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Short transient receptor potential channel 6 (TrpC6) (Transient receptor protein 6) (TRP-6)

 TRPC6_HUMAN             Reviewed;         931 AA.
Q9Y210; Q52M59; Q9HCW3; Q9NQA8; Q9NQA9;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
25-OCT-2017, entry version 164.
RecName: Full=Short transient receptor potential channel 6;
Short=TrpC6;
AltName: Full=Transient receptor protein 6;
Short=TRP-6;
Name=TRPC6; Synonyms=TRP6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta, and Testis;
PubMed=9930701; DOI=10.1038/16711;
Hofmann T., Obukhov A.G., Schaefer M., Harteneck C., Gudermann T.,
Schultz G.;
"Direct activation of human TRPC6 and TRPC3 channels by
diacylglycerol.";
Nature 397:259-263(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
PubMed=9925922;
D'Esposito M., Strazzullo M., Cuccurese M., Spalluto C., Rocchi M.,
D'Urso M., Ciccodicola A.;
"Identification and assignment of the human transient receptor
potential channel 6 gene TRPC6 to chromosome 11q21-22.";
Cytogenet. Cell Genet. 83:46-47(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Placenta;
PubMed=10816590; DOI=10.1074/jbc.M003408200;
Philipp S., Trost C., Warnat J., Rautmann J., Himmerkus N.,
Schroth G., Kretz O., Nastainczyk W., Cavalie A., Hoth M.,
Flockerzi V.;
"TRP4 (CCE1) protein is part of native calcium release-activated Ca2+-
like channels in adrenal cells.";
J. Biol. Chem. 275:23965-23972(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 487-643.
Fenech C.J., Prestwich S.A., Zholos A.V., Bolton T.B.;
"The capacitative calcium entry cation channel Trp6 is expressed in
the muscularis externa of the guinea pig ileum and in a human jejunum
smooth muscle cell line.";
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[6]
GLYCOSYLATION AT ASN-473 AND ASN-561, AND MUTAGENESIS OF ASN-561.
PubMed=12970363; DOI=10.1074/jbc.M302983200;
Dietrich A., Mederos y Schnitzler M., Emmel J., Kalwa H., Hofmann T.,
Gudermann T.;
"N-linked protein glycosylation is a major determinant for basal TRPC3
and TRPC6 channel activity.";
J. Biol. Chem. 278:47842-47852(2003).
[7]
INTERACTION WITH MX1.
PubMed=15757897; DOI=10.1074/jbc.M500391200;
Lussier M.P., Cayouette S., Lepage P.K., Bernier C.L., Francoeur N.,
St-Hilaire M., Pinard M., Boulay G.;
"MxA, a member of the dynamin superfamily, interacts with the ankyrin-
like repeat domain of TRPC.";
J. Biol. Chem. 280:19393-19400(2005).
[8]
INTERACTION WITH RNF24, AND MUTAGENESIS OF ASN-125; ASN-127; CYS-128
AND ASP-130.
PubMed=17850865; DOI=10.1016/j.ceca.2007.07.009;
Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.;
"RNF24, a new TRPC interacting protein, causes the intracellular
retention of TRPC.";
Cell Calcium 43:432-443(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[10]
VARIANTS FSGS2 SER-143; THR-270; CYS-895 AND LYS-897, AND TISSUE
SPECIFICITY.
PubMed=15924139; DOI=10.1038/ng1592;
Reiser J., Polu K.R., Moller C.C., Kenlan P., Altintas M.M., Wei C.,
Faul C., Herbert S., Villegas I., Avila-Casado C., McGee M.,
Sugimoto H., Brown D., Kalluri R., Mundel P., Smith P.L.,
Clapham D.E., Pollak M.R.;
"TRPC6 is a glomerular slit diaphragm-associated channel required for
normal renal function.";
Nat. Genet. 37:739-744(2005).
[11]
VARIANT FSGS2 GLN-112.
PubMed=15879175; DOI=10.1126/science.1106215;
Winn M.P., Conlon P.J., Lynn K.L., Farrington M.K., Creazzo T.,
Hawkins A.F., Daskalakis N., Kwan S.Y., Ebersviller S.,
Burchette J.L., Pericak-Vance M.A., Howell D.N., Vance J.M.,
Rosenberg P.B.;
"A mutation in the TRPC6 cation channel causes familial focal
segmental glomerulosclerosis.";
Science 308:1801-1804(2005).
[12]
VARIANT FSGS2 LEU-218, AND VARIANTS SER-125 AND LEU-895.
