ID TRPC4_RAT Reviewed; 977 AA.
AC O35119; Q9EQ74; Q9EQ75;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 24-JAN-2024, entry version 159.
DE RecName: Full=Short transient receptor potential channel 4;
DE Short=Trp4;
DE Short=TrpC4;
DE AltName: Full=Capacitative calcium entry channel 1;
DE Short=CCE1;
GN Name=Trpc4;
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] (ISOFORM ALPHA).
RC STRAIN=Wistar Imamichi; TISSUE=Brain;
RX PubMed=9037541; DOI=10.1016/s0169-328x(96)00208-2;
RA Funayama M., Goto K., Kondo H.;
RT "Cloning and expression localization of cDNA for rat homolog of TRP
RT protein, a possible store-operated calcium (Ca2+) channel.";
RL Brain Res. Mol. Brain Res. 43:259-266(1996).
RN [2]
RP SEQUENCE REVISION.
RA Otsuka Y., Kondo H.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RC STRAIN=Sprague-Dawley;
RX PubMed=10980202; DOI=10.1074/jbc.m006635200;
RA Tang Y., Tang J., Chen Z., Trost C., Flockerzi V., Li M., Ramesh V.,
RA Zhu M.X.;
RT "Association of mammalian trp4 and phospholipase C isozymes with a PDZ
RT domain-containing protein, NHERF.";
RL J. Biol. Chem. 275:37559-37564(2000).
RN [4]
RP SUBUNIT.
RX PubMed=12857742; DOI=10.1074/jbc.m306705200;
RA Strubing C., Krapivinsky G., Krapivinsky L., Clapham D.E.;
RT "Formation of novel TRPC channels by complex subunit interactions in
RT embryonic brain.";
RL J. Biol. Chem. 278:39014-39019(2003).
CC -!- FUNCTION: Thought to form non-selective a receptor-activated 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. Acts as a cell-cell contact-dependent
CC endothelial calcium entry channel. Has also been shown to be calcium-
CC selective (By similarity). May also be activated by intracellular
CC calcium store depletion. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer and heterotetramer with TRPC1 and/or TRPC5
CC (PubMed:12857742). Isoform alpha but not isoform beta interacts with
CC ITPR1, ITPR2 and ITPR3 (By similarity). Interacts with NHERF1 (By
CC similarity). Interacts with MX1 and RNF24 (By similarity). Interacts
CC (via CIRB domain) with SESTD1 (via the spectrin 1 repeat) and SPTBN5
CC (via C-terminus) (By similarity). Interacts with CDH5 and CTNNB1 (By
CC similarity). Interacts (via protein 4.1-binding domain) with EPB41L2
CC (By similarity). Interacts with TRPC4AP (By similarity). Interacts with
CC PLSCR1 (By similarity). {ECO:0000250|UniProtKB:Q9QUQ5,
CC ECO:0000250|UniProtKB:Q9UBN4, ECO:0000269|PubMed:12857742}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=O35119-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=O35119-2; Sequence=VSP_006571;
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC4 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23599.2; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB008889; BAA23599.2; ALT_FRAME; mRNA.
DR EMBL; AF288407; AAG21809.1; -; mRNA.
DR EMBL; AF288408; AAG21810.1; -; mRNA.
DR AlphaFoldDB; O35119; -.
DR SMR; O35119; -.
DR STRING; 10116.ENSRNOP00000042886; -.
DR PhosphoSitePlus; O35119; -.
DR PaxDb; 10116-ENSRNOP00000042886; -.
DR UCSC; RGD:621276; rat. [O35119-1]
DR AGR; RGD:621276; -.
DR RGD; 621276; Trpc4.
DR eggNOG; KOG3609; Eukaryota.
DR InParanoid; O35119; -.
DR PhylomeDB; O35119; -.
DR Reactome; R-RNO-3295583; TRP channels.
DR PRO; PR:O35119; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0034704; C:calcium channel complex; ISO:RGD.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005901; C:caveola; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0030863; C:cortical cytoskeleton; 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:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0045296; F:cadherin binding; ISO:RGD.
DR GO; GO:0005262; F:calcium channel activity; IDA:RGD.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:RGD.
DR GO; GO:0015279; F:store-operated calcium channel activity; ISO:RGD.
DR GO; GO:0070509; P:calcium ion import; ISO:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IDA:RGD.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; ISO:RGD.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0106129; P:positive regulation of store-operated calcium entry; IMP:RGD.
DR GO; GO:0099605; P:regulation of action potential firing rate; IMP:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
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; IPR005460; TRPC4_channel.
DR InterPro; IPR002153; TRPC_channel.
DR NCBIfam; TIGR00870; trp; 1.
DR PANTHER; PTHR10117:SF25; SHORT TRANSIENT RECEPTOR POTENTIAL CHANNEL 4; 1.
DR PANTHER; PTHR10117; TRANSIENT RECEPTOR POTENTIAL CHANNEL; 1.
DR Pfam; PF00023; Ank; 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; PR01645; TRPCHANNEL4.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01420; TRP_2; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Coiled coil; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..977
FT /note="Short transient receptor potential channel 4"
FT /id="PRO_0000215316"
FT TOPO_DOM 1..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..469
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..974
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 31..60
FT /note="ANK 1"
FT REPEAT 69..97
FT /note="ANK 2"
FT REPEAT 98..124
FT /note="ANK 3"
FT REPEAT 141..170
FT /note="ANK 4"
FT REGION 87..172
FT /note="Multimerization domain"
FT /evidence="ECO:0000250"
FT REGION 254..304
FT /note="Multimerization domain"
FT /evidence="ECO:0000250"
FT REGION 615..977
FT /note="Binds to ITPR1, ITPR2 and ITPR3"
FT /evidence="ECO:0000250"
FT REGION 767..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..977
FT /note="PDZ-binding domain"
FT /evidence="ECO:0000250"
FT COILED 223..260
FT /evidence="ECO:0000255"
FT COMPBIAS 776..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 959
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN4"
FT MOD_RES 972
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN4"
FT VAR_SEQ 784..867
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10980202"
FT /id="VSP_006571"
FT CONFLICT 337
FT /note="Missing (in Ref. 1; BAA23599)"
FT /evidence="ECO:0000305"
FT CONFLICT 390..411
FT /note="Missing (in Ref. 1; BAA23599)"
FT /evidence="ECO:0000305"
FT CONFLICT 594
FT /note="D -> E (in Ref. 1; BAA23599)"
FT /evidence="ECO:0000305"
FT CONFLICT 888
FT /note="K -> Q (in Ref. 1; BAA23599)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 977 AA; 111848 MW; 6F86DA95261E0ECD CRC64;
MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK
ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK
PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE
CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE
YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF
VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR
KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ
MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL
FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY
YEETKGLSCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTDFVGATM
FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI
PSPKSLWYLV KWIWTHLCKK KMRRKPESFG TIGRRAADNL RRHHQYQEVM RNLVKRYVAA
MIREAKTEEG LTEENVKELK QDISSFRFEV LGLLRGSKLS TIQSANAASS ASSADSDEKS
HSEGNGKDKR KNLSLFDLTT LIHPRSAVIA SERHNLSNGS ALVVQEPPRE KQRKVNFVAD
IKNFGLFHRR SKQNAAEQNA NQIFSVSEEI TRQQAAGALE RNIQLESKGL ASRGDRSIPG
LNEQCVLVDH RERNTDTLGL QVGKRVCSSF KSEKVVVEDT VPIIPKEKHA QEEDSSIDYD
LSPTDTVAHE DYVTTRL
//
