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Short transient receptor potential channel 4 (TrpC4) (Trp-related protein 4) (hTrp-4) (hTrp4)

 TRPC4_HUMAN             Reviewed;         977 AA.
Q9UBN4; B1ALE0; B1ALE1; B1ALE2; Q15721; Q3SWS6; Q96P03; Q96P04;
Q96P05; Q9UIB0; Q9UIB1; Q9UIB2;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 169.
RecName: Full=Short transient receptor potential channel 4;
Short=TrpC4;
AltName: Full=Trp-related protein 4;
Short=hTrp-4;
Short=hTrp4;
Name=TRPC4;
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 ALPHA).
TISSUE=Kidney;
PubMed=11042129; DOI=10.1042/bj3510735;
McKay R.R., Szymeczek-Seay C.L., Lievremont J.-P., Bird G.S., Zitt C.,
Juengling E., Lueckhoff A., Putney J.W. Jr.;
"Cloning and expression of the human transient receptor potential 4
(TRP4) gene: localization and functional expression of human TRP4 and
TRP3.";
Biochem. J. 351:735-746(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; DELTA AND GAMMA).
TISSUE=Embryonic kidney;
PubMed=11163362; DOI=10.1016/S0014-5793(00)02362-0;
Mery L., Magnino F., Schmidt K., Krause K.-H., Dufour J.-F.;
"Alternative splice variants of hTrp4 differentially interact with the
C-terminal portion of the inositol 1,4,5-trisphosphate receptors.";
FEBS Lett. 487:377-383(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; EPSILON; ETA AND
ZETA), AND SUBCELLULAR LOCATION.
PubMed=11713258; DOI=10.1074/jbc.M109850200;
Schaefer M., Plant T.D., Stresow N., Albrecht N., Schultz G.;
"Functional differences between TRPC4 splice variants.";
J. Biol. Chem. 277:3752-3759(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 514-633.
TISSUE=Kidney;
PubMed=8646775; DOI=10.1016/S0092-8674(00)81233-7;
Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E.,
Birnbaumer L.;
"trp, a novel mammalian gene family essential for agonist-activated
capacitative Ca2+ entry.";
Cell 85:661-671(1996).
[8]
MUTAGENESIS OF 975-THR--LEU-977, INTERACTION WITH SLC9A3R1, AND
SUBCELLULAR LOCATION.
PubMed=12154080;
Mery L., Strauss B., Dufour J.F., Krause K.H., Hoth M.;
"The PDZ-interacting domain of TRPC4 controls its localization and
surface expression in HEK293 cells.";
J. Cell Sci. 115:3497-3508(2002).
[9]
SUBUNIT.
PubMed=12032305; DOI=10.1073/pnas.102596199;
Hofmann T., Schaefer M., Schultz G., Gudermann T.;
"Subunit composition of mammalian transient receptor potential
channels in living cells.";
Proc. Natl. Acad. Sci. U.S.A. 99:7461-7466(2002).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH EPB41L2.
PubMed=16254212; DOI=10.1161/01.RES.0000193597.65217.00;
Cioffi D.L., Wu S., Alexeyev M., Goodman S.R., Zhu M.X., Stevens T.;
"Activation of the endothelial store-operated ISOC Ca2+ channel
requires interaction of protein 4.1 with TRPC4.";
Circ. Res. 97:1164-1172(2005).
[11]
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).
[12]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-959 AND
TYR-972, AND MUTAGENESIS OF TYR-959 AND TYR-972.
PubMed=16144838; DOI=10.1074/jbc.M503646200;
Odell A.F., Scott J.L., Van Helden D.F.;
"Epidermal growth factor induces tyrosine phosphorylation, membrane
insertion, and activation of transient receptor potential channel 4.";
J. Biol. Chem. 280:37974-37987(2005).
[13]
INTERACTION WITH RNF24.
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).
[14]
INTERACTION WITH SPTAN1 AND SPTBN5.
PubMed=18048348; DOI=10.1074/jbc.M709729200;
Odell A.F., Van Helden D.F., Scott J.L.;
"The spectrin cytoskeleton influences the surface expression and
activation of human transient receptor potential channel 4 channels.";
J. Biol. Chem. 283:4395-4407(2008).
[15]
INTERACTION WITH SESTD1.
