TRPC1_HUMAN
ID TRPC1_HUMAN Reviewed; 793 AA.
AC P48995; Q14CE4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Short transient receptor potential channel 1;
DE Short=TrpC1;
DE AltName: Full=Transient receptor protein 1;
DE Short=TRP-1;
GN Name=TRPC1; Synonyms=TRP1;
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 LONG), AND ALTERNATIVE SPLICING
RP (ISOFORM SHORT).
RX PubMed=7589464; DOI=10.1016/0014-5793(95)01038-g;
RA Zhu X., Chu P.B., Peyton M., Birnbaumer L.;
RT "Molecular cloning of a widely expressed human homologue for the Drosophila
RT trp gene.";
RL FEBS Lett. 373:193-198(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Brain;
RX PubMed=8663995; DOI=10.1016/s0896-6273(00)80145-2;
RA Zitt C., Zobel A., Obukhov A.G., Harteneck C., Kalkbrenner F.,
RA Lueckhoff A., Schultz G.;
RT "Cloning and functional expression of a human Ca2+-permeable cation channel
RT activated by calcium store depletion.";
RL Neuron 16:1189-1196(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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 [6]
RP INTERACTION WITH TRPC3 (ISOFORM SHORT).
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 [7]
RP INTERACTION WITH ITPR3.
RX PubMed=10766822; DOI=10.1074/jbc.275.16.11934;
RA Lockwich T.P., Liu X., Singh B.B., Jadlowiec J., Weiland S., Ambudkar I.S.;
RT "Assembly of Trp1 in a signaling complex associated with caveolin-
RT scaffolding lipid raft domains.";
RL J. Biol. Chem. 275:11934-11942(2000).
RN [8]
RP CHARACTERIZATION.
RX PubMed=11139478; DOI=10.1161/01.res.88.1.84;
RA Xu S.-Z., Beech D.J.;
RT "TrpC1 is a membrane-spanning subunit of store-operated Ca(2+) channels in
RT native vascular smooth muscle cells.";
RL Circ. Res. 88:84-87(2001).
RN [9]
RP SUBUNIT.
RX PubMed=12032305; DOI=10.1073/pnas.102596199;
RA Hofmann T., Schaefer M., Schultz G., Gudermann T.;
RT "Subunit composition of mammalian transient receptor potential channels in
RT living cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002).
RN [10]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=15016832; DOI=10.1074/jbc.m313975200;
RA Ahmmed G.U., Mehta D., Vogel S., Holinstat M., Paria B.C., Tiruppathi C.,
RA Malik A.B.;
RT "Protein kinase Calpha phosphorylates the TRPC1 channel and regulates
RT store-operated Ca2+ entry in endothelial cells.";
RL J. Biol. Chem. 279:20941-20949(2004).
RN [11]
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 [12]
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 [13]
RP INTERACTION WITH FKBP4.
RX PubMed=19945390; DOI=10.1016/j.neuron.2009.09.025;
RA Shim S., Yuan J.P., Kim J.Y., Zeng W., Huang G., Milshteyn A., Kern D.,
RA Muallem S., Ming G.L., Worley P.F.;
RT "Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of neuronal
RT growth cones via regulation of TRPC1 channel opening.";
RL Neuron 64:471-483(2009).
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. Seems to be also activated by intracellular
CC calcium store depletion. {ECO:0000269|PubMed:15016832}.
CC -!- SUBUNIT: Interacts with TRPC4AP (By similarity). Homotetramer and
CC heterotetramer with TRPC4 and/or TRPC5 (PubMed:12032305). Interacts
CC with TRPC4 and TRPC5 (By similarity). Interacts with ITPR3
CC (PubMed:10766822). Interacts with MX1 and RNF24 (PubMed:15757897,
CC PubMed:17850865). Interacts with FKBP4 (PubMed:19945390). Interacts
CC with PLSCR1 (By similarity). {ECO:0000250|UniProtKB:Q61056,
CC ECO:0000250|UniProtKB:Q9QX01, ECO:0000269|PubMed:10766822,
CC ECO:0000269|PubMed:12032305, ECO:0000269|PubMed:15757897,
CC ECO:0000269|PubMed:17850865, ECO:0000269|PubMed:19945390}.
CC -!- SUBUNIT: [Isoform Short]: Interacts with isoform 2 of TRPC3.
