ID   TRPV5_HUMAN             Reviewed;         729 AA.
AC   Q9NQA5; A0A0A6YY98; A4D2H7; E9PBZ6; Q8N4C1; Q8NDW5; Q8NDX7; Q8NDX8; Q96PM6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 3.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Transient receptor potential cation channel subfamily V member 5;
DE            Short=TrpV5;
DE   AltName: Full=Calcium transport protein 2;
DE            Short=CaT2;
DE   AltName: Full=Epithelial calcium channel 1 {ECO:0000303|PubMed:10945469};
DE            Short=ECaC;
DE            Short=ECaC1;
DE   AltName: Full=Osm-9-like TRP channel 3;
DE            Short=OTRPC3;
GN   Name=TRPV5; Synonyms=ECAC1 {ECO:0000303|PubMed:10945469};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-154 AND ALA-563, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=10945469; DOI=10.1006/geno.2000.6203;
RA   Mueller D., Hoenderop J.G., Meij I.C., van den Heuvel L.P.J., Knoers N.V.,
RA   den Hollander A.I., Eggert P., Garcia-Nieto V., Claverie-Martin F.,
RA   Bindels R.J.M.;
RT   "Molecular cloning, tissue distribution, and chromosomal mapping of the
RT   human epithelial calcium channel (ECAC1).";
RL   Genomics 67:48-53(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-154 AND ALA-563,
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11549322; DOI=10.1006/geno.2001.6606;
RA   Peng J.-B., Brown E.M., Hediger M.A.;
RT   "Structural conservation of the genes encoding CaT1, CaT2, and related
RT   cation channels.";
RL   Genomics 76:99-109(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-563.
RA   Kelsell R.E.;
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-8; ARG-154; ALA-563 AND
RP   PHE-712.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ARG-154 AND
RP   ALA-563.
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon;
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   [9]
RP   FUNCTION, GLYCOSYLATION AT ASN-358, SUBCELLULAR LOCATION, ACTIVITY
RP   REGULATION, AND MUTAGENESIS OF ASN-358.
RX   PubMed=18768590; DOI=10.1152/ajprenal.90229.2008;
RA   Zhang W., Na T., Peng J.B.;
RT   "WNK3 positively regulates epithelial calcium channels TRPV5 and TRPV6 via
RT   a kinase-dependent pathway.";
RL   Am. J. Physiol. 295:F1472-F1484(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC   -!- FUNCTION: Constitutively active calcium selective cation channel
CC       thought to be involved in Ca(2+) reabsorption in kidney and intestine
CC       (PubMed:11549322, PubMed:18768590). Required for normal Ca(2+)
CC       reabsorption in the kidney distal convoluted tubules (By similarity).
CC       The channel is activated by low internal calcium level and the current
CC       exhibits an inward rectification (PubMed:11549322, PubMed:18768590). A
CC       Ca(2+)-dependent feedback regulation includes fast channel inactivation
CC       and slow current decay (By similarity). Heteromeric assembly with TRPV6
CC       seems to modify channel properties. TRPV5-TRPV6 heteromultimeric
CC       concatemers exhibit voltage-dependent gating (By similarity).
CC       {ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9XSM3,
CC       ECO:0000269|PubMed:11549322, ECO:0000269|PubMed:18768590}.
CC   -!- ACTIVITY REGULATION: Activated by WNK3. {ECO:0000269|PubMed:18768590}.
CC   -!- SUBUNIT: Homotetramer and probably heterotetramer with TRPV6. Interacts
CC       with TRPV6 (By similarity). Interacts with S100A10 and probably with
CC       the ANAX2-S100A10 heterotetramer. The interaction with S100A10 is
CC       required for the trafficking to the plasma membrane. Interacts with
CC       calmodulin. Interacts with BSPRY, which results in its inactivation.
CC       {ECO:0000250|UniProtKB:P69744, ECO:0000250|UniProtKB:Q9XSM3}.
