STRAND 123..131 FT /evidence="ECO:0007829|PDB:4HQU" FT STRAND 140..159 FT /evidence="ECO:0007829|PDB:4HQU" FT STRAND 162..181 FT /evidence="ECO:0007829|PDB:4HQU" SQ SEQUENCE 241 AA; 27283 MW; 9F9A3474CE203C0B CRC64; MNRCWALFLS LCCYLRLVSA EGDPIPEELY EMLSDHSIRS FDDLQRLLHG DPGEEDGAEL DLNMTRSHSG GELESLARGR RSLGSLTIAE PAMIAECKTR TEVFEISRRL IDRTNANFLV WPPCVEVQRC SGCCNNRNVQ CRPTQVQLRP VQVRKIEIVR KKPIFKKATV TLEDHLACKC ETVAAARPVT RSPGGSQEQR AKTPQTRVTI RTVRVRRPPK GKHRKFKHTH DKTALKETLG A // ID S20A2_HUMAN Reviewed; 652 AA. AC Q08357; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 28-JAN-2026, entry version 184. DE RecName: Full=Sodium-dependent phosphate transporter 2; DE AltName: Full=Gibbon ape leukemia virus receptor 2; DE Short=GLVR-2; DE AltName: Full=Phosphate transporter 2; DE Short=PiT-2; DE Short=Pit2; DE Short=hPit2; DE AltName: Full=Solute carrier family 20 member 2; GN Name=SLC20A2; Synonyms=GLVR2, PIT2; 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], AND FUNCTION AS RETROVIRAL RECEPTOR (MICROBIAL RP FUNCTION). RC TISSUE=Placenta; RX PubMed=8302848; DOI=10.1073/pnas.91.3.1168; RA van Zeijl M., Johann S.V., Closs E., Cunningham J., Eddy R., Shows T.B., RA O'Hara B.; RT "A human amphotropic retrovirus receptor is a second member of the gibbon RT ape leukemia virus receptor family."; RL Proc. Natl. Acad. Sci. U.S.A. 91:1168-1172(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP TOPOLOGY, GLYCOSYLATION AT ASN-81, AND MUTAGENESIS OF ASN-81. RX PubMed=11356966; DOI=10.1128/jvi.75.12.5584-5592.2001; RA Salauen C., Rodrigues P., Heard J.M.; RT "Transmembrane topology of PiT-2, a phosphate transporter-retrovirus RT receptor."; RL J. Virol. 75:5584-5592(2001). RN [5] RP TOPOLOGY, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=9151850; DOI=10.1128/jvi.71.6.4564-4570.1997; RA Chien M.L., Foster J.L., Douglas J.L., Garcia J.V.; RT "The amphotropic murine leukemia virus receptor gene encodes a 71- RT kilodalton protein that is induced by phosphate depletion."; RL J. Virol. 71:4564-4570(1997). RN [6] RP FUNCTION AS RETROVIRAL RECEPTOR (MICROBIAL FUNCTION). RX PubMed=11435563; DOI=10.1128/jvi.75.15.6841-6849.2001; RA Sugai J., Eiden M., Anderson M.M., Van Hoeven N., Meiering C.D., RA Overbaugh J.; RT "Identification of envelope determinants of feline leukemia virus subgroup RT B that permit infection and gene transfer to cells expressing human Pit1 or RT Pit2."; RL J. Virol. 75:6841-6849(2001). RN [7] RP FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, FUNCTION AS RETROVIRAL RECEPTOR RP (MICROBIAL FUNCTION), SUBUNIT, MUTAGENESIS OF GLU-55 AND GLU-575, AND RP TRANSPORTER ACTIVITY. RX PubMed=12205090; DOI=10.1074/jbc.m207096200; RA Boettger P., Pedersen L.; RT "Two highly conserved glutamate residues critical for type III sodium- RT dependent phosphate transport revealed by uncoupling transport function RT from retroviral receptor function."; RL J. Biol. Chem. 277:42741-42747(2002). RN [8] RP FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, FUNCTION AS RETROVIRAL RECEPTOR RP (MICROBIAL FUNCTION), SUBUNIT, MUTAGENESIS OF ASP-506, CHARACTERIZATION OF RP VARIANT IBGC1 ASN-28, AND TRANSPORTER ACTIVITY. RX PubMed=15955065; DOI=10.1111/j.1742-4658.2005.04720.x; RA Boettger P., Pedersen L.; RT "Evolutionary and experimental analyses of inorganic phosphate transporter RT PiT family reveals two related signature sequences harboring highly RT conserved aspartic acids critical for sodium-dependent