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Q9ESQ5 (TRPM4_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transient receptor potential cation channel subfamily M member 4
Alternative name(s):
Calcium-activated non-selective cation channel 1
Long transient receptor potential channel 4
Short name=LTrpC-4
Short name=LTrpC4
MLS2s
Melastatin-like 2
Gene names
Name:Trpm4
Synonyms:Ltrpc4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1208 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-activated non selective (CAN) cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca2+, it is impermeable to it. Mediates transport of monovalent cations (Na+ > K+ > Cs+ > Li+), leading to depolarize the membrane. It thereby plays a central role in cadiomyocytes, neurons from entorhinal cortex, dorsal root and vomeronasal neurons, endocrine pancreas cells, kidney epithelial cells, cochlea hair cells etc. Participates in T-cell activation by modulating Ca2+ oscillations after T lymphocyte activation, which is required for NFAT-dependent IL2 production. Involved in myogenic constriction of cerebral arteries. Controls insulin secretion in pancreatic beta-cells. May also be involved in pacemaking or could cause irregular electrical activity under conditions of Ca2+ overload. Affects T-helper 1 (Th1) and T-helper 2 (Th2) cell motility and cytokine production through differential regulation of calcium signaling and NFATC1 localization. Enhances cell proliferation through up-regulation of the beta-catenin signaling pathway. Essential for the migration but not the maturation of dendritic cells By similarity. Ref.2 Ref.5

Enzyme regulation

Gating is voltage-dependent and repressed by decavanadate. Calmodulin-binding confers the Ca2+ sensitivity. ATP is able to restore Ca2+ sensitivity after desensitization. Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding strongly enhances activity, by increasing the channel's Ca2+ sensitivity and shifting its voltage dependence of activation towards negative potentials. Activity is also enhanced by 3,5-bis(trifluoromethyl)pyrazole derivative (BTP2) By similarity.

Subunit structure

Homomultimer By similarity.

Subcellular location

Isoform 1: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum. Golgi apparatus Ref.2.

Isoform 2: Endoplasmic reticulum. Golgi apparatus Ref.2.

Tissue specificity

Isoform 1 is highly expressed in the testis with a moderate expression in the brain, spleen and thymus. Isoform 2 is only expressed in the brain and spleen. Ref.2

Post-translational modification

Sumoylated. Desumoylated by SENP1 By similarity.

Phosphorylation by PKC leads to increase the sensitivity to Ca2+.

Sequence similarities

Belongs to the transient receptor (TC 1.A.4) family. LTrpC subfamily. TRPM4 sub-subfamily. [View classification]

Sequence caution

The sequence BAB15808.1 differs from that shown. Reason: Chimeric cDNA.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
Ion transport
Transport
   Cellular componentCell membrane
Endoplasmic reticulum
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Transmembrane
Transmembrane helix
   LigandATP-binding
Calcium
Calmodulin-binding
Nucleotide-binding
   Molecular functionIon channel
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdendritic cell chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

protein sumoylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of T cell cytokine production

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.2. Source: UniProtKB

endoplasmic reticulum

Inferred from direct assay Ref.2. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium activated cation channel activity

Inferred from direct assay Ref.2. Source: UniProtKB

calcium channel activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms may exist.
Isoform 1 (identifier: Q9ESQ5-1)

Also known as: TRPM4b;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9ESQ5-2)

Also known as: TRPM4a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-186: Missing.
Note: Probably non-functional.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12081208Transient receptor potential cation channel subfamily M member 4
PRO_0000259531

Regions

Topological domain1 – 687687Cytoplasmic Potential
Transmembrane688 – 70821Helical; Potential
Topological domain709 – 77668Extracellular Potential
Transmembrane777 – 79721Helical; Potential
Topological domain7981Cytoplasmic Potential
Transmembrane799 – 81921Helical; Potential
Topological domain820 – 88667Extracellular Potential
Transmembrane887 – 90721Helical; Potential
Topological domain908 – 92417Cytoplasmic Potential
Transmembrane925 – 94521Helical; Potential
Topological domain946 – 95914Extracellular Potential
Intramembrane960 – 98728Pore-forming; Potential
Topological domain988 – 101326Extracellular Potential
Transmembrane1014 – 103421Helical; Potential
Topological domain1035 – 1208174Cytoplasmic Potential
Region1070 – 1170101Calmodulin-binding By similarity
Region1130 – 11356Mediates modulation by decavanadate and PIP2-binding By similarity
Coiled coil1128 – 118053 Potential
Motif975 – 9806Selectivity filter By similarity

Amino acid modifications

Modified residue11391Phosphoserine; by PKC By similarity
Modified residue11461Phosphoserine; by PKC By similarity

Natural variations

Alternative sequence1 – 186186Missing in isoform 2.
VSP_040337

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (TRPM4b) [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 324CEC9A6B9F7EA6

FASTA1,208135,341
        10         20         30         40         50         60 
MVGQEKEQSW IPKIFRKKVC TTFIVDLHDD AGGTLCQCGQ PRDAHPSVAV EDAFGAAVVT 

        70         80         90        100        110        120 
EWNSDEHTTE KPTDAYGDLD FTYSGRKSSN FLRLSDRTDP ATVYSLVTRS WGFRAPNLVV 

       130        140        150        160        170        180 
SVLGGSEGPV LQTWLQDLLR RGLVRAAQST GAWIVTGGLH TGIGRHVGVA VRDHQTASTG 

       190        200        210        220        230        240 
GSKVVAMGVA PWGVVRNRDM LINPKGSFPA RYRWRGDPED GVEFPLDYNY SAFFLVDDGT 

