TRPC6_MOUSE
ID TRPC6_MOUSE Reviewed; 930 AA.
AC Q61143; B9EIW2; Q9Z2J1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Short transient receptor potential channel 6 {ECO:0000250|UniProtKB:Q9Y210};
DE Short=TrpC6 {ECO:0000303|PubMed:14761972};
DE AltName: Full=Calcium entry channel;
DE AltName: Full=Transient receptor protein 6;
DE Short=TRP-6;
GN Name=Trpc6 {ECO:0000303|PubMed:14761972, ECO:0000312|MGI:MGI:109523};
GN Synonyms=Trp6, Trrp6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=9368034; DOI=10.1074/jbc.272.47.29672;
RA Boulay G., Zhu X., Peyton M., Jiang M., Hurst R., Stefani E.,
RA Birnbaumer L.;
RT "Cloning and expression of a novel mammalian homolog of Drosophila
RT transient receptor potential (Trp) involved in calcium entry secondary to
RT activation of receptors coupled by the Gq class of G protein.";
RL J. Biol. Chem. 272:29672-29680(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J;
RX PubMed=10050885; DOI=10.1038/sj.onc.1202445;
RA Buess M., Engler O., Hirsch H.H., Moroni C.;
RT "Search for oncogenic regulators in an autocrine tumor model using
RT differential display PCR: identification of novel candidate genes including
RT the calcium channel mtrp6.";
RL Oncogene 18:1487-1494(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 631-739.
RC TISSUE=Brain;
RX 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 [6]
RP PHOSPHORYLATION BY FYN.
RX PubMed=14761972; DOI=10.1074/jbc.m311274200;
RA Hisatsune C., Kuroda Y., Nakamura K., Inoue T., Nakamura T., Michikawa T.,
RA Mizutani A., Mikoshiba K.;
RT "Regulation of TRPC6 channel activity by tyrosine phosphorylation.";
RL J. Biol. Chem. 279:18887-18894(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-814, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Activated by diacylglycerol (DAG) in a
CC membrane-delimited fashion, independently of protein kinase C. Seems
CC not to be activated by intracellular calcium store depletion.
CC {ECO:0000250|UniProtKB:Q9Y210}.
CC -!- SUBUNIT: Homodimer; forms channel complex. Interacts with MX1 and
CC RNF24. {ECO:0000250|UniProtKB:Q9Y210}.
CC -!- INTERACTION:
CC Q61143; Q96D31: ORAI1; Xeno; NbExp=2; IntAct=EBI-15563578, EBI-2291476;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y210};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y210}.
CC -!- TISSUE SPECIFICITY: Lung and brain.
CC -!- PTM: Phosphorylated by FYN, leading to an increase of TRPC6 channel
CC activity. {ECO:0000269|PubMed:14761972}.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC6 sub-subfamily. {ECO:0000305}.
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DR EMBL; U49069; AAC06146.1; -; mRNA.
DR EMBL; AF057748; AAC64394.1; -; mRNA.
DR EMBL; CH466522; EDL24958.1; -; Genomic_DNA.
DR EMBL; BC141131; AAI41132.1; -; mRNA.
DR CCDS; CCDS22815.1; -.
DR RefSeq; NP_038866.2; NM_013838.2.
DR RefSeq; XP_006509913.1; XM_006509850.3.
DR PDB; 6CV9; EM; 3.80 A; A/B/C/D=94-930.
DR PDBsum; 6CV9; -.
DR AlphaFoldDB; Q61143; -.
DR SMR; Q61143; -.
DR BioGRID; 204332; 3.
DR DIP; DIP-60893N; -.
DR IntAct; Q61143; 3.
DR STRING; 10090.ENSMUSP00000057965; -.
DR BindingDB; Q61143; -.
DR ChEMBL; CHEMBL1795081; -.
DR GuidetoPHARMACOLOGY; 491; -.
DR GlyGen; Q61143; 1 site.
DR iPTMnet; Q61143; -.
DR PhosphoSitePlus; Q61143; -.
DR MaxQB; Q61143; -.
DR PaxDb; Q61143; -.
DR PRIDE; Q61143; -.
DR ProteomicsDB; 300018; -.
DR Antibodypedia; 17956; 424 antibodies from 40 providers.
DR DNASU; 22068; -.
DR Ensembl; ENSMUST00000050433; ENSMUSP00000057965; ENSMUSG00000031997.
DR GeneID; 22068; -.
DR KEGG; mmu:22068; -.
DR UCSC; uc009odl.1; mouse.
DR CTD; 7225; -.
DR MGI; MGI:109523; Trpc6.
DR VEuPathDB; HostDB:ENSMUSG00000031997; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR HOGENOM; CLU_005716_4_2_1; -.
