TRPC7_HUMAN
ID TRPC7_HUMAN Reviewed; 862 AA.
AC Q9HCX4; A1A4Z4; F5H5U9; Q70T26; Q8IWP7;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 171.
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=hTRP7;
GN Name=TRPC7; Synonyms=TRP7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Murphy C.T., Li S., Jordan N.J., Reaves B.J., Wolstenholme A.J.,
RA Westwick J.;
RT "Distribution of a novel human capacitative calcium entry channel, htrp7.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Xu S.-Z., Beech D.J.;
RT "Localization of TRPC7 and splice variants in human tissues.";
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RA Aptel H., Murphy C.T., Li S.W., Chen P.B., Rogers A.T., Franklin I.,
RA Westwick J., Reaves B.J., Woodward B., Wolstenholme A.J.;
RT "Tissue distribution, alternative splicing and function of human TRPC7.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
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-like
RT repeat domain of TRPC.";
RL J. Biol. Chem. 280:19393-19400(2005).
RN [7]
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 retention
RT of TRPC.";
RL Cell Calcium 43:432-443(2008).
RN [8]
RP PHOSPHORYLATION AT THR-15 BY PRKG1, INTERACTION WITH PRKG1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=21402151; DOI=10.1016/j.cellsig.2011.03.005;
RA Yuasa K., Matsuda T., Tsuji A.;
RT "Functional regulation of transient receptor potential canonical 7 by cGMP-
RT dependent protein kinase Ialpha.";
RL Cell. Signal. 23:1179-1187(2011).
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) (By
CC similarity). May also be activated by intracellular calcium store
CC depletion. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MX1 and RNF24. Interacts (via ANK-repeat
CC domains) with PRKG1. {ECO:0000269|PubMed:15757897,
CC ECO:0000269|PubMed:17850865, ECO:0000269|PubMed:21402151}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21402151};
CC Multi-pass membrane protein {ECO:0000269|PubMed:21402151}. Nucleus
CC envelope {ECO:0000269|PubMed:21402151}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HCX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCX4-2; Sequence=VSP_043035;
CC Name=3;
CC IsoId=Q9HCX4-3; Sequence=VSP_044897;
CC -!- PTM: Phosphorylation by PRKG1 at Thr-15 negatively regulates TRPC7
CC activity. {ECO:0000269|PubMed:21402151}.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC7 sub-subfamily. {ECO:0000305}.
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DR EMBL; AJ272034; CAC03489.1; -; mRNA.
DR EMBL; AY167927; AAO12125.1; -; mRNA.
DR EMBL; AJ549088; CAD70161.1; -; mRNA.
DR EMBL; AC008661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128185; AAI28186.1; -; mRNA.
DR CCDS; CCDS47267.2; -. [Q9HCX4-1]
DR CCDS; CCDS54905.1; -. [Q9HCX4-2]
DR CCDS; CCDS54906.1; -. [Q9HCX4-3]
DR RefSeq; NP_001161048.1; NM_001167576.1. [Q9HCX4-2]
DR RefSeq; NP_001161049.1; NM_001167577.1. [Q9HCX4-3]
DR RefSeq; NP_065122.1; NM_020389.2. [Q9HCX4-1]
DR AlphaFoldDB; Q9HCX4; -.
DR SMR; Q9HCX4; -.
DR BioGRID; 121378; 5.
DR CORUM; Q9HCX4; -.
DR IntAct; Q9HCX4; 1.
DR STRING; 9606.ENSP00000426070; -.
DR BindingDB; Q9HCX4; -.
DR ChEMBL; CHEMBL4105799; -.
DR GuidetoPHARMACOLOGY; 492; -.
DR GlyGen; Q9HCX4; 1 site.
DR iPTMnet; Q9HCX4; -.
DR PhosphoSitePlus; Q9HCX4; -.
DR BioMuta; TRPC7; -.
DR DMDM; 18202960; -.
DR MassIVE; Q9HCX4; -.
DR PaxDb; Q9HCX4; -.
DR PeptideAtlas; Q9HCX4; -.
DR PRIDE; Q9HCX4; -.
DR ProteomicsDB; 26990; -.
DR ProteomicsDB; 81805; -. [Q9HCX4-1]
DR ProteomicsDB; 81806; -. [Q9HCX4-2]
DR Antibodypedia; 26493; 314 antibodies from 35 providers.
DR DNASU; 57113; -.