       250        260        270        280        290        300 
YGRMGGENRF RLRFESYVAQ QKTGVGGTGI DIPVLLLLIE GDEKMLKRIE DATQAQLPCL 

       310        320        330        340        350        360 
LVAGSGGAAD CLVETLEDTL APGSGGLRRG EARDRIRRYF PKGDPEVLQA QVERIMTRKE 

       370        380        390        400        410        420 
LLTVYSSEDG SEEFETIVLR ALVKACGSSE ASAYLDELRL AVAWNRVDIA QSELFRGDIQ 

       430        440        450        460        470        480 
WRSFHLEASL MDALLNDRPE FVRLLISHGL SLGHFLTPVR LAQLYSAVSP NSLIRNLLDQ 

       490        500        510        520        530        540 
ASHASSSKSP PANGAAELRP PNVGQVLRTL LGETCAPRYP ARNTRHSLLG QDHRENDSLL 

       550        560        570        580        590        600 
MDWANMQQDA SFEQAPWSDL LIWALLLNRA QMAIYFWEKG SNSVASALGA CLLLRVMARL 

       610        620        630        640        650        660 
EWEAEEAARR KDLAAKFESM SVDLFGECYH NSEYRAARLL LRRCPLWGEA TCLQLAMQAD 

       670        680        690        700        710        720 
ARAFFAQDGV QSLLTQKWWG EMDSTNPIWA LLLTFFCPPL IYTNLILFRK SEEEPTQKDL 

       730        740        750        760        770        780 
DFDMDSSMNG AGPLGPAEPS AKVALERRRR RRPGHTLCCG GCSKRWSYFW GAPVTAFLGN 

       790        800        810        820        830        840 
VVSYLLFLLL FAHVLLVDFQ PTKPGVFELL LYFWAFTLLC EELRQGLGGG WGTLANGGPG 

       850        860        870        880        890        900 
PGKAPLRHRL HLYLLDTWNQ CDLLALTCFL LGVGCRLTPG LFDLGRTVLC LDFMIFTLRL 

       910        920        930        940        950        960 
LHIFTVNKQL GPKIVIVSKM MKDVFFFLFF LCVWLVAYGV ATEGILRPQD RSLPSILRRV 

       970        980        990       1000       1010       1020 
FYRPYLQIFG QIPQEEMDVA LMNPSNCSAE RGSWAHPEGP VAGSCVSQYA NWLVVLLLIV 

      1030       1040       1050       1060       1070       1080 
FLLVANILLL NLLIAMFSYT FNKVHGNSDL YWKAQRYSLI REFHSRPALA PPLIIISHLR 

      1090       1100       1110       1120       1130       1140 
LLFKWLRRCH RTNLPASPVF EHFRVCLSKE AERTLLTWES VHKENFLLAQ ARDKRDSDSE 

      1150       1160       1170       1180       1190       1200 
RLKRTSQKVD TALKQLGQIR EYDRRLRGLE REVQHCSRVL TWMAEALSHS ALLPPGGPPP 


PSPTGSKD 

« Hide

Isoform 2 (TRPM4a) [UniParc].

Checksum: 68246240BDC5FECB
Show »

FASTA1,022115,277

References

« Hide 'large scale' references
[1]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[2]"Cloning and characterization of rat transient receptor potential-melastatin 4 (TRPM4)."
Yoo J.C., Yarishkin O.V., Hwang E.M., Kim E., Kim D.G., Park N., Hong S.G., Park J.Y.
Biochem. Biophys. Res. Commun. 391:806-811(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]"Cloning of novel Ca-permeable channels."
Ohki G., Ishibashi K., Suzuki M.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 717-1208.
Tissue: Brain.
[4]"Activation of the Ca(2+)-activated nonselective cation channel by diacylglycerol analogues in rat cardiomyocytes."
Guinamard R., Chatelier A., Lenfant J., Bois P.
J. Cardiovasc. Electrophysiol. 15:342-348(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[5]"Functional expression of the TRPM4 cationic current in ventricular cardiomyocytes from spontaneously hypertensive rats."
Guinamard R., Demion M., Magaud C., Potreau D., Bois P.
Hypertension 48:587-594(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AABR03000917 Genomic DNA. No translation available.
AABR03004552 Genomic DNA. No translation available.
AB040807 mRNA. Translation: BAB15808.1. Sequence problems.
RefSeqNP_001129701.1. NM_001136229.1. [Q9ESQ5-1]
UniGeneRn.205004.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9ESQ5.
PRIDEQ9ESQ5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000041513; ENSRNOP00000041387; ENSRNOG00000020714. [Q9ESQ5-1]
GeneID171143.
KEGGrno:171143.
UCSCRGD:620244. rat. [Q9ESQ5-1]

Organism-specific databases

CTD54795.
RGD620244. Trpm4.

Phylogenomic databases

eggNOGNOG253824.
GeneTreeENSGT00650000093200.
HOGENOMHOG000236350.
HOVERGENHBG108337.
InParanoidQ9ESQ5.
KOK04979.
OMARTWGFRA.
OrthoDBEOG725DH1.
PhylomeDBQ9ESQ5.
TreeFamTF314204.

Gene expression databases

GenevestigatorQ9ESQ5.

Family and domain databases

InterProIPR005821. Ion_trans_dom.
[Graphical view]
PfamPF00520. Ion_trans. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio621940.

Entry information

Entry nameTRPM4_RAT
AccessionPrimary (citable) accession number: Q9ESQ5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 14, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families