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   24-JAN-2024, entry version 194.
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   EMDB; EMD-7637; -.
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   GlyCosmos; Q61143; 1 site, No reported glycans.
DR   GlyGen; Q61143; 1 site.
DR   iPTMnet; Q61143; -.
DR   PhosphoSitePlus; Q61143; -.
DR   MaxQB; Q61143; -.
DR   PaxDb; 10090-ENSMUSP00000057965; -.
DR   ProteomicsDB; 300018; -.
DR   Antibodypedia; 17956; 482 antibodies from 40 providers.
DR   DNASU; 22068; -.
DR   Ensembl; ENSMUST00000050433.8; ENSMUSP00000057965.7; ENSMUSG00000031997.10.
DR   GeneID; 22068; -.
DR   KEGG; mmu:22068; -.
DR   UCSC; uc009odl.1; mouse.
DR   AGR; MGI:109523; -.
DR   CTD; 7225; -.
DR   MGI; MGI:109523; Trpc6.
DR   VEuPathDB; HostDB:ENSMUSG00000031997; -.
DR   eggNOG; KOG3609; Eukaryota.
DR   GeneTree; ENSGT01060000248588; -.
DR   HOGENOM; CLU_005716_4_2_1; -.
DR   InParanoid; Q61143; -.
DR   OMA; DDGCPQL; -.
DR   OrthoDB; 5406916at2759; -.
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 76 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 81 other cell types or tissues.
DR   ExpressionAtlas; Q61143; baseline and differential.
DR   GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISO: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:0030276; F:clathrin binding; ISO:MGI.
DR   GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:MGI.
DR   GO; GO:0005261; F:monoatomic cation channel activity; ISO:MGI.
DR   GO; GO:0005216; F:monoatomic 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: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: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; 1.10.287.70; -; 1.
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; IPR005462; TRPC6_channel.
DR   InterPro; IPR002153; TRPC_channel.
DR   NCBIfam; TIGR00870; trp; 1.
DR   PANTHER; PTHR10117:SF7; SHORT TRANSIENT RECEPTOR POTENTIAL CHANNEL 6; 1.
DR   PANTHER; PTHR10117; TRANSIENT RECEPTOR POTENTIAL CHANNEL; 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   SMART; SM01420; TRP_2; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   Genevisible; Q61143; MM.
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
//