TRPC3_HUMAN
ID TRPC3_HUMAN Reviewed; 921 AA.
AC Q13507; A7VJS1; E9PCJ9; O00593; Q15660; Q52M35; Q5G1L5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 4.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Short transient receptor potential channel 3;
DE Short=TrpC3;
DE AltName: Full=Transient receptor protein 3;
DE Short=TRP-3;
DE Short=hTrp-3;
DE Short=hTrp3;
GN Name=TRPC3; Synonyms=TRP3;
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 FUNCTION.
RC TISSUE=Embryonic kidney;
RX PubMed=8646775; DOI=10.1016/s0092-8674(00)81233-7;
RA Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E.,
RA Birnbaumer L.;
RT "trp, a novel mammalian gene family essential for agonist-activated
RT capacitative Ca2+ entry.";
RL Cell 85:661-671(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH TRPC1 (ISOFORM
RP 2).
RX PubMed=9215637; DOI=10.1016/s0092-8674(00)80302-5;
RA Xu X.-Z.S., Li H.-S., Guggino W.B., Montell C.;
RT "Coassembly of TRP and TRPL produces a distinct store-operated
RT conductance.";
RL Cell 89:1155-1164(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=15728370; DOI=10.1073/pnas.0409908102;
RA Yildirim E., Kawasaki B.T., Birnbaumer L.;
RT "Molecular cloning of TRPC3a, an N-terminally extended, store-operated
RT variant of the human C3 transient receptor potential channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3307-3311(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Yamazaki D., Yamamura H., Ohya S., Asai K., Imaizumi Y.;
RT "Molecular cloning of novel TRPC3 isoform.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 705-820.
RC TISSUE=Fetal brain;
RX PubMed=7568191; DOI=10.1073/pnas.92.21.9652;
RA Wes P.D., Chevesich J., Jeromin A., Rosenberg C., Stetten G., Montell C.;
RT "TRPC1, a human homolog of a Drosophila store-operated channel.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:9652-9656(1995).
RN [8]
RP GLYCOSYLATION AT ASN-489, AND MEMBRANE TOPOLOGY.
RX PubMed=9535843; DOI=10.1074/jbc.273.15.8675;
RA Vannier B., Zhu X., Brown D., Birnbaumer L.;
RT "The membrane topology of human transient receptor potential 3 as inferred
RT from glycosylation-scanning mutagenesis and epitope immunocytochemistry.";
RL J. Biol. Chem. 273:8675-8679(1998).
RN [9]
RP FUNCTION.
RX PubMed=9417057; DOI=10.1074/jbc.273.1.133;
RA Zhu X., Jiang M., Birnbaumer L.;
RT "Receptor-activated Ca2+ influx via human Trp3 stably expressed in human
RT embryonic kidney (HEK)293 cells. Evidence for a non-capacitative Ca2+
RT entry.";
RL J. Biol. Chem. 273:133-142(1998).
RN [10]
RP INTERACTION WITH ITPR1.
RX PubMed=9853757; DOI=10.1038/24890;
RA Kiselyov K., Xu X., Mozhayeva G., Kuo T., Pessah I., Mignery G., Zhu X.,
RA Birnbaumer L., Muallem S.;
RT "Functional interaction between InsP3 receptors and store-operated Htrp3
RT channels.";
RL Nature 396:478-482(1998).
RN [11]
RP FUNCTION.
RX PubMed=9930701; DOI=10.1038/16711;
RA Hofmann T., Obukhov A.G., Schaefer M., Harteneck C., Gudermann T.,
RA Schultz G.;
RT "Direct activation of human TRPC6 and TRPC3 channels by diacylglycerol.";
RL Nature 397:259-263(1999).
RN [12]
RP INTERACTION WITH ITPR3.
