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   24-JAN-2024, entry version 146.
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.
DR   AlphaFoldDB; Q9QX01; -.
DR   SMR; Q9QX01; -.
DR   BioGRID; 250144; 5.
DR   CORUM; Q9QX01; -.
DR   STRING; 10116.ENSRNOP00000074229; -.
DR   iPTMnet; Q9QX01; -.
DR   PhosphoSitePlus; Q9QX01; -.
DR   PaxDb; 10116-ENSRNOP00000013144; -.
DR   ABCD; Q9QX01; 1 sequenced antibody.
DR   GeneID; 89821; -.
DR   KEGG; rno:89821; -.
DR   UCSC; RGD:619783; rat. [Q9QX01-1]
DR   AGR; RGD:619783; -.
DR   CTD; 7220; -.
DR   RGD; 619783; Trpc1.
DR   eggNOG; KOG3609; Eukaryota.
DR   InParanoid; Q9QX01; -.
DR   OrthoDB; 5406916at2759; -.
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: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:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:RGD.
DR   GO; GO:0005261; F:monoatomic cation channel activity; 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: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; Ankyrin repeat-containing domain; 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   NCBIfam; TIGR00870; trp; 1.
DR   PANTHER; PTHR10117:SF56; SHORT TRANSIENT RECEPTOR POTENTIAL CHANNEL 1; 1.
DR   PANTHER; PTHR10117; TRANSIENT RECEPTOR POTENTIAL CHANNEL; 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; PR01642; TRPCHANNEL1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM01420; TRP_2; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 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
//