TRPC7_MOUSE
ID TRPC7_MOUSE Reviewed; 862 AA.
AC Q9WVC5;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Short transient receptor potential channel 7;
DE Short=TrpC7;
DE AltName: Full=Transient receptor protein 7;
DE Short=TRP-7;
DE Short=mTRP7;
GN Name=Trpc7; Synonyms=Trp7, Trrp8;
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].
RX PubMed=10488066; DOI=10.1074/jbc.274.39.27359;
RA Okada T., Inoue R., Yamazaki K., Maeda A., Kurosaki T., Yamakuni T.,
RA Tanaka I., Shimizu S., Ikenaka K., Imoto K., Mori Y.;
RT "Molecular and functional characterization of a novel mouse transient
RT receptor potential protein homologue TRP7. Ca(2+)-permeable cation channel
RT that is constitutively activated and enhanced by stimulation of G protein-
RT coupled receptor.";
RL J. Biol. Chem. 274:27359-27370(1999).
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). May also
CC be activated by intracellular calcium store depletion.
CC -!- SUBUNIT: Interacts with MX1 and RNF24. Interacts (via ANK-repeat
CC domains) with PRKG1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Nucleus envelope {ECO:0000250}.
CC -!- PTM: Phosphorylation by PRKG1 at Thr-15 negatively regulates TRPC7
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC7 sub-subfamily. {ECO:0000305}.
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; AF139923; AAD42069.1; -; mRNA.
DR CCDS; CCDS26566.1; -.
DR RefSeq; NP_036165.1; NM_012035.3.
DR AlphaFoldDB; Q9WVC5; -.
DR SMR; Q9WVC5; -.
DR IntAct; Q9WVC5; 1.
DR STRING; 10090.ENSMUSP00000022023; -.
DR BindingDB; Q9WVC5; -.
DR ChEMBL; CHEMBL4523502; -.
DR TCDB; 1.A.4.1.2; the transient receptor potential ca(2+) channel (trp-cc) family.
DR GlyGen; Q9WVC5; 1 site.
DR iPTMnet; Q9WVC5; -.
DR PhosphoSitePlus; Q9WVC5; -.
DR MaxQB; Q9WVC5; -.
DR PaxDb; Q9WVC5; -.
DR PRIDE; Q9WVC5; -.
DR ProteomicsDB; 258985; -.
DR Antibodypedia; 26493; 314 antibodies from 35 providers.
DR DNASU; 26946; -.
DR Ensembl; ENSMUST00000022023; ENSMUSP00000022023; ENSMUSG00000021541.
DR GeneID; 26946; -.
DR KEGG; mmu:26946; -.
DR UCSC; uc007qtb.2; mouse.
DR CTD; 57113; -.
DR MGI; MGI:1349470; Trpc7.
DR VEuPathDB; HostDB:ENSMUSG00000021541; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR InParanoid; Q9WVC5; -.
DR OMA; YFTFARN; -.
DR OrthoDB; 1018075at2759; -.
DR PhylomeDB; Q9WVC5; -.
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; 26946; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9WVC5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9WVC5; protein.
DR Bgee; ENSMUSG00000021541; Expressed in lateral septal nucleus and 81 other tissues.
DR ExpressionAtlas; Q9WVC5; baseline and differential.
DR Genevisible; Q9WVC5; MM.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005801; C:cis-Golgi network; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IC:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
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 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; IPR005463; TRPC7_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF9; PTHR10117:SF9; 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; PR01648; TRPCHANNEL7.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..862
FT /note="Short transient receptor potential channel 7"
FT /id="PRO_0000215325"
FT TOPO_DOM 1..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..372
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 373..383
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..537
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 538..558
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 559..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 603..651
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..862
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 42..71
FT /note="ANK 1"
FT REPEAT 77..106
FT /note="ANK 2"
FT REPEAT 108..134
FT /note="ANK 3"
FT REPEAT 163..192
FT /note="ANK 4"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphothreonine; by PKG/PRKG1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCX4"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 862 AA; 99475 MW; C2EB2CE1A6AF9C3D CRC64;
MLGSNTFKNM QRRHTTLREK GRRQAIRGPA YMFNEKGTSL TPEEERFLDS AEYGNIPVVR
KMLEESKTLN FNCVDYMGQN ALQLAVGNEH LEVTELLLKK ENLARVGDAL LLAISKGYVR
IVEAILSHPA FAQGQRLTLS PLEQELRDDD FYAYDEDGTR FSHDITPIIL AAHCQEYEIV
HILLLKGARI ERPHDYFCKC NECTEKQRKD SFSHSRSRMN AYKGLASAAY LSLSSEDPVL
TALELSNELA RLANIETEFK NDYRKLSMQC KDFVVGVLDL CRDTEEVEAI LNGDVNLQVW
SDHHRPSLSR IKLAIKYEVK KFVAHPNCQQ QLLTMWYENL SGLRQQSIAV KFLAVFGVSI
GLPFLAIAYW IAPCSKLGQT LRSPFMKFVA HAVSFTIFLG LLVVNASDRF EGVKTLPNET
FTDYPKQIFR VKTTQFSWTE MLIMKWVLGM IWSECKEIWE EGPREYVLHL WNLLDFGMLS
IFVASFTARF MAFLKASEAQ LYVDQYVQDV TLHNVSLPPE VAYFTYARDK WWPSDPQIIS
EGLYAIAVVL SFSRIAYILP ANESFGPLQI SLGRTVKDIF KFMVIFIMVF VAFMIGMFNL
YSYYRGAKYN PAFTTVEESF KTLFWSIFGL SEVISVVLKY DHKFIENIGY VLYGVYNVTM
VVVLLNMLIA MINNSYQEIE EDADVEWKFA RAKLWLSYFD EGRTLPAPFN LVPSPKSFYY
LIMRIKMCLI ELCQSKAKRC ENDLEMGMLN SKFRKTRYQA GMRNSENLTA NSTFSKPTRY
QKIMKRLIKR YVLKAQVDRE NDEVNEGELK EIKQDISSLR YELLEEKSQA TGELADLIQQ
LSEKFGKNLN KDHLRVNQGK DI
