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Transient receptor potential cation channel subfamily V member 6 (TrpV6) (CaT-like) (CaT-L) (Calcium transport protein 1) (CaT1) (Epithelial calcium channel 2) (ECaC2)

 TRPV6_HUMAN             Reviewed;         765 AA.
Q9H1D0; A4D2I8; Q8TDL3; Q8WXR8; Q96LC5; Q9H1D1; Q9H296;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-APR-2015, sequence version 3.
25-OCT-2017, entry version 157.
RecName: Full=Transient receptor potential cation channel subfamily V member 6;
Short=TrpV6;
AltName: Full=CaT-like {ECO:0000303|PubMed:11278579};
Short=CaT-L {ECO:0000303|PubMed:11278579};
AltName: Full=Calcium transport protein 1 {ECO:0000303|PubMed:11097838};
Short=CaT1 {ECO:0000303|PubMed:11097838};
AltName: Full=Epithelial calcium channel 2;
Short=ECaC2;
Name=TRPV6; Synonyms=ECAC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=11097838; DOI=10.1006/bbrc.2000.3716;
Peng J.-B., Chen X.Z., Berger U.V., Weremowicz S., Morton C.C.,
Vassilev P.M., Brown E.M., Hediger M.A.;
"Human calcium transport protein CaT1.";
Biochem. Biophys. Res. Commun. 278:326-332(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=11545681; DOI=10.1186/1472-6793-1-11;
Wood R.J., Tchack L., Taparia S.;
"1,25-dihydroxyvitamin D3 increases the expression of the CaT1
epithelial calcium channel in the Caco-2 human intestinal cell line.";
BMC Physiol. 1:11-11(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Kidney;
PubMed=11549322; DOI=10.1006/geno.2001.6606;
Peng J.-B., Brown E.M., Hediger M.A.;
"Structural conservation of the genes encoding CaT1, CaT2, and related
cation channels.";
Genomics 76:99-109(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-197; VAL-418 AND
THR-721, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=11278579; DOI=10.1074/jbc.M009895200;
Wissenbach U., Niemeyer B.A., Fixemer T., Schneidewind A., Trost C.,
Cavalie A., Reus K., Meese E., Bonkhoff H., Flockerzi V.;
"Expression of CaT-like, a novel calcium selective channel, correlates
with the malignancy of prostate cancer.";
J. Biol. Chem. 276:19461-19468(2001).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Peng J.-B., Brown E.M., Hediger M.A.;
"A CaT1 splice variant lacking ankyrin repeats.";
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kelsell R.E.;
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-197; VAL-418 AND
THR-721.
SeattleSNPs variation discovery resource;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 41-765.
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[10]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CALMODULIN,
PHOSPHORYLATION AT THR-742, AND MUTAGENESIS OF THR-742.
PubMed=11248124; DOI=10.1073/pnas.051511398;
Niemeyer B.A., Bergs C., Wissenbach U., Flockerzi V., Trost C.;
"Competitive regulation of CaT-like-mediated Ca2+ entry by protein
kinase C and calmodulin.";
Proc. Natl. Acad. Sci. U.S.A. 98:3600-3605(2001).
[11]
FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-582, AND
CALMODULIN-BINDING REGION.
PubMed=15184369; DOI=10.1074/jbc.M404679200;
Bodding M., Flockerzi V.;
"Ca2+ dependence of the Ca2+-selective TRPV6 channel.";
J. Biol. Chem. 279:36546-36552(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION OF
NON-CANONICAL INITIATION CODON, SUBCELLULAR LOCATION, GLYCOSYLATION,
AND TISSUE SPECIFICITY.
PubMed=23612980; DOI=10.1074/jbc.M113.469726;
Fecher-Trost C., Wissenbach U., Beck A., Schalkowsky P., Stoerger C.,
Doerr J., Dembek A., Simon-Thomas M., Weber A., Wollenberg P.,
Ruppert T., Middendorff R., Maurer H.H., Flockerzi V.;
"The in vivo TRPV6 protein starts at a non-AUG triplet, decoded as
methionine, upstream of canonical initiation at AUG.";
J. Biol. Chem. 288:16629-16644(2013).
[14]
INTERACTION WITH TCAF1 AND TCAF2.