CC {ECO:0000269|PubMed:9215637}.
CC -!- INTERACTION:
CC P48995; Q03135: CAV1; NbExp=7; IntAct=EBI-929665, EBI-603614;
CC P48995; Q96D31: ORAI1; NbExp=2; IntAct=EBI-929665, EBI-2291476;
CC P48995; Q13563: PKD2; NbExp=12; IntAct=EBI-929665, EBI-7813714;
CC P48995; Q13586: STIM1; NbExp=6; IntAct=EBI-929665, EBI-448878;
CC P48995; Q9EPK8: Trpv4; Xeno; NbExp=10; IntAct=EBI-929665, EBI-7091763;
CC P48995-2; Q13563: PKD2; NbExp=4; IntAct=EBI-9830970, EBI-7813714;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P48995-1; Sequence=Displayed;
CC Name=Short; Synonyms=TRPC1A {ECO:0000303|PubMed:8663995};
CC IsoId=P48995-2; Sequence=VSP_006560;
CC -!- TISSUE SPECIFICITY: Seems to be ubiquitous.
CC -!- PTM: Activation of PRKCA induces phosphorylation of TRPC1 and
CC subsequent Ca2+ entry into cells. {ECO:0000269|PubMed:15016832}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC1 sub-subfamily. {ECO:0000305}.
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DR EMBL; U31110; AAA93251.1; -; mRNA.
DR EMBL; U31110; AAA93252.1; -; mRNA.
DR EMBL; X89066; CAA61447.1; -; mRNA.
DR EMBL; Z73903; CAA98108.1; -; mRNA.
DR EMBL; CH471052; EAW78963.1; -; Genomic_DNA.
DR EMBL; BC112338; AAI12339.1; -; mRNA.
DR EMBL; BC113953; AAI13954.1; -; mRNA.
DR CCDS; CCDS3126.1; -. [P48995-2]
DR CCDS; CCDS58856.1; -. [P48995-1]
DR PIR; S68238; S68238.
DR RefSeq; NP_001238774.1; NM_001251845.1. [P48995-1]
DR RefSeq; NP_003295.1; NM_003304.4. [P48995-2]
DR AlphaFoldDB; P48995; -.
DR SMR; P48995; -.
DR BioGRID; 113071; 24.
DR CORUM; P48995; -.
DR DIP; DIP-35698N; -.
DR IntAct; P48995; 44.
DR STRING; 9606.ENSP00000419313; -.
DR BindingDB; P48995; -.
DR ChEMBL; CHEMBL4296083; -.
DR ChEMBL; CHEMBL4523660; -.
DR ChEMBL; CHEMBL4523661; -.
DR TCDB; 1.A.4.1.3; the transient receptor potential ca(2+) channel (trp-cc) family.
DR iPTMnet; P48995; -.
DR PhosphoSitePlus; P48995; -.
DR SwissPalm; P48995; -.
DR BioMuta; TRPC1; -.
DR DMDM; 1351302; -.
DR jPOST; P48995; -.
DR MassIVE; P48995; -.
DR MaxQB; P48995; -.
DR PaxDb; P48995; -.
DR PeptideAtlas; P48995; -.
DR PRIDE; P48995; -.
DR ProteomicsDB; 55952; -. [P48995-1]
DR ProteomicsDB; 55953; -. [P48995-2]
DR ABCD; P48995; 3 sequenced antibodies.
DR Antibodypedia; 3996; 264 antibodies from 33 providers.
DR DNASU; 7220; -.
DR Ensembl; ENST00000273482.10; ENSP00000273482.6; ENSG00000144935.16. [P48995-2]
DR Ensembl; ENST00000476941.6; ENSP00000419313.1; ENSG00000144935.16. [P48995-1]
DR GeneID; 7220; -.
DR KEGG; hsa:7220; -.
DR MANE-Select; ENST00000476941.6; ENSP00000419313.1; NM_001251845.2; NP_001238774.1.
DR UCSC; uc003evb.4; human. [P48995-1]
DR CTD; 7220; -.
DR DisGeNET; 7220; -.
DR GeneCards; TRPC1; -.
DR HGNC; HGNC:12333; TRPC1.
DR HPA; ENSG00000144935; Low tissue specificity.
DR MIM; 602343; gene.