phosphate transport RT function of human PiT2."; RL FEBS J. 272:3060-3074(2005). RN [9] RP FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, BIOPHYSICOCHEMICAL PROPERTIES, RP MUTAGENESIS OF GLU-55; GLU-91 AND GLU-575, 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 [10] RP FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, TRANSPORTER ACTIVITY, AND RP 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 [11] 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256; SER-259; SER-268; RP SER-316 AND SER-385, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259 AND SER-316, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP VARIANTS IBGC1 VAL-42 DEL; ARG-498; LYS-575; MET-595; TRP-601 AND LEU-601, RP CHARACTERIZATION OF VARIANTS IBGC1 VAL-42 DEL; ARG-498; LYS-575; MET-595; RP TRP-601 AND LEU-601, FUNCTION AS SODIUM-PHOSPHATE SYMPORTER, AND RP TRANSPORTER ACTIVITY. RX PubMed=22327515; DOI=10.1038/ng.1077; RA Wang C., Li Y., Shi L., Ren J., Patti M., Wang T., de Oliveira J.R., RA Sobrido M.J., Quintans B., Baquero M., Cui X., Zhang X.Y., Wang L., Xu H., RA Wang J., Yao J., Dai X., Liu J., Zhang L., Ma H., Gao Y., Ma X., Feng S., RA Liu M., Wang Q.K., Forster I.C., Zhang X., Liu J.Y.; RT "Mutations in SLC20A2 link familial idiopathic basal ganglia calcification RT with phosphate homeostasis."; RL Nat. Genet. 44:254-256(2012). RN [16] RP INVOLVEMENT IN IBGC1. RX PubMed=23406454; DOI=10.1111/ene.12044; RA Lemos R.R., Oliveira M.F., Oliveira J.R.; RT "Reporting a new mutation at the SLC20A2 gene in familial idiopathic basal RT ganglia calcification."; RL Eur. J. Neurol. 20:E43-43(2013). RN [17] RP VARIANTS IBGC1 LEU-11; ASN-28 AND PRO-62. RX PubMed=23939468; DOI=10.1016/j.gene.2013.07.071; RA Chen W.J., Yao X.P., Zhang Q.J., Ni W., He J., Li H.F., Liu X.Y., RA Zhao G.X., Murong S.X., Wang N., Wu Z.Y.; RT "Novel SLC20A2 mutations identified in southern Chinese patients with RT idiopathic basal ganglia calcification."; RL Gene 529:159-162(2013). RN [18] RP VARIANTS IBGC1 GLN-382; GLN-502; LEU-568 AND LEU-601. RX PubMed=23334463; DOI=10.1007/s10048-012-0349-2; RA Hsu S.C., Sears R.L., Lemos R.R., Quintans B., Huang A., Spiteri E., RA Nevarez L., Mamah C., Zatz M., Pierce K.D., Fullerton J.M., Adair J.C., RA Berner J.E., Bower M., Brodaty H., Carmona O., Dobricic V., Fogel B.L., RA Garcia-Estevez D., Goldman J., Goudreau J.L., Hopfer S., Jankovic M., RA Jauma S., Jen J.C., Kirdlarp S., Klepper J., Kostic V., Lang A.E., RA Linglart A., Maisenbacher M.K., Manyam B.V., Mazzoni P., Miedzybrodzka Z., RA Mitarnun W., Mitchell P.B., Mueller J., Novakovic I., Paucar M., RA Paulson H., Simpson S.A., Svenningsson P., Tuite P., Vitek J., RA Wetchaphanphesat S., Williams C., Yang M., Schofield P.R., RA de Oliveira J.R., Sobrido M.J., Geschwind D.H., Coppola G.; RT "Mutations in SLC20A2 are a major cause of familial idiopathic basal RT ganglia calcification."; RL Neurogenetics 14:11-22(2013). RN [19] RP VARIANTS IBGC1 ASN-28; LEU-184; SER-194 AND SER-571. RX PubMed=24065723; DOI=10.1093/brain/awt255; RG French IBGC Study Group; RA Nicolas G., Pottier C., Charbonnier C., Guyant-Marechal L., Le Ber I., RA Pariente J., Labauge P., Ayrignac X., Defebvre L., Maltete D., RA Martinaud O., Lefaucheur R., Guillin O., Wallon D., Chaumette B., RA Rondepierre P., Derache N., Fromager G., Schaeffer S., Krystkowiak P., RA Verny C., Jurici S., Sauvee M., Verin M., Lebouvier T., Rouaud O., RA Thauvin-Robinet C., Rousseau S., Rovelet-Lecrux