ID TRPC1_RABIT Reviewed; 759 AA.
AC Q9TUN9;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=Short transient receptor potential channel 1;
DE Short=TrpC1;
DE AltName: Full=Calcium influx channel TRPC1A;
GN Name=TRPC1; Synonyms=TRPC1A;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Cornea;
RA Rae J.L.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Interacts with PLSCR1 (By similarity).
CC {ECO:0000250|UniProtKB:P48995, ECO:0000250|UniProtKB:Q61056,
CC ECO:0000250|UniProtKB:Q9QX01}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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; AF170493; AAD50982.1; -; mRNA.
DR RefSeq; NP_001076120.1; NM_001082651.1.
DR AlphaFoldDB; Q9TUN9; -.
DR SMR; Q9TUN9; -.
DR STRING; 9986.ENSOCUP00000015208; -.
DR PaxDb; 9986-ENSOCUP00000015208; -.
DR GeneID; 100009352; -.
DR KEGG; ocu:100009352; -.
DR CTD; 7220; -.
DR eggNOG; KOG3609; Eukaryota.
DR InParanoid; Q9TUN9; -.
DR OrthoDB; 5406916at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW ANK repeat; Calcium; Calcium channel; Calcium transport; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..759
FT /note="Short transient receptor potential channel 1"
FT /id="PRO_0000215305"
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; 87627 MW; 71225584A59462EF CRC64;
MMAALYPSTD LSGASSSSLP SSPSSSSPNE VMALKDVREV KEENTLNEKL FLLACDKGDY
YMVKKILEEN SSGDLNINCV DVLGRNAVTI TIENENLDIL QLLLDYGCQK LMERIQNPEY
STTMDVAPVI LAAHRNNYEI LTMLLKQDVS LPKPHAVGCE CTLCSAKNKK DSLRHSRFRL
DIYRCLASPA LIMLTEEDPI LRAFELSADL KELSLVEVEF RNDYEELARQ 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 PKEQKDCVGI
FCEQQSNDTF HSFIGTCFAL FWYIFSLAHV AIFVTRFSYG EELQSFVGAV IVGTYNVVVV
IVLTKLLVAM LHKSFQLIAN HEDKEWKFAR AKLWLSYFDD KCTLPPPFNI IPSPKTICYM
ISSLSKWICS HTSKGKVKRQ NSLKEWRNLK QKRDENYQKV MCCLVHRYLT SMRQKMQSTD
QATVENLNEL RQDLSKFRNE IRDLLGFRTS KYAMFYPRN
//