PubMed=25559186; DOI=10.1083/jcb.201402076;
Gkika D., Lemonnier L., Shapovalov G., Gordienko D., Poux C.,
Bernardini M., Bokhobza A., Bidaux G., Degerny C., Verreman K.,
Guarmit B., Benahmed M., de Launoit Y., Bindels R.J., Fiorio Pla A.,
Prevarskaya N.;
"TRP channel-associated factors are a novel protein family that
regulates TRPM8 trafficking and activity.";
J. Cell Biol. 208:89-107(2015).
-!- FUNCTION: Calcium selective cation channel that mediates Ca(2+)
uptake in various tissues, including the intestine
(PubMed:11097838, PubMed:11278579, PubMed:11248124
PubMed:15184369, PubMed:23612980). Important for normal Ca(2+) ion
homeostasis in the body, including bone and skin (By similarity).
The channel is activated by low internal calcium level, probably
including intracellular calcium store depletion, and the current
exhibits an inward rectification (PubMed:15184369). Inactivation
includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-
calmodulin-dependent mechanism; the latter may be regulated by
phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a
voltage-independent manner. Heteromeric assembly with TRPV5 seems
to modify channel properties. TRPV5-TRPV6 heteromultimeric
concatemers exhibit voltage-dependent gating.
{ECO:0000250|UniProtKB:Q91WD2, ECO:0000269|PubMed:11097838,
ECO:0000269|PubMed:11248124, ECO:0000269|PubMed:11278579,
ECO:0000269|PubMed:15184369, ECO:0000269|PubMed:23612980}.
-!- SUBUNIT: Homotetramer and probably heterotetramer with TRPV5.
Interacts with TRPV5. Interacts with S100A10 and probably with the
ANAX2-S100A10 heterotetramer. The interaction with S100A10 is
required for the trafficking to the plasma membrane. Interacts
with BSPRY (By similarity). Interacts with TCAF1 and TCAF2 isoform
2 (PubMed:25559186). Interacts with calmodulin (PubMed:11248124).
{ECO:0000250|UniProtKB:Q91WD2, ECO:0000269|PubMed:11248124,
ECO:0000269|PubMed:25559186}.
-!- INTERACTION:
P18031:PTPN1; NbExp=6; IntAct=EBI-7198335, EBI-968788;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11097838,
ECO:0000269|PubMed:11248124, ECO:0000269|PubMed:11278579,
ECO:0000269|PubMed:15184369, ECO:0000269|PubMed:23612980}; Multi-
pass membrane protein {ECO:0000250|UniProtKB:Q91WD2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H1D0-1; Sequence=Displayed;
Name=2;
IsoId=Q9H1D0-2; Sequence=VSP_013439;
-!- TISSUE SPECIFICITY: Expressed at high levels in the
gastrointestinal tract, including esophagus, stomach, duodenum,
jejunum, ileum and colon, and in pancreas, placenta, prostate and
salivary gland. Expressed at moderate levels in liver, kidney and
testis. Expressed in trophoblasts of placenta villus trees (at
protein level)(PubMed:23612980). Expressed in locally advanced
prostate cancer, metastatic and androgen-insensitive prostatic
lesions but not detected in healthy prostate tissue and benign
prostatic hyperplasia. {ECO:0000269|PubMed:11097838,
ECO:0000269|PubMed:11278579, ECO:0000269|PubMed:23612980}.
-!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q91WD2,
ECO:0000269|PubMed:23612980}.
-!- PTM: Phosphorylation at Tyr-201 by SRC leads to an increased
calcium influx through the channel. Probably dephosphorylated at
this site by PTPN1 (By similarity). Phosphorylation by PRKCA at
the calmodulin binding site delays channel inactivation
(PubMed:11248124). {ECO:0000250|UniProtKB:Q9R186,
ECO:0000269|PubMed:11248124}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
TrpV subfamily. TRPV6 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK50426.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
Sequence=AAL40230.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
Sequence=AAM00356.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
Sequence=AAO38052.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
Sequence=BAF84396.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
Sequence=CAC20416.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
Sequence=CAC20417.2; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
Sequence=CAD32311.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
-!- WEB RESOURCE: Name=Wikipedia; Note=TRPV6 entry;
URL="https://en.wikipedia.org/wiki/TRPV6";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/trpv5/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TRPV6ID44425ch7q34.html";
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EMBL; AF304463; AAG41951.1; -; mRNA.
EMBL; AF365927; AAL40230.1; ALT_SEQ; mRNA.
EMBL; AF365928; AAM00356.1; ALT_SEQ; mRNA.
EMBL; AH010730; AAK50426.1; ALT_SEQ; Genomic_DNA.
