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Short transient receptor potential channel 1 (TrpC1) (Transient receptor protein 1) (TRP-1)

 TRPC1_HUMAN             Reviewed;         793 AA.
P48995; Q14CE4;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 162.
RecName: Full=Short transient receptor potential channel 1;
Short=TrpC1;
AltName: Full=Transient receptor protein 1;
Short=TRP-1;
Name=TRPC1; Synonyms=TRP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7589464; DOI=10.1016/0014-5793(95)01038-G;
Zhu X., Chu P.B., Peyton M., Birnbaumer L.;
"Molecular cloning of a widely expressed human homologue for the
Drosophila trp gene.";
FEBS Lett. 373:193-198(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Brain;
PubMed=7568191; DOI=10.1073/pnas.92.21.9652;
Wes P.D., Chevesich J., Jeromin A., Rosenberg C., Stetten G.,
Montell C.;
"TRPC1, a human homolog of a Drosophila store-operated channel.";
Proc. Natl. Acad. Sci. U.S.A. 92:9652-9656(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
TISSUE=Brain;
PubMed=8663995; DOI=10.1016/S0896-6273(00)80145-2;
Zitt C., Zobel A., Obukhov A.G., Harteneck C., Kalkbrenner F.,
Lueckhoff A., Schultz G.;
"Cloning and functional expression of a human Ca2+-permeable cation
channel activated by calcium store depletion.";
Neuron 16:1189-1196(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH ITPR3.
PubMed=10766822; DOI=10.1074/jbc.275.16.11934;
Lockwich T.P., Liu X., Singh B.B., Jadlowiec J., Weiland S.,
Ambudkar I.S.;
"Assembly of Trp1 in a signaling complex associated with caveolin-
scaffolding lipid raft domains.";
J. Biol. Chem. 275:11934-11942(2000).
[7]
CHARACTERIZATION.
PubMed=11139478; DOI=10.1161/01.RES.88.1.84;
Xu S.-Z., Beech D.J.;
"TrpC1 is a membrane-spanning subunit of store-operated Ca(2+)
channels in native vascular smooth muscle cells.";
Circ. Res. 88:84-87(2001).
[8]
SUBUNIT.
PubMed=12032305; DOI=10.1073/pnas.102596199;
Hofmann T., Schaefer M., Schultz G., Gudermann T.;
"Subunit composition of mammalian transient receptor potential
channels in living cells.";
Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002).
[9]
FUNCTION, AND PHOSPHORYLATION.
PubMed=15016832; DOI=10.1074/jbc.M313975200;
Ahmmed G.U., Mehta D., Vogel S., Holinstat M., Paria B.C.,
Tiruppathi C., Malik A.B.;
"Protein kinase Calpha phosphorylates the TRPC1 channel and regulates
store-operated Ca2+ entry in endothelial cells.";
J. Biol. Chem. 279:20941-20949(2004).
[10]
INTERACTION WITH MX1.
PubMed=15757897; DOI=10.1074/jbc.M500391200;
Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N.,
St-Hilaire M., Pinard M., Boulay G.;
"MxA, a member of the dynamin superfamily, interacts with the ankyrin-
like repeat domain of TRPC.";
J. Biol. Chem. 280:19393-19400(2005).
[11]
INTERACTION WITH RNF24.
PubMed=17850865; DOI=10.1016/j.ceca.2007.07.009;
Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.;
"RNF24, a new TRPC interacting protein, causes the intracellular
retention of TRPC.";
Cell Calcium 43:432-443(2008).
[12]
INTERACTION WITH FKBP4.
PubMed=19945390; DOI=10.1016/j.neuron.2009.09.025;
Shim S., Yuan J.P., Kim J.Y., Zeng W., Huang G., Milshteyn A.,
Kern D., Muallem S., Ming G.L., Worley P.F.;
"Peptidyl-prolyl isomerase FKBP52 controls chemotropic guidance of
neuronal growth cones via regulation of TRPC1 channel opening.";
Neuron 64:471-483(2009).
-!- FUNCTION: Thought to form a receptor-activated non-selective
calcium permeant cation channel. Probably is operated by a
phosphatidylinositol second messenger system activated by receptor
tyrosine kinases or G-protein coupled receptors. Seems to be also
activated by intracellular calcium store depletion.
{ECO:0000269|PubMed:15016832}.
-!- SUBUNIT: Interacts with TRPC4AP (By similarity). Homotetramer and
heterotetramer with TRPC4 and/or TRPC5. Interacts with TRPC3,
TRPC4 and TRPC5. Interacts with ITPR3. Interacts with MX1 and
RNF24. Interacts with FKBP4. {ECO:0000250,
ECO:0000269|PubMed:10766822, ECO:0000269|PubMed:12032305,
ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:17850865,
ECO:0000269|PubMed:19945390}.
-!- INTERACTION:
Q03135:CAV1; NbExp=7; IntAct=EBI-929665, EBI-603614;
Q96D31:ORAI1; NbExp=2; IntAct=EBI-929665, EBI-2291476;
Q13563:PKD2; NbExp=4; IntAct=EBI-9830970, EBI-7813714;
Q13586:STIM1; NbExp=6; IntAct=EBI-929665, EBI-448878;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P48995-1; Sequence=Displayed;
Name=Short;
IsoId=P48995-2; Sequence=VSP_006560;
-!- TISSUE SPECIFICITY: Seems to be ubiquitous.
-!- PTM: Activation of PRKCA induces phosphorylation of TRPC1 and
subsequent Ca2+ entry into cells. {ECO:0000269|PubMed:15016832}.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
STrpC subfamily. TRPC1 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U31110; AAA93251.1; -; mRNA.
