CAC1I_HUMAN
ID CAC1I_HUMAN Reviewed; 2223 AA.
AC Q9P0X4; B0QY12; B0QY13; B0QY14; O95504; Q5JZ88; Q7Z6S9; Q8NFX6; Q9NZC8;
AC Q9UH15; Q9UH30; Q9ULU9; Q9UNE6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1I;
DE AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.3;
DE Short=Ca(v)3.3;
GN Name=CACNA1I; Synonyms=KIAA1120;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=10454147; DOI=10.1016/s0304-3940(99)00319-5;
RA Mittman S., Guo J., Emerick M.C., Agnew W.S.;
RT "Structure and alternative splicing of the gene encoding alpha1I, a human
RT brain T calcium channel alpha1 subunit.";
RL Neurosci. Lett. 269:121-124(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10749850; DOI=10.1074/jbc.c000090200;
RA Monteil A., Chemin J., Leuranguer V., Altier C., Mennessier G.,
RA Bourinet E., Lory P., Nargeot J.;
RT "Specific properties of T-type calcium channels generated by the human
RT alpha1I subunit.";
RL J. Biol. Chem. 275:16530-16535(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT VAL-1040.
RC TISSUE=Brain;
RX PubMed=12080115; DOI=10.1016/s0006-3495(02)75164-3;
RA Gomora J.C., Murbartian J., Arias J.M., Lee J.-H., Perez-Reyes E.;
RT "Cloning and expression of the human T-type channel Ca(v)3.3: insights into
RT prepulse facilitation.";
RL Biophys. J. 83:229-241(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1200-2223 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [6]
RP INTERACTION WITH CATSPER1 AND CATSPER2.
RX PubMed=16740636; DOI=10.1074/jbc.m511288200;
RA Zhang D., Chen J., Saraf A., Cassar S., Han P., Rogers J.C., Brioni J.D.,
RA Sullivan J.P., Gopalakrishnan M.;
RT "Association of Catsper1 or -2 with Ca(v)3.3 leads to suppression of T-type
RT calcium channel activity.";
RL J. Biol. Chem. 281:22332-22341(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry
CC of calcium ions into excitable cells and are also involved in a variety
CC of calcium-dependent processes, including muscle contraction, hormone
CC or neurotransmitter release, gene expression, cell motility, cell
CC division and cell death. This channel gives rise to T-type calcium
CC currents. T-type calcium channels belong to the 'low-voltage activated
CC (LVA)' group and are strongly blocked by nickel and mibefradil. A
CC particularity of this type of channels is an opening at quite negative
CC potentials, and a voltage-dependent inactivation. T-type channels serve
CC pacemaking functions in both central neurons and cardiac nodal cells
CC and support calcium signaling in secretory cells and vascular smooth
CC muscle. They may also be involved in the modulation of firing patterns
CC of neurons which is important for information processing as well as in
CC cell growth processes. Gates in voltage ranges similar to, but higher
CC than alpha 1G or alpha 1H (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CATSPER1 and CATSPER2, leading to suppress T-
CC type calcium channel activity. {ECO:0000269|PubMed:16740636}.
CC -!- INTERACTION:
CC Q9P0X4; Q8NEC5: CATSPER1; NbExp=5; IntAct=EBI-1220829, EBI-744545;
CC Q9P0X4; Q96P56: CATSPER2; NbExp=3; IntAct=EBI-1220829, EBI-2215024;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Delta36b;
CC IsoId=Q9P0X4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9P0X4-2; Sequence=VSP_000951;
CC Name=3; Synonyms=Alpha1I-a;
CC IsoId=Q9P0X4-3; Sequence=VSP_000950, VSP_000951;
CC Name=4;
CC IsoId=Q9P0X4-4; Sequence=VSP_000950;
CC -!- TISSUE SPECIFICITY: Brain specific.
CC -!- DOMAIN: Each of the four internal repeats contains five hydrophobic
CC transmembrane segments (S1, S2, S3, S5, S6) and one positively charged
CC transmembrane segment (S4). S4 segments probably represent the voltage-
CC sensor and are characterized by a series of positively charged amino
CC acids at every third position.
CC -!- PTM: In response to raising of intracellular calcium, the T-type
CC channels are activated by CaM-kinase II. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit (TC
CC 1.A.1.11) family. CACNA1I subfamily. {ECO:0000305}.
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DR EMBL; AF129133; AAD45251.1; -; mRNA.
DR EMBL; AF142567; AAF25722.1; -; mRNA.
DR EMBL; AF211189; AAF44626.1; -; mRNA.
DR EMBL; AF393329; AAM67414.1; -; mRNA.