PubMed=20164195; DOI=10.1074/jbc.M109.068304;
Miehe S., Bieberstein A., Arnould I., Ihdene O., Rutten H.,
Strubing C.;
"The phospholipid-binding protein SESTD1 is a novel regulator of the
transient receptor potential channels TRPC4 and TRPC5.";
J. Biol. Chem. 285:12426-12434(2010).
[16]
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH CDH5 AND CTNNB1.
PubMed=19996314; DOI=10.1074/jbc.M109.060301;
Graziani A., Poteser M., Heupel W.M., Schleifer H., Krenn M.,
Drenckhahn D., Romanin C., Baumgartner W., Groschner K.;
"Cell-cell contact formation governs Ca2+ signaling by TRPC4 in the
vascular endothelium: evidence for a regulatory TRPC4-beta-catenin
interaction.";
J. Biol. Chem. 285:4213-4223(2010).
[17]
VARIANT [LARGE SCALE ANALYSIS] LYS-138.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Form a receptor-activated non-selective calcium permeant
cation channel. Acts as a cell-cell contact-dependent endothelial
calcium entry channel. Probably operated by a phosphatidylinositol
second messenger system activated by receptor tyrosine kinases or
G-protein coupled receptors. Mediates cation entry, with an
enhanced permeability to barium over calcium. May also be
activated by intracellular calcium store depletion.
{ECO:0000269|PubMed:16144838, ECO:0000269|PubMed:19996314}.
-!- SUBUNIT: Interacts with TRPC4AP (By similarity). Homotetramer and
heterotetramer with TRPC1 and/or TRPC5. Isoform alpha but not
isoform beta associates with inositol 1,4,5-trisphosphate receptor
(ITPR). Interacts with (via PDZ-binding domain) with
SLC9A3R1/NHERF. Interacts with MX1 and RNF24. Interacts (via CIRB
domain) with SESTD1 (via spectrin 1 repeat). Interacts with CDH5
and CTNNB1. Interacts with SPTAN1 (via C-terminal spectrin
repeats) and SPTBN5 (via C-terminus). Interacts (via protein 4.1-
binding domain) with EPB41L2. {ECO:0000250,
ECO:0000269|PubMed:12032305, ECO:0000269|PubMed:12154080,
ECO:0000269|PubMed:15757897, ECO:0000269|PubMed:16254212,
ECO:0000269|PubMed:17850865, ECO:0000269|PubMed:18048348,
ECO:0000269|PubMed:19996314, ECO:0000269|PubMed:20164195}.
-!- INTERACTION:
P20591:MX1; NbExp=2; IntAct=EBI-929504, EBI-929476;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
membrane; Multi-pass membrane protein. Note=Enhanced insertion
into the cell membrane after activation of the EGF receptor.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=7;
Name=Alpha;
IsoId=Q9UBN4-1; Sequence=Displayed;
Name=Beta;
IsoId=Q9UBN4-2; Sequence=VSP_006569;
Name=Delta;
IsoId=Q9UBN4-3; Sequence=VSP_006568;
Name=Gamma;
IsoId=Q9UBN4-4; Sequence=VSP_006567, VSP_006569;
Name=Epsilon;
IsoId=Q9UBN4-5; Sequence=VSP_041262;
Name=Zeta;
IsoId=Q9UBN4-6; Sequence=VSP_041439;
Name=Eta;
IsoId=Q9UBN4-7; Sequence=VSP_047747, VSP_047748;
-!- TISSUE SPECIFICITY: Strongly expressed in placenta. Expressed at
lower levels in heart, pancreas, kidney and brain. Expressed in
endothelial cells. Isoform alpha was found to be the predominant
isoform. Isoform beta was not found in pancreas and brain.
{ECO:0000269|PubMed:19996314}.
-!- DOMAIN: The protein 4.1-binding domain (654-685) is required for
binding to EPB41L2 and channel activation.
-!- DOMAIN: The calmodulin- and inositol 1,4,5-trisphosphate receptor-
binding (CIRB) domain (695-724) is sufficient for the interaction
with SESTD1.
-!- DOMAIN: The spectrin-binding domain (730-758) is required for
binding to SPTAN1 and SPTBN5.
-!- PTM: Phosphorylation modulates TRPC channel function by regulating
the level of TRPC4 at the cell surface and by increasing the
association with SLC9A3R1/NHERF. {ECO:0000269|PubMed:16144838}.
-!- MISCELLANEOUS: The interaction with spectrin is important in
controlling the translocation of TRPC4 channels to the plasma
membrane following EGF stimulation.