EMBL; U31110; AAA93252.1; -; mRNA.
EMBL; X89066; CAA61447.1; -; mRNA.
EMBL; Z73903; CAA98108.1; -; mRNA.
EMBL; CH471052; EAW78963.1; -; Genomic_DNA.
EMBL; BC112338; AAI12339.1; -; mRNA.
EMBL; BC113953; AAI13954.1; -; mRNA.
CCDS; CCDS3126.1; -. [P48995-2]
CCDS; CCDS58856.1; -. [P48995-1]
PIR; S68238; S68238.
RefSeq; NP_001238774.1; NM_001251845.1. [P48995-1]
RefSeq; NP_003295.1; NM_003304.4. [P48995-2]
UniGene; Hs.250687; -.
UniGene; Hs.684389; -.
ProteinModelPortal; P48995; -.
BioGrid; 113071; 16.
CORUM; P48995; -.
DIP; DIP-35698N; -.
IntAct; P48995; 42.
STRING; 9606.ENSP00000273482; -.
GuidetoPHARMACOLOGY; 486; -.
TCDB; 1.A.4.1.3; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; P48995; -.
PhosphoSitePlus; P48995; -.
SwissPalm; P48995; -.
BioMuta; TRPC1; -.
DMDM; 1351302; -.
MaxQB; P48995; -.
PaxDb; P48995; -.
PeptideAtlas; P48995; -.
PRIDE; P48995; -.
Ensembl; ENST00000273482; ENSP00000273482; ENSG00000144935. [P48995-2]
Ensembl; ENST00000476941; ENSP00000419313; ENSG00000144935. [P48995-1]
Ensembl; ENST00000612385; ENSP00000481537; ENSG00000144935. [P48995-2]
GeneID; 7220; -.
KEGG; hsa:7220; -.
UCSC; uc003evb.4; human. [P48995-1]
CTD; 7220; -.
DisGeNET; 7220; -.
EuPathDB; HostDB:ENSG00000144935.14; -.
GeneCards; TRPC1; -.
HGNC; HGNC:12333; TRPC1.
HPA; CAB009387; -.
HPA; HPA021130; -.
MIM; 602343; gene.
neXtProt; NX_P48995; -.
OpenTargets; ENSG00000144935; -.
PharmGKB; PA357; -.
eggNOG; KOG3609; Eukaryota.
eggNOG; ENOG410XQ0Y; LUCA.
GeneTree; ENSGT00760000119180; -.
HOGENOM; HOG000020589; -.
HOVERGEN; HBG068337; -.
InParanoid; P48995; -.
KO; K04964; -.
OMA; FVAQSNC; -.
OrthoDB; EOG091G029I; -.
PhylomeDB; P48995; -.
TreeFam; TF313147; -.
Reactome; R-HSA-3295583; TRP channels.
Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
Reactome; R-HSA-5578775; Ion homeostasis.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
ChiTaRS; TRPC1; human.
GeneWiki; TRPC1; -.
GenomeRNAi; 7220; -.
PRO; PR:P48995; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144935; -.
CleanEx; HS_TRPC1; -.
ExpressionAtlas; P48995; baseline and differential.
Genevisible; P48995; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0043235; C:receptor complex; IDA:MGI.
GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
GO; GO:0005261; F:cation channel activity; EXP:Reactome.
GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
GO; GO:0044325; F:ion channel binding; IPI:BHF-UCL.
GO; GO:0015279; F:store-operated calcium channel activity; TAS:ProtInc.
GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
GO; GO:0042438; P:melanin biosynthetic process; IDA:CACAO.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:BHF-UCL.
GO; GO:0051592; P:response to calcium ion; IDA:BHF-UCL.
CDD; cd00204; ANK; 1.
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; IPR013555; TRP_dom.
InterPro; IPR005457; TRPC1_channel.
InterPro; IPR002153; TRPC_channel.
PANTHER; PTHR10117; PTHR10117; 1.
PANTHER; PTHR10117:SF56; PTHR10117:SF56; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF08344; TRP_2; 1.
PRINTS; PR01097; TRNSRECEPTRP.
PRINTS; PR01642; TRPCHANNEL1.
SMART; SM00248; ANK; 3.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Calcium; Calcium channel;
Calcium transport; Complete proteome; Ion channel; Ion transport;
Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
Transmembrane helix; Transport.
CHAIN 1 793 Short transient receptor potential
channel 1.
/FTId=PRO_0000215303.
TOPO_DOM 1 386 Cytoplasmic. {ECO:0000255}.
TRANSMEM 387 407 Helical. {ECO:0000255}.
TOPO_DOM 408 415 Extracellular. {ECO:0000255}.
TRANSMEM 416 436 Helical. {ECO:0000255}.
TOPO_DOM 437 457 Cytoplasmic. {ECO:0000255}.
TRANSMEM 458 475 Helical. {ECO:0000255}.
TOPO_DOM 476 539 Extracellular. {ECO:0000255}.
TRANSMEM 540 560 Helical. {ECO:0000255}.
TOPO_DOM 561 586 Cytoplasmic. {ECO:0000255}.
TRANSMEM 587 607 Helical. {ECO:0000255}.
TOPO_DOM 608 616 Extracellular. {ECO:0000255}.
TRANSMEM 617 637 Helical. {ECO:0000255}.
REPEAT 46 75 ANK 1.
REPEAT 83 111 ANK 2.
REPEAT 112 138 ANK 3.
REPEAT 158 187 ANK 4.
VAR_SEQ 110 143 Missing (in isoform Short).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7568191,
ECO:0000303|PubMed:8663995}.
/FTId=VSP_006560.
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


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