TRPC1_RAT
ID TRPC1_RAT Reviewed; 759 AA.
AC Q9QX01;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 138.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10199829; DOI=10.1152/ajpcell.1999.276.4.c969;
RA Wang W., O'Connell B., Dykeman R., Sakai T., Delporte C., Swaim W., Zhu X.,
RA Birnbaumer L., Ambudkar I.S.;
RT "Cloning of Trp1beta isoform from rat brain: immunodetection and
RT localization of the endogenous Trp1 protein.";
RL Am. J. Physiol. 276:C969-C979(1999).
RN [2]
RP TISSUE SPECIFICITY, AND INTERACTION WITH TRPC4 AND TRPC5.
RX PubMed=11301024; DOI=10.1016/s0896-6273(01)00240-9;
RA Strubing C., Krapivinsky G., Krapivinsky L., Clapham D.E.;
RT "TRPC1 and TRPC5 form a novel cation channel in mammalian brain.";
RL Neuron 29:645-655(2001).
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: Heteromer with TRPC4 and/or TRPC5 (PubMed:11301024). Interacts
CC with TRPC4 and TRPC5 (By similarity). Interacts with ITPR3 (By
CC similarity). Interacts with MX1 and RNF24 (By similarity). Interacts
CC with FKBP4 (By similarity). Interacts with TRPC4AP (By similarity).
CC Interacts with PLSCR1 (By similarity). {ECO:0000250|UniProtKB:P48995,
CC ECO:0000250|UniProtKB:Q61056, ECO:0000269|PubMed:11301024}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta;
CC IsoId=Q9QX01-1; Sequence=Displayed;
CC Name=Alpha;
CC IsoId=Q9QX01-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Expressed in brain, hippocampus, amygdala, Purkinje
CC cells and single neurons in the cortex and striatum.
CC {ECO:0000269|PubMed:11301024}.
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}.
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DR EMBL; AF061266; AAC67387.1; -; mRNA.
DR RefSeq; NP_446010.1; NM_053558.1. [Q9QX01-1]
DR AlphaFoldDB; Q9QX01; -.
DR SMR; Q9QX01; -.
DR BioGRID; 250144; 5.
DR CORUM; Q9QX01; -.
DR STRING; 10116.ENSRNOP00000013144; -.
DR iPTMnet; Q9QX01; -.
DR PaxDb; Q9QX01; -.
DR PRIDE; Q9QX01; -.
DR ABCD; Q9QX01; 1 sequenced antibody.
DR GeneID; 89821; -.
DR KEGG; rno:89821; -.
DR UCSC; RGD:619783; rat. [Q9QX01-1]
DR CTD; 7220; -.
DR RGD; 619783; Trpc1.
DR eggNOG; KOG3609; Eukaryota.
DR InParanoid; Q9QX01; -.
DR PhylomeDB; Q9QX01; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR Reactome; R-RNO-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR PRO; PR:Q9QX01; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0043034; C:costamere; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0030017; C:sarcomere; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0005261; F:cation channel activity; ISO:RGD.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0015279; F:store-operated calcium channel activity; ISO:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0042438; P:melanin biosynthetic process; ISO:RGD.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0051592; P:response to calcium ion; ISO:RGD.
DR GO; GO:0046541; P:saliva secretion; ISO:RGD.
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; 2.
DR PANTHER; PTHR10117:SF56; PTHR10117:SF56; 2.
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..759
FT /note="Short transient receptor potential channel 1"
FT /id="PRO_0000215306"
FT TOPO_DOM 1..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..381
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..505
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..552
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..582
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 583..603
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..759
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 46..75
FT /note="ANK 1"
FT REPEAT 83..112
FT /note="ANK 2"
FT REPEAT 124..153
FT /note="ANK 3"
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"
SQ SEQUENCE 759 AA; 87618 MW; CEBB27A1DF6420F4 CRC64;
MMAALYPSTD LSGVSSSSLP SSPSSSSPNE VMALKDVREV KEENTLNEKL FLLACDKGDY
YMVKKILEEN SSGDLNINCV DVLGRNAVTI TIENESLDIL QLLLDYGCQK LMERIQNPEY
STTMDVAPVI LAAHRNNYEI LTMLLKQDVA LPKPHAVGCE CTLCSAKNKK DSLRHSRFRL
DIYRCLASPA LIMLTEEDPI LRAFELSADL KELSLVEVEF WNDYEELARQ CKMFAKDLLA
QARNSRELEV ILNHTSSDEP LDKRGLLEER MNLSRLKLAI KYNQKEFVSQ SNCQQFLNTV
WFGQMSGYRR KPTCKKIMTV LTVGIFWPVL SLCYLIAPKS QFGRIIHTPF MKFIIHGASY
FTFLLLLNLY SLVYNEDKKN TMGPALERID YLLILWIIGM IWSDIKRLWY EGLEDFLEES
RNQLSFVMNS LYLATFALKV VAHNKFHDFA DRKDWDAFHP TLVAEGLFAF ANVLSYLRLF
FMYTTSSILG PLQISMGQML QDFGKFLGMF LLVLFSFTIG LTQLYDKGYT SKEQKDCVGI
FCEQQSNDTF HSFIGTCFAL FWYIFSLAHV AIFVTRFSYG EELQSFVGAV IVGTYNVVVV
IVLTKLLVAM LHKSFQLIAN HEDKEWKFAR AKLWLSYFDD KCTLPPPFNI IPSPKTICYM
ISSLSKWVCS HTSKGKVRRQ NSLKEWRNLK QKRDENYQKV MCCLVHRYLT SMRQKMQSTD
QATVENLNEL RQDLSKFRNE IRDLLGFRTS KYAMFYPKN