A., Frebourg T., RA Campion D., Hannequin D.; RT "Phenotypic spectrum of probable and genetically-confirmed idiopathic basal RT ganglia calcification."; RL Brain 136:3395-3407(2013). RN [20] RP VARIANTS IBGC1 TRP-434 AND MET-595. RX PubMed=25284758; DOI=10.1002/mds.26053; RA Taglia I., Mignarri A., Olgiati S., Menci E., Petrocelli P.L., RA Breedveld G.J., Scaglione C., Martinelli P., Federico A., Bonifati V., RA Dotti M.T.; RT "Primary familial brain calcification: Genetic analysis and clinical RT spectrum."; RL Mov. Disord. 29:1691-1695(2014). RN [21] RP VARIANTS IBGC1 VAL-51; HIS-71; MET-115 AND ARG-637. RX PubMed=24463626; DOI=10.1212/wnl.0000000000000143; RA Yamada M., Tanaka M., Takagi M., Kobayashi S., Taguchi Y., Takashima S., RA Tanaka K., Touge T., Hatsuta H., Murayama S., Hayashi Y., Kaneko M., RA Ishiura H., Mitsui J., Atsuta N., Sobue G., Shimozawa N., Inuzuka T., RA Tsuji S., Hozumi I.; RT "Evaluation of SLC20A2 mutations that cause idiopathic basal ganglia RT calcification in Japan."; RL Neurology 82:705-712(2014). RN [22] RP CHARACTERIZATION OF VARIANT IBGC1 GLN-PHE-VAL-THR-629 INS, FUNCTION AS RP SODIUM-PHOSPHATE SYMPORTER, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=28722801; DOI=10.1002/jcp.26104; RA Taglia I., Formichi P., Battisti C., Peppoloni G., Barghigiani M., RA Tessa A., Federico A.; RT "Primary familial brain calcification with a novel SLC20A2 mutation: RT Analysis of PiT-2 expression and localization."; RL J. Cell. Physiol. 233:2324-2331(2018). RN [23] RP CHARACTERIZATION OF VARIANTS IBGC1 MET-115 AND ARG-637, FUNCTION AS RP SODIUM-PHOSPHATE SYMPORTER, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=30704756; DOI=10.1016/j.bbrc.2019.01.096; RA Sekine S.I., Nishii K., Masaka T., Kurita H., Inden M., Hozumi I.; RT "SLC20A2 variants cause dysfunctional phosphate transport activity in RT endothelial cells induced from Idiopathic Basal Ganglia Calcification RT patients-derived iPSCs."; RL Biochem. Biophys. Res. Commun. 510:303-308(2019). 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:12205090, PubMed:15955065, CC PubMed:16790504, PubMed:17494632, PubMed:22327515, PubMed:28722801, CC PubMed:30704756). Plays a critical role in the determination of bone CC quality and strength by providing phosphate for bone mineralization (By CC similarity). Required to maintain normal cerebrospinal fluid phosphate CC levels (By similarity). Mediates phosphate-induced calcification of CC vascular smooth muscle cells (VCMCs) and can functionally compensate CC for loss of SLC20A1 in VCMCs (By similarity). CC {ECO:0000250|UniProtKB:Q80UP8, ECO:0000269|PubMed:12205090, CC ECO:0000269|PubMed:15955065, ECO:0000269|PubMed:16790504, CC ECO:0000269|PubMed:17494632, ECO:0000269|PubMed:22327515, CC ECO:0000269|PubMed:28722801, ECO:0000269|PubMed:30704756}. CC -!- FUNCTION: (Microbial infection) Functions as a retroviral receptor and CC confers human cells susceptibility to infection to amphotropic murine CC leukemia virus (A-MuLV), 10A1 murine leukemia virus (10A1 MLV) and some CC feline leukemia virus subgroup B (FeLV-B) variants. CC {ECO:0000269|PubMed:11435563, ECO:0000269|PubMed:12205090, CC ECO:0000269|PubMed:15955065, ECO:0000269|PubMed:8302848}. 