Trpm2
entrez
28240
canonical
uniprot
Q91YD4
canonical
ensembl
ENSMUSG00000009292
resolver
ensp
ENSMUSP00000101040
resolver
ensp
ENSMUSP00000254672
resolver
enst
ENSMUST00000105401
resolver
genesymbol
Trpm2
resolver
genesymbol_syn
Ltrpc2
resolver
genesymbol_syn
Trpc7
resolver
uniprot
Q3UYE9
resolver
uniprot
Q5KTC0
resolver
uniprot_entry
Q3UYE9_MOUSE
resolver
uniprot_entry
TRPM2_MOUSE
resolver
uniprot_sec
Q5KTC0
resolver
activity_regulation
ACTIVITY REGULATION: Activated by intracellular ADP-ribose, beta-NAD (NAD(+)) and similar compounds, and by oxidative stress caused by reactive oxygen or nitrogen species (PubMed:19454650, PubMed:21753080, PubMed:22493272). Ca(2+) and PI(4,5)P2 are required for channel opening by ADP-ribose (By similarity). Activated by moderate heat (35 to 40 degrees Celsius) (PubMed:27533035, PubMed:27562954). Activation by ADP-ribose and beta-NAD is strongly increased by moderate heat (35 to 40 degrees Celsius). Likewise, reactive oxygen species lower the threshold for activation by moderate heat (37 degrees Celsius) (PubMed:22493272, PubMed:25817999). Inactivated by exposure to extracellular pH between 4.0 and 6.5; irreversibly inactivated when open channels are exposed to extracellular pH between 4.0 and 6.5, while pre-exposure of closed channels to extracellular pH 5.5 gives rise to currents that rapidly inactivate, but protects against irreversible inactivation. Inactivated by intracellular ATP. Activated by arachidonic acid. Inhibited by 2-aminoethyl diphenylborinate (2-APB) (By similarity). {ECO:0000250|UniProtKB:O94759, ECO:0000269|PubMed:19454650, ECO:0000269|PubMed:21753080, ECO:0000269|PubMed:22493272, ECO:0000269|PubMed:25817999, ECO:0000269|PubMed:27533035, ECO:0000269|PubMed:27562954}.
uniprot
proteins
amino_acid_sequence
MESLDRRRTGSEQEEGFGVQSRRATDLGMVPNLRRSNSSLCKSRRFLCSFSSEKQENLSSWIPENIKKKECVYFVESSKLSDAGKVVCACGYTHEQHLEVAIKPHTFQGKEWDPKKHVQEMPTDAFGDIVFTDLSQKVGKYVRVSQDTPSSVIYQLMTQHWGLDVPNLLISVTGGAKNFNMKLRLKSIFRRGLVKVAQTTGAWIITGGSHTGVMKQVGEAVRDFSLSSSCKEGEVITIGVATWGTIHNREGLIHPMGGFPAEYMLDEEGQGNLTCLDSNHSHFILVDDGTHGQYGVEIPLRTKLEKFISEQTKERGGVAIKIPIVCVVLEGGPGTLHTIYNAINNGTPCVIVEGSGRVADVIAQVATLPVSEITISLIQQKLSIFFQEMFETFTENQIVEWTKKIQDIVRRRQLLTIFREGKDGQQDVDVAILQALLKASRSQDHFGHENWDHQLKLAVAWNRVDIARSEIFTDEWQWKPADLHPMMTAALISNKPEFVRLFLENGVRLKEFVTWDTLLCLYENLEPSCLFHSKLQKVLAEEQRLAYASATPRLHMHHVAQVLRELLGDSTQLLYPRPRYTDRPRLSMTVPHIKLNVQGVSLRSLYKRSTGHVTFTIDPVRDLLIWAVIQNHRELAGIIWAQSQDCTAAALACSKILKELSKEEEDTDSSEEMLALADEFEHRAIGVFTECYRKDEERAQKLLVRVSEAWGKTTCLQLALEAKDMKFVSHGGIQAFLTKVWWGQLCVDNGLWRIILCMLAFPLLFTGFISFREKRLQALCRPARVRAFFNAPVVIFHMNILSYFAFLCLFAYVLMVDFQPSPSWCEYLIYLWLFSLVCEETRQLFYDPDGCGLMKMASLYFSDFWNKLDVGAILLFIVGLTCRLIPATLYPGRIILSLDFIMFCLRLMHIFTISKTLGPKIIIVKRMMKDVFFFLFLLAVWVVSFGVAKQAILIHNESRVDWIFRGVVYHSYLTIFGQIPTYIDGVNFSMDQCSPNGTDPYKPKCPESDWTGQAPAFPEWLTVTLLCLYLLFANILLLNLLIAMFNYTFQEVQEHTDQIWKFQRHDLIEEYHGRPPAPPPLILLSHLQLLIKRIVLKIPAKRHKQLKNKLEKNEETALLSWELYLKENYLQNQQYQQKQRPEQKIQDISEKVDTMVDLLDMDQVKRSGSTEQRLASLEEQVTQVTRALHWIVTTLKDSGFGSGAGALTLAPQRAFDEPDAELSIRRKVEEPGDGYHVSARHLLYPNARIMRFPVPNEKVPWAAEFLIYDPPFYTAEKDVALTDPVGDTAEPLSKISYNVVDGPTDRRSFHGVYVVEYGFPLNPMGRTGLRGRGSLSWFGPNHTLQPVVTRWKRNQGGAICRKSVRKMLEVLVMKLPRSEHWALPGGSREPGEMLPRKLKRVLRQEFWVAFETLLMQGTEVYKGYVDDPRNTDNAWIETVAVSIHFQDQNDMELKRLEENLHTHDPKELTRDLKLSTEWQVVDRRIPLYANHKTILQKVASLFGAHF
uniprot
proteins
function
FUNCTION: Nonselective, voltage-independent cation channel that mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels (PubMed:11804595, PubMed:19454650, PubMed:21753080, PubMed:22493272). Functions as a ligand-gated ion channel, gated by intracellular adenosine diphosphate ribose (ADP-ribose), Ca(2+), warm temperature, and oxidative stress. The precise physiological activators are under debate; the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate (By similarity). Binding of ADP-ribose to the cytoplasmic Nudix domain causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening. Extracellular Ca(2+) passes through the channel and increases channel activity (By similarity). Also contributes to Ca(2+) release from intracellular stores