Trpm4
entrez
68667
canonical
uniprot
Q7TN37
canonical
ensembl
ENSMUSG00000038260
resolver
ensp
ENSMUSP00000040367
resolver
ensp
ENSMUSP00000147793
resolver
enst
ENSMUST00000211743
resolver
genesymbol
Trpm4
resolver
genesymbol_syn
Ltrpc4
resolver
uniprot
A0A1B0GS49
resolver
uniprot
Q6PDM0
resolver
uniprot
Q769E2
resolver
uniprot
Q769E4
resolver
uniprot
Q80Y94
resolver
uniprot
Q80YB3
resolver
uniprot
Q811E2
resolver
uniprot_entry
A0A1B0GS49_MOUSE
resolver
uniprot_entry
TRPM4_MOUSE
resolver
uniprot_sec
Q6PDM0
resolver
uniprot_sec
Q769E2
resolver
uniprot_sec
Q769E4
resolver
uniprot_sec
Q80Y94
resolver
uniprot_sec
Q80YB3
resolver
uniprot_sec
Q811E2
resolver
activity_regulation
ACTIVITY REGULATION: Gating is voltage-dependent and repressed by decavanadate. Calmodulin-binding confers the Ca(2+) sensitivity. ATP is able to restore Ca(2+) sensitivity after desensitization. Phosphatidylinositol 4,5-bisphosphate (PIP2)-binding strongly enhances activity, by increasing the channel's Ca(2+) sensitivity and shifting its voltage dependence of activation towards negative potentials (PubMed:17188667). Activity is also enhanced by 3,5-bis(trifluoromethyl)pyrazole derivative (BTP2) (By similarity). Inhibited by flufenamic acid and glibenclamide (PubMed:17188667). Exhibits pronounced temperature sensitivity, with activities strongly intensifying near physiological temperatures. TRPM4 can adopt distinct conformations at different temperatures, markedly influencing where and how ligands interact with them. {ECO:0000250|UniProtKB:Q8TD43, ECO:0000269|PubMed:17188667}.
uniprot
proteins
amino_acid_sequence
MVGPEKEQSWIPKIFRKKVCTTFIVDLSDDAGGTLCQCGQPRDAHPSVAVEDAFGAAVVTEWNSDEHTTEKPTDAYGDLDFTYSGRKHSNFLRLSDRTDPATVYSLVTRSWGFRAPNLVVSVLGGSGGPVLQTWLQDLLRRGLVRAAQSTGAWIVTGGLHTGIGRHVGVAVRDHQTASTGSSKVVAMGVAPWGVVRNRDMLINPKGSFPARYRWRGDPEDGVEFPLDYNYSAFFLVDDGTYGRLGGENRFRLRFESYVAQQKTGVGGTGIDIPVLLLLIDGDEKMLKRIEDATQAQLPCLLVAGSGGAADCLVETLEDTLAPGSGGLRRGEARDRIRRYFPKGDPEVLQAQVERIMTRKELLTVYSSEDGSEEFETIVLRALVKACGSSEASAYLDELRLAVAWNRVDIAQSELFRGDIQWRSFHLEASLMDALLNDRPEFVRLLISHGLSLGHFLTPVRLAQLYSAVSPNSLIRNLLDQASHASSSKSPPVNGTVELRPPNVGQVLRTLLGETCAPRYPARNTRDSYLGQDHRENDSLLMDWANKQPSTDASFEQAPWSDLLIWALLLNRAQMAIYFWEKGSNSVASALGACLLLRVMARLESEAEEAARRKDLAATFESMSVDLFGECYHNSEERAARLLLRRCPLWGEATCLQLAMQADARAFFAQDGVQSLLTQKWWGEMDSTTPIWALLLAFFCPPLIYTNLIVFRKSEEEPTQKDLDFDMDSSINGAGPPGTVEPSAKVALERRQRRRPGRALCCGKFSKRWSDFWGAPVTAFLGNVVSYLLFLLLFAHVLLVDFQPTKPSVSELLLYFWAFTLLCEELRQGLGGGWGSLASGGRGPDRAPLRHRLHLYLSDTWNQCDLLALTCFLLGVGCRLTPGLFDLGRTVLCLDFMIFTLRLLHIFTVNKQLGPKIVIVSKMMKDVFFFLFFLCVWLVAYGVATEGILRPQDRSLPSILRRVFYRPYLQIFGQIPQEEMDVALMIPGNCSMERGSWAHPEGPVAGSCVSQYANWLVVLLLIVFLLVANILLLNLLIAMFSYTFSKVHGNSDLYWKAQRYSLIREFHSRPALAPPLIIISHVRLLIKWLRRCRRCRRANLPASPVFEHFRVCLSKEAERKLLTWESVHKENFLLAQARDKRDSDSERLKRTSQKVDTALKQLGQIREYDRRLRGLEREVQHCSRVLTWMAEALSHSALLPPGAPPPPSPTGSKD
uniprot
proteins
function
