NTCP7_HUMAN
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 03-AUG-2022, entry version 131.
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) (TC
CC 2.A.28) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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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; Q0GE19; -.
DR PeptideAtlas; Q0GE19; -.
DR PRIDE; 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; 96 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 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; 949808at2759; -.
DR PhylomeDB; Q0GE19; -.
DR TreeFam; TF329411; -.
DR PathwayCommons; Q0GE19; -.
DR SignaLink; Q0GE19; -.
DR BioGRID-ORCS; 84068; 20 hits in 1077 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 156 other tissues.
DR Genevisible; Q0GE19; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0006874; P:cellular calcium ion homeostasis; 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: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; PTHR18640; 1.
DR Pfam; PF13593; SBF_like; 1.
DR PIRSF; PIRSF026166; UCP026166; 1.
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; unknown pathological
FT significance; 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
