TRPC1_MOUSE
ID TRPC1_MOUSE Reviewed; 793 AA.
AC Q61056; O35722;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 5.
DT 25-MAY-2022, entry version 185.
DE RecName: Full=Short transient receptor potential channel 1;
DE Short=TrpC1;
DE AltName: Full=Transient receptor protein 1;
DE Short=TRP-1;
DE Short=mTrp1;
DE AltName: Full=Trp-related protein 1;
GN Name=Trpc1; Synonyms=Trp1, Trrp1;
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 [MRNA], AND ALTERNATIVE SPLICING.
RC TISSUE=Insulinoma;
RX PubMed=9165220; DOI=10.1007/s001250050711;
RA Sakura H., Ashcroft F.M.;
RT "Identification of four trp1 gene variants murine pancreatic beta-cells.";
RL Diabetologia 40:528-532(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RC TISSUE=Lens epithelium;
RA Rae J.L.;
RT "Ion channels in lens epithelia.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 535-658.
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 [4]
RP INTERACTION WITH TRPC4AP.
RX PubMed=20458742; DOI=10.1002/jcp.22221;
RA Mace K.E., Lussier M.P., Boulay G., Terry-Powers J.L., Parfrey H.,
RA Perraud A.L., Riches D.W.H.;
RT "TRUSS, TNF-R1, and TRPC ion channels synergistically reverse endoplasmic
RT reticulum Ca2+ storage reduction in response to m1 muscarinic acetylcholine
RT receptor signaling.";
RL J. Cell. Physiol. 225:444-453(2010).
RN [5]
RP INTERACTION WITH PLSCR1.
RX PubMed=32110987; DOI=10.3390/cells9030547;
RA Guo J., Li J., Xia L., Wang Y., Zhu J., Du J., Lu Y., Liu G., Yao X.,
RA Shen B.;
RT "Transient Receptor Potential Canonical 5-Scramblase Signaling Complex
RT Mediates Neuronal Phosphatidylserine Externalization and Apoptosis.";
RL Cells 9:0-0(2020).
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.
CC -!- SUBUNIT: Homotetramer and heterotetramer with TRPC4 and/or TRPC5 (By
CC similarity). Interacts with TRPC4 and TRPC5 (By similarity). Interacts
CC with ITPR3 (By similarity). Interacts with MX1 and RNF24 (By
CC similarity). Interacts with FKBP4 (By similarity). Interacts with
CC TRPC4AP (PubMed:20458742). Interacts with PLSCR1 (PubMed:32110987).
CC {ECO:0000250|UniProtKB:P48995, ECO:0000250|UniProtKB:Q9QX01,
CC ECO:0000269|PubMed:20458742, ECO:0000269|PubMed:32110987}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q61056-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q61056-2; Sequence=VSP_006561;
CC -!- PTM: Activation of PRKCA induces phosphorylation of TRPC1 and
CC subsequent Ca2+ entry into cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB50622.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC53162.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF05725.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U73625; AAB50622.1; ALT_INIT; mRNA.
DR EMBL; U95167; AAC53162.1; ALT_INIT; mRNA.
DR EMBL; AF191551; AAF05725.1; ALT_INIT; mRNA.
DR EMBL; U40980; AAC52699.1; -; mRNA.
DR CCDS; CCDS23411.1; -. [Q61056-1]
DR CCDS; CCDS81052.1; -. [Q61056-2]
DR RefSeq; NP_001298052.1; NM_001311123.1. [Q61056-2]
DR RefSeq; NP_035773.1; NM_011643.3. [Q61056-1]
DR AlphaFoldDB; Q61056; -.
DR SMR; Q61056; -.
DR BioGRID; 204327; 3.
DR CORUM; Q61056; -.
DR DIP; DIP-33928N; -.
DR IntAct; Q61056; 4.
DR STRING; 10090.ENSMUSP00000139672; -.
DR iPTMnet; Q61056; -.
DR PhosphoSitePlus; Q61056; -.
DR MaxQB; Q61056; -.
DR PaxDb; Q61056; -.
DR PRIDE; Q61056; -.
DR ProteomicsDB; 300125; -. [Q61056-1]
DR ProteomicsDB; 300126; -. [Q61056-2]
DR ABCD; Q61056; 1 sequenced antibody.
DR DNASU; 22063; -.
DR GeneID; 22063; -.
DR KEGG; mmu:22063; -.
DR UCSC; uc009rbj.1; mouse. [Q61056-1]
DR CTD; 7220; -.
DR MGI; MGI:109528; Trpc1.
DR eggNOG; KOG3609; Eukaryota.
DR InParanoid; Q61056; -.
DR OrthoDB; 824310at2759; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR Reactome; R-MMU-5578775; Ion homeostasis.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 22063; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Trpc1; mouse.
DR PRO; PR:Q61056; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q61056; protein.
DR GO; GO:0016323; C:basolateral plasma membrane; IMP:MGI.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0043034; C:costamere; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0043235; C:receptor complex; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; IDA:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005261; F:cation channel activity; ISO:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0015279; F:store-operated calcium channel activity; IMP:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0042438; P:melanin biosynthetic process; ISO:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0046541; P:saliva secretion; IMP:MGI.
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_0000215304"
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..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..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 TOPO_DOM 638..793
FT /note="Cytoplasmic"
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 Beta)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_006561"
SQ SEQUENCE 793 AA; 91213 MW; CBECB08C0D72E5DF CRC64;
MMAALYPSTD LSGVSSSSLP SSPSSSSPNE VMALKDVREV KEENTLNEKL FLLACDKGDY
YMVKKILEEN SSGDLNINCV DVLGRNAVTI TIENESLDIL 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