PubMed=21734084; DOI=10.2215/CJN.07830910;
Gigante M., Caridi G., Montemurno E., Soccio M., d'Apolito M.,
Cerullo G., Aucella F., Schirinzi A., Emma F., Massella L.,
Messina G., De Palo T., Ranieri E., Ghiggeri G.M., Gesualdo L.;
"TRPC6 mutations in children with steroid-resistant nephrotic syndrome
and atypical phenotype.";
Clin. J. Am. Soc. Nephrol. 6:1626-1634(2011).
-!- FUNCTION: Thought to form a receptor-activated non-selective
calcium permeant cation channel. Probably is operated by a
phosphatidylinositol second messenger system activated by receptor
tyrosine kinases or G-protein coupled receptors. Activated by
diacylglycerol (DAG) in a membrane-delimited fashion,
independently of protein kinase C. Seems not to be activated by
intracellular calcium store depletion.
-!- SUBUNIT: Interacts with MX1 and RNF24.
{ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:17850865}.
-!- INTERACTION:
P20591:MX1; NbExp=4; IntAct=EBI-929362, EBI-929476;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9Y210-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y210-2; Sequence=VSP_006572;
Name=3;
IsoId=Q9Y210-3; Sequence=VSP_006573;
-!- TISSUE SPECIFICITY: Expressed primarily in placenta, lung, spleen,
ovary and small intestine. Expressed in podocytes and is a
component of the glomerular slit diaphragm.
{ECO:0000269|PubMed:15924139}.
-!- PTM: Phosphorylated by FYN, leading to an increase of TRPC6
channel activity. {ECO:0000250}.
-!- DISEASE: Focal segmental glomerulosclerosis 2 (FSGS2)
[MIM:603965]: A renal pathology defined by the presence of
segmental sclerosis in glomeruli and resulting in proteinuria,
reduced glomerular filtration rate and progressive decline in
renal function. Renal insufficiency often progresses to end-stage
renal disease, a highly morbid state requiring either dialysis
therapy or kidney transplantation. {ECO:0000269|PubMed:15879175,
ECO:0000269|PubMed:15924139, ECO:0000269|PubMed:21734084}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
STrpC subfamily. TRPC6 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF080394; AAC63289.2; -; mRNA.
EMBL; AJ006276; CAA06943.1; -; mRNA.
EMBL; AJ271066; CAC01684.1; -; mRNA.
EMBL; AJ271067; CAC01685.1; -; mRNA.
EMBL; AJ271068; CAC01686.1; -; mRNA.
EMBL; BC093658; AAH93658.1; -; mRNA.
EMBL; BC093660; AAH93660.1; -; mRNA.
EMBL; AJ007018; CAC06090.1; -; mRNA.
CCDS; CCDS8311.1; -. [Q9Y210-1]
RefSeq; NP_004612.2; NM_004621.5. [Q9Y210-1]
RefSeq; XP_016873710.1; XM_017018221.1. [Q9Y210-2]
UniGene; Hs.159003; -.
ProteinModelPortal; Q9Y210; -.
BioGrid; 113076; 12.
IntAct; Q9Y210; 2.
STRING; 9606.ENSP00000340913; -.
BindingDB; Q9Y210; -.
ChEMBL; CHEMBL2417347; -.
GuidetoPHARMACOLOGY; 491; -.
TCDB; 1.A.4.1.5; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; Q9Y210; -.
PhosphoSitePlus; Q9Y210; -.
BioMuta; TRPC6; -.
DMDM; 6686048; -.
EPD; Q9Y210; -.
PaxDb; Q9Y210; -.
PeptideAtlas; Q9Y210; -.
PRIDE; Q9Y210; -.
Ensembl; ENST00000344327; ENSP00000340913; ENSG00000137672. [Q9Y210-1]
Ensembl; ENST00000348423; ENSP00000343672; ENSG00000137672. [Q9Y210-2]
Ensembl; ENST00000360497; ENSP00000353687; ENSG00000137672. [Q9Y210-3]
GeneID; 7225; -.
KEGG; hsa:7225; -.
UCSC; uc001pgk.4; human. [Q9Y210-1]
CTD; 7225; -.
DisGeNET; 7225; -.
EuPathDB; HostDB:ENSG00000137672.12; -.
GeneCards; TRPC6; -.
HGNC; HGNC:12338; TRPC6.
HPA; HPA045098; -.
HPA; HPA062164; -.
MalaCards; TRPC6; -.
MIM; 603652; gene.
MIM; 603965; phenotype.
neXtProt; NX_Q9Y210; -.
OpenTargets; ENSG00000137672; -.