EMBL; AJ243500; CAC20416.2; ALT_SEQ; mRNA.
EMBL; AJ243501; CAC20417.2; ALT_SEQ; mRNA.
EMBL; AJ487964; CAD32311.1; ALT_SEQ; mRNA.
EMBL; AY225461; AAO38052.1; ALT_SEQ; Genomic_DNA.
EMBL; AK291707; BAF84396.1; ALT_SEQ; mRNA.
EMBL; CH236959; EAL23776.1; -; Genomic_DNA.
CCDS; CCDS5874.2; -. [Q9H1D0-1]
PIR; JC7531; JC7531.
RefSeq; NP_061116.5; NM_018646.5. [Q9H1D0-1]
UniGene; Hs.302740; -.
ProteinModelPortal; Q9H1D0; -.
SMR; Q9H1D0; -.
BioGrid; 120683; 15.
IntAct; Q9H1D0; 2.
MINT; MINT-1472896; -.
STRING; 9606.ENSP00000352358; -.
BindingDB; Q9H1D0; -.
ChEMBL; CHEMBL1628465; -.
TCDB; 1.A.4.2.11; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; Q9H1D0; -.
PhosphoSitePlus; Q9H1D0; -.
DMDM; 62901469; -.
PaxDb; Q9H1D0; -.
PeptideAtlas; Q9H1D0; -.
PRIDE; Q9H1D0; -.
DNASU; 55503; -.
Ensembl; ENST00000638686; ENSP00000492723; ENSG00000165125. [Q9H1D0-1]
GeneID; 55503; -.
KEGG; hsa:55503; -.
UCSC; uc003wbx.4; human. [Q9H1D0-1]
CTD; 55503; -.
DisGeNET; 55503; -.
EuPathDB; HostDB:ENSG00000165125.17; -.
GeneCards; TRPV6; -.
H-InvDB; HIX0007162; -.
HGNC; HGNC:14006; TRPV6.
HPA; HPA062864; -.
MIM; 606680; gene.
neXtProt; NX_Q9H1D0; -.
OpenTargets; ENSG00000165125; -.
PharmGKB; PA37832; -.
eggNOG; KOG3676; Eukaryota.
eggNOG; ENOG4110DG4; LUCA.
GeneTree; ENSGT00550000074425; -.
HOVERGEN; HBG061442; -.
InParanoid; Q9H1D0; -.
KO; K04975; -.
OrthoDB; EOG091G0314; -.
TreeFam; TF314711; -.
Reactome; R-HSA-3295583; TRP channels.
SIGNOR; Q9H1D0; -.
GeneWiki; TRPV6; -.
GenomeRNAi; 55503; -.
PRO; PR:Q9H1D0; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000165125; -.
CleanEx; HS_TRPV6; -.
ExpressionAtlas; Q9H1D0; baseline and differential.
Genevisible; Q9H1D0; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005262; F:calcium channel activity; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0055074; P:calcium ion homeostasis; ISS:UniProtKB.
GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:UniProtKB.
GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; NAS:UniProtKB.
GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
CDD; cd00204; ANK; 2.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR004729; TRP_channel.
InterPro; IPR024862; TRPV.
InterPro; IPR008344; TRPV5/TRPV6.
InterPro; IPR008345; TRPV6_channel.
PANTHER; PTHR10582; PTHR10582; 1.
Pfam; PF00023; Ank; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR01415; ANKYRIN.
PRINTS; PR01765; ECACCHANNEL.
PRINTS; PR01766; ECACCHANNEL1.
SMART; SM00248; ANK; 5.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 2.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Calcium; Calcium channel;
Calcium transport; Calmodulin-binding; Cell membrane;
Complete proteome; Glycoprotein; Ion channel; Ion transport; Membrane;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 765 Transient receptor potential cation
channel subfamily V member 6.
/FTId=PRO_0000215354.
TRANSMEM 368 388 Helical. {ECO:0000250|UniProtKB:Q9R186}.
TRANSMEM 426 448 Helical. {ECO:0000250|UniProtKB:Q9R186}.
TRANSMEM 464 483 Helical. {ECO:0000250|UniProtKB:Q9R186}.
TRANSMEM 490 509 Helical. {ECO:0000250|UniProtKB:Q9R186}.
TRANSMEM 530 552 Helical. {ECO:0000250|UniProtKB:Q9R186}.
INTRAMEM 566 585 Pore-forming.