RX PubMed=10611319; DOI=10.1073/pnas.96.26.14955;
RA Boulay G., Brown D.M., Qin N., Jiang M., Dietrich A., Zhu M.X., Chen Z.,
RA Birnbaumer M., Mikoshiba K., Birnbaumer L.;
RT "Modulation of Ca(2+) entry by polypeptides of the inositol 1,4, 5-
RT trisphosphate receptor (IP3R) that bind transient receptor potential (TRP):
RT evidence for roles of TRP and IP3R in store depletion-activated Ca(2+)
RT entry.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14955-14960(1999).
RN [13]
RP INTERACTION WITH MX1.
RX PubMed=15757897; DOI=10.1074/jbc.m500391200;
RA Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N.,
RA St-Hilaire M., Pinard M., Boulay G.;
RT "MxA, a member of the dynamin superfamily, interacts with the ankyrin-like
RT repeat domain of TRPC.";
RL J. Biol. Chem. 280:19393-19400(2005).
RN [14]
RP INTERACTION WITH RNF24.
RX PubMed=17850865; DOI=10.1016/j.ceca.2007.07.009;
RA Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.;
RT "RNF24, a new TRPC interacting protein, causes the intracellular retention
RT of TRPC.";
RL Cell Calcium 43:432-443(2008).
RN [15]
RP INTERACTION WITH JPH2, AND FUNCTION.
RX PubMed=20095964; DOI=10.1042/bj20091225;
RA Woo J.S., Hwang J.H., Ko J.K., Weisleder N., Kim do H., Ma J., Lee E.H.;
RT "S165F mutation of junctophilin 2 affects Ca2+ signalling in skeletal
RT muscle.";
RL Biochem. J. 427:125-134(2010).
RN [16]
RP ELECTRON MICROSCOPY (15 ANGSTROMS), AND MEMBRANE TOPOLOGY.
RX PubMed=17258231; DOI=10.1016/j.jmb.2006.12.043;
RA Mio K., Ogura T., Kiyonaka S., Hiroaki Y., Tanimura Y., Fujiyoshi Y.,
RA Mori Y., Sato C.;
RT "The TRPC3 channel has a large internal chamber surrounded by signal
RT sensing antennas.";
RL J. Mol. Biol. 367:373-383(2007).
RN [17]
RP INVOLVEMENT IN SCA41, VARIANT SCA41 HIS-847, AND CHARACTERIZATION OF
RP VARIANT SCA41 HIS-847.
RX PubMed=25477146; DOI=10.1002/mds.26096;
RA Fogel B.L., Hanson S.M., Becker E.B.;
RT "Do mutations in the murine ataxia gene TRPC3 cause cerebellar ataxia in
RT humans?";
RL Mov. Disord. 30:284-286(2015).
CC -!- FUNCTION: Thought to form a receptor-activated non-selective calcium
CC permeant cation channel. Probably is operated by a phosphatidylinositol
CC second messenger system activated by receptor tyrosine kinases or G-
CC protein coupled receptors. Activated by diacylglycerol (DAG) in a
CC membrane-delimited fashion, independently of protein kinase C, and by
CC inositol 1,4,5-triphosphate receptors (ITPR) with bound IP3. May also
CC be activated by internal calcium store depletion.
CC {ECO:0000269|PubMed:20095964, ECO:0000269|PubMed:8646775,
CC ECO:0000269|PubMed:9417057, ECO:0000269|PubMed:9930701}.
CC -!- SUBUNIT: Interacts with ITPR1 (PubMed:9853757). Interacts with ITPR3
CC (PubMed:10611319). Interacts with MX1 (PubMed:15757897). Interacts with
CC RNF24 (PubMed:17850865). Interacts with JPH2; the interaction is
CC involved in maintaining Ca(2+) homeostasis in skeletal muscle and is
CC mediated by JPH2 'Ser-165' phosphorylation (PubMed:20095964).
CC {ECO:0000269|PubMed:10611319, ECO:0000269|PubMed:15757897,
CC ECO:0000269|PubMed:17850865, ECO:0000269|PubMed:20095964,
CC ECO:0000269|PubMed:9853757}.
