ID NTCP7_HUMAN Reviewed; 340 AA. AC Q0GE19; A7E2E6; A7MAX9; Q0VAP9; Q45NG1; Q45NG2; Q5H9S6; Q6P4E6; Q8IZ62; AC Q8NBP8; Q9H0M9; DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 28-FEB-2018, sequence version 2. DT 27-MAR-2024, entry version 140. DE RecName: Full=Sodium/bile acid cotransporter 7; DE AltName: Full=Na(+)/bile acid cotransporter 7; DE AltName: Full=Solute carrier family 10 member 7; GN Name=SLC10A7; Synonyms=C4orf13, P7; ORFNames=PSEC0051; 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 2), AND TISSUE SPECIFICITY. RX PubMed=15932064; DOI=10.1007/s10528-005-1509-y; RA Zou X., Wang D., Qiu G., Ji C., Jin F., Wu M., Zheng H., Li X., Sun L., RA Wang Y., Tang R., Zhao R.C., Mao Y.; RT "Molecular cloning and characterization of a novel human C4orf13 gene, RT tentatively a member of the sodium bile acid cotransporter family."; RL Biochem. Genet. 43:165-173(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), LACK OF FUNCTION AS RP STEROID TRANSPORTER, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND RP TOPOLOGY. RC TISSUE=Heart; RX PubMed=17628207; DOI=10.1016/j.ejcb.2007.06.001; RA Godoy J.R., Fernandes C., Doering B., Beuerlein K., Petzinger E., Geyer J.; RT "Molecular and phylogenetic characterization of a novel putative membrane RT transporter (SLC10A7), conserved in vertebrates and bacteria."; RL Eur. J. Cell Biol. 86:445-460(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Heart; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5; 6 AND 7). RC TISSUE=Prostate; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-145. RC TISSUE=Kidney; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-340 (ISOFORM 2). RC TISSUE=Teratocarcinoma; 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 [8] RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN SSASKS, AND VARIANT SSASKS RP ASP-112. RX PubMed=29878199; DOI=10.1093/hmg/ddy213; RG CDG group; RA Ashikov A., Abu Bakar N., Wen X.Y., Niemeijer M., RA Rodrigues Pinto Osorio G., Brand-Arzamendi K., Hasadsri L., Hansikova H., RA Raymond K., Vicogne D., Ondruskova N., Simon M.E.H., Pfundt R., Timal S., RA Beumers R., Biot C., Smeets R., Kersten M., Huijben K., Linders P.T.A., RA van den Bogaart G., van Hijum S.A.F.T., Rodenburg R., van den Heuvel L.P., RA van Spronsen F., Honzik T., Foulquier F., van Scherpenzeel M., RA Lefeber D.J., Mirjam W., Han B., Helen M., Helen M., Peter V.H., RA Jiddeke V.K., Diego M., Lars M., Katja B.H., Jozef H., Majid A., Kevin C., RA Johann T.W.N.; RT "Integrating glycomics and genomics uncovers SLC10A7 as essential factor RT for bone mineralization by regulating post-Golgi protein transport and RT glycosylation."; RL Hum. Mol. Genet. 27:3029-3045(2018). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INVOLVEMENT IN SSASKS, RP VARIANTS SSASKS PRO-74; ARG-130 AND 185-GLN--VAL-340 DEL, AND RP CHARACTERIZATION OF VARIANT SSASKS PRO-74. RX PubMed=30082715; DOI=10.1038/s41467-018-05191-8; RA Dubail J., Huber C., Chantepie S., Sonntag S., Tueysuez B., Mihci E., RA Gordon C.T., Steichen-Gersdorf E., Amiel J., Nur B., Stolte-Dijkstra I., RA van Eerde A.M., van Gassen K.L., Breugem C.C., Stegmann A., Lekszas C., RA Maroofian R., Karimiani E.G., Bruneel A., Seta N., Munnich A., RA Papy-Garcia D., De La Dure-Molla M., Cormier-Daire V.; RT "SLC10A7 mutations cause a skeletal dysplasia with amelogenesis imperfecta RT mediated by GAG biosynthesis defects."; RL Nat. Commun. 