TRPV6_MOUSE
ID TRPV6_MOUSE Reviewed; 767 AA.
AC Q91WD2;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-2015, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transient receptor potential cation channel subfamily V member 6;
DE Short=TrpV6;
DE AltName: Full=Calcium transport protein 1;
DE Short=CaT1;
DE AltName: Full=Epithelial calcium channel 2;
DE Short=ECaC2;
GN Name=Trpv6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 41-767, FUNCTION, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, INTERACTION WITH CALMODULIN, TISSUE SPECIFICITY, AND CALCIUM
RP BINDING.
RC STRAIN=129/SvJ; TISSUE=Placenta;
RX PubMed=12765696; DOI=10.1016/s0143-4160(03)00066-6;
RA Hirnet D., Olausson J., Fecher-Trost C., Boedding M., Nastainczyk W.,
RA Wissenbach U., Flockerzi V., Freichel M.;
RT "The TRPV6 gene, cDNA and protein.";
RL Cell Calcium 33:509-518(2003).
RN [4]
RP IDENTIFICATION OF NON-CANONICAL INITIATION CODON.
RX PubMed=23612980; DOI=10.1074/jbc.m113.469726;
RA Fecher-Trost C., Wissenbach U., Beck A., Schalkowsky P., Stoerger C.,
RA Doerr J., Dembek A., Simon-Thomas M., Weber A., Wollenberg P., Ruppert T.,
RA Middendorff R., Maurer H.H., Flockerzi V.;
RT "The in vivo TRPV6 protein starts at a non-AUG triplet, decoded as
RT methionine, upstream of canonical initiation at AUG.";
RL J. Biol. Chem. 288:16629-16644(2013).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-581.
RX PubMed=12601087; DOI=10.1085/jgp.20028752;
RA Voets T., Janssens A., Prenen J., Droogmans G., Nilius B.;
RT "Mg2+-dependent gating and strong inward rectification of the cation
RT channel TRPV6.";
RL J. Gen. Physiol. 121:245-260(2003).
RN [6]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=12574114; DOI=10.1093/emboj/cdg080;
RA Hoenderop J.G., Voets T., Hoefs S., Weidema F., Prenen J., Nilius B.,
RA Bindels R.J.M.;
RT "Homo- and heterotetrameric architecture of the epithelial Ca2+ channels
RT TRPV5 and TRPV6.";
RL EMBO J. 22:776-785(2003).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH S100A10 AND ANAX2, AND
RP MUTAGENESIS OF THR-639.
RX PubMed=12660155; DOI=10.1093/emboj/cdg162;
RA van de Graaf S.F., Hoenderop J.G., Gkika D., Lamers D., Prenen J.,
RA Rescher U., Gerke V., Staub O., Nilius B., Bindels R.J.M.;
RT "Functional expression of the epithelial Ca(2+) channels (TRPV5 and TRPV6)
RT requires association of the S100A10-annexin 2 complex.";
RL EMBO J. 22:1478-1487(2003).
RN [8]
RP FUNCTION, CHARACTERIZATION OF CHANNEL PORE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF LEU-577; ASP-581 AND TYR-586.
RX PubMed=14736889; DOI=10.1074/jbc.m312076200;
RA Voets T., Janssens A., Droogmans G., Nilius B.;
RT "Outer pore architecture of a Ca2+-selective TRP channel.";
RL J. Biol. Chem. 279:15223-15230(2004).
RN [9]
RP FUNCTION, AND INTERACTION WITH CALMODULIN.
RX PubMed=15123711; DOI=10.1074/jbc.m313637200;
RA Lambers T.T., Weidema A.F., Nilius B., Hoenderop J.G., Bindels R.J.M.;
RT "Regulation of the mouse epithelial Ca2(+) channel TRPV6 by the Ca(2+)-
RT sensor calmodulin.";
RL J. Biol. Chem. 279:28855-28861(2004).
RN [10]
RP INTERACTION WITH BSPRY.
RX PubMed=16380433; DOI=10.1681/asn.2005101025;
RA van de Graaf S.F.J., van der Kemp A.W.C.M., van den Berg D.,
RA van Oorschot M., Hoenderop J.G.J., Bindels R.J.M.;
RT "Identification of BSPRY as a novel auxiliary protein inhibiting TRPV5
RT activity.";
RL J. Am. Soc. Nephrol. 17:26-30(2006).
RN [11]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, INDUCTION BY LOW CALCIUM DIET,
RP AND GLYCOSYLATION.