Orphanet; 93213; Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKB; PA37011; -.
eggNOG; KOG3609; Eukaryota.
eggNOG; ENOG410XQ0Y; LUCA.
GeneTree; ENSGT00760000119180; -.
HOGENOM; HOG000020590; -.
HOVERGEN; HBG068337; -.
InParanoid; Q9Y210; -.
KO; K04969; -.
OMA; NRGPAYM; -.
OrthoDB; EOG091G01FB; -.
PhylomeDB; Q9Y210; -.
TreeFam; TF313147; -.
Reactome; R-HSA-114508; Effects of PIP2 hydrolysis.
Reactome; R-HSA-139853; Elevation of cytosolic Ca2+ levels.
Reactome; R-HSA-3295583; TRP channels.
Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
SIGNOR; Q9Y210; -.
ChiTaRS; TRPC6; human.
GeneWiki; TRPC6; -.
GenomeRNAi; 7225; -.
PRO; PR:Q9Y210; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137672; -.
CleanEx; HS_TRPC6; -.
ExpressionAtlas; Q9Y210; baseline and differential.
Genevisible; Q9Y210; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0036057; C:slit diaphragm; IEA:Ensembl.
GO; GO:0003779; F:actin binding; IEA:Ensembl.
GO; GO:0042805; F:actinin binding; IEA:Ensembl.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
GO; GO:0015279; F:store-operated calcium channel activity; IBA:GO_Central.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
GO; GO:0006812; P:cation transport; TAS:ProtInc.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:MGI.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; IDA:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
GO; GO:0007338; P:single fertilization; IBA:GO_Central.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR004729; TRP_channel.
InterPro; IPR013555; TRP_dom.
InterPro; IPR005462; TRPC6_channel.
InterPro; IPR002153; TRPC_channel.
PANTHER; PTHR10117; PTHR10117; 1.
PANTHER; PTHR10117:SF7; PTHR10117:SF7; 1.
Pfam; PF12796; Ank_2; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF08344; TRP_2; 1.
PRINTS; PR01097; TRNSRECEPTRP.
PRINTS; PR01647; TRPCHANNEL6.
SMART; SM00248; ANK; 3.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 2.
PROSITE; PS50088; ANK_REPEAT; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Calcium; Calcium channel;
Calcium transport; Complete proteome; Disease mutation; Glycoprotein;
Ion channel; Ion transport; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 931 Short transient receptor potential
channel 6.
/FTId=PRO_0000215322.
TOPO_DOM 1 438 Cytoplasmic. {ECO:0000255}.
TRANSMEM 439 459 Helical. {ECO:0000255}.
TOPO_DOM 460 487 Extracellular. {ECO:0000255}.
TRANSMEM 488 508 Helical. {ECO:0000255}.
TOPO_DOM 509 521 Cytoplasmic. {ECO:0000255}.
TRANSMEM 522 542 Helical. {ECO:0000255}.
TOPO_DOM 543 592 Extracellular. {ECO:0000255}.
TRANSMEM 593 613 Helical. {ECO:0000255}.
TOPO_DOM 614 636 Cytoplasmic. {ECO:0000255}.
TRANSMEM 637 657 Helical. {ECO:0000255}.
TOPO_DOM 658 706 Extracellular. {ECO:0000255}.
TRANSMEM 707 727 Helical. {ECO:0000255}.
TOPO_DOM 728 931 Cytoplasmic. {ECO:0000255}.
REPEAT 97 126 ANK 1.
REPEAT 132 161 ANK 2.
REPEAT 163 189 ANK 3.
REPEAT 218 247 ANK 4.
MOD_RES 815 815 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
CARBOHYD 473 473 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12970363}.
CARBOHYD 561 561 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12970363}.
VAR_SEQ 316 431 Missing (in isoform 2).
{ECO:0000303|PubMed:10816590}.
/FTId=VSP_006572.
VAR_SEQ 377 431 Missing (in isoform 3).
{ECO:0000303|PubMed:10816590}.
/FTId=VSP_006573.
VARIANT 112 112 P -> Q (in FSGS2; dbSNP:rs121434390).
{ECO:0000269|PubMed:15879175}.
/FTId=VAR_026730.
VARIANT 125 125 N -> S (found in two siblings with early-
onset steroid-resistant nephrotic
syndrome; dbSNP:rs146776939).
{ECO:0000269|PubMed:21734084}.
/FTId=VAR_067247.
VARIANT 143 143 N -> S (in FSGS2; dbSNP:rs121434391).
{ECO:0000269|PubMed:15924139}.
/FTId=VAR_026731.