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:12205090, ECO:0000269|PubMed:15955065, CC ECO:0000269|PubMed:16790504, ECO:0000269|PubMed:17494632, CC ECO:0000269|PubMed:22327515, ECO:0000269|PubMed:28722801, CC ECO:0000269|PubMed:30704756}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=163.5 uM for phosphate {ECO:0000269|PubMed:16790504}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12205090, CC ECO:0000269|PubMed:15955065}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28722801, CC ECO:0000269|PubMed:30704756, ECO:0000269|PubMed:9151850}; Multi-pass CC membrane protein {ECO:0000269|PubMed:9151850}. Apical cell membrane CC {ECO:0000250|UniProtKB:Q63488}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC -!- INDUCTION: Increased by phosphate depletion in osteosarcoma cell lines. CC {ECO:0000269|PubMed:9151850}. CC -!- DISEASE: Basal ganglia calcification, idiopathic, 1 (IBGC1) CC [MIM:213600]: A form of basal ganglia calcification, an autosomal CC dominant condition characterized by symmetric calcification in the CC basal ganglia and other brain regions. Affected individuals can either CC be asymptomatic or show a wide spectrum of neuropsychiatric symptoms, CC including parkinsonism, dystonia, tremor, ataxia, dementia, psychosis, CC seizures, and chronic headache. Serum levels of calcium, phosphate, CC alkaline phosphatase and parathyroid hormone are normal. The CC neuropathological hallmark of the disease is vascular and pericapillary CC calcification, mainly of calcium phosphate, in the affected brain CC areas. {ECO:0000269|PubMed:15955065, ECO:0000269|PubMed:22327515, CC ECO:0000269|PubMed:23334463, ECO:0000269|PubMed:23406454, CC ECO:0000269|PubMed:23939468, ECO:0000269|PubMed:24065723, CC ECO:0000269|PubMed:24463626, ECO:0000269|PubMed:25284758, CC ECO:0000269|PubMed:28722801, ECO:0000269|PubMed:30704756}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) (TC CC 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; L20852; AAA18018.1; -; mRNA. DR EMBL; AK291202; BAF83891.1; -; mRNA. DR EMBL; BC028600; AAH28600.1; -; mRNA. DR CCDS; CCDS6132.1; -. DR PIR; A37000; A37000. DR RefSeq; NP_001244109.1; NM_001257180.2. DR RefSeq; NP_001244110.1; NM_001257181.2. DR RefSeq; NP_006740.1; NM_006749.5. DR RefSeq; XP_005273670.1; XM_005273613.4. DR RefSeq; XP_016869237.1; XM_017013748.2. DR RefSeq; XP_024303003.1; XM_024447235.2. DR RefSeq; XP_024303004.1; XM_024447236.2. DR RefSeq; XP_047278076.1; XM_047422120.1. DR RefSeq; XP_047278077.1; XM_047422121.1. DR RefSeq; XP_047278078.1; XM_047422122.1. DR RefSeq; XP_054217019.1; XM_054361044.1. DR RefSeq; XP_054217020.1; XM_054361045.1. DR RefSeq; XP_054217021.1; XM_054361046.1. DR RefSeq; XP_054217022.1; XM_054361047.1. DR RefSeq; XP_054217023.1; XM_054361048.1. DR RefSeq; XP_054217024.1; XM_054361049.1. DR RefSeq; XP_054217025.1; XM_054361050.1. DR AlphaFoldDB; Q08357; -. DR SMR; Q08357; -. DR BioGRID; 112463; 130. DR FunCoup; Q08357; 652. DR IntAct; Q08357; 80. DR MINT; Q08357; -. DR STRING; 9606.ENSP00000429754; -. DR BindingDB; Q08357; -. DR ChEMBL; CHEMBL4295806; -. 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.20.2.3; the inorganic phosphate transporter (pit) family. DR GlyCosmos; Q08357; 1 site, No reported glycans. DR GlyGen; Q08357; 3 sites, 1 N-linked glycan (1 site). DR iPTMnet; Q08357; -. DR PhosphoSitePlus; Q08357; -. DR BioMuta; SLC20A2; -. DR DMDM; 74735615; -. DR jPOST; Q08357; -. DR MassIVE; Q08357; -. DR PaxDb; 9606-ENSP00000340465; -. DR PeptideAtlas; Q08357; -. DR ProteomicsDB; 58600; -. DR Pumba; Q08357; -. DR Antibodypedia; 11470; 154 antibodies from 27 providers. DR DNASU; 6575; -. DR Ensembl; ENST00000342228.7; ENSP00000340465.3; ENSG00000168575.12. DR