CC   -!- INTERACTION:
CC       Q9NQA5; P05937: CALB1; NbExp=4; IntAct=EBI-751281, EBI-4286943;
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:18768590}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:18768590}. Note=Colocalized with S100A10 and ANAX2
CC       along the apical domain of kidney distal tubular cells (By similarity).
CC       The expression of the glycosylated form in the cell membrane is
CC       increased in the presence of WNK3 (PubMed:18768590).
CC       {ECO:0000250|UniProtKB:P69744, ECO:0000269|PubMed:18768590}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9NQA5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9NQA5-2; Sequence=VSP_057199, VSP_057200;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in kidney, small intestine
CC       and pancreas, and at lower levels in testis, prostate, placenta, brain,
CC       colon and rectum. {ECO:0000269|PubMed:10945469,
CC       ECO:0000269|PubMed:11549322}.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:18768590}.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC       subfamily. TRPV5 sub-subfamily. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=SeattleSNPs;
CC       URL="http://pga.gs.washington.edu/data/trpv5/";
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DR   EMBL; AJ271207; CAB96365.2; -; mRNA.
DR   EMBL; AF304464; AAL04015.1; -; mRNA.
DR   EMBL; AJ487965; CAD32312.2; -; mRNA.
DR   EMBL; AY206695; AAO13488.1; -; Genomic_DNA.
DR   EMBL; AC245427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236959; EAL23777.1; -; Genomic_DNA.
DR   EMBL; CH471198; EAW51896.1; -; Genomic_DNA.
DR   EMBL; BC034740; AAH34740.1; -; mRNA.
DR   CCDS; CCDS5875.1; -. [Q9NQA5-1]
DR   RefSeq; NP_062815.3; NM_019841.6. [Q9NQA5-1]
DR   PDB; 5OEO; NMR; -; C=655-725.
DR   PDBsum; 5OEO; -.
DR   AlphaFoldDB; Q9NQA5; -.
DR   BMRB; Q9NQA5; -.
DR   SMR; Q9NQA5; -.
DR   BioGRID; 121137; 29.
DR   IntAct; Q9NQA5; 13.
DR   MINT; Q9NQA5; -.
DR   STRING; 9606.ENSP00000265310; -.
DR   BindingDB; Q9NQA5; -.
DR   ChEMBL; CHEMBL1628474; -.
DR   DrugBank; DB11093; Calcium citrate.
DR   DrugBank; DB11348; Calcium Phosphate.
DR   DrugBank; DB14481; Calcium phosphate dihydrate.
DR   GuidetoPHARMACOLOGY; 511; -.
DR   TCDB; 1.A.4.2.10; the transient receptor potential ca2+/cation channel (trp-cc) family.
DR   GlyCosmos; Q9NQA5; 1 site, No reported glycans.
DR   GlyGen; Q9NQA5; 1 site.
DR   iPTMnet; Q9NQA5; -.
DR   PhosphoSitePlus; Q9NQA5; -.
DR   SwissPalm; Q9NQA5; -.
DR   BioMuta; TRPV5; -.
DR   DMDM; 62901471; -.
DR   EPD; Q9NQA5; -.
DR   MassIVE; Q9NQA5; -.
DR   MaxQB; Q9NQA5; -.
DR   PaxDb; 9606-ENSP00000265310; -.
DR   PeptideAtlas; Q9NQA5; -.
DR   ProteomicsDB; 19327; -.
DR   ProteomicsDB; 82119; -. [Q9NQA5-1]
DR   Antibodypedia; 32594; 354 antibodies from 35 providers.
DR   DNASU; 56302; -.
DR   Ensembl; ENST00000265310.6; ENSP00000265310.1; ENSG00000127412.7. [Q9NQA5-1]
DR   Ensembl; ENST00000442623.1; ENSP00000406572.1; ENSG00000127412.7. [Q9NQA5-2]
DR   Ensembl; ENST00000621710.2; ENSP00000483049.1; ENSG00000274348.2. [Q9NQA5-1]
DR   Ensembl; ENST00000633067.1; ENSP00000488418.1; ENSG00000274348.2. [Q9NQA5-2]
DR   GeneID; 56302; -.