9:3087-3087(2018). RN [10] RP FUNCTION, INVOLVEMENT IN SSASKS, VARIANT SSASKS LEU-303, AND RP CHARACTERIZATION OF VARIANT SSASKS LEU-303. RX PubMed=31191616; DOI=10.3389/fgene.2019.00504; RA Laugel-Haushalter V., Baer S., Schaefer E., Stoetzel C., Geoffroy V., RA Alembik Y., Kharouf N., Huckert M., Hamm P., Hemmerle J., Maniere M.C., RA Friant S., Dollfus H., Bloch-Zupan A.; RT "A new SLC10A7 homozygous missense mutation responsible for a milder RT phenotype of skeletal dysplasia with amelogenesis imperfecta."; RL Front. Genet. 10:504-504(2019). CC -!- FUNCTION: Involved in teeth and skeletal development. Has an essential CC role in the biosynthesis and trafficking of glycosaminoglycans and CC glycoproteins, to produce a proper functioning extracellular matrix. CC Required for extracellular matrix mineralization (PubMed:30082715, CC PubMed:29878199). Also involved in the regulation of cellular calcium CC homeostasis (PubMed:30082715, PubMed:31191616). Does not show transport CC activity towards bile acids or steroid sulfates (including CC taurocholate, cholate, chenodeoxycholate, estrone-3-sulfate, CC dehydroepiandrosterone sulfate (DHEAS) and pregnenolone sulfate). CC {ECO:0000269|PubMed:17628207, ECO:0000269|PubMed:29878199, CC ECO:0000269|PubMed:30082715, ECO:0000269|PubMed:31191616}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17628207, CC ECO:0000269|PubMed:30082715}; Multi-pass membrane protein CC {ECO:0000305|PubMed:17628207}. Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:17628207}; Multi-pass membrane protein CC {ECO:0000305|PubMed:17628207}. Golgi apparatus membrane CC {ECO:0000269|PubMed:29878199}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=2; Synonyms=A; CC IsoId=Q0GE19-2; Sequence=Displayed; CC Name=1; Synonyms=C; CC IsoId=Q0GE19-1; Sequence=VSP_059321; CC Name=3; CC IsoId=Q0GE19-3; Sequence=VSP_023219; CC Name=4; Synonyms=B; CC IsoId=Q0GE19-4; Sequence=VSP_023222, VSP_023223; CC Name=5; CC IsoId=Q0GE19-5; Sequence=VSP_023220, VSP_023221; CC Name=6; CC IsoId=Q0GE19-6; Sequence=VSP_023216, VSP_023217; CC Name=7; CC IsoId=Q0GE19-7; Sequence=VSP_023215, VSP_023218; CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:15932064, CC PubMed:17628207). Expressed at high levels in liver and at lower levels CC in prostate, placenta, kidney, heart, lung, thymus and spleen CC (PubMed:15932064, PubMed:17628207). Strongly expressed in testis and CC also detected in brain, ovary, colon and small intestine CC (PubMed:17628207). Weakly expressed in testis and not detected in CC brain, ovary, colon or small intestine (PubMed:15932064). Isoform 1: CC Expressed in liver, testis and placenta (PubMed:17628207). Isoform 4: CC Expressed in liver, testis and placenta (PubMed:17628207). CC {ECO:0000269|PubMed:15932064, ECO:0000269|PubMed:17628207}. CC -!