DR neXtProt; NX_P48995; -.
DR OpenTargets; ENSG00000144935; -.
DR PharmGKB; PA357; -.
DR VEuPathDB; HostDB:ENSG00000144935; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244985; -.
DR HOGENOM; CLU_005716_4_1_1; -.
DR InParanoid; P48995; -.
DR OMA; YLGDYYM; -.
DR OrthoDB; 824310at2759; -.
DR PhylomeDB; P48995; -.
DR TreeFam; TF313147; -.
DR PathwayCommons; P48995; -.
DR Reactome; R-HSA-3295583; TRP channels.
DR Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR SignaLink; P48995; -.
DR BioGRID-ORCS; 7220; 11 hits in 1081 CRISPR screens.
DR ChiTaRS; TRPC1; human.
DR GeneWiki; TRPC1; -.
DR GenomeRNAi; 7220; -.
DR Pharos; P48995; Tbio.
DR PRO; PR:P48995; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P48995; protein.
DR Bgee; ENSG00000144935; Expressed in germinal epithelium of ovary and 183 other tissues.
DR ExpressionAtlas; P48995; baseline and differential.
DR Genevisible; P48995; HS.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0043235; C:receptor complex; IDA:MGI.
DR GO; GO:0051117; F:ATPase binding; IPI:ARUK-UCL.
DR GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
DR GO; GO:0005261; F:cation channel activity; EXP:Reactome.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:ARUK-UCL.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0042438; P:melanin biosynthetic process; IDA:CACAO.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
DR GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
DR GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
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; IPR005457; TRPC1_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF56; PTHR10117:SF56; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08344; TRP_2; 1.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR PRINTS; PR01642; TRPCHANNEL1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW Calcium transport; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..793
FT /note="Short transient receptor potential channel 1"
FT /id="PRO_0000215303"
FT TOPO_DOM 1..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..475
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..539
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..560
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..586
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 587..607
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 608..616
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 617..637
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 46..75
FT /note="ANK 1"
FT REPEAT 83..111
FT /note="ANK 2"
FT REPEAT 112..138
FT /note="ANK 3"
FT REPEAT 158..187
FT /note="ANK 4"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 110..143
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7568191, ECO:0000303|PubMed:8663995"
FT /id="VSP_006560"
SQ SEQUENCE 793 AA; 91212 MW; F4CC57ADDFA320AE CRC64;
MMAALYPSTD LSGASSSSLP SSPSSSSPNE VMALKDVREV KEENTLNEKL FLLACDKGDY
YMVKKILEEN SSGDLNINCV DVLGRNAVTI TIENENLDIL QLLLDYGCQS ADALLVAIDS
EVVGAVDILL NHRPKRSSRP TIVKLMERIQ NPEYSTTMDV APVILAAHRN NYEILTMLLK
QDVSLPKPHA VGCECTLCSA KNKKDSLRHS RFRLDIYRCL ASPALIMLTE EDPILRAFEL
SADLKELSLV EVEFRNDYEE LARQCKMFAK DLLAQARNSR ELEVILNHTS SDEPLDKRGL
LEERMNLSRL KLAIKYNQKE FVSQSNCQQF LNTVWFGQMS GYRRKPTCKK IMTVLTVGIF
WPVLSLCYLI APKSQFGRII HTPFMKFIIH GASYFTFLLL LNLYSLVYNE DKKNTMGPAL
ERIDYLLILW IIGMIWSDIK RLWYEGLEDF LEESRNQLSF VMNSLYLATF ALKVVAHNKF
HDFADRKDWD AFHPTLVAEG LFAFANVLSY LRLFFMYTTS SILGPLQISM GQMLQDFGKF
LGMFLLVLFS FTIGLTQLYD KGYTSKEQKD CVGIFCEQQS NDTFHSFIGT CFALFWYIFS
LAHVAIFVTR FSYGEELQSF VGAVIVGTYN VVVVIVLTKL LVAMLHKSFQ LIANHEDKEW
KFARAKLWLS YFDDKCTLPP PFNIIPSPKT ICYMISSLSK WICSHTSKGK VKRQNSLKEW
RNLKQKRDEN YQKVMCCLVH RYLTSMRQKM QSTDQATVEN LNELRQDLSK FRNEIRDLLG
FRTSKYAMFY PRN