FUNCTION: Calcium-activated selective cation channel that mediates membrane depolarization. While it is activated by increase in intracellular Ca(2+), it is impermeable to it. Mediates transport of monovalent cations (Na(+) > K(+) > Cs(+) > Li(+)), leading to depolarize the membrane (PubMed:17188667, PubMed:29211714). 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 Ca(2+) 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 Ca(2+) 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 (PubMed:18758465). Plays a role in keratinocyte differentiation (By similarity) (PubMed:18758465). {ECO:0000250|UniProtKB:Q8TD43, ECO:0000269|PubMed:17188667, ECO:0000269|PubMed:18758465, ECO:0000269|PubMed:29211714}.; FUNCTION: [Isoform 3]: Lacks channel activity. {ECO:0000269|Ref.3}.
uniprot
proteins
mass_dalton
135760
uniprot
proteins
mutagenesis
MUTAGEN 160; /note="H->A: Near loss of channel sensitivity to inhibition by ATP."; /evidence="ECO:0000269|PubMed:29211714"; MUTAGEN 214; /note="W->A: Decreases channel sensitivity to inhibition by ATP."; /evidence="ECO:0000269|PubMed:29211714"; MUTAGEN 228; /note="Y->A: Strongly decreases channel sensitivity to inhibition by ATP."; /evidence="ECO:0000269|PubMed:29211714"; MUTAGEN 973; /note="Q->D,N: Strongly decreased selectivity for monovalent cations and increased permeability for Ca(2+)."; /evidence="ECO:0000269|PubMed:29211714"; MUTAGEN 973; /note="Q->E: Decreased selectivity for monovalent cations and increased permeability for Ca(2+)."; /evidence="ECO:0000269|PubMed:29211714
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKC leads to increase the sensitivity to Ca(2+). {ECO:0000250|UniProtKB:Q8TD43}.; PTM: Sumoylated. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q8TD43}.
uniprot
proteins
protein_family
LTrpC subfamily
uniprot
proteins
protein_family
TRPM4 sub-subfamily
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
pubmed
12799367
uniprot
proteins
pubmed
12893253
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17188667
uniprot
proteins
pubmed
18758465
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
29211714
uniprot
proteins
sequence_length
1213
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12893253, ECO:0000269|PubMed:29211714}; Multi-pass membrane protein {ECO:0000269|PubMed:29211714}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8TD43}. Golgi apparatus {ECO:0000250|UniProtKB:Q8TD43}.
uniprot
proteins
transmembrane_region
TRANSMEM 779..799; /note="Helical"; /evidence="ECO:0000269|PubMed:29211714"; TRANSMEM 811..831; /note="Helical"; /evidence="ECO:0000269|PubMed:29211714"; TRANSMEM 860..880; /note="Helical"; /evidence="ECO:0000269|PubMed:29211714"; TRANSMEM 883..906; /note="Helical"; /evidence="ECO:0000269|PubMed:29211714"; TRANSMEM 927..947; /note="Helical"; /evidence="ECO:0000269|PubMed:29211714"; TRANSMEM 1016..1036; /note="Helical"; /evidence="ECO:0000269|PubMed:29211714
uniprot
proteins