- DEVELOPMENTAL STAGE: Detected in the heart and vertebrae in embryos at CC 8 weeks of gestation (Carnegie stage 16), and in the long-bone CC cartilage at 9 weeks (Carnegie stages 19). CC {ECO:0000269|PubMed:30082715}. CC -!- DISEASE: Short stature, amelogenesis imperfecta, and skeletal dysplasia CC with scoliosis (SSASKS) [MIM:618363]: An autosomal recessive disorder CC characterized by disproportionate short stature, defective tooth enamel CC formation, and skeletal dysplasia with severe scoliosis in some CC patients. Variable features include facial dysmorphism, hearing CC impairment, and mildly impaired intellectual development. CC {ECO:0000269|PubMed:29878199, ECO:0000269|PubMed:30082715, CC ECO:0000269|PubMed:31191616}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the bile acid:sodium symporter (BASS) CC (TC 2.A.28) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC11571.1; 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; AY346324; AAQ84722.1; -; mRNA. DR EMBL; DQ122860; AAZ32256.1; -; mRNA. DR EMBL; DQ122861; AAZ32257.1; -; mRNA. DR EMBL; DQ871036; ABI31650.1; -; mRNA. DR EMBL; CR933647; CAI45948.1; -; mRNA. DR EMBL; CH471056; EAX05026.1; -; Genomic_DNA. DR EMBL; BC023288; AAH23288.1; -; mRNA. DR EMBL; BC063471; AAH63471.1; -; mRNA. DR EMBL; BC120971; AAI20972.1; -; mRNA. DR EMBL; BC127626; AAI27627.1; -; mRNA. DR EMBL; BC127627; AAI27628.1; -; mRNA. DR EMBL; BC120970; AAI20971.1; -; mRNA. DR EMBL; BC148252; AAI48253.1; -; mRNA. DR EMBL; BC150308; AAI50309.1; -; mRNA. DR EMBL; AL136728; CAB66662.2; -; mRNA. DR EMBL; AK075364; BAC11571.1; ALT_INIT; mRNA. DR CCDS; CCDS34073.1; -. [Q0GE19-2] DR CCDS; CCDS3768.1; -. [Q0GE19-5] DR CCDS; CCDS75198.1; -. [Q0GE19-1] DR CCDS; CCDS82962.1; -. [Q0GE19-7] DR CCDS; CCDS82963.1; -. [Q0GE19-3] DR CCDS; CCDS82964.1; -. [Q0GE19-6] DR RefSeq; NP_001025169.1; NM_001029998.5. [Q0GE19-2] DR RefSeq; NP_001287771.1; NM_001300842.2. [Q0GE19-1] DR RefSeq; NP_001304745.1; NM_001317816.1. [Q0GE19-3] DR RefSeq; NP_001304746.1; NM_001317817.1. [Q0GE19-7] DR RefSeq; NP_001304747.1; NM_001317818.1. [Q0GE19-6] DR RefSeq; NP_115504.1; NM_032128.4. [Q0GE19-5] DR RefSeq; XP_016864181.1; XM_017008692.1. [Q0GE19-7] DR AlphaFoldDB; Q0GE19; -. DR SMR; Q0GE19; -. DR BioGRID; 123863; 25. DR IntAct; Q0GE19; 11. DR STRING; 9606.ENSP00000421275; -. DR TCDB; 2.A.28.3.1; the bile acid:na(+) symporter (bass) family. DR iPTMnet; Q0GE19; -. DR BioMuta; SLC10A7; -. DR DMDM; 121946408; -. DR EPD; Q0GE19; -. DR jPOST; Q0GE19; -. DR MassIVE; Q0GE19; -. DR MaxQB; Q0GE19; -. DR PaxDb; 9606-ENSP00000421275; -. DR PeptideAtlas; Q0GE19; -. DR ProteomicsDB; 58749; -. [Q0GE19-1] DR ProteomicsDB; 58750; -. [Q0GE19-2] DR ProteomicsDB; 58751; -. [Q0GE19-3] DR ProteomicsDB; 58752; -. [Q0GE19-4] DR ProteomicsDB; 58753; -. [Q0GE19-5] DR Antibodypedia; 27520; 112 antibodies from 21 providers. DR DNASU; 84068; -. DR Ensembl; ENST00000335472.12; ENSP00000334594.8; ENSG00000120519.16. [Q0GE19-2] DR Ensembl; ENST00000394059.8; ENSP00000377623.4; ENSG00000120519.16. [Q0GE19-5] DR Ensembl; ENST00000432059.6; ENSP00000411297.2; ENSG00000120519.16. [Q0GE19-3] DR Ensembl; ENST00000502607.1; ENSP00000422577.1; ENSG00000120519.16. [Q0GE19-6] DR