DR   KEGG; hsa:56302; -.
DR   MANE-Select; ENST00000265310.6; ENSP00000265310.1; NM_019841.7; NP_062815.3.
DR   UCSC; uc003wbz.3; human. [Q9NQA5-1]
DR   AGR; HGNC:3145; -.
DR   CTD; 56302; -.
DR   DisGeNET; 56302; -.
DR   GeneCards; TRPV5; -.
DR   HGNC; HGNC:3145; TRPV5.
DR   HPA; ENSG00000127412; Group enriched (brain, kidney).
DR   MIM; 606679; gene.
DR   neXtProt; NX_Q9NQA5; -.
DR   OpenTargets; ENSG00000127412; -.
DR   PharmGKB; PA35045; -.
DR   VEuPathDB; HostDB:ENSG00000127412; -.
DR   eggNOG; KOG3676; Eukaryota.
DR   GeneTree; ENSGT00940000161809; -.
DR   HOGENOM; CLU_062553_0_0_1; -.
DR   InParanoid; Q9NQA5; -.
DR   OMA; AYETHED; -.
DR   OrthoDB; 1003028at2759; -.
DR   PhylomeDB; Q9NQA5; -.
DR   TreeFam; TF314711; -.
DR   PathwayCommons; Q9NQA5; -.
DR   Reactome; R-HSA-3295583; TRP channels.
DR   SignaLink; Q9NQA5; -.
DR   SIGNOR; Q9NQA5; -.
DR   BioGRID-ORCS; 56302; 13 hits in 1139 CRISPR screens.
DR   GeneWiki; TRPV5; -.
DR   GenomeRNAi; 56302; -.
DR   Pharos; Q9NQA5; Tchem.
DR   PRO; PR:Q9NQA5; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9NQA5; Protein.
DR   Bgee; ENSG00000127412; Expressed in C1 segment of cervical spinal cord and 29 other cell types or tissues.
DR   ExpressionAtlas; Q9NQA5; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:UniProtKB.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; ISS:UniProtKB.
DR   GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR   GO; GO:0035809; P:regulation of urine volume; ISS:UniProtKB.
DR   CDD; cd22296; CBD_TRPV5_C; 1.
DR   CDD; cd22192; TRPV5-6; 1.
DR   DisProt; DP01765; -.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR024862; TRPV.
DR   InterPro; IPR008346; TRPV5.
DR   InterPro; IPR008344; TRPV5/TRPV6.
DR   NCBIfam; TIGR00870; trp; 1.
DR   PANTHER; PTHR10582:SF11; TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V MEMBER 5; 1.
DR   PANTHER; PTHR10582; TRANSIENT RECEPTOR POTENTIAL ION CHANNEL PROTEIN; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   PRINTS; PR01765; ECACCHANNEL.
DR   PRINTS; PR01767; ECACCHANNEL2.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   Genevisible; Q9NQA5; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW   Calcium transport; Calmodulin-binding; Cell membrane; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Metal-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..729
FT                   /note="Transient receptor potential cation channel
FT                   subfamily V member 5"
FT                   /id="PRO_0000215350"
FT   TOPO_DOM        1..327
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TRANSMEM        328..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TOPO_DOM        349..385
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TRANSMEM        386..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TOPO_DOM        409..419
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TRANSMEM        420..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TOPO_DOM        443..448
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TRANSMEM        449..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TOPO_DOM        470..492
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   INTRAMEM        524..544
FT                   /note="Pore-forming"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TRANSMEM        557..577
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   TOPO_DOM        578..729
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XSM3"
FT   REPEAT          44..74
FT                   /note="ANK 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          78..107
FT                   /note="ANK 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          116..145
