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TRPC4_RAT
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   03-AUG-2022, entry version 153.
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 SLC9A3R1/NHERF
CC       (By similarity). Interacts with MX1 and RNF24 (By similarity).
CC       Interacts (via CIRB domain) with SESTD1 (via the spectrin 1 repeat) and
CC       SPTBN5 (via C-terminus) (By similarity). Interacts with CDH5 and CTNNB1
CC       (By similarity). Interacts (via protein 4.1-binding domain) with
CC       EPB41L2 (By similarity). Interacts with TRPC4AP (By similarity).
CC       Interacts with 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; O35119; -.
DR   UCSC; RGD:621276; rat. [O35119-1]
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:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA: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:0006828; P:manganese ion transport; IBA:GO_Central.
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; -; 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   PANTHER; PTHR10117; PTHR10117; 1.
DR   PANTHER; PTHR10117:SF25; PTHR10117:SF25; 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   SUPFAM; SSF48403; SSF48403; 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
 
 
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