DR EMBL; AL008716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL022312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL022319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB032946; BAA86434.1; -; mRNA.
DR CCDS; CCDS46710.1; -. [Q9P0X4-1]
DR CCDS; CCDS46711.1; -. [Q9P0X4-4]
DR RefSeq; NP_001003406.1; NM_001003406.1. [Q9P0X4-4]
DR RefSeq; NP_066919.2; NM_021096.3. [Q9P0X4-1]
DR AlphaFoldDB; Q9P0X4; -.
DR SMR; Q9P0X4; -.
DR BioGRID; 114425; 3.
DR IntAct; Q9P0X4; 3.
DR STRING; 9606.ENSP00000385019; -.
DR BindingDB; Q9P0X4; -.
DR ChEMBL; CHEMBL5558; -.
DR DrugBank; DB01118; Amiodarone.
DR DrugBank; DB00381; Amlodipine.
DR DrugBank; DB09231; Benidipine.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB09061; Cannabidiol.
DR DrugBank; DB00568; Cinnarizine.
DR DrugBank; DB09235; Efonidipine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB00153; Ergocalciferol.
DR DrugBank; DB04841; Flunarizine.
DR DrugBank; DB09238; Manidipine.
DR DrugBank; DB14009; Medical Cannabis.
DR DrugBank; DB01388; Mibefradil.
DR DrugBank; DB14011; Nabiximols.
DR DrugBank; DB01115; Nifedipine.
DR DrugBank; DB06152; Nylidrin.
DR DrugBank; DB00617; Paramethadione.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB09498; Strontium chloride Sr-89.
DR DrugBank; DB09089; Trimebutine.
DR DrugBank; DB00909; Zonisamide.
DR DrugCentral; Q9P0X4; -.
DR GuidetoPHARMACOLOGY; 537; -.
DR TCDB; 1.A.1.11.7; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q9P0X4; 5 sites.
DR iPTMnet; Q9P0X4; -.
DR PhosphoSitePlus; Q9P0X4; -.
DR BioMuta; CACNA1I; -.
DR DMDM; 23396521; -.
DR EPD; Q9P0X4; -.
DR MassIVE; Q9P0X4; -.
DR PaxDb; Q9P0X4; -.
DR PeptideAtlas; Q9P0X4; -.
DR PRIDE; Q9P0X4; -.
DR ProteomicsDB; 83622; -. [Q9P0X4-1]
DR ProteomicsDB; 83623; -. [Q9P0X4-2]
DR ProteomicsDB; 83624; -. [Q9P0X4-3]
DR ProteomicsDB; 83625; -. [Q9P0X4-4]
DR Antibodypedia; 26656; 101 antibodies from 25 providers.
DR DNASU; 8911; -.
DR Ensembl; ENST00000401624.5; ENSP00000383887.1; ENSG00000100346.18. [Q9P0X4-2]
DR Ensembl; ENST00000402142.4; ENSP00000385019.3; ENSG00000100346.18. [Q9P0X4-1]
DR Ensembl; ENST00000404898.5; ENSP00000384093.1; ENSG00000100346.18. [Q9P0X4-4]
DR Ensembl; ENST00000407673.5; ENSP00000385680.1; ENSG00000100346.18. [Q9P0X4-3]
DR GeneID; 8911; -.
DR KEGG; hsa:8911; -.
DR MANE-Select; ENST00000402142.4; ENSP00000385019.3; NM_021096.4; NP_066919.2.
DR UCSC; uc003ayc.5; human. [Q9P0X4-1]
DR CTD; 8911; -.
DR DisGeNET; 8911; -.
DR GeneCards; CACNA1I; -.
DR HGNC; HGNC:1396; CACNA1I.
DR HPA; ENSG00000100346; Tissue enhanced (brain, thyroid gland).
DR MIM; 608230; gene.
DR neXtProt; NX_Q9P0X4; -.
DR OpenTargets; ENSG00000100346; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR PharmGKB; PA26011; -.
DR VEuPathDB; HostDB:ENSG00000100346; -.
DR eggNOG; KOG2302; Eukaryota.
DR GeneTree; ENSGT00940000158594; -.
DR HOGENOM; CLU_000540_2_0_1; -.
DR InParanoid; Q9P0X4; -.
DR OMA; NWCIKMA; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; Q9P0X4; -.
DR TreeFam; TF313555; -.
DR PathwayCommons; Q9P0X4; -.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR SignaLink; Q9P0X4; -.
DR BioGRID-ORCS; 8911; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; CACNA1I; human.
DR GeneWiki; CACNA1I; -.
