ID TRPC3_HUMAN Reviewed; 848 AA. AC Q13507; O00593; Q15660; Q52M35; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 2. DT 15-JUN-2010, entry version 99. DE RecName: Full=Short transient receptor potential channel 3; DE Short=TrpC3; DE AltName: Full=Transient receptor protein 3; DE Short=TRP-3; DE Short=hTrp-3; DE Short=hTrp3; GN Name=TRPC3; Synonyms=TRP3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Embryonic kidney; RX MEDLINE=96234226; PubMed=8646775; DOI=10.1016/S0092-8674(00)81233-7; RA Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E., RA Birnbaumer L.; RT "trp, a novel mammalian gene family essential for agonist-activated RT capacitative Ca2+ entry."; RL Cell 85:661-671(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97358541; PubMed=9215637; DOI=10.1016/S0092-8674(00)80302-5; RA Xu X.-Z.S., Li H.-S., Guggino W.B., Montell C.; RT "Coassembly of TRP and TRPL produces a distinct store-operated RT conductance."; RL Cell 89:1155-1164(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 632-747. RC TISSUE=Fetal brain; RX MEDLINE=96003837; PubMed=7568191; DOI=10.1073/pnas.92.21.9652; RA Wes P.D., Chevesich J., Jeromin A., Rosenberg C., Stetten G., RA Montell C.; RT "TRPC1, a human homolog of a Drosophila store-operated channel."; RL Proc. Natl. Acad. Sci. U.S.A. 92:9652-9656(1995). RN [5] RP CHARACTERIZATION. RX MEDLINE=98204851; PubMed=9535843; DOI=10.1074/jbc.273.15.8675; RA Vannier B., Zhu X., Brown D., Birnbaumer L.; RT "The membrane topology of human transient receptor potential 3 as RT inferred from glycosylation-scanning mutagenesis and epitope RT immunocytochemistry."; RL J. Biol. Chem. 273:8675-8679(1998). RN [6] RP FUNCTION. RX MEDLINE=98079037; PubMed=9417057; DOI=10.1074/jbc.273.1.133; RA Zhu X., Jiang M., Birnbaumer L.; RT "Receptor-activated Ca2+ influx via human Trp3 stably expressed in RT human embryonic kidney (HEK)293 cells. Evidence for a non-capacitative RT Ca2+ entry."; RL J. Biol. Chem. 273:133-142(1998). RN [7] RP INTERACTION WITH IP3 RECEPTOR. RX MEDLINE=99068646; PubMed=9853757; DOI=10.1038/24890; RA Kiselyov K., Xu X., Mozhayeva G., Kuo T., Pessah I., Mignery G., RA Zhu X., Birnbaumer L., Muallem S.; RT "Functional interaction between InsP3 receptors and store-operated RT Htrp3 channels."; RL Nature 396:478-482(1998). RN [8] RP FUNCTION. RX MEDLINE=99127891; PubMed=9930701; DOI=10.1038/16711; RA Hofmann T., Obukhov A.G., Schaefer M., Harteneck C., Gudermann T., RA Schultz G.; RT "Direct activation of human TRPC6 and TRPC3 channels by RT diacylglycerol."; RL Nature 397:259-263(1999). RN [9] RP INTERACTION WITH IP3 RECEPTOR. RX MEDLINE=20079588; PubMed=10611319; DOI=10.1073/pnas.96.26.14955; RA Boulay G., Brown D.M., Qin N., Jiang M., Dietrich A., Zhu M.X., RA Chen Z., Birnbaumer M., Mikoshiba K., Birnbaumer L.; RT "Modulation of Ca(2+) entry by polypeptides of the inositol 1,4, 5- RT trisphosphate receptor (IP3R) that bind transient receptor potential RT (TRP): evidence for roles of TRP and IP3R in store depletion-activated RT Ca(2+) entry."; RL Proc. Natl. Acad. Sci. U.S.A. 96:14955-14960(1999). RN [10] RP INTERACTION WITH MX1. RX PubMed=15757897; DOI=10.1074/jbc.M500391200; RA Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N., RA St-Hilaire M., Pinard M., Boulay G.; RT "MxA, a member of the dynamin superfamily, interacts with the ankyrin- RT like repeat domain of TRPC."; RL J. Biol. Chem. 280:19393-19400(2005). RN [11] RP INTERACTION WITH RNF24. RX PubMed=17850865; DOI=10.1016/j.ceca.2007.07.009; RA Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.; RT "RNF24, a new TRPC interacting protein, causes the intracellular RT retention of TRPC."; RL Cell Calcium 43:432-443(2008). CC -!- FUNCTION: Thought to form a receptor-activated non-selective CC calcium permeant cation channel. Probably is operated by a CC phosphatidylinositol second messenger system activated by receptor CC tyrosine kinases or G-protein coupled receptors. Activated by CC diacylglycerol (DAG) in a membrane-delimited fashion, CC independently of protein kinase C, and by inositol-1,4,5- CC triphosphate receptors (ITPR) with bound IP3. May also be CC activated by internal calcium store depletion. CC -!- SUBUNIT: Interacts with TRPC1. Interacts with ITPR3. Interacts CC with MX1 and RNF24. CC -!- INTERACTION: CC Q14573:ITPR3; NbExp=3; IntAct=EBI-520807, EBI-351055; CC P20591:MX1; NbExp=2; IntAct=EBI-520807, EBI-929476; CC P10686:Plcg1 (xeno); NbExp=1; IntAct=EBI-520807, EBI-520788; CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain and at much CC lower levels in ovary, colon, small intestine, lung, prostate, CC placenta and testis. CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) CC superfamily. STrpC family. TRPC3 subfamily. CC -!- SIMILARITY: Contains 5 ANK repeats. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U47050; AAC51653.1; -; mRNA. DR EMBL; Y13758; CAA74083.1; -; mRNA. DR EMBL; BC093682; AAH93682.1; -; mRNA. DR EMBL; BC093684; AAH93684.1; -; mRNA. DR EMBL; X89068; CAA61448.1; -; mRNA. DR IPI; IPI00748783; -. DR RefSeq; NP_001124170.1; -. DR RefSeq; NP_003296.1; -. DR UniGene; Hs.150981; -. DR SMR; Q13507; 43-187. DR IntAct; Q13507; 3. DR STRING; Q13507; -. DR TCDB; 1.A.4.1.4; transient receptor potential Ca2+ channel (TRP-CC) family. DR PhosphoSite; Q13507; -. DR PRIDE; Q13507; -. DR Ensembl; ENST00000264811; ENSP00000264811; ENSG00000138741; Homo sapiens. DR Ensembl; ENST00000379645; ENSP00000368966; ENSG00000138741; Homo sapiens. DR GeneID; 7222; -. DR KEGG; hsa:7222; -. DR UCSC; uc003ief.1; human. DR CTD; 7222; -. DR GeneCards; GC04M123079; -. DR H-InvDB; HIX0031423; -. DR HGNC; HGNC:12335; TRPC3. DR MIM; 602345; gene. DR PharmGKB; PA37008; -. DR eggNOG; prNOG18516; -. DR HOVERGEN; HBG068337; -. DR InParanoid; Q13507; -. DR PhylomeDB; Q13507; -. DR Pathway_Interaction_DB; pi3kplctrkpathway; Trk receptor signaling mediated by PI3K and PLC-gamma. DR NextBio; 28283; -. DR ArrayExpress; Q13507; -. DR Bgee; Q13507; -. DR CleanEx; HS_TRPC3; -. DR Genevestigator; Q13507; -. DR GermOnline; ENSG00000138741; Homo sapiens. DR GO; GO:0005887; C:integral to plasma membrane; IDA:MGI. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0015279; F:store-operated calcium channel activity; TAS:ProtInc. DR GO; GO:0006816; P:calcium ion transport; TAS:ProtInc. DR GO; GO:0007602; P:phototransduction; TAS:ProtInc. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR020683; Ankyrin_rpt-contain_dom. DR InterPro; IPR005821; Ion_trans. DR InterPro; IPR002153; Trans_rcpt. DR InterPro; IPR013555; TRP_2. DR InterPro; IPR004729; TRP_channel. DR InterPro; IPR005459; TRP_channel3. DR Gene3D; G3DSA:1.25.40.20; ANK; 1. DR Pfam; PF00520; Ion_trans; 1. DR Pfam; PF08344; TRP_2; 1. DR PRINTS; PR01097; TRNSRECEPTRP. DR PRINTS; PR01644; TRPCHANNEL3. DR SMART; SM00248; ANK; 3. DR SUPFAM; SSF48403; ANK; 1. DR TIGRFAMs; TIGR00870; trp; 1. DR PROSITE; PS50297; ANK_REP_REGION; 1. DR PROSITE; PS50088; ANK_REPEAT; FALSE_NEG. PE 1: Evidence at protein level; KW ANK repeat; Calcium; Calcium channel; Calcium transport; KW Complete proteome; Ion transport; Ionic channel; Membrane; Repeat; KW Transmembrane; Transport. FT CHAIN 1 848 Short transient receptor potential FT channel 3. FT /FTId=PRO_0000215310. FT TOPO_DOM 1 349 Cytoplasmic (Potential). FT TRANSMEM 350 370 Helical; (Potential). FT TOPO_DOM 371 381 Extracellular (Potential). FT TRANSMEM 382 402 Helical; (Potential). FT TOPO_DOM 403 430 Cytoplasmic (Potential). FT TRANSMEM 431 451 Helical; (Potential). FT TOPO_DOM 452 463 Extracellular (Potential). FT TRANSMEM 464 484 Helical; (Potential). FT TOPO_DOM 485 535 Cytoplasmic (Potential). FT TRANSMEM 536 556 Helical; (Potential). FT TOPO_DOM 557 579 Extracellular (Potential). FT TRANSMEM 580 600 Helical; (Potential). FT TOPO_DOM 601 615 Cytoplasmic (Potential). FT TRANSMEM 616 636 Helical; (Potential). FT TOPO_DOM 637 649 Extracellular (Potential). FT TRANSMEM 650 670 Helical; (Potential). FT TOPO_DOM 671 706 Cytoplasmic (Potential). FT TRANSMEM 707 726 Helical; (Potential). FT TOPO_DOM 727 848 Extracellular (Potential). FT REPEAT 38 67 ANK 1. FT REPEAT 73 102 ANK 2. FT REPEAT 104 130 ANK 3. FT REPEAT 159 188 ANK 4. FT REPEAT 561 590 ANK 5. FT REGION 777 797 Binds to IP3R3. FT CONFLICT 739 742 EMGM -> GNGEW (in Ref. 4; CAA61448). SQ SEQUENCE 848 AA; 97355 MW; 1DBC92BC941DF416 CRC64; MEGSPSLRRM TVMREKGRRQ AVRGPAFMFN DRGTSLTAEE ERFLDAAEYG NIPVVRKMLE ESKTLNVNCV DYMGQNALQL AVGNEHLEVT ELLLKKENLA RIGDALLLAI SKGYVRIVEA ILNHPGFAAS KRLTLSPCEQ ELQDDDFYAY DEDGTRFSPD ITPIILAAHC QKYEVVHMLL MKGARIERPH DYFCKCGDCM EKQRHDSFSH SRSRINAYKG LASPAYLSLS SEDPVLTALE LSNELAKLAN IEKEFKNDYR KLSMQCKDFV VGVLDLCRDS EEVEAILNGD LESAEPLEVH RHKASLSRVK LAIKYEVKKF VAHPNCQQQL LTIWYENLSG LREQTIAIKC LVVLVVALGL PFLAIGYWIA PCSRLGKILR SPFMKFVAHA ASFIIFLGLL VFNASDRFEG ITTLPNITVT DYPKQIFRVK TTQFTWTEML IMVWVLGMMW SECKELWLEG PREYILQLWN VLDFGMLSIF IAAFTARFLA FLQATKAQQY VDSYVQESDL SEVTLPPEIQ YFTYARDKWL PSDPQIISEG LYAIAVVLSF SRIAYILPAN ESFGPLQISL GRTVKDIFKF MVLFIMVFFA FMIGMFILYS YYLGAKVNAA FTTVEESFKT LFWSIFGLSE VTSVVLKYDH KFIENIGYVL YGIYNVTMVV VLLNMLIAMI NSSYQEIEDD SDVEWKFARS KLWLSYFDDG KTLPPPFSLV PSPKSFVYFI MRIVNFPKCR RRRLQKDIEM GMGNSKSRLN LFTQSNSRVF ESHSFNSILN QPTRYQQIMK RLIKRYVLKA QVDKENDEVN EGELKEIKQD ISSLRYELLE DKSQATEELA ILIHKLSEKL NPSMLRCE //