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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.
18-JUL-2018, entry version 170.
RecName: Full=Short transient receptor potential channel 6;
Short=TrpC6 {ECO:0000303|PubMed:9930701};
AltName: Full=Transient receptor protein 6;
Short=TRP-6;
Name=TRPC6 {ECO:0000303|PubMed:9930701, ECO:0000312|HGNC:HGNC:12338};
Synonyms=TRP6 {ECO:0000303|Ref.5};
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 SER-15, AND MUTAGENESIS OF GLN-889.
PubMed=19124028; DOI=10.1016/j.mrfmmm.2008.11.021;
Zhu B., Chen N., Wang Z.H., Pan X.X., Ren H., Zhang W., Wang W.M.;
"Identification and functional analysis of a novel TRPC6 mutation
associated with late onset familial focal segmental glomerulosclerosis
in Chinese patients.";
Mutat. Res. 664:84-90(2009).
[13]
VARIANTS FSGS2 SER-109; SER-125 AND PRO-780.
PubMed=19458060; DOI=10.1093/ndt/gfp229;
FSGS Study Group;
Santin S., Ars E., Rossetti S., Salido E., Silva I., Garcia-Maset R.,
Gimenez I., Ruiz P., Mendizabal S., Luciano Nieto J., Pena A.,
Camacho J.A., Fraga G., Cobo M.A., Bernis C., Ortiz A.,
de Pablos A.L., Sanchez-Moreno A., Pintos G., Mirapeix E.,
Fernandez-Llama P., Ballarin J., Torra R., Zamora I., Lopez-Hellin J.,
Madrid A., Ventura C., Vilalta R., Espinosa L., Garcia C., Melgosa M.,
Navarro M., Gimenez A., Cots J.V., Alexandra S., Caramelo C.,
Egido J., San Jose M.D., de la Cerda F., Sala P., Raspall F., Vila A.,
Daza A.M., Vazquez M., Ecija J.L., Espinosa M., Justa M.L., Poveda R.,
Aparicio C., Rosell J., Muley R., Montenegro J., Gonzalez D.,
Hidalgo E., de Frutos D.B., Trillo E., Gracia S., de los Rios F.J.;
"TRPC6 mutational analysis in a large cohort of patients with focal
segmental glomerulosclerosis.";
Nephrol. Dial. Transplant. 24:3089-3096(2009).
[14]
VARIANTS SER-15 AND VAL-404, VARIANTS FSGS2 SER-143; THR-270 AND
874-LYS--ARG-931 DEL, CHARACTERIZATION OF VARIANT FSGS2 SER-143,
MUTAGENESIS OF MET-132, AND FUNCTION.
PubMed=19936226; DOI=10.1371/journal.pone.0007771;
Heeringa S.F., Moeller C.C., Du J., Yue L., Hinkes B., Chernin G.,
Vlangos C.N., Hoyer P.F., Reiser J., Hildebrandt F.;
"A novel TRPC6 mutation that causes childhood FSGS.";
PLoS ONE 4:E7771-E7771(2009).
[15]
VARIANTS FSGS2 ALA-TYR-MET-PHE-88 INS AND ASP-757.
PubMed=20798252; DOI=10.2215/CJN.01190210;
Buescher A.K., Kranz B., Buescher R., Hildebrandt F., Dworniczak B.,
Pennekamp P., Kuwertz-Broeking E., Wingen A.M., John U., Kemper M.,
Monnens L., Hoyer P.F., Weber S., Konrad M.;
"Immunosuppression and renal outcome in congenital and pediatric
steroid-resistant nephrotic syndrome.";
Clin. J. Am. Soc. Nephrol. 5:2075-2084(2010).
[16]
VARIANTS FSGS2 SER-125 AND LEU-218, AND VARIANT 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).
[17]
VARIANT FSGS2 HIS-360.
PubMed=22732337;
Buescher A.K., Konrad M., Nagel M., Witzke O., Kribben A., Hoyer P.F.,
Weber S.;
"Mutations in podocyte genes are a rare cause of primary FSGS
associated with ESRD in adult patients.";
Clin. Nephrol. 78:47-53(2012).
[18]
VARIANT FSGS2 ALA-395, AND VARIANT VAL-404.
PubMed=21511817; DOI=10.1093/ndt/gfr202;
Mir S., Yavascan O., Berdeli A., Sozeri B.;
"TRPC6 gene variants in Turkish children with steroid-resistant
nephrotic syndrome.";
Nephrol. Dial. Transplant. 27:205-209(2012).
[19]
VARIANTS FSGS2 THR-270; CYS-895; GLU-897 DEL AND LYS-897.