RX PubMed=17129178; DOI=10.1359/jbmr.061110;
RA Bianco S.D., Peng J.B., Takanaga H., Suzuki Y., Crescenzi A., Kos C.H.,
RA Zhuang L., Freeman M.R., Gouveia C.H., Wu J., Luo H., Mauro T., Brown E.M.,
RA Hediger M.A.;
RT "Marked disturbance of calcium homeostasis in mice with targeted disruption
RT of the Trpv6 calcium channel gene.";
RL J. Bone Miner. Res. 22:274-285(2007).
RN [12]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=20399919; DOI=10.1016/j.bone.2010.04.595;
RA Lieben L., Benn B.S., Ajibade D., Stockmans I., Moermans K., Hediger M.A.,
RA Peng J.B., Christakos S., Bouillon R., Carmeliet G.;
RT "Trpv6 mediates intestinal calcium absorption during calcium restriction
RT and contributes to bone homeostasis.";
RL Bone 47:301-308(2010).
RN [13]
RP FUNCTION, MUTAGENESIS OF ASP-581, AND INDUCTION BY LOW CALCIUM DIET.
RX PubMed=22878123; DOI=10.1152/ajpgi.00089.2012;
RA Woudenberg-Vrenken T.E., Lameris A.L., Weissgerber P., Olausson J.,
RA Flockerzi V., Bindels R.J., Freichel M., Hoenderop J.G.;
RT "Functional TRPV6 channels are crucial for transepithelial Ca2+
RT absorption.";
RL Am. J. Physiol. 303:G879-G885(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 84-305, AND ANK REPEATS.
RX PubMed=18232717; DOI=10.1021/bi702109w;
RA Phelps C.B., Huang R.J., Lishko P.V., Wang R.R., Gaudet R.;
RT "Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV
RT ion channels.";
RL Biochemistry 47:2476-2484(2008).
CC -!- FUNCTION: Calcium selective cation channel that mediates Ca(2+) uptake
CC in various tissues, including the intestine (PubMed:12765696,
CC PubMed:12601087, PubMed:12574114, PubMed:14736889, PubMed:15123711,
CC PubMed:17129178). Important for normal Ca(2+) ion homeostasis in the
CC body, including bone and skin (PubMed:17129178, PubMed:22878123). The
CC channel is activated by low internal calcium level, probably including
CC intracellular calcium store depletion, and the current exhibits an
CC inward rectification. Inactivation includes both a rapid Ca(2+)-
CC dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the
CC latter may be regulated by phosphorylation (PubMed:15123711). In vitro,
CC is slowly inhibited by Mg(2+) in a voltage-independent manner
CC (PubMed:12601087). Heteromeric assembly with TRPV5 seems to modify
CC channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit
CC voltage-dependent gating (PubMed:12574114).
CC {ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12601087,
CC ECO:0000269|PubMed:12660155, ECO:0000269|PubMed:12765696,
CC ECO:0000269|PubMed:14736889, ECO:0000269|PubMed:15123711,
CC ECO:0000269|PubMed:17129178, ECO:0000269|PubMed:22878123}.
CC -!- SUBUNIT: Interacts with TCAF1 and TCAF2 (By similarity). Homotetramer
CC and probably heterotetramer with TRPV5 (PubMed:12574114). Interacts
CC with TRPV5 (PubMed:12574114). 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 (PubMed:12660155).
CC Interacts with calmodulin (PubMed:12765696, PubMed:15123711). Interacts
CC with BSPRY (PubMed:16380433). {ECO:0000250|UniProtKB:Q9H1D0,
CC ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12660155,
CC ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:15123711,
CC ECO:0000269|PubMed:16380433}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12574114,
CC ECO:0000269|PubMed:12601087, ECO:0000269|PubMed:12660155,
CC ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:14736889}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:12660155}.
CC -!- TISSUE SPECIFICITY: Detected in intestine (at protein level)
CC (PubMed:17129178). Abundantly expressed in pancreas and placenta, and
CC to a much lesser extent in stomach and kidney (PubMed:12765696).
CC Detected in kidney and duodenum (PubMed:17129178, PubMed:20399919).
CC {ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:17129178,
CC ECO:0000269|PubMed:20399919}.
CC -!- INDUCTION: Up-regulated in intestine by exposure to a low-calcium diet
CC (PubMed:17129178, PubMed:22878123). Down-regulated in intestine in
CC response to a high-calcium diet (PubMed:17129178).
CC {ECO:0000269|PubMed:17129178, ECO:0000269|PubMed:22878123}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:12574114,
CC ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:17129178}.