DR GenomeRNAi; 8911; -.
DR Pharos; Q9P0X4; Tclin.
DR PRO; PR:Q9P0X4; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9P0X4; protein.
DR Bgee; ENSG00000100346; Expressed in Brodmann (1909) area 23 and 116 other tissues.
DR Genevisible; Q9P0X4; HS.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0008332; F:low voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; TAS:ProtInc.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0070509; P:calcium ion import; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; IEA:InterPro.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0030431; P:sleep; IEA:Ensembl.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR030162; CACNA1I.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR005445; VDCC_T_a1.
DR InterPro; IPR002077; VDCCAlpha1.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR PANTHER; PTHR10037:SF209; PTHR10037:SF209; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR PRINTS; PR00167; CACHANNEL.
DR PRINTS; PR01629; TVDCCALPHA1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..2223
FT /note="Voltage-dependent T-type calcium channel subunit
FT alpha-1I"
FT /id="PRO_0000053957"
FT TOPO_DOM 1..78
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 79..99
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 100..120
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..168
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..191
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..640
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..676
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 677..697
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 698..702
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 703..721
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 722..729
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..753
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..764
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 765..785
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 786..841
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 842..862
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000255"
FT TOPO_DOM 863..1166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1167..1187
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1188..1209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1210..1230
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1231..1244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1245..1265
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1266..1272
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1273..1294
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1295..1304
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1305..1325
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1326..1410
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1411..1431
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1432..1485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1486..1506
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1507..1522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1523..1543
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1544..1556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1557..1577
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1578..1583
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1584..1607
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1608..1621
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1622..1642
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1643..1709
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1710..1730
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1731..2223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 66..401
FT /note="I"
FT REPEAT 626..865
FT /note="II"
FT REPEAT 1157..1434
FT /note="III"
FT REPEAT 1472..1733
