ID Q99N78_RAT Unreviewed; 930 AA.
AC Q99N78;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 166.
DE SubName: Full=Transient receptor potential Ca2+ channel 6A {ECO:0000313|EMBL:BAB41215.1};
DE SubName: Full=Transient receptor potential cation channel, subfamily C, member 6, isoform CRA_b {ECO:0000313|EMBL:EDL78511.1};
GN Name=Trpc6 {ECO:0000313|EMBL:EDL78511.1, ECO:0000313|RGD:619788};
GN Synonyms=trp6A {ECO:0000313|EMBL:BAB41215.1};
GN ORFNames=rCG_31778 {ECO:0000313|EMBL:EDL78511.1};
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 {ECO:0000313|EMBL:BAB41215.1};
RN [1] {ECO:0000313|EMBL:BAB41215.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Lung {ECO:0000313|EMBL:BAB41215.1};
RX PubMed=11278449; DOI=10.1074/jbc.M008914200;
RA Zhang L., Saffen D.;
RT "Muscarinic acetylcholine receptor regulation of TRP6 Ca2+ channel
RT isoforms. Molecular structures and functional characterization.";
RL J. Biol. Chem. 276:13331-13339(2001).
RN [2] {ECO:0000313|EMBL:EDL78511.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BN {ECO:0000313|EMBL:EDL78511.1};
RX PubMed=15632090; DOI=10.1101/gr.2889405;
RA Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA Istrail S., Li P., Sutton G.;
RT "Gene and alternative splicing annotation with AIR.";
RL Genome Res. 15:54-66(2005).
RN [3] {ECO:0000313|EMBL:EDL78511.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BN {ECO:0000313|EMBL:EDL78511.1};
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007829|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AB051212; BAB41215.1; -; Genomic_DNA.
DR EMBL; CH473993; EDL78511.1; -; Genomic_DNA.
DR RefSeq; NP_446011.1; NM_053559.1.
DR AlphaFoldDB; Q99N78; -.
DR SMR; Q99N78; -.
DR STRING; 10116.ENSRNOP00000008905; -.
DR PhosphoSitePlus; Q99N78; -.
DR PaxDb; 10116-ENSRNOP00000008905; -.
DR GeneID; 89823; -.
DR KEGG; rno:89823; -.
DR UCSC; RGD:619788; rat.
DR AGR; RGD:619788; -.
DR CTD; 7225; -.
DR RGD; 619788; Trpc6.
DR VEuPathDB; HostDB:ENSRNOG00000006324; -.
DR eggNOG; KOG3609; Eukaryota.
DR OrthoDB; 5406916at2759; -.
DR TreeFam; TF313147; -.
DR Reactome; R-RNO-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-RNO-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-RNO-3295583; TRP channels.
DR ChiTaRS; Trpc6; rat.
DR Proteomes; UP000234681; Chromosome 8.
DR Bgee; ENSRNOG00000006324; Expressed in frontal cortex and 16 other cell types or tissues.
DR ExpressionAtlas; Q99N78; baseline and differential.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0036057; C:slit diaphragm; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0042805; F:actinin binding; IDA:RGD.
DR GO; GO:0051117; F:ATPase binding; IPI:RGD.
DR GO; GO:0005262; F:calcium channel activity; IDA:RGD.
DR GO; GO:0030276; F:clathrin binding; IDA:RGD.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; ISO:RGD.
DR GO; GO:0005261; F:monoatomic cation channel activity; IDA:RGD.
DR GO; GO:0005216; F:monoatomic ion channel activity; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0015279; F:store-operated calcium channel activity; ISO:RGD.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:RGD.
DR GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:RGD.
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; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|EMBL:BAB41215.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 403..422
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 442..461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 489..507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..546
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 633..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 702..723
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 217..249
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 252..314
FT /note="Transient receptor ion channel"
FT /evidence="ECO:0000259|SMART:SM01420"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 883..918
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 930 AA; 106560 MW; F3F333C23A0EB2CA CRC64;
MSQSPGFVTR RGGSPKAAPG AGARRNESQD YLLMDELGDD GYPQLQQPPY GYYPSFRGNE
NRLTHRRQTV LREKGRRLAN RGPAYMFNDH STSLSIEEER FLDAAEYGNI PVVRKMLEEC
LSLNVNCVDY MGQNALQLAV ANEHLEITEL LLKKENLSRV GDALLLAISK GYVRIVEAIL
NHPAFAEGKR LATSPSQSEL QQDDFYAYDE DGTRFSHDVT PIILAAHCQE YEIVHTLLRK
GARIERPHDY FCKCTECSQK QKHDSFSHSR SRINAYKGLA SPAYLSLSSE DPVMTALELS
NELAVLANIE KEFKNDYRKL SMQCKDFVVG LLDLCRNTEE VEAILNGDAE TRQPGDLARP
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
KWMSELIQGH KKGFQEDAEM NKRNEEKKFG ILGSHEDLSK FSLDRNQLAH NKQSSTRSSE
DFHLNSFSNP PRQYQKIMKR LIKRYVLQAQ IDKESDEVNE GELKEIKQDI SSLRYELLEE
KSQNTEDLAE LIRKLGERLS LESKQEESRR
//