CC -!- SUBUNIT: [Isoform 2]: Interacts with isoform short of TRPC1.
CC {ECO:0000269|PubMed:9215637}.
CC -!- INTERACTION:
CC Q13507; Q14573: ITPR3; NbExp=5; IntAct=EBI-520807, EBI-351055;
CC Q13507; P20591: MX1; NbExp=2; IntAct=EBI-520807, EBI-929476;
CC Q13507; Q96D31: ORAI1; NbExp=2; IntAct=EBI-520807, EBI-2291476;
CC Q13507; P10686: Plcg1; Xeno; NbExp=2; IntAct=EBI-520807, EBI-520788;
CC Q13507-3; P05480: Src; Xeno; NbExp=4; IntAct=EBI-15563545, EBI-298680;
CC Q13507-3; Q80UE6: Wnk4; Xeno; NbExp=2; IntAct=EBI-15563545, EBI-295378;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13507-2; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13507-3; Sequence=VSP_061592;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain and at much lower
CC levels in ovary, colon, small intestine, lung, prostate, placenta and
CC testis.
CC -!- DISEASE: Spinocerebellar ataxia 41 (SCA41) [MIM:616410]: A form of
CC spinocerebellar ataxia, a clinically and genetically heterogeneous
CC group of cerebellar disorders. Patients show progressive incoordination
CC of gait and often poor coordination of hands, speech and eye movements,
CC due to degeneration of the cerebellum with variable involvement of the
CC brainstem and spinal cord. {ECO:0000269|PubMed:25477146}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC3 sub-subfamily. {ECO:0000305}.
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DR EMBL; U47050; AAC51653.1; -; mRNA.
DR EMBL; Y13758; CAA74083.1; -; mRNA.
DR EMBL; AY865574; AAW62292.1; -; mRNA.
DR EMBL; AB255424; BAF76424.1; -; mRNA.
DR EMBL; AC079341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093682; AAH93682.1; -; mRNA.
DR EMBL; BC093684; AAH93684.1; -; mRNA.
DR EMBL; X89068; CAA61448.1; -; mRNA.
DR CCDS; CCDS3725.1; -. [Q13507-3]
DR CCDS; CCDS47130.1; -. [Q13507-2]
DR RefSeq; NP_001124170.1; NM_001130698.1. [Q13507-2]
DR RefSeq; NP_003296.1; NM_003305.2. [Q13507-3]
DR PDB; 5ZBG; EM; 4.36 A; A/B/C/D=86-921.
DR PDB; 6CUD; EM; 3.30 A; A/B/C/D=86-891.
DR PDB; 6D7L; EM; 4.00 A; A/B/C/D=86-921.
DR PDB; 6DJS; EM; 5.80 A; A/B/C/D=86-384.
DR PDB; 7DXB; EM; 2.70 A; A/B/C/D=1-836.
DR PDB; 7DXC; EM; 3.06 A; A/B/C/D=1-836.
DR PDB; 7DXD; EM; 3.90 A; A/B/C/D=86-921.
DR PDB; 7DXE; EM; 3.20 A; A/B/C/D=1-836.
DR PDBsum; 5ZBG; -.
DR PDBsum; 6CUD; -.
DR PDBsum; 6D7L; -.
DR PDBsum; 6DJS; -.
DR PDBsum; 7DXB; -.
DR PDBsum; 7DXC; -.
DR PDBsum; 7DXD; -.
DR PDBsum; 7DXE; -.
DR AlphaFoldDB; Q13507; -.
DR SMR; Q13507; -.
DR BioGRID; 113073; 17.
DR CORUM; Q13507; -.
DR DIP; DIP-34311N; -.
DR IntAct; Q13507; 8.
DR STRING; 9606.ENSP00000368966; -.