FT /note="IV"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1758..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1868..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1937..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2013..2062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2076..2223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1881..1897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2013..2038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2082..2100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2193..2211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 357
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 821
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1380
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT SITE 1678
FT /note="Calcium ion selectivity and permeability"
FT /evidence="ECO:0000250"
FT MOD_RES 1058
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0Y8"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 488..523
FT /note="HGKTKGQGDEGRHLGSRHCQTLHGPASPGNDHSGRE -> Q (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10749850,
FT ECO:0000303|PubMed:12080115"
FT /id="VSP_000950"
FT VAR_SEQ 2010..2223
FT /note="ATGSDTSLDASPSSSAGSLQTTLEDSLTLSDSPRRALGPPAPAPGPRAGLSP
FT AARRRLSLRGRGLFSLRGLRAHQRSHSSGGSTSPGCTHHDSMDPSDEEGRGGAGGGGAG
FT SEHSETLSSLSLTSLFCPPPPPPAPGLTPARKFSSTSSLAAPGRPHAAALAHGLARSPS
FT WAADRSKDPPGRAPLPMGLGPLAPPPQPLPGELEPGDAASKRKR -> VPTPPRP (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10454147,
FT ECO:0000303|PubMed:10749850"
FT /id="VSP_000951"
FT VARIANT 1040
FT /note="I -> V (in dbSNP:rs136853)"
FT /evidence="ECO:0000269|PubMed:12080115"
FT /id="VAR_013883"
FT VARIANT 1513
FT /note="T -> M (in dbSNP:rs8141262)"
FT /id="VAR_048745"
FT VARIANT 1782
FT /note="G -> A (in dbSNP:rs2294369)"
FT /id="VAR_013884"
FT VARIANT 1782
FT /note="G -> R (in dbSNP:rs2294369)"
FT /id="VAR_020050"
SQ SEQUENCE 2223 AA; 245103 MW; 3CAE4D1C4289D08B CRC64;
MAESASPPSS SAAAPAAEPG VTTEQPGPRS PPSSPPGLEE PLDGADPHVP HPDLAPIAFF
CLRQTTSPRN WCIKMVCNPW FECVSMLVIL LNCVTLGMYQ PCDDMDCLSD RCKILQVFDD
FIFIFFAMEM VLKMVALGIF GKKCYLGDTW NRLDFFIVMA GMVEYSLDLQ NINLSAIRTV
RVLRPLKAIN RVPSMRILVN LLLDTLPMLG NVLLLCFFVF FIFGIIGVQL WAGLLRNRCF
LEENFTIQGD VALPPYYQPE EDDEMPFICS LSGDNGIMGC HEIPPLKEQG RECCLSKDDV
YDFGAGRQDL NASGLCVNWN RYYNVCRTGS ANPHKGAINF DNIGYAWIVI FQVITLEGWV
EIMYYVMDAH SFYNFIYFIL LIIVGSFFMI NLCLVVIATQ FSETKQREHR LMLEQRQRYL
SSSTVASYAE PGDCYEEIFQ YVCHILRKAK RRALGLYQAL QSRRQALGPE APAPAKPGPH
AKEPRHYHGK TKGQGDEGRH LGSRHCQTLH GPASPGNDHS GRELCPQHSP LDATPHTLVQ
PIPATLASDP ASCPCCQHED GRRPSGLGST DSGQEGSGSG SSAGGEDEAD GDGARSSEDG
ASSELGKEEE EEEQADGAVW LCGDVWRETR AKLRGIVDSK YFNRGIMMAI LVNTVSMGIE
HHEQPEELTN ILEICNVVFT SMFALEMILK LAAFGLFDYL RNPYNIFDSI IVIISIWEIV
GQADGGLSVL RTFRLLRVLK LVRFMPALRR QLVVLMKTMD NVATFCMLLM LFIFIFSILG
MHIFGCKFSL RTDTGDTVPD RKNFDSLLWA IVTVFQILTQ EDWNVVLYNG MASTSPWASL
YFVALMTFGN YVLFNLLVAI LVEGFQAEGD ANRSYSDEDQ SSSNIEEFDK LQEGLDSSGD
PKLCPIPMTP NGHLDPSLPL GGHLGPAGAA GPAPRLSLQP DPMLVALGSR KSSVMSLGRM
SYDQRSLSSS RSSYYGPWGR SAAWASRRSS WNSLKHKPPS AEHESLLSAE RGGGARVCEV
AADEGPPRAA PLHTPHAHHI HHGPHLAHRH RHHRRTLSLD NRDSVDLAEL VPAVGAHPRA
AWRAAGPAPG HEDCNGRMPS IAKDVFTKMG DRGDRGEDEE EIDYTLCFRV RKMIDVYKPD
WCEVREDWSV YLFSPENRFR VLCQTIIAHK LFDYVVLAFI FLNCITIALE RPQIEAGSTE
RIFLTVSNYI FTAIFVGEMT LKVVSLGLYF GEQAYLRSSW NVLDGFLVFV SIIDIVVSLA
SAGGAKILGV LRVLRLLRTL RPLRVISRAP GLKLVVETLI SSLKPIGNIV LICCAFFIIF
GILGVQLFKG KFYHCLGVDT RNITNRSDCM AANYRWVHHK YNFDNLGQAL MSLFVLASKD
GWVNIMYNGL DAVAVDQQPV TNHNPWMLLY FISFLLIVSF FVLNMFVGVV VENFHKCRQH
QEAEEARRRE EKRLRRLEKK RRKAQRLPYY ATYCHTRLLI HSMCTSHYLD IFITFIICLN
VVTMSLEHYN QPTSLETALK YCNYMFTTVF VLEAVLKLVA FGLRRFFKDR WNQLDLAIVL
LSVMGITLEE IEINAALPIN PTIIRIMRVL RIARVLKLLK MATGMRALLD TVVQALPQVG
NLGLLFMLLF FIYAALGVEL FGKLVCNDEN PCEGMSRHAT FENFGMAFLT LFQVSTGDNW
NGIMKDTLRD CTHDERSCLS SLQFVSPLYF VSFVLTAQFV LINVVVAVLM KHLDDSNKEA
QEDAEMDAEL ELEMAHGLGP GPRLPTGSPG APGRGPGGAG GGGDTEGGLC RRCYSPAQEN
LWLDSVSLII KDSLEGELTI IDNLSGSIFH HYSSPAGCKK CHHDKQEVQL AETEAFSLNS
DRSSSILLGD DLSLEDPTAC PPGRKDSKGE LDPPEPMRVG DLGECFFPLS STAVSPDPEN
FLCEMEEIPF NPVRSWLKHD SSQAPPSPFS PDASSPLLPM PAEFFHPAVS ASQKGPEKGT
GTGTLPKIAL QGSWASLRSP RVNCTLLRQA TGSDTSLDAS PSSSAGSLQT TLEDSLTLSD
SPRRALGPPA PAPGPRAGLS PAARRRLSLR GRGLFSLRGL RAHQRSHSSG GSTSPGCTHH
DSMDPSDEEG RGGAGGGGAG SEHSETLSSL SLTSLFCPPP PPPAPGLTPA RKFSSTSSLA
APGRPHAAAL AHGLARSPSW AADRSKDPPG RAPLPMGLGP LAPPPQPLPG ELEPGDAASK
RKR