CC -!- PTM: Phosphorylation at Tyr-201 and Tyr-202 by SRC leads to an
CC increased calcium influx through the channel. Probably dephosphorylated
CC at these sites by PTPN1 (By similarity). {ECO:0000250|UniProtKB:Q9H1D0,
CC ECO:0000250|UniProtKB:Q9R186}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice have lower body weight than their
CC littermates throughout their lifespan and low fertility, due to
CC impaired calcium homeostasis. Mutant mice display strongly impaired
CC intestinal Ca(2+) uptake and increased urinary Ca(2+) levels
CC (PubMed:17129178). Still, their serum Ca(2+) levels are normal,
CC probably due to compensation by another calcium channel
CC (PubMed:17129178, PubMed:20399919). In spite of this, mutant mice
CC display decreased femoral mineral density; also when they are fed a
CC high-calcium diet (PubMed:17129178). In contrast, no difference in bone
CC density was observed in another study; mutant and wild-type mice
CC displayed similar values when fed a normal diet, and a similar
CC reduction in bone mass when fed a low-calcium diet (PubMed:20399919).
CC Besides, the majority of mutant mice display alopecia and develop
CC dermatitis (PubMed:17129178). {ECO:0000269|PubMed:17129178,
CC ECO:0000269|PubMed:20399919}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. TrpV
CC subfamily. TRPV6 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16101.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
CC Sequence=BAC36699.1; Type=Miscellaneous discrepancy; Note=Unusual initiator. The initiator methionine is coded by a non-canonical ACG threonine codon.; Evidence={ECO:0000305|PubMed:23612980};
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DR EMBL; AK077234; BAC36699.1; ALT_SEQ; mRNA.
DR EMBL; BC016101; AAH16101.1; ALT_SEQ; mRNA.
DR EMBL; AJ542487; CAD62684.1; -; mRNA.
DR CCDS; CCDS20052.2; -.
DR PIR; JC7796; JC7796.
DR RefSeq; NP_071858.3; NM_022413.4.
DR PDB; 2RFA; X-ray; 1.70 A; A=84-305.
DR PDBsum; 2RFA; -.
DR AlphaFoldDB; Q91WD2; -.
DR SMR; Q91WD2; -.
DR STRING; 10090.ENSMUSP00000031902; -.
DR GuidetoPHARMACOLOGY; 512; -.
DR GlyGen; Q91WD2; 1 site.
DR iPTMnet; Q91WD2; -.
DR PhosphoSitePlus; Q91WD2; -.
DR PaxDb; Q91WD2; -.
DR PRIDE; Q91WD2; -.
DR ProteomicsDB; 298318; -.
DR Antibodypedia; 32586; 211 antibodies from 32 providers.
DR DNASU; 64177; -.
DR Ensembl; ENSMUST00000031902; ENSMUSP00000031902; ENSMUSG00000029868.
DR GeneID; 64177; -.
DR KEGG; mmu:64177; -.
DR UCSC; uc009bqc.2; mouse.
DR CTD; 55503; -.
DR MGI; MGI:1927259; Trpv6.
DR eggNOG; KOG3676; Eukaryota.
DR GeneTree; ENSGT00940000156687; -.
DR InParanoid; Q91WD2; -.
DR OMA; ILCLWNK; -.
DR OrthoDB; 693004at2759; -.
DR TreeFam; TF314711; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 64177; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Trpv6; mouse.
DR EvolutionaryTrace; Q91WD2; -.
DR PRO; PR:Q91WD2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q91WD2; protein.
DR Bgee; ENSMUSG00000029868; Expressed in prostate gland ventral lobe and 94 other tissues.
DR ExpressionAtlas; Q91WD2; baseline and differential.
DR GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0005216; F:ion channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB.
DR GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR GO; GO:0098703; P:calcium ion import across plasma membrane; IMP:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IMP:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR GO; GO:0035898; P:parathyroid hormone secretion; IMP:MGI.
DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; -; 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; IPR008344; TRPV5/TRPV6.
DR InterPro; IPR008345; TrpV6.
DR PANTHER; PTHR10582; PTHR10582; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01415; ANKYRIN.
DR PRINTS; PR01765; ECACCHANNEL.