-!- MISCELLANEOUS: The cell membrane presentation, the calcium entry
function and the interaction with junctional proteins (CTNNB1 and
CDH5) are controlled by endothelial cell-cell contacts.
-!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
STrpC subfamily. TRPC4 sub-subfamily. {ECO:0000305}.
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EMBL; AF063822; AAF22927.1; -; mRNA.
EMBL; AF063823; AAF22928.1; -; mRNA.
EMBL; AF063824; AAF22929.1; -; mRNA.
EMBL; AF063825; AAF22930.1; -; mRNA.
EMBL; AF175406; AAD51736.1; -; mRNA.
EMBL; AF421358; AAL24549.1; -; mRNA.
EMBL; AF421359; AAL24550.1; -; mRNA.
EMBL; AF421360; AAL24551.1; -; mRNA.
EMBL; AF421361; AAL24552.1; -; mRNA.
EMBL; AF421362; AAL24553.1; -; mRNA.
EMBL; AL138679; CAH70109.1; -; Genomic_DNA.
EMBL; AL354802; CAH70109.1; JOINED; Genomic_DNA.
EMBL; AL138679; CAH70110.1; -; Genomic_DNA.
EMBL; AL354802; CAH70110.1; JOINED; Genomic_DNA.
EMBL; AL138679; CAH70111.1; -; Genomic_DNA.
EMBL; AL354802; CAH70111.1; JOINED; Genomic_DNA.
EMBL; AL138679; CAH70114.1; -; Genomic_DNA.
EMBL; AL354802; CAH70114.1; JOINED; Genomic_DNA.
EMBL; AL354802; CAI15556.1; -; Genomic_DNA.
EMBL; AL138679; CAI15556.1; JOINED; Genomic_DNA.
EMBL; AL354802; CAI15557.1; -; Genomic_DNA.
EMBL; AL138679; CAI15557.1; JOINED; Genomic_DNA.
EMBL; AL354802; CAI15558.1; -; Genomic_DNA.
EMBL; AL138679; CAI15558.1; JOINED; Genomic_DNA.
EMBL; AL354802; CAI15560.1; -; Genomic_DNA.
EMBL; AL138679; CAI15560.1; JOINED; Genomic_DNA.
EMBL; AL138679; CAH70112.1; -; Genomic_DNA.
EMBL; AL354802; CAH70112.1; JOINED; Genomic_DNA.
EMBL; AL354802; CAI15561.1; -; Genomic_DNA.
EMBL; AL138679; CAI15561.1; JOINED; Genomic_DNA.
EMBL; CH471075; EAX08595.1; -; Genomic_DNA.
EMBL; CH471075; EAX08596.1; -; Genomic_DNA.
EMBL; CH471075; EAX08597.1; -; Genomic_DNA.
EMBL; CH471075; EAX08598.1; -; Genomic_DNA.
EMBL; CH471075; EAX08600.1; -; Genomic_DNA.
EMBL; CH471075; EAX08601.1; -; Genomic_DNA.
EMBL; BC104725; AAI04726.1; -; mRNA.
EMBL; U40983; AAC50630.1; -; mRNA.
CCDS; CCDS45035.1; -. [Q9UBN4-6]
CCDS; CCDS45036.1; -. [Q9UBN4-4]
CCDS; CCDS45037.1; -. [Q9UBN4-5]
CCDS; CCDS45038.1; -. [Q9UBN4-2]
CCDS; CCDS45039.1; -. [Q9UBN4-3]
CCDS; CCDS9365.1; -. [Q9UBN4-1]
RefSeq; NP_001129427.1; NM_001135955.1. [Q9UBN4-2]
RefSeq; NP_001129428.1; NM_001135956.1. [Q9UBN4-4]
RefSeq; NP_001129429.1; NM_001135957.1. [Q9UBN4-3]
RefSeq; NP_001129430.1; NM_001135958.1. [Q9UBN4-6]
RefSeq; NP_003297.1; NM_003306.1. [Q9UBN4-5]
RefSeq; NP_057263.1; NM_016179.2. [Q9UBN4-1]
UniGene; Hs.262960; -.
ProteinModelPortal; Q9UBN4; -.
BioGrid; 113074; 12.
CORUM; Q9UBN4; -.
IntAct; Q9UBN4; 2.
MINT; MINT-157838; -.
STRING; 9606.ENSP00000369003; -.
GuidetoPHARMACOLOGY; 489; -.
TCDB; 1.A.4.1.12; the transient receptor potential ca(2+) channel (trp-cc) family.
iPTMnet; Q9UBN4; -.