Ensembl; ENST00000507030.5; ENSP00000421275.1; ENSG00000120519.16. [Q0GE19-1] DR Ensembl; ENST00000511374.5; ENSP00000421603.1; ENSG00000120519.16. [Q0GE19-7] DR GeneID; 84068; -. DR KEGG; hsa:84068; -. DR MANE-Select; ENST00000335472.12; ENSP00000334594.8; NM_001029998.6; NP_001025169.1. DR UCSC; uc003ikr.3; human. [Q0GE19-2] DR AGR; HGNC:23088; -. DR CTD; 84068; -. DR DisGeNET; 84068; -. DR GeneCards; SLC10A7; -. DR HGNC; HGNC:23088; SLC10A7. DR HPA; ENSG00000120519; Low tissue specificity. DR MalaCards; SLC10A7; -. DR MIM; 611459; gene. DR MIM; 618363; phenotype. DR neXtProt; NX_Q0GE19; -. DR OpenTargets; ENSG00000120519; -. DR PharmGKB; PA162403478; -. DR VEuPathDB; HostDB:ENSG00000120519; -. DR eggNOG; KOG4821; Eukaryota. DR GeneTree; ENSGT00390000011932; -. DR HOGENOM; CLU_039013_0_0_1; -. DR InParanoid; Q0GE19; -. DR OMA; FFFYGLK; -. DR OrthoDB; 3290500at2759; -. DR PhylomeDB; Q0GE19; -. DR TreeFam; TF329411; -. DR PathwayCommons; Q0GE19; -. DR SignaLink; Q0GE19; -. DR BioGRID-ORCS; 84068; 21 hits in 1155 CRISPR screens. DR ChiTaRS; SLC10A7; human. DR GeneWiki; SLC10A7; -. DR GenomeRNAi; 84068; -. DR Pharos; Q0GE19; Tbio. DR PRO; PR:Q0GE19; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q0GE19; Protein. DR Bgee; ENSG00000120519; Expressed in epithelial cell of pancreas and 158 other cell types or tissues. DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0005797; C:Golgi medial cisterna; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR GO; GO:0060348; P:bone development; IMP:UniProtKB. DR GO; GO:0034436; P:glycoprotein transport; IDA:UniProtKB. DR GO; GO:0048193; P:Golgi vesicle transport; IDA:UniProtKB. DR GO; GO:0030210; P:heparin biosynthetic process; IMP:UniProtKB. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IMP:UniProtKB. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW. DR Gene3D; 1.20.1530.20; -; 1. DR InterPro; IPR038770; Na+/solute_symporter_sf. DR InterPro; IPR016833; Put_Na-Bile_cotransptr. DR PANTHER; PTHR18640:SF5; SODIUM_BILE ACID COTRANSPORTER 7; 1. DR PANTHER; PTHR18640; SOLUTE CARRIER FAMILY 10 MEMBER 7; 1. DR Pfam; PF13593; SBF_like; 1. DR PIRSF; PIRSF026166; UCP026166; 1. DR Genevisible; Q0GE19; HS. PE 1: Evidence at protein level; KW Alternative splicing; Amelogenesis imperfecta; Cell membrane; KW Disease variant; Dwarfism; Endoplasmic reticulum; Golgi apparatus; KW Ion transport; Membrane; Reference proteome; Sodium; Sodium transport; KW Symport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..340 FT /note="Sodium/bile acid cotransporter 7" FT /id="PRO_0000278250" FT TOPO_DOM 1..10 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 11..31 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 32..37 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 38..58 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 59..71 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 72..92 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 93..116 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 117..137 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 138 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 139..159 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 