DR BindingDB; Q13507; -.
DR ChEMBL; CHEMBL2417348; -.
DR GuidetoPHARMACOLOGY; 488; -.
DR TCDB; 1.A.4.1.4; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q13507; 1 site.
DR iPTMnet; Q13507; -.
DR PhosphoSitePlus; Q13507; -.
DR BioMuta; TRPC3; -.
DR DMDM; 332278239; -.
DR MassIVE; Q13507; -.
DR PaxDb; Q13507; -.
DR PeptideAtlas; Q13507; -.
DR PRIDE; Q13507; -.
DR ProteomicsDB; 59505; -. [Q13507-2]
DR ProteomicsDB; 59506; -. [Q13507-3]
DR Antibodypedia; 15891; 287 antibodies from 34 providers.
DR DNASU; 7222; -.
DR Ensembl; ENST00000264811.9; ENSP00000264811.5; ENSG00000138741.11. [Q13507-3]
DR Ensembl; ENST00000379645.8; ENSP00000368966.3; ENSG00000138741.11. [Q13507-2]
DR GeneID; 7222; -.
DR KEGG; hsa:7222; -.
DR MANE-Select; ENST00000379645.8; ENSP00000368966.3; NM_001130698.2; NP_001124170.1. [Q13507-2]
DR CTD; 7222; -.
DR DisGeNET; 7222; -.
DR GeneCards; TRPC3; -.
DR HGNC; HGNC:12335; TRPC3.
DR HPA; ENSG00000138741; Tissue enhanced (brain, pituitary gland).
DR MalaCards; TRPC3; -.
DR MIM; 602345; gene.
DR MIM; 616410; phenotype.
DR neXtProt; NX_Q13507; -.
DR OpenTargets; ENSG00000138741; -.
DR Orphanet; 458798; Spinocerebellar ataxia type 41.
DR PharmGKB; PA37008; -.
DR VEuPathDB; HostDB:ENSG00000138741; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR HOGENOM; CLU_005716_4_2_1; -.
DR InParanoid; Q13507; -.
DR OMA; AGMRDKG; -.
DR OrthoDB; 1018075at2759; -.
DR TreeFam; TF313147; -.
DR PathwayCommons; Q13507; -.
DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-3295583; TRP channels.
DR Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
DR Reactome; R-HSA-9022699; MECP2 regulates neuronal receptors and channels.
DR SignaLink; Q13507; -.
DR SIGNOR; Q13507; -.
DR BioGRID-ORCS; 7222; 9 hits in 1068 CRISPR screens.
DR ChiTaRS; TRPC3; human.
DR GeneWiki; TRPC3; -.
DR GenomeRNAi; 7222; -.
DR Pharos; Q13507; Tchem.
DR PRO; PR:Q13507; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q13507; protein.
DR Bgee; ENSG00000138741; Expressed in buccal mucosa cell and 113 other tissues.
DR ExpressionAtlas; Q13507; baseline and differential.
DR Genevisible; Q13507; HS.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0007602; P:phototransduction; TAS:ProtInc.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; IDA:UniProtKB.
DR GO; GO:1903244; P:positive regulation of cardiac muscle hypertrophy in response to stress; IDA:BHF-UCL.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0033198; P:response to ATP; IDA:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA:UniProtKB.
DR GO; GO:0007338; P:single fertilization; IBA:GO_Central.
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; IPR013555; TRP_dom.