PhosphoSitePlus; Q9UBN4; -.
BioMuta; TRPC4; -.
DMDM; 13633994; -.
EPD; Q9UBN4; -.
PaxDb; Q9UBN4; -.
PeptideAtlas; Q9UBN4; -.
PRIDE; Q9UBN4; -.
Ensembl; ENST00000338947; ENSP00000342580; ENSG00000133107. [Q9UBN4-6]
Ensembl; ENST00000355779; ENSP00000348025; ENSG00000133107. [Q9UBN4-3]
Ensembl; ENST00000358477; ENSP00000351264; ENSG00000133107. [Q9UBN4-2]
Ensembl; ENST00000379673; ENSP00000368995; ENSG00000133107. [Q9UBN4-4]
Ensembl; ENST00000379679; ENSP00000369001; ENSG00000133107. [Q9UBN4-6]
Ensembl; ENST00000379705; ENSP00000369027; ENSG00000133107. [Q9UBN4-1]
Ensembl; ENST00000488717; ENSP00000435969; ENSG00000133107. [Q9UBN4-7]
Ensembl; ENST00000625583; ENSP00000486109; ENSG00000133107. [Q9UBN4-5]
GeneID; 7223; -.
KEGG; hsa:7223; -.
UCSC; uc001uws.4; human. [Q9UBN4-1]
CTD; 7223; -.
DisGeNET; 7223; -.
EuPathDB; HostDB:ENSG00000133107.14; -.
GeneCards; TRPC4; -.
HGNC; HGNC:12336; TRPC4.
MIM; 603651; gene.
neXtProt; NX_Q9UBN4; -.
OpenTargets; ENSG00000133107; -.
PharmGKB; PA37009; -.
eggNOG; KOG3609; Eukaryota.
eggNOG; ENOG410XQ0Y; LUCA.
GeneTree; ENSGT00760000119180; -.
HOGENOM; HOG000151279; -.
HOVERGEN; HBG068337; -.
InParanoid; Q9UBN4; -.
KO; K04967; -.
OMA; CILVDHR; -.
OrthoDB; EOG091G029I; -.
PhylomeDB; Q9UBN4; -.
TreeFam; TF313147; -.
Reactome; R-HSA-3295583; TRP channels.
Reactome; R-HSA-418890; Role of second messengers in netrin-1 signaling.
ChiTaRS; TRPC4; human.
GeneWiki; TRPC4; -.
GenomeRNAi; 7223; -.
PRO; PR:Q9UBN4; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000133107; -.
CleanEx; HS_TRPC4; -.
ExpressionAtlas; Q9UBN4; baseline and differential.
Genevisible; Q9UBN4; HS.
GO; GO:0016323; C:basolateral plasma membrane; IDA:BHF-UCL.
GO; GO:0034704; C:calcium channel complex; IDA:UniProtKB.
GO; GO:0005901; C:caveola; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0030863; C:cortical cytoskeleton; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0008013; F:beta-catenin binding; IPI:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IPI:BHF-UCL.
GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IEA:Ensembl.
GO; GO:0015279; F:store-operated calcium channel activity; IMP:UniProtKB.
GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
GO; GO:0006816; P:calcium ion transport; TAS:ProtInc.
GO; GO:0014051; P:gamma-aminobutyric acid secretion; IEA:Ensembl.
GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; 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; IPR005460; TRPC4_channel.
InterPro; IPR002153; TRPC_channel.
PANTHER; PTHR10117; PTHR10117; 1.
PANTHER; PTHR10117:SF25; PTHR10117:SF25; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF08344; TRP_2; 1.
PRINTS; PR01097; TRNSRECEPTRP.
PRINTS; PR01645; TRPCHANNEL4.
SMART; SM00248; ANK; 2.
SUPFAM; SSF48403; SSF48403; 1.
TIGRFAMs; TIGR00870; trp; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Calcium; Calcium channel;
Calcium transport; Cell membrane; Coiled coil; Complete proteome;
Ion channel; Ion transport; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 977 Short transient receptor potential
channel 4.
/FTId=PRO_0000215314.
TOPO_DOM 1 329 Cytoplasmic. {ECO:0000255}.
TRANSMEM 330 350 Helical. {ECO:0000255}.
TOPO_DOM 351 362 Extracellular. {ECO:0000255}.
TRANSMEM 363 383 Helical. {ECO:0000255}.
TOPO_DOM 384 436 Cytoplasmic. {ECO:0000255}.