FT                   /note="ANK 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          162..191
FT                   /note="ANK 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          195..228
FT                   /note="ANK 5"
FT                   /evidence="ECO:0000255"
FT   REPEAT          239..268
FT                   /note="ANK 6"
FT                   /evidence="ECO:0000255"
FT   REGION          598..602
FT                   /note="Interaction with S100A10"
FT                   /evidence="ECO:0000250|UniProtKB:P69744"
FT   REGION          650..653
FT                   /note="Involved in Ca(2+)-dependent inactivation"
FT                   /evidence="ECO:0000250"
FT   REGION          654..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..729
FT                   /note="Involved in Ca(2+)-dependent inactivation"
FT                   /evidence="ECO:0000250"
FT   BINDING         542
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_note="ligand shared between two neighboring
FT                   subunits"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R186"
FT   MOD_RES         685
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P69744"
FT   MOD_RES         689
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P69744"
FT   CARBOHYD        358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18768590"
FT   VAR_SEQ         375..381
FT                   /note="EAYETRE -> VILLRRG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057199"
FT   VAR_SEQ         382..729
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057200"
FT   VARIANT         8
FT                   /note="A -> V (in dbSNP:rs4252372)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_022247"
FT   VARIANT         154
FT                   /note="H -> R (in dbSNP:rs4236480)"
FT                   /evidence="ECO:0000269|PubMed:10945469,
FT                   ECO:0000269|PubMed:11549322, ECO:0000269|Ref.4,
FT                   ECO:0000269|Ref.7"
FT                   /id="VAR_022248"
FT   VARIANT         563
FT                   /note="T -> A (in dbSNP:rs4252499)"
FT                   /evidence="ECO:0000269|PubMed:10945469,
FT                   ECO:0000269|PubMed:11549322, ECO:0000269|Ref.3,
FT                   ECO:0000269|Ref.4, ECO:0000269|Ref.7"
FT                   /id="VAR_022249"
FT   VARIANT         712
FT                   /note="L -> F (in dbSNP:rs4252509)"
FT                   /evidence="ECO:0000269|Ref.4"
FT                   /id="VAR_022250"
FT   MUTAGEN         358
FT                   /note="N->Q: Loss of glycosylation."
FT                   /evidence="ECO:0000269|PubMed:18768590"
FT   HELIX           699..709
FT                   /evidence="ECO:0007829|PDB:5OEO"
FT   STRAND          719..722
FT                   /evidence="ECO:0007829|PDB:5OEO"
SQ   SEQUENCE   729 AA;  82562 MW;  DAF91FF9E9ECE118 CRC64;
     MGGFLPKAEG PGSQLQKLLP SFLVREQDWD QHLDKLHMLQ QKRILESPLL RASKENDLSV
     LRQLLLDCTC DVRQRGALGE TALHIAALYD NLEAALVLME AAPELVFEPT TCEAFAGQTA
     LHIAVVNQNV NLVRALLTRR ASVSARATGT AFRHSPRNLI YFGEHPLSFA ACVNSEEIVR
     LLIEHGADIR AQDSLGNTVL HILILQPNKT FACQMYNLLL SYDGHGDHLQ PLDLVPNHQG
     LTPFKLAGVE GNTVMFQHLM QKRRHIQWTY GPLTSILYDL TEIDSWGEEL SFLELVVSSD
     KREARQILEQ TPVKELVSFK WNKYGRPYFC ILAALYLLYM ICFTTCCVYR PLKFRGGNRT
     HSRDITILQQ KLLQEAYETR EDIIRLVGEL VSIVGAVIIL LLEIPDIFRV GASRYFGKTI
     LGGPFHVIII TYASLVLVTM VMRLTNTNGE VVPMSFALVL GWCSVMYFTR GFQMLGPFTI
     MIQKMIFGDL MRFCWLMAVV ILGFASAFYI IFQTEDPTSL GQFYDYPMAL FTTFELFLTV
     IDAPANYDVD LPFMFSIVNF AFTIIATLLM LNLFIAMMGD THWRVAQERD ELWRAQVVAT
     TVMLERKLPR CLWPRSGICG CEFGLGDRWF LRVENHNDQN PLRVLRYVEV FKNSDKEDDQ
     EHPSEKQPSG AESGTLARAS LALPTSSLSR TASQSSSHRG WEILRQNTLG HLNLGLNLSE
     GDGEEVYHF
//