DR InterPro; IPR005459; TRPC3_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF8; PTHR10117:SF8; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08344; TRP_2; 1.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR PRINTS; PR01644; TRPCHANNEL3.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Disease variant; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Neurodegeneration;
KW Reference proteome; Repeat; Spinocerebellar ataxia; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..921
FT /note="Short transient receptor potential channel 3"
FT /id="PRO_0000215310"
FT TOPO_DOM 1..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..503
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..608
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 609..629
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..652
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 653..673
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 674..722
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 723..743
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 744..921
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 111..140
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 146..175
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 177..203
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 232..261
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 634..663
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REGION 850..870
FT /note="Binds to IP3R3"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9535843"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2)"
FT /id="VSP_061592"
FT VARIANT 847
FT /note="R -> H (in SCA41; toxic gain of function effect)"
FT /evidence="ECO:0000269|PubMed:25477146"
FT /id="VAR_073835"
FT CONFLICT 610
FT /note="I -> L (in Ref. 4; BAF76424)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="Y -> C (in Ref. 4; BAF76424)"
FT /evidence="ECO:0000305"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 125..134
FT /evidence="ECO:0007829|PDB:6CUD"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:6CUD"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6CUD"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6CUD"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 270..277
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 280..294
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 297..303
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 307..325
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 329..348
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 353..359
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 380..387
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 397..407
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 419..431
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 433..435
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 436..441
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 455..476
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 500..505
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 509..532
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 534..539
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 541..577
FT /evidence="ECO:0007829|PDB:6CUD"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 590..593
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 607..621
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 622..628
FT /evidence="ECO:0007829|PDB:6CUD"
FT TURN 629..631
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 632..636
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 637..671
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 672..674
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 676..681
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 687..696
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 697..699
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 709..712
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 714..749
FT /evidence="ECO:0007829|PDB:6CUD"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 754..770
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 847..870
FT /evidence="ECO:0007829|PDB:6CUD"
FT HELIX 873..890
FT /evidence="ECO:0007829|PDB:6CUD"
SQ SEQUENCE 921 AA; 105538 MW; 8D7E0D144EF4BE51 CRC64;
MSTKVRKCKE QARVTFPAPE EEEDEGEDEG AEPQRRRRGW RGVNGGLEPR SAPSQREPHG
YCPPPFSHGP DLSMEGSPSL RRMTVMREKG RRQAVRGPAF MFNDRGTSLT AEEERFLDAA
EYGNIPVVRK MLEESKTLNV NCVDYMGQNA LQLAVGNEHL EVTELLLKKE NLARIGDALL
LAISKGYVRI VEAILNHPGF AASKRLTLSP CEQELQDDDF YAYDEDGTRF SPDITPIILA
AHCQKYEVVH MLLMKGARIE RPHDYFCKCG DCMEKQRHDS FSHSRSRINA YKGLASPAYL
SLSSEDPVLT ALELSNELAK LANIEKEFKN DYRKLSMQCK DFVVGVLDLC RDSEEVEAIL
NGDLESAEPL EVHRHKASLS RVKLAIKYEV KKFVAHPNCQ QQLLTIWYEN LSGLREQTIA
IKCLVVLVVA LGLPFLAIGY WIAPCSRLGK ILRSPFMKFV AHAASFIIFL GLLVFNASDR
FEGITTLPNI TVTDYPKQIF RVKTTQFTWT EMLIMVWVLG MMWSECKELW LEGPREYILQ
LWNVLDFGML SIFIAAFTAR FLAFLQATKA QQYVDSYVQE SDLSEVTLPP EIQYFTYARD
KWLPSDPQII SEGLYAIAVV LSFSRIAYIL PANESFGPLQ ISLGRTVKDI FKFMVLFIMV
FFAFMIGMFI LYSYYLGAKV NAAFTTVEES FKTLFWSIFG LSEVTSVVLK YDHKFIENIG
YVLYGIYNVT MVVVLLNMLI AMINSSYQEI EDDSDVEWKF ARSKLWLSYF DDGKTLPPPF
SLVPSPKSFV YFIMRIVNFP KCRRRRLQKD IEMGMGNSKS RLNLFTQSNS RVFESHSFNS
ILNQPTRYQQ IMKRLIKRYV LKAQVDKEND EVNEGELKEI KQDISSLRYE LLEDKSQATE
ELAILIHKLS EKLNPSMLRC E