TRANSMEM 437 457 Helical. {ECO:0000255}.
TOPO_DOM 458 469 Extracellular. {ECO:0000255}.
TRANSMEM 470 490 Helical. {ECO:0000255}.
TOPO_DOM 491 511 Cytoplasmic. {ECO:0000255}.
TRANSMEM 512 532 Helical. {ECO:0000255}.
TOPO_DOM 533 599 Extracellular. {ECO:0000255}.
TRANSMEM 600 620 Helical. {ECO:0000255}.
TOPO_DOM 621 977 Cytoplasmic. {ECO:0000255}.
REPEAT 31 60 ANK 1.
REPEAT 69 97 ANK 2.
REPEAT 98 124 ANK 3.
REPEAT 141 170 ANK 4.
REGION 87 172 Multimerization domain. {ECO:0000250}.
REGION 254 304 Multimerization domain. {ECO:0000250}.
REGION 615 977 Binds to ITPR1, ITPR2 and ITPR3.
REGION 975 977 PDZ-binding domain.
COILED 223 260 {ECO:0000255}.
COMPBIAS 377 382 Poly-Leu.
MOD_RES 959 959 Phosphotyrosine; by FYN.
{ECO:0000269|PubMed:16144838}.
MOD_RES 972 972 Phosphotyrosine; by FYN.
{ECO:0000269|PubMed:16144838}.
VAR_SEQ 127 299 Missing (in isoform Zeta).
{ECO:0000303|PubMed:11713258}.
/FTId=VSP_041439.
VAR_SEQ 300 323 FVAQPNCQQLLASRWYDEFPGWRR -> ASYGEKLNRCGMA
DFRTTSMIGGI (in isoform Eta).
{ECO:0000303|PubMed:11713258}.
/FTId=VSP_047747.
VAR_SEQ 324 977 Missing (in isoform Eta).
{ECO:0000303|PubMed:11713258}.
/FTId=VSP_047748.
VAR_SEQ 629 693 Missing (in isoform Gamma).
{ECO:0000303|PubMed:11163362}.
/FTId=VSP_006567.
VAR_SEQ 693 693 G -> GVRTQH (in isoform Epsilon).
{ECO:0000303|PubMed:11713258}.
/FTId=VSP_041262.
VAR_SEQ 730 870 Missing (in isoform Delta).
{ECO:0000303|PubMed:11163362}.
/FTId=VSP_006568.
VAR_SEQ 785 868 Missing (in isoform Beta and isoform
Gamma). {ECO:0000303|PubMed:11163362,
ECO:0000303|PubMed:11713258}.
/FTId=VSP_006569.
VARIANT 138 138 E -> K (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036452.
MUTAGEN 959 959 Y->F: Reduced EGF-induced phosphorylation
and decreased association with
SLC9A3R1/NHERF. Loss of EGF-induced
phosphorylation and decreased association
with SLC9A3R1/NHERF; when associated with
F-972. {ECO:0000269|PubMed:16144838}.
MUTAGEN 972 972 Y->F: Reduced EGF-induced phosphorylation
and decreased association with
SLC9A3R1/NHERF. Loss of EGF-induced
phosphorylation and decreased association
with SLC9A3R1/NHERF; when associated with
F-959. {ECO:0000269|PubMed:16144838}.
MUTAGEN 975 977 Missing: Loss of interaction with
SLC9A3R1/NHERF.
{ECO:0000269|PubMed:12154080}.
SEQUENCE 977 AA; 112101 MW; 77E4D27C374D660E CRC64;
MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK
ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK
PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE
CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE
YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF
VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR
KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ
MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL
FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY
YEETKGLTCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM
FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI
PSPKSLWYLI KWIWTHLCKK KMRRKPESFG TIGRRAADNL RRHHQYQEVM RNLVKRYVAA
MIRDAKTEEG LTEENFKELK QDISSFRFEV LGLLRGSKLS TIQSANASKE SSNSADSDEK
SDSEGNSKDK KKNFSLFDLT TLIHPRSAAI ASERHNISNG SALVVQEPPR EKQRKVNFVT
DIKNFGLFHR RSKQNAAEQN ANQIFSVSEE VARQQAAGPL ERNIQLESRG LASRGDLSIP
GLSEQCVLVD HRERNTDTLG LQVGKRVCPF KSEKVVVEDT VPIIPKEKHA KEEDSSIDYD
LNLPDTVTHE DYVTTRL


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