160..163 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 185..201 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 202..222 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 223..234 FT /note="Extracellular" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 235..255 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 256..270 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:17628207" FT TRANSMEM 271..291 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 292..298 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:17628207" FT TRANSMEM 299..319 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 320..340 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:17628207" FT VAR_SEQ 62..85 FT /note="ELTSALVHLKLHLFIQIFTLAFFP -> FADSRLHASACVFCSDFNQGSWWK FT (in isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023215" FT VAR_SEQ 62 FT /note="E -> L (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023216" FT VAR_SEQ 65..340 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023217" FT VAR_SEQ 86..340 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023218" FT VAR_SEQ 133..145 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_023219" FT VAR_SEQ 146..159 FT /note="GIVITPLLLLLFLG -> VSKHSLTCLLQLLL (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023220" FT VAR_SEQ 160..340 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_023221" FT VAR_SEQ 186 FT /note="I -> E (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17628207" FT /id="VSP_023222" FT VAR_SEQ 187..340 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17628207" FT /id="VSP_023223" FT VAR_SEQ 332..340 FT /note="GVKLTRPTV -> KLLQTRGPLANLNNPEGLEYLSIKFGH (in isoform FT 1)" FT /evidence="ECO:0000303|PubMed:17628207" FT /id="VSP_059321" FT VARIANT 74 FT /note="L -> P (in SSASKS; decreased protein levels; FT decreased expression at the cell membrane; FT dbSNP:rs1560980659)" FT /evidence="ECO:0000269|PubMed:30082715" FT /id="VAR_082056" FT VARIANT 112 FT /note="G -> D (in SSASKS; dbSNP:rs1560973571)" FT /evidence="ECO:0000269|PubMed:29878199" FT /id="VAR_082057" FT VARIANT 130 FT /note="G -> R (in SSASKS; uncertain significance; FT dbSNP:rs1560973467)" FT /evidence="ECO:0000269|PubMed:30082715" FT /id="VAR_082058" FT VARIANT 185..340 FT /note="Missing (in SSASKS)" FT /evidence="ECO:0000269|PubMed:30082715" FT /id="VAR_082059" FT VARIANT 303 FT /note="P -> L (in SSASKS; mild skeletal features; results FT in altered regulation of calcium homeostasis and abnormal FT distribution of cellular calcium in patient fibroblasts)" FT /evidence="ECO:0000269|PubMed:31191616" FT /id="VAR_082060" FT CONFLICT 296 FT /note="H -> Y (in Ref. 7; BAC11571)" FT /evidence="ECO:0000305" SQ SEQUENCE 340 AA; 37432 MW; B9D4F4FFAF6DC9DF CRC64; MRLLERMRKD WFMVGIVLAI AGAKLEPSIG VNGGPLKPEI TVSYIAVATI FFNSGLSLKT EELTSALVHL KLHLFIQIFT LAFFPATIWL FLQLLSITPI NEWLLKGLQT VGCMPPPVSS AVILTKAVGG NEAAAIFNSA FGSFLGIVIT PLLLLLFLGS SSSVPFTSIF SQLFMTVVVP LIIGQIVRRY IKDWLERKKP PFGAISSSVL LMIIYTTFCD TFSNPNIDLD KFSLVLILFI IFSIQLSFML LTFIFSTRNN SGFTPADTVA IIFCSTHKSL TLGIPMLKIV FAGHEHLSLI SVPLLIYHPA QILLGSVLVP TIKSWMVSRQ KGVKLTRPTV //