VARIANT 157 157 N -> T (in dbSNP:rs35857503).
/FTId=VAR_038419.
VARIANT 218 218 H -> L (in FSGS2; dbSNP:rs779430565).
{ECO:0000269|PubMed:21734084}.
/FTId=VAR_067248.
VARIANT 270 270 S -> T (in FSGS2; dbSNP:rs121434392).
{ECO:0000269|PubMed:15924139}.
/FTId=VAR_026732.
VARIANT 404 404 A -> V (in dbSNP:rs36111323).
/FTId=VAR_061861.
VARIANT 895 895 R -> C (in FSGS2; dbSNP:rs121434394).
{ECO:0000269|PubMed:15924139}.
/FTId=VAR_026733.
VARIANT 895 895 R -> L (in a patient with collapsing
glomerulosclerosis).
{ECO:0000269|PubMed:21734084}.
/FTId=VAR_067249.
VARIANT 897 897 E -> K (in FSGS2; dbSNP:rs121434395).
{ECO:0000269|PubMed:15924139}.
/FTId=VAR_026734.
MUTAGEN 125 125 N->A: No effect on RNF24-binding; when
associated with A-127; A-128 and A-130.
{ECO:0000269|PubMed:17850865}.
MUTAGEN 127 127 N->A: No effect on RNF24-binding; when
associated with A-125; A-128 and A-130.
{ECO:0000269|PubMed:17850865}.
MUTAGEN 128 128 C->A: No effect on RNF24-binding; when
associated with A-125; A-127 and A-130.
{ECO:0000269|PubMed:17850865}.
MUTAGEN 130 130 D->A: No effect on RNF24-binding; when
associated with A-125; A-127 and A-128.
{ECO:0000269|PubMed:17850865}.
MUTAGEN 561 561 N->Q: Constitutively activates channel.
{ECO:0000269|PubMed:12970363}.
CONFLICT 336 336 C -> R (in Ref. 3; CAC01686).
{ECO:0000305}.
CONFLICT 585 585 K -> R (in Ref. 5; CAC06090).
{ECO:0000305}.
CONFLICT 613 613 I -> T (in Ref. 3; CAC01686).
{ECO:0000305}.
SEQUENCE 931 AA; 106326 MW; 7C955C2B0389AC47 CRC64;
MSQSPAFGPR RGSSPRGAAG AAARRNESQD YLLMDSELGE DGCPQAPLPC YGYYPCFRGS
DNRLAHRRQT VLREKGRRLA NRGPAYMFSD RSTSLSIEEE RFLDAAEYGN IPVVRKMLEE
CHSLNVNCVD YMGQNALQLA VANEHLEITE LLLKKENLSR VGDALLLAIS KGYVRIVEAI
LSHPAFAEGK RLATSPSQSE LQQDDFYAYD EDGTRFSHDV TPIILAAHCQ EYEIVHTLLR
KGARIERPHD YFCKCNDCNQ KQKHDSFSHS RSRINAYKGL ASPAYLSLSS EDPVMTALEL
SNELAVLANI EKEFKNDYKK LSMQCKDFVV GLLDLCRNTE EVEAILNGDV ETLQSGDHGR
PNLSRLKLAI KYEVKKFVAH PNCQQQLLSI WYENLSGLRQ QTMAVKFLVV LAVAIGLPFL
ALIYWFAPCS KMGKIMRGPF MKFVAHAASF TIFLGLLVMN AADRFEGTKL LPNETSTDNA
KQLFRMKTSC FSWMEMLIIS WVIGMIWAEC KEIWTQGPKE YLFELWNMLD FGMLAIFAAS
FIARFMAFWH ASKAQSIIDA NDTLKDLTKV TLGDNVKYYN LARIKWDPSD PQIISEGLYA
IAVVLSFSRI AYILPANESF GPLQISLGRT VKDIFKFMVI FIMVFVAFMI GMFNLYSYYI
GAKQNEAFTT VEESFKTLFW AIFGLSEVKS VVINYNHKFI ENIGYVLYGV YNVTMVIVLL
NMLIAMINSS FQEIEDDADV EWKFARAKLW FSYFEEGRTL PVPFNLVPSP KSLFYLLLKL
KKWISELFQG HKKGFQEDAE MNKINEEKKL GILGSHEDLS KLSLDKKQVG HNKQPSIRSS
EDFHLNSFNN PPRQYQKIMK RLIKRYVLQA QIDKESDEVN EGELKEIKQD ISSLRYELLE
EKSQNTEDLA ELIRELGEKL SMEPNQEETN R


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