DR Ensembl; ENST00000352189.8; ENSP00000330322.5; ENSG00000069018.19. [Q9HCX4-2]
DR Ensembl; ENST00000378459.7; ENSP00000367720.3; ENSG00000069018.19. [Q9HCX4-3]
DR Ensembl; ENST00000513104.6; ENSP00000426070.2; ENSG00000069018.19. [Q9HCX4-1]
DR GeneID; 57113; -.
DR KEGG; hsa:57113; -.
DR MANE-Select; ENST00000513104.6; ENSP00000426070.2; NM_020389.3; NP_065122.1.
DR UCSC; uc003lbn.3; human. [Q9HCX4-1]
DR CTD; 57113; -.
DR DisGeNET; 57113; -.
DR GeneCards; TRPC7; -.
DR HGNC; HGNC:20754; TRPC7.
DR HPA; ENSG00000069018; Not detected.
DR neXtProt; NX_Q9HCX4; -.
DR OpenTargets; ENSG00000069018; -.
DR PharmGKB; PA164742693; -.
DR VEuPathDB; HostDB:ENSG00000069018; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR HOGENOM; CLU_005716_4_2_1; -.
DR InParanoid; Q9HCX4; -.
DR OMA; YFTFARN; -.
DR OrthoDB; 1018075at2759; -.
DR PhylomeDB; Q9HCX4; -.
DR TreeFam; TF313147; -.
DR PathwayCommons; Q9HCX4; -.
DR Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
DR Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
DR Reactome; R-HSA-3295583; TRP channels.
DR Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
DR SignaLink; Q9HCX4; -.
DR SIGNOR; Q9HCX4; -.
DR BioGRID-ORCS; 57113; 9 hits in 1063 CRISPR screens.
DR ChiTaRS; TRPC7; human.
DR GeneWiki; TRPC7; -.
DR GenomeRNAi; 57113; -.
DR Pharos; Q9HCX4; Tchem.
DR PRO; PR:Q9HCX4; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9HCX4; protein.
DR Bgee; ENSG00000069018; Expressed in buccal mucosa cell and 37 other tissues.
DR ExpressionAtlas; Q9HCX4; baseline and differential.
DR Genevisible; Q9HCX4; HS.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
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 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..862
FT /note="Short transient receptor potential channel 7"
FT /id="PRO_0000215324"
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:0000269|PubMed:21402151"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 260..375
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_043035"
FT VAR_SEQ 260..320
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_044897"
FT CONFLICT 412
FT /note="G -> S (in Ref. 3; CAD70161)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="F -> S (in Ref. 3; CAD70161)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 862 AA; 99562 MW; C516E59E80AEF4B0 CRC64;
MLRNSTFKNM QRRHTTLREK GRRQAIRGPA YMFNEKGTSL TPEEERFLDS AEYGNIPVVR
KMLEESKTLN FNCVDYMGQN ALQLAVGNEH LEVTELLLKK ENLARVGDAL LLAISKGYVR
IVEAILNHPA FAQGQRLTLS PLEQELRDDD FYAYDEDGTR FSHDITPIIL AAHCQEYEIV
HILLLKGARI ERPHDYFCKC NECTEKQRKD SFSHSRSRMN AYKGLASAAY LSLSSEDPVL
TALELSNELA RLANIETEFK NDYRKLSMQC KDFVVGVLDL CRDTEEVEAI LNGDVNFQVW
SDHHRPSLSR IKLAIKYEVK KFVAHPNCQQ QLLTMWYENL SGLRQQSIAV KFLAVFGVSI
GLPFLAIAYW IAPCSKLGRT LRSPFMKFVA HAVSFTIFLG LLVVNASDRF EGVKTLPNET
FTDYPKQIFR VKTTQFSWTE MLIMKWVLGM IWSECKEIWE EGPREYVLHL WNLLDFGMLS
IFVASFTARF MAFLKATEAQ LYVDQHVQDD TLHNVSLPPE VAYFTYARDK WWPSDPQIIS
EGLYAIAVVL SFSRIAYILP ANESFGPLQI SLGRTVKDIF KFMVIFIMVF VAFMIGMFNL
YSYYRGAKYN PAFTTVEESF KTLFWSIFGL SEVISVVLKY DHKFIENIGY VLYGVYNVTM
VVVLLNMLIA MINNSYQEIE EDADVEWKFA RAKLWLSYFD EGRTLPAPFN LVPSPKSFYY
LIMRIKMCLI KLCKSKAKSC ENDLEMGMLN SKFKKTRYQA GMRNSENLTA NNTLSKPTRY
QKIMKRLIKR YVLKAQVDRE NDEVNEGELK EIKQDISSLR YELLEEKSQA TGELADLIQQ
LSEKFGKNLN KDHLRVNKGK DI