Ensembl; ENST00000517366.2; ENSP00000427756.2; ENSG00000168575.12. DR Ensembl; ENST00000518384.2; ENSP00000430462.2; ENSG00000168575.12. DR Ensembl; ENST00000518717.2; ENSP00000430166.2; ENSG00000168575.12. DR Ensembl; ENST00000520179.5; ENSP00000429712.1; ENSG00000168575.12. DR Ensembl; ENST00000520262.6; ENSP00000429754.1; ENSG00000168575.12. DR Ensembl; ENST00000713988.1; ENSP00000519279.1; ENSG00000168575.12. DR GeneID; 6575; -. DR KEGG; hsa:6575; -. DR MANE-Select; ENST00000520262.6; ENSP00000429754.1; NM_001257180.2; NP_001244109.1. DR UCSC; uc003xpe.5; human. DR AGR; HGNC:10947; -. DR ClinPGx; PA35834; -. DR CTD; 6575; -. DR DisGeNET; 6575; -. DR GeneCards; SLC20A2; -. DR GeneReviews; SLC20A2; -. DR HGNC; HGNC:10947; SLC20A2. DR HPA; ENSG00000168575; Tissue enhanced (choroid plexus, skeletal muscle). DR MalaCards; SLC20A2; -. DR MIM; 158378; gene. DR MIM; 213600; phenotype. DR OpenTargets; ENSG00000168575; -. DR Orphanet; 1980; Bilateral striopallidodentate calcinosis. DR VEuPathDB; HostDB:ENSG00000168575; -. DR eggNOG; KOG2493; Eukaryota. DR GeneTree; ENSGT00390000014879; -. DR HOGENOM; CLU_015355_3_1_1; -. DR InParanoid; Q08357; -. DR OMA; MQAFCIA; -. DR OrthoDB; 260807at2759; -. DR PAN-GO; Q08357; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q08357; -. DR BioCyc; MetaCyc:ENSG00000168575-MONOMER; -. DR PathwayCommons; Q08357; -. DR Reactome; R-HSA-427652; Sodium-coupled phosphate cotransporters. DR Reactome; R-HSA-5619111; Defective SLC20A2 causes idiopathic basal ganglia calcification 1 (IBGC1). DR SignaLink; Q08357; -. DR SIGNOR; Q08357; -. DR Agora; ENSG00000168575; -. DR BioGRID-ORCS; 6575; 14 hits in 1159 CRISPR screens. DR ChiTaRS; SLC20A2; human. DR GeneWiki; SLC20A2; -. DR GenomeRNAi; 6575; -. DR Pharos; Q08357; Tbio. DR PRO; PR:Q08357; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q08357; protein. DR Bgee; ENSG00000168575; Expressed in left lobe of thyroid gland and 198 other cell types or tissues. DR ExpressionAtlas; Q08357; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0031526; C:brush border membrane; ISS:UniProtKB. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB. DR GO; GO:0005315; F: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:0001618; F:virus receptor activity; IMP: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:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB. DR InterPro; IPR001204; Phos_transporter. DR PANTHER; PTHR11101; PHOSPHATE TRANSPORTER; 1. DR PANTHER; PTHR11101:SF83; SODIUM-DEPENDENT PHOSPHATE TRANSPORTER 2; 1. DR Pfam; PF01384; PHO4; 1. PE 1: Evidence at protein level; KW Cell membrane; Disease variant; Glycoprotein; KW Host cell receptor for virus entry; Host-virus interaction; Ion transport; KW Membrane; Phosphate transport; Phosphoprotein; Proteomics identification; KW Receptor; Reference proteome; Sodium; Sodium transport; Symport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..652 FT /note="Sodium-dependent phosphate transporter 2" FT /id="PRO_0000341268" FT TOPO_DOM 1..5 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 27..46 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 47..67 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 68..86 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 87..107 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 108..109 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 110..130 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 131..142 