DR PRINTS; PR01766; ECACCHANNEL1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Calmodulin-binding; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..767
FT /note="Transient receptor potential cation channel
FT subfamily V member 6"
FT /id="PRO_0000215355"
FT TOPO_DOM 1..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TOPO_DOM 388..424
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TOPO_DOM 448..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TRANSMEM 463..482
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TOPO_DOM 483..488
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TRANSMEM 489..508
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TOPO_DOM 509..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TRANSMEM 529..551
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TOPO_DOM 552..564
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT INTRAMEM 565..584
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TOPO_DOM 585..595
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT TOPO_DOM 617..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT REPEAT 84..114
FT /note="ANK 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:18232717"
FT REPEAT 118..147
FT /note="ANK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:18232717"
FT REPEAT 156..185
FT /note="ANK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:18232717"
FT REPEAT 202..231
FT /note="ANK 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:18232717"
FT REPEAT 235..276
FT /note="ANK 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:18232717"
FT REPEAT 278..307
FT /note="ANK 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:18232717"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..143
FT /note="Interaction with calmodulin"
FT REGION 637..641
FT /note="Interaction with S100A10"
FT /evidence="ECO:0000250"
FT REGION 689..707
FT /note="Interaction with calmodulin"
FT MOTIF 580..584
FT /note="Selectivity filter"
FT /evidence="ECO:0000269|PubMed:14736889"
FT BINDING 581
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 201
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT MOD_RES 202
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:Q9R186"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 577
FT /note="L->C: Abolishes channel activity."
FT /evidence="ECO:0000269|PubMed:14736889"
FT MUTAGEN 581
FT /note="D->A: Abolishes binding of Mg(2+) and increases pore
FT diameter. Impairs intestinal Ca(2+) uptake."
FT /evidence="ECO:0000269|PubMed:12601087,
FT ECO:0000269|PubMed:14736889, ECO:0000269|PubMed:22878123"
FT MUTAGEN 581
FT /note="D->C: Abolishes channel activity."
FT /evidence="ECO:0000269|PubMed:12601087,
FT ECO:0000269|PubMed:14736889"
FT MUTAGEN 581
FT /note="D->G: Increases pore diameter."
FT /evidence="ECO:0000269|PubMed:12601087,
FT ECO:0000269|PubMed:14736889"
FT MUTAGEN 586
FT /note="Y->C: Abolishes channel activity."
FT /evidence="ECO:0000269|PubMed:14736889"
FT MUTAGEN 639
FT /note="T->A: Abolishes plasma membrane localization and
FT channel activity."
FT /evidence="ECO:0000269|PubMed:12660155"
FT CONFLICT 1
FT /note="M -> E (in Ref. 1; BAC36699)"
FT /evidence="ECO:0000305"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 122..128
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:2RFA"
FT TURN 153..157
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 216..224
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 239..244
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 282..289
FT /evidence="ECO:0007829|PDB:2RFA"
FT HELIX 292..304
FT /evidence="ECO:0007829|PDB:2RFA"
SQ SEQUENCE 767 AA; 87387 MW; FBD937FB9C55F9BA CRC64;
MGPLQREDRP ALGGANVAPG SSPVGVWHQP QPPKEPAFHP MGWSLPKEKG LILCLWNKFC
RWFHRQESWA QSRDEQNLLQ QKRIWESPLL LAAKENDVQA LSKLLKFEGC EVHQRGAMGE
TALHIAALYD NLEAAMVLME AAPELVFEPM TSELYEGQTA LHIAVINQNV NLVRALLARG
ASVSARATGS VFHYRPHNLI YYGEHPLSFA ACVGSEEIVR LLIEHGADIR AQDSLGNTVL
HILILQPNKT FACQMYNLLL SYDGGDHLKS LELVPNNQGL TPFKLAGVEG NIVMFQHLMQ
KRKHIQWTYG PLTSTLYDLT EIDSSGDDQS LLELIVTTKK REARQILDQT PVKELVSLKW
KRYGRPYFCV LGAIYVLYII CFTMCCVYRP LKPRITNRTN PRDNTLMQQK LLQEAYVTPK
DDLRLVGELV SIVGAVIILL VEIPDIFRLG VTRFFGQTIL GGPFHVIIIT YAFMVLVTMV
MRLTNVDGEV VPMSFALVLG WCNVMYFARG FQMLGPFTIM IQKMIFGDLM RFCWLMAVVI
LGFASAFYII FQTEDPDELG HFYDYPMALF STFELFLTII DGPANYDVDL PFMYSVTYAA
FAIIATLLML NLLIAMMGDT HWRVAHERDE LWRAQVVATT VMLERKLPRC LWPRSGICGR
EYGLGDRWFL RVEDRQDLNR QRIRRYAQAF QQQDGLYSED LEKDSGEKLE TARPFGAYLS
FPTPSVSRST SRSSTNWERL RQGALRKDLR GIINRGLEDG EGWEYQI