{ECO:0000250|UniProtKB:Q9R186}.
TRANSMEM 597 617 Helical. {ECO:0000250|UniProtKB:Q9R186}.
REPEAT 84 114 ANK 1.
REPEAT 118 147 ANK 2.
REPEAT 156 185 ANK 3.
REPEAT 202 231 ANK 4.
REPEAT 235 277 ANK 5.
REPEAT 279 308 ANK 5.
REGION 133 143 Interaction with calmodulin.
{ECO:0000250}.
REGION 638 642 Interaction with S100A10. {ECO:0000250}.
REGION 731 751 Interaction with calmodulin.
{ECO:0000269|PubMed:11248124,
ECO:0000269|PubMed:15184369}.
MOTIF 581 585 Selectivity filter.
{ECO:0000250|UniProtKB:Q9R186}.
METAL 582 582 Calcium; shared with neighboring
subunits. {ECO:0000250|UniProtKB:Q9R186}.
MOD_RES 201 201 Phosphotyrosine; by SRC.
{ECO:0000250|UniProtKB:Q9R186}.
MOD_RES 742 742 Phosphothreonine; by PKC/PRKCA.
{ECO:0000269|PubMed:11248124}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 65 232 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_013439.
VARIANT 197 197 C -> R (in dbSNP:rs4987657).
{ECO:0000269|PubMed:11278579,
ECO:0000269|Ref.7}.
/FTId=VAR_022251.
VARIANT 399 399 R -> Q (in dbSNP:rs4987665).
/FTId=VAR_052393.
VARIANT 418 418 M -> V (in dbSNP:rs4987667).
{ECO:0000269|PubMed:11278579,
ECO:0000269|Ref.7}.
/FTId=VAR_022252.
VARIANT 721 721 M -> T (in dbSNP:rs4987682).
{ECO:0000269|PubMed:11278579,
ECO:0000269|Ref.7}.
/FTId=VAR_022253.
MUTAGEN 582 582 D->A: Abolishes channel activity.
{ECO:0000269|PubMed:15184369}.
MUTAGEN 742 742 T->A: Abolishes phosphorylation by
PKC/PRKCA, achieves faster channel
inactivation and no effect on binding to
calmodulin.
{ECO:0000269|PubMed:11248124}.
CONFLICT 77 77 N -> D (in Ref. 1; AAG41951).
{ECO:0000305}.
CONFLICT 114 114 Q -> H (in Ref. 1; AAG41951).
{ECO:0000305}.
SEQUENCE 765 AA; 87286 MW; 626D515E12112546 CRC64;
MGPLQGDGGP ALGGADVAPR LSPVRVWPRP QAPKEPALHP MGLSLPKEKG LILCLWSKFC
RWFQRRESWA QSRDEQNLLQ QKRIWESPLL LAAKDNDVQA LNKLLKYEDC KVHQRGAMGE
TALHIAALYD NLEAAMVLME AAPELVFEPM TSELYEGQTA LHIAVVNQNM NLVRALLARR
ASVSARATGT AFRRSPCNLI YFGEHPLSFA ACVNSEEIVR LLIEHGADIR AQDSLGNTVL
HILILQPNKT FACQMYNLLL SYDRHGDHLQ PLDLVPNHQG LTPFKLAGVE GNTVMFQHLM
QKRKHTQWTY GPLTSTLYDL TEIDSSGDEQ SLLELIITTK KREARQILDQ TPVKELVSLK
WKRYGRPYFC MLGAIYLLYI ICFTMCCIYR PLKPRTNNRT SPRDNTLLQQ KLLQEAYMTP
KDDIRLVGEL VTVIGAIIIL LVEVPDIFRM GVTRFFGQTI LGGPFHVLII TYAFMVLVTM
VMRLISASGE VVPMSFALVL GWCNVMYFAR GFQMLGPFTI MIQKMIFGDL MRFCWLMAVV
ILGFASAFYI IFQTEDPEEL GHFYDYPMAL FSTFELFLTI IDGPANYNVD LPFMYSITYA
AFAIIATLLM LNLLIAMMGD THWRVAHERD ELWRAQIVAT TVMLERKLPR CLWPRSGICG
REYGLGDRWF LRVEDRQDLN RQRIQRYAQA FHTRGSEDLD KDSVEKLELG CPFSPHLSLP
MPSVSRSTSR SSANWERLRQ GTLRRDLRGI INRGLEDGES WEYQI


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