PubMed=23014460; DOI=10.1038/ki.2012.349;
Barua M., Brown E.J., Charoonratana V.T., Genovese G., Sun H.,
Pollak M.R.;
"Mutations in the INF2 gene account for a significant proportion of
familial but not sporadic focal and segmental glomerulosclerosis.";
Kidney Int. 83:316-322(2013).
[20]
VARIANTS FSGS2 GLN-175 AND CYS-895, CHARACTERIZATION OF VARIANTS FSGS2
GLN-175 AND CYS-895, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23291369; DOI=10.1093/ndt/gfs572;
Hofstra J.M., Lainez S., van Kuijk W.H., Schoots J., Baltissen M.P.,
Hoefsloot L.H., Knoers N.V., Berden J.H., Bindels R.J.,
van der Vlag J., Hoenderop J.G., Wetzels J.F., Nijenhuis T.;
"New TRPC6 gain-of-function mutation in a non-consanguineous Dutch
family with late-onset focal segmental glomerulosclerosis.";
Nephrol. Dial. Transplant. 28:1830-1838(2013).
[21]
MUTAGENESIS OF ASN-110; MET-132; 755-GLU--GLY-757; 755-GLU-GLU-756;
826-LYS-LYS-827 AND GLN-889, VARIANTS FSGS2 SER-109; GLN-112; SER-125;
SER-143; GLN-175; LEU-218; ALA-395; ASP-757; PRO-780; CYS-895; LEU-895
AND LYS-897, CHARACTERIZATION OF VARIANTS FSGS2 SER-109; GLN-112;
SER-125; SER-143; GLN-175; LEU-218; ALA-395; ASP-757; PRO-780;
CYS-895; LEU-895 AND LYS-897, VARIANT VAL-404, CHARACTERIZATION OF
VARIANT VAL-404, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=26892346; DOI=10.1681/ASN.2015030318;
Riehle M., Buescher A.K., Gohlke B.O., Kassmann M.,
Kolatsi-Joannou M., Braesen J.H., Nagel M., Becker J.U., Winyard P.,
Hoyer P.F., Preissner R., Krautwurst D., Gollasch M., Weber S.,
Harteneck C.;
"TRPC6 G757D Loss-of-Function Mutation Associates with FSGS.";
J. Am. Soc. Nephrol. 27:2771-2783(2016).
-!- FUNCTION: Thought to form a receptor-activated non-selective
calcium permeant cation channel (PubMed:19936226,
PubMed:23291369). 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
(PubMed:26892346). Seems not to be activated by intracellular
calcium store depletion. {ECO:0000269|PubMed:19936226,
ECO:0000269|PubMed:23291369, ECO:0000269|PubMed:26892346}.
-!- SUBUNIT: Homodimer; forms channel complex (PubMed:26892346).
Interacts with MX1 and RNF24 (PubMed:15757897, PubMed:17850865).
{ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:17850865,
ECO:0000269|PubMed:26892346}.
-!- INTERACTION:
P20591:MX1; NbExp=4; IntAct=EBI-929362, EBI-929476;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23291369,
ECO:0000269|PubMed:26892346}; 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|UniProtKB:Q61143}.
-!- 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:19458060,
ECO:0000269|PubMed:19936226, ECO:0000269|PubMed:20798252,
ECO:0000269|PubMed:21511817, ECO:0000269|PubMed:21734084,
ECO:0000269|PubMed:22732337, ECO:0000269|PubMed:23014460,
ECO:0000269|PubMed:23291369, ECO:0000269|PubMed:26892346}.
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; -.
PDB; 5YX9; EM; 3.80 A; A/B/C/D=1-931.
PDBsum; 5YX9; -.
ProteinModelPortal; Q9Y210; -.
SMR; 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; -.
ProteomicsDB; 85580; -.
ProteomicsDB; 85581; -. [Q9Y210-2]
ProteomicsDB; 85582; -. [Q9Y210-3]
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:UniProtKB.
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:0005261; F:cation channel activity; IDA:UniProtKB.
GO; GO:0030276; F:clathrin binding; IEA:Ensembl.
GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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;
3D-structure; Alternative splicing; ANK repeat; Calcium;
Calcium channel; Calcium transport; Cell membrane; 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 15 15 P -> S (polymorphism; dbSNP:rs3802829).
{ECO:0000269|PubMed:19124028,
ECO:0000269|PubMed:19936226}.
/FTId=VAR_079784.
VARIANT 88 88 F -> FAYMF (in FSGS2; unknown
pathological significance).
{ECO:0000269|PubMed:20798252}.
/FTId=VAR_079785.
VARIANT 109 109 G -> S (in FSGS2; increases calcium ion
transport). {ECO:0000269|PubMed:19458060,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_079786.