DR InParanoid; Q61143; -.
DR OMA; WISELFW; -.
DR OrthoDB; 1018075at2759; -.
DR PhylomeDB; Q61143; -.
DR TreeFam; TF313147; -.
DR Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-MMU-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 22068; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Trpc6; mouse.
DR PRO; PR:Q61143; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q61143; protein.
DR Bgee; ENSMUSG00000031997; Expressed in lumbar dorsal root ganglion and 79 other tissues.
DR ExpressionAtlas; Q61143; baseline and differential.
DR Genevisible; Q61143; MM.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISA:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0036057; C:slit diaphragm; IDA:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0042805; F:actinin binding; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; ISO:MGI.
DR GO; GO:0005261; F:cation channel activity; ISO:MGI.
DR GO; GO:0030276; F:clathrin binding; ISO:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:MGI.
DR GO; GO:0005216; F:ion channel activity; IDA:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0015279; F:store-operated calcium channel activity; IDA:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:MGI.
DR GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0007338; P:single fertilization; 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; IPR005462; TRPC6_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF7; PTHR10117:SF7; 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; PR01647; TRPCHANNEL6.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Calcium; Calcium channel; Calcium transport;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..930
FT /note="Short transient receptor potential channel 6"
FT /id="PRO_0000215323"
FT TOPO_DOM 1..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..486
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 508..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..591
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 592..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 613..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..705
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 727..930
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 96..125
FT /note="ANK 1"
FT REPEAT 131..160
FT /note="ANK 2"
FT REPEAT 162..188
FT /note="ANK 3"
FT REPEAT 217..246
FT /note="ANK 4"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 3..56
FT /note="Missing (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="A -> V (in Ref. 1; AAC06146)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="R -> W (in Ref. 1; AAC06146)"
FT /evidence="ECO:0000305"
FT CONFLICT 134
FT /note="N -> D (in Ref. 2; AAC64394)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="A -> S (in Ref. 1; AAC06146)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="Y -> D (in Ref. 1; AAC06146)"
FT /evidence="ECO:0000305"
FT CONFLICT 436..437
FT /note="RG -> PR (in Ref. 1; AAC06146)"
FT /evidence="ECO:0000305"
FT CONFLICT 905
FT /note="T -> S (in Ref. 1; AAC06146)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 930 AA; 106681 MW; 9501C8D50FF33430 CRC64;
MSQSPRFVTR RGGSLKAAPG AGTRRNESQD YLLMDELGDD GYPQLPLPPY GYYPSFRGNE
NRLTHRRQTI LREKGRRLAN RGPAYMFNDH STSLSIEEER FLDAAEYGNI PVVRKMLEEC
HSLNVNCVDY MGQNALQLAV ANEHLEITEL LLKKENLSRV GDALLLAISK GYVRIVEAIL
NHPAFAEGKR LATSPSQSEL QQDDFYAYDE DGTRFSHDVT PIILAAHCQE YEIVHTLLRK
GARIERPHDY FCKCTECSQK QKHDSFSHSR SRINAYKGLA SPAYLSLSSE DPVMTALELS
NELAVLANIE KEFKNDYRKL SMQCKDFVVG LLDLCRNTEE VEAILNGDAE TRQPGDFGRP
NLSRLKLAIK YEVKKFVAHP NCQQQLLSIW YENLSGLRQQ TMAVKFLVVL AVAIGLPFLA
LIYWCAPCSK MGKILRGPFM KFVAHAASFT IFLGLLVMNA ADRFEGTKLL PNETSTDNAR
QLFRMKTSCF SWMEMLIISW VIGMIWAECK EIWTQGPKEY LFELWNMLDF GMLAIFAASF
IARFMAFWHA SKAQSIIDAN DTLKDLTKVT LGDNVKYYNL ARIKWDPTDP QIISEGLYAI
AVVLSFSRIA YILPANESFG PLQISLGRTV KDIFKFMVIF IMVFVAFMIG MFNLYSYYIG
AKQNEAFTTV EESFKTLFWA IFGLSEVKSV VINYNHKFIE NIGYVLYGVY NVTMVIVLLN
MLIAMINSSF QEIEDDADVE WKFARAKLWF SYFEEGRTLP VPFNLVPSPK SLLYLLLKFK
KWMCELIQGQ KQGFQEDAEM NKRNEEKKFG ISGSHEDLSK FSLDKNQLAH NKQSSTRSSE
DYHLNSFSNP PRQYQKIMKR LIKRYVLQAQ IDKESDEVNE GELKEIKQDI SSLRYELLEE
KSQNTEDLAE LIRKLGERLS LEPKLEESRR