in response to ADP-ribose (PubMed:21753080). Plays a role in numerous processes that involve signaling via intracellular Ca(2+) levels (PubMed:21753080). Besides, mediates the release of lysosomal Zn(2+) stores in response to reactive oxygen species, leading to increased cytosolic Zn(2+) levels (By similarity). Plays a role in mediating behavorial and physiological responses to moderate heat and thereby contributes to body temperature homeostasis (PubMed:27533035, PubMed:27562954). Plays a role in insulin secretion, a process that requires increased cytoplasmic Ca(2+) levels (PubMed:20921208, PubMed:25817999). Required for normal IFNG and cytokine secretion and normal innate immune immunity in response to bacterial infection (PubMed:21709234). Required for normal phagocytosis and cytokine release by macrophages exposed to zymosan (in vitro) (PubMed:22493272). Plays a role in dendritic cell differentiation and maturation, and in dendritic cell chemotaxis via its role in regulating cytoplasmic Ca(2+) levels (PubMed:21753080). Plays a role in the regulation of the reorganization of the actin cytoskeleton and filopodia formation in response to reactive oxygen species via its function in increasing cytoplasmic Ca(2+) and Zn(2+) levels (By similarity). Confers susceptibility to cell death following oxidative stress (PubMed:25562606). {ECO:0000250|UniProtKB:O94759, ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:19454650, ECO:0000269|PubMed:21753080, ECO:0000269|PubMed:22493272, ECO:0000269|PubMed:25562606, ECO:0000269|PubMed:25817999, ECO:0000269|PubMed:27533035, ECO:0000269|PubMed:27562954}.
uniprot
proteins
mass_dalton
172202
uniprot
proteins
mutagenesis
MUTAGEN 214; /note="M->A: Abolishes lowering of temperature threshold for activation in response to reactive oxygen species."; /evidence="ECO:0000269|PubMed:22493272
uniprot
proteins
post_translational_modification
PTM: Protein kinase C (PKC)-mediated phosphorylation of TRPM2 at Thr-738 counteracts the effect of cytosolic Ca(2+) and elevates the temperature threshold. {ECO:0000269|PubMed:36042566}.
uniprot
proteins
protein_family
LTrpC subfamily
uniprot
proteins
protein_family
TRPM2 sub-subfamily
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
pubmed
11804595
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15708008
uniprot
proteins
pubmed
16260005
uniprot
proteins
pubmed
16601673
uniprot
proteins
pubmed
19454650
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20921208
uniprot
proteins
pubmed
21709234
uniprot
proteins
pubmed
21753080
uniprot
proteins
pubmed
22493272
uniprot
proteins
pubmed
25562606
uniprot
proteins
pubmed
25817999
uniprot
proteins
pubmed
27533035
uniprot
proteins
pubmed
27562954
uniprot
proteins
pubmed
36042566
uniprot
proteins
sequence_length
1506
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:19454650, ECO:0000269|PubMed:21753080, ECO:0000269|PubMed:22493272}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O94759}. Perikaryon {ECO:0000250|UniProtKB:E9PTA2}. Cell projection {ECO:0000250|UniProtKB:E9PTA2}. Cytoplasmic vesicle {ECO:0000269|PubMed:21753080}. Lysosome {ECO:0000269|PubMed:21753080}. Note=Detected at the cell membrane and in intracellular vesicles in cortical neurons. Detected on neuronal cell bodies and neurites (By similarity). Detected on the cell membrane in polymorphonuclear neutrophils (PubMed:21753080). Detected on cytoplasmic vesicles and lysosomes in immature bone marrow dendritic cells (PubMed:21753080). {ECO:0000250|UniProtKB:E9PTA2, ECO:0000269|PubMed:21753080}.
uniprot
proteins
transmembrane_region
TRANSMEM 793..813; /note="Helical"; /evidence="ECO:0000250|UniProtKB:O94759"; TRANSMEM 825..845; /note="Helical"; /evidence="ECO:0000250|UniProtKB:O94759"; TRANSMEM 865..885; /note="Helical"; /evidence="ECO:0000250|UniProtKB:O94759"; TRANSMEM 894..914; /note="Helical"; /evidence="ECO:0000250|UniProtKB:O94759"; TRANSMEM 927..947; /note="Helical"; /evidence="ECO:0000250|UniProtKB:O94759"; TRANSMEM 1020..1041; /note="Helical"; /evidence="ECO:0000250|UniProtKB:O94759
uniprot
proteins