VARIANT 112 112 P -> Q (in FSGS2; increases calcium ion
transport; dbSNP:rs121434390).
{ECO:0000269|PubMed:15879175,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_026730.
VARIANT 125 125 N -> S (in FSGS2; unknown pathological
significance; decreases calcium ion
transport; dbSNP:rs146776939).
{ECO:0000269|PubMed:19458060,
ECO:0000269|PubMed:21734084,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_067247.
VARIANT 143 143 N -> S (in FSGS2; increases cation
channel activity; does not change the
outward peak current; increases
significantly the inward peak current
amplitude; increases calcium ion
transport; dbSNP:rs121434391).
{ECO:0000269|PubMed:15924139,
ECO:0000269|PubMed:19936226,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_026731.
VARIANT 157 157 N -> T (in dbSNP:rs35857503).
/FTId=VAR_038419.
VARIANT 175 175 R -> Q (in FSGS2; increases cation
channel activity; does not change plasma
membrane expression; increases calcium
ion transport).
{ECO:0000269|PubMed:23291369,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_079787.
VARIANT 218 218 H -> L (in FSGS2; increases calcium ion
transport; dbSNP:rs779430565).
{ECO:0000269|PubMed:21734084,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_067248.
VARIANT 270 270 S -> T (in FSGS2; dbSNP:rs121434392).
{ECO:0000269|PubMed:15924139,
ECO:0000269|PubMed:19936226,
ECO:0000269|PubMed:23014460}.
/FTId=VAR_026732.
VARIANT 360 360 R -> H (in FSGS2; unknown pathological
significance; dbSNP:rs777715086).
{ECO:0000269|PubMed:22732337}.
/FTId=VAR_079788.
VARIANT 395 395 L -> A (in FSGS2; unknown pathological
significance; requires 2 nucleotide
substitutions; decreases calcium ion
transport). {ECO:0000269|PubMed:21511817,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_079789.
VARIANT 404 404 A -> V (polymorphism; increases calcium
ion transport; dbSNP:rs36111323).
{ECO:0000269|PubMed:19936226,
ECO:0000269|PubMed:21511817,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_061861.
VARIANT 757 757 G -> D (in FSGS2; decreases calcium ion
transport; does not change localization
at cell membrane; does not affect
homodimer formation).
{ECO:0000269|PubMed:20798252,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_079790.
VARIANT 780 780 L -> P (in FSGS2; unknown pathological
significance; decreases calcium ion
transport; dbSNP:rs771594597).
{ECO:0000269|PubMed:19458060,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_079791.
VARIANT 874 931 Missing (in FSGS2).
{ECO:0000269|PubMed:19936226}.
/FTId=VAR_079792.
VARIANT 895 895 R -> C (in FSGS2; increases cation
channel activity; does not change plasma
membrane expression; significantly
reduces the ratio of cell-surface to
total expression; increases calcium ion
transport; dbSNP:rs121434394).
{ECO:0000269|PubMed:15924139,
ECO:0000269|PubMed:23014460,
ECO:0000269|PubMed:23291369,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_026733.
VARIANT 895 895 R -> L (in FSGS2; decreases calcium ion
transport). {ECO:0000269|PubMed:21734084,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_067249.
VARIANT 897 897 E -> K (in FSGS2; increases calcium ion
transport; dbSNP:rs121434395).
{ECO:0000269|PubMed:15924139,
ECO:0000269|PubMed:23014460,
ECO:0000269|PubMed:26892346}.
/FTId=VAR_026734.
VARIANT 897 897 Missing (in FSGS2).
{ECO:0000269|PubMed:23014460}.
/FTId=VAR_079793.
MUTAGEN 110 110 N->H: Increases calcium ion transport.
{ECO:0000269|PubMed:26892346}.
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 132 132 M->T: Increases cation channel activity.
Increases significantly inward and
outward currents and does not show
channel inactivation. Increases calcium
ion transport.
{ECO:0000269|PubMed:19936226,
ECO:0000269|PubMed:26892346}.
MUTAGEN 561 561 N->Q: Constitutively activates channel.
{ECO:0000269|PubMed:12970363}.
MUTAGEN 755 757 EEG->KKR: Decreases calcium ion
transport. {ECO:0000269|PubMed:26892346}.
MUTAGEN 755 756 EE->KK: Increases calcium ion transport.
{ECO:0000269|PubMed:26892346}.
MUTAGEN 826 827 KK->EE: Decreases calcium ion transport.
{ECO:0000269|PubMed:26892346}.
MUTAGEN 889 889 Q->K: Increases calcium transport.
Increases calcium ion transport.
{ECO:0000269|PubMed:19124028,
ECO:0000269|PubMed:26892346}.
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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