TRPC4_BOVIN
ID TRPC4_BOVIN Reviewed; 979 AA.
AC P79100;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Short transient receptor potential channel 4;
DE Short=TrpC4;
DE AltName: Full=Capacitative calcium entry channel 1;
DE Short=CCE1;
GN Name=TRPC4;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC TISSUE=Adrenal gland, and Retina;
RX PubMed=8947038; DOI=10.1002/j.1460-2075.1996.tb01004.x;
RA Philipp S., Cavalie A., Freichel M., Wissenbach U., Zimmer S., Trost C.,
RA Marquart A., Murakami M., Flockerzi V.;
RT "A mammalian capacitative calcium entry channel homologous to Drosophila
RT TRP and TRPL.";
RL EMBO J. 15:6166-6171(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RC TISSUE=Adrenal gland;
RX PubMed=9498815; DOI=10.1016/s0014-5793(98)00041-6;
RA Freichel M., Wissenbach U., Philipp S., Flockerzi V.;
RT "Alternative splicing and tissue specific expression of the 5' truncated
RT bCCE 1 variant bCCE 1delta514.";
RL FEBS Lett. 422:354-358(1998).
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. Has also been shown to be calcium-selective.
CC May also be activated by intracellular calcium store depletion. Acts as
CC a cell-cell contact-dependent endothelial calcium entry channel (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer and heterotetramer with TRPC1 and/or TRPC5 (By
CC similarity). Isoform alpha interacts with ITPR1, ITPR2 and ITPR3 (By
CC similarity). Interacts with (via the PDZ-binding domain) with
CC SLC9A3R1/NHERF (By similarity). Interacts with MX1 and RNF24 (By
CC similarity). Interacts (via CIRB domain) with SESTD1 (via the spectrin
CC 1 repeat) (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}.
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=P79100-1; Sequence=Displayed;
CC Name=Beta; Synonyms=Delta 514;
CC IsoId=P79100-2; Sequence=VSP_006566;
CC -!- TISSUE SPECIFICITY: Expressed in adrenal gland. Lower expression in
CC heart and retina. Also expressed in testis. The short isoform is
CC specifically expressed in the adrenal gland.
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=CAA68125.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X99792; CAA68125.1; ALT_INIT; mRNA.
DR EMBL; AJ224862; CAA12161.1; -; mRNA.
DR RefSeq; NP_776903.1; NM_174478.2.
DR RefSeq; XP_005213611.1; XM_005213554.3.
DR RefSeq; XP_010808964.1; XM_010810662.2.
DR RefSeq; XP_015329236.1; XM_015473750.1.
DR RefSeq; XP_015329237.1; XM_015473751.1.
DR RefSeq; XP_015329238.1; XM_015473752.1.
DR AlphaFoldDB; P79100; -.
DR SMR; P79100; -.
DR STRING; 9913.ENSBTAP00000012378; -.
DR PaxDb; P79100; -.
DR PRIDE; P79100; -.
DR Ensembl; ENSBTAT00000065392; ENSBTAP00000055610; ENSBTAG00000009405. [P79100-2]
DR GeneID; 282102; -.
DR KEGG; bta:282102; -.
DR CTD; 7223; -.
DR VEuPathDB; HostDB:ENSBTAG00000009405; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR HOGENOM; CLU_005716_4_1_1; -.
DR InParanoid; P79100; -.
DR OMA; QSPDEKC; -.
DR OrthoDB; 824310at2759; -.
DR TreeFam; TF313147; -.
DR Reactome; R-BTA-3295583; TRP channels.
DR Proteomes; UP000009136; Chromosome 12.
DR Bgee; ENSBTAG00000009405; Expressed in myometrium and 86 other tissues.
DR ExpressionAtlas; P79100; baseline.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IBA:GO_Central.
DR GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
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 2: Evidence at transcript 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..979
FT /note="Short transient receptor potential channel 4"
FT /id="PRO_0000215313"
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..979
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..979
FT /note="Binds to ITPR1, ITPR2 and ITPR3"
FT /evidence="ECO:0000250"
FT REGION 762..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..979
FT /note="PDZ-binding domain"
FT /evidence="ECO:0000250"
FT COILED 223..260
FT /evidence="ECO:0000255"
FT COMPBIAS 773..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 961
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN4"
FT MOD_RES 974
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN4"
FT VAR_SEQ 1..511
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:9498815"
FT /id="VSP_006566"
SQ SEQUENCE 979 AA; 112287 MW; E9365645BE640E09 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 YRDDNSLLEE QSGNDLARLK LAIKYRQKEF
VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIVGLLF 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 EFTEFVGATM
FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI
PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGRRAADNL RRHHQYQEVM RNLVKRYVAA
MIRDAKTEEG LTEENFKELK QDISSFRFEV LGLLRGSKLS TVQSAQGTKE SSNSADSDEK
SDNEGSSKDK KKNFSLFDLT TLIHPRSAAI AAERHTISNG SALVVQEPPR EKQRKVNFVT
DIRHFGLFHR RSKQHAAAEQ NANQIFSVSE GVARQQAEGP LERSIQLESR TLASRGDLNI
PGLSEQCILV DHRERNTDSL GVQVSKRVCS FKSEKVVVED TVPIIPKEKK HAKEEDSSAD
YDANLTDTIT HEDYVTTRL