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 143..163 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 164..190 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 191..211 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 212..213 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 214..234 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 235..482 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 483..503 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 504..530 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 531..551 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 552..571 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 572..586 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 587..593 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 594..609 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 610..621 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 622..642 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 643..652 FT /note="Extracellular" FT /evidence="ECO:0000255" FT REGION 273..307 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 458..477 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 295..304 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63488" FT MOD_RES 256 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 259 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 268 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 316 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 385 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 81 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11356966" FT VARIANT 11 FT /note="I -> L (in IBGC1; dbSNP:rs201836672)" FT /evidence="ECO:0000269|PubMed:23939468" FT /id="VAR_072255" FT VARIANT 28 FT /note="D -> N (in IBGC1; Impairs phosphate transport; no FT effect on retroviral receptor function; FT dbSNP:rs1554561099)" FT /evidence="ECO:0000269|PubMed:15955065, FT ECO:0000269|PubMed:23939468, ECO:0000269|PubMed:24065723" FT /id="VAR_072256" FT VARIANT 42 FT /note="Missing (in IBGC1; substantially impaired phosphate FT transport)" FT /evidence="ECO:0000269|PubMed:22327515" FT /id="VAR_067545" FT VARIANT 51 FT /note="A -> V (in IBGC1)" FT /evidence="ECO:0000269|PubMed:24463626" FT /id="VAR_072257" FT VARIANT 62 FT /note="L -> P (in IBGC1)" FT /evidence="ECO:0000269|PubMed:23939468" FT /id="VAR_072258" FT VARIANT 71 FT /note="R -> H (in IBGC1)" FT /evidence="ECO:0000269|PubMed:24463626" FT /id="VAR_072259" FT VARIANT 115 FT /note="T -> M (in IBGC1; loss of sodium-dependent phosphate FT transport but no effect on cell membrane localization; FT dbSNP:rs775911275)" FT /evidence="ECO:0000269|PubMed:24463626, FT ECO:0000269|PubMed:30704756" FT /id="VAR_072260" FT VARIANT 184 FT /note="P -> L (in IBGC1; uncertain significance)" FT /evidence="ECO:0000269|PubMed:24065723" FT /id="VAR_075396" FT VARIANT 194 FT /note="N -> S (in IBGC1; uncertain significance; FT dbSNP:rs748252183)" FT /evidence="ECO:0000269|PubMed:24065723" FT /id="VAR_075397" FT VARIANT 382 FT /note="R -> Q (in IBGC1; dbSNP:rs200010919)" FT /evidence="ECO:0000269|PubMed:23334463" FT /id="VAR_072261" FT VARIANT 434 FT /note="S -> W (in IBGC1; dbSNP:rs1357615935)" FT /evidence="ECO:0000269|PubMed:25284758" FT /id="VAR_072262" FT VARIANT 498 FT /note="G -> R (in IBGC1; substantially impaired phosphate FT transport)" FT /evidence="ECO:0000269|PubMed:22327515" FT /id="VAR_067546" FT VARIANT 502 FT /note="H -> Q (in IBGC1)" FT /evidence="ECO:0000269|PubMed:23334463" FT /id="VAR_072263" FT VARIANT 568 FT /note="P -> L (in IBGC1; dbSNP:rs763252801)" FT /evidence="ECO:0000269|PubMed:23334463" FT /id="VAR_072264" FT VARIANT 571 FT /note="G -> S (in IBGC1; dbSNP:rs1388992742)" FT /evidence="ECO:0000269|PubMed:24065723" FT /id="VAR_075398" FT VARIANT 575 FT /note="E -> K (in IBGC1; substantially impaired phosphate FT transport; dbSNP:rs387906653)" FT /evidence="ECO:0000269|PubMed:22327515" FT /id="VAR_067547" FT VARIANT 595 FT /note="T -> M (in IBGC1; substantially impaired phosphate FT transport; dbSNP:rs387906654)" FT /evidence="ECO:0000269|PubMed:22327515, FT ECO:0000269|PubMed:25284758" FT /id="VAR_067548" FT VARIANT 601 FT /note="S -> L (in IBGC1; substantially impaired phosphate FT transport; dbSNP:rs387906652)" FT /evidence="ECO:0000269|PubMed:22327515, FT ECO:0000269|PubMed:23334463" FT /id="VAR_067549" FT VARIANT 601 FT /note="S -> W (in IBGC1; substantially impaired phosphate FT transport; dbSNP:rs387906652)" FT /evidence="ECO:0000269|PubMed:22327515" FT /id="VAR_067550" FT VARIANT 629 FT /note="T -> TWFVT (in IBGC1; uncertain significance; FT reduced sodium-dependent phosphate transport and cell FT membrane localization)" FT /evidence="ECO:0000269|PubMed:28722801" FT /id="VAR_088078" FT VARIANT 637 FT /note="S -> R (in IBGC1; loss of sodium-dependent phosphate FT transport but no effect on cell membrane localization)" FT /evidence="ECO:0000269|PubMed:24463626, FT ECO:0000269|PubMed:30704756" FT /id="VAR_072265" FT MUTAGEN 55 FT /note="E->D,K: Abolishes sodium-dependent phosphate FT transport; no effect on retroviral receptor function." FT /evidence="ECO:0000269|PubMed:12205090, FT ECO:0000269|PubMed:16790504" FT MUTAGEN 55 FT /note="E->Q: Abolishes phosphate but not sodium uptake; FT when associated with Q-91 and Q-575." FT /evidence="ECO:0000269|PubMed:12205090, FT ECO:0000269|PubMed:16790504" FT MUTAGEN 81 FT /note="N->V: Abolishes N-glycosylation." FT /evidence="ECO:0000269|PubMed:11356966" FT MUTAGEN 91 FT /note="E->Q: Abolishes phosphate but not sodium uptake; FT when associated with Q-55 and Q-575." FT /evidence="ECO:0000269|PubMed:16790504" FT MUTAGEN 506 FT /note="D->N: Impairs phosphate transport; no effect on FT retroviral receptor function." FT /evidence="ECO:0000269|PubMed:15955065" FT MUTAGEN 575 FT /note="E->D,K: Abolishes sodium-dependent phosphate FT transport; no effect on retroviral receptor function." FT /evidence="ECO:0000269|PubMed:12205090, FT ECO:0000269|PubMed:16790504" FT MUTAGEN 575 FT /note="E->Q: Abolishes phosphate but not sodium uptake; FT when associated with Q-55 and Q-91." FT /evidence="ECO:0000269|PubMed:12205090, FT ECO:0000269|PubMed:16790504" SQ SEQUENCE 652 AA; 70392 MW; A0A870C7927DE39C CRC64; MAMDEYLWMV ILGFIIAFIL AFSVGANDVA NSFGTAVGSG VVTLRQACIL ASIFETTGSV LLGAKVGETI RKGIIDVNLY NETVETLMAG EVSAMVGSAV WQLIASFLRL PISGTHCIVG STIGFSLVAI GTKGVQWMEL VKIVASWFIS PLLSGFMSGL LFVLIRIFIL KKEDPVPNGL RALPVFYAAT IAINVFSIMY TGAPVLGLVL PMWAIALISF GVALLFAFFV WLFVCPWMRR KITGKLQKEG ALSRVSDESL SKVQEAESPV FKELPGAKAN DDSTIPLTGA AGETLGTSEG TSAGSHPRAA YGRALSMTHG SVKSPISNGT FGFDGHTRSD GHVYHTVHKD SGLYKDLLHK IHIDRGPEEK PAQESNYRLL RRNNSYTCYT AAICGLPVHA TFRAADSSAP EDSEKLVGDT VSYSKKRLRY DSYSSYCNAV AEAEIEAEEG GVEMKLASEL ADPDQPREDP AEEEKEEKDA PEVHLLFHFL QVLTACFGSF AHGGNDVSNA IGPLVALWLI YKQGGVTQEA ATPVWLLFYG GVGICTGLWV WGRRVIQTMG KDLTPITPSS GFTIELASAF TVVIASNIGL PVSTTHCKVG SVVAVGWIRS RKAVDWRLFR NIFVAWFVTV PVAGLFSAAV MALLMYGILP YV //