Trpm5
entrez
56843
canonical
uniprot
Q9JJH7
canonical
ensembl
ENSMUSG00000009246
resolver
ensp
ENSMUSP00000009390
resolver
ensp
ENSMUSP00000114302
resolver
genesymbol
Trpm5
resolver
genesymbol_syn
Ltrpc5
resolver
genesymbol_syn
Mtr1
resolver
uniprot
A3KN89
resolver
uniprot
Q3TU14
resolver
uniprot
Q7TPL4
resolver
uniprot
Q99NF9
resolver
uniprot
Q9EPM3
resolver
uniprot
Q9EPM4
resolver
uniprot_entry
TRPM5_MOUSE
resolver
uniprot_sec
A3KN89
resolver
uniprot_sec
Q3TU14
resolver
uniprot_sec
Q7TPL4
resolver
uniprot_sec
Q99NF9
resolver
uniprot_sec
Q9EPM3
resolver
uniprot_sec
Q9EPM4
resolver
activity_regulation
ACTIVITY REGULATION: Ca(2+)-activated cation channel (PubMed:12842017, PubMed:14657398, PubMed:17522321). Displays voltage dependence modulation (PubMed:12842017). Regulated by PI(4,5)P2 levels. PI(4,5)P 2 reverses the Ca(2+) -induced desensitization of channels (PubMed:14657398, PubMed:17522321). Inhibited by flufenamic acid with an IC(50) of 24.5 uM and spermine with an IC(50) of 37 uM (PubMed:15670874). Is a highly temperature-sensitive, heat activated channel showing a steep increase of inward currents at temperatures between 15 and 35 degrees Celsius. Heat activation is due to a shift of the voltage-dependent activation curve to negative potentials (PubMed:16355226). The channel is blocked by extracellular acidification (PubMed:15731110). {ECO:0000269|PubMed:12842017, ECO:0000269|PubMed:14657398, ECO:0000269|PubMed:15670874, ECO:0000269|PubMed:15731110, ECO:0000269|PubMed:16355226, ECO:0000269|PubMed:17522321}.
uniprot
proteins
amino_acid_sequence
MQTTQSSCPGSPPDTEDGWEPILCRGEINFGGSGKKRGKFVKVPSSVAPSVLFELLLTEWHLPAPNLVVSLVGEERPLAMKSWLRDVLRKGLVKAAQSTGAWILTSALHVGLARHVGQAVRDHSLASTSTKIRVVAIGMASLDRILHRQLLDGVHQKEDTPIHYPADEGNIQGPLCPLDSNLSHFILVESGALGSGNDGLTELQLSLEKHISQQRTGYGGTSCIQIPVLCLLVNGDPNTLERISRAVEQAAPWLILAGSGGIADVLAALVSQPHLLVPQVAEKQFREKFPSECFSWEAIVHWTELLQNIAAHPHLLTVYDFEQEGSEDLDTVILKALVKACKSHSQEAQDYLDELKLAVAWDRVDIAKSEIFNGDVEWKSCDLEEVMTDALVSNKPDFVRLFVDSGADMAEFLTYGRLQQLYHSVSPKSLLFELLQRKHEEGRLTLAGLGAQQARELPIGLPAFSLHEVSRVLKDFLHDACRGFYQDGRRMEERGPPKRPAGQKWLPDLSRKSEDPWRDLFLWAVLQNRYEMATYFWAMGREGVAAALAACKIIKEMSHLEKEAEVARTMREAKYEQLALDLFSECYGNSEDRAFALLVRRNHSWSRTTCLHLATEADAKAFFAHDGVQAFLTKIWWGDMATGTPILRLLGAFTCPALIYTNLISFSEDAPQRMDLEDLQEPDSLDMEKSFLCSRGGQLEKLTEAPRAPGDLGPQAAFLLTRWRKFWGAPVTVFLGNVVMYFAFLFLFTYVLLVDFRPPPQGPSGSEVTLYFWVFTLVLEEIRQGFFTDEDTHLVKKFTLYVEDNWNKCDMVAIFLFIVGVTCRMVPSVFEAGRTVLAIDFMVFTLRLIHIFAIHKQLGPKIIIVERMMKDVFFFLFFLSVWLVAYGVTTQALLHPHDGRLEWIFRRVLYRPYLQIFGQIPLDEIDEARVNCSLHPLLLESSASCPNLYANWLVILLLVTFLLVTNVLLMNLLIAMFSYTFQVVQGNADMFWKFQRYHLIVEYHGRPALAPPFILLSHLSLVLKQVFRKEAQHKRQHLERDLPDPLDQKIITWETVQKENFLSTMEKRRRDSEGEVLRKTAHRVDLIAKYIGGLREQEKRIKCLESQANYCMLLLSSMTDTLAPGGTYSSSQNCGCRSQPASARDREYLESGLPPSDT
uniprot
proteins
function
FUNCTION: Monovalent cation-selective ion channel activated by intracellular Ca(2+) in a voltage- and temperature-dependent manner (PubMed:12842017, PubMed:14657398, PubMed:17522321, PubMed:38538847). Mediates the transport of Na(+), K(+) and Cs(+) ions equally well (PubMed:12842017). Activated directly by increase in intracellular Ca(2+), but is impermeable to it (PubMed:12842017). The activation mechanism of TRPM5 involves a multistep process. TRPM5 activation involves ligand binding (i.e., tastant molecule, glucose stimulation) to Gq/G protein-coupled receptors (GPCR) and leads to the breakdown of phosphatidylinositol bisphosphate (PIP2) into diacylglycerol (DAG) and inositol trisphosphate (IP3), IP3 binds to its receptors in the endoplasmic reticulum and cause Ca(2+) release. Simultaneously with the intracellular Ca(2+) release, DAG activates the protein kinase C (PKC), which phosphorylates the TRPM5 channel. This phosphorylation combined with the bound Ca(2+), leads to a robust inward current allowing the entry of sodium ions (Na+) into the cell. This ion influx depolarizes the cell membrane, generating action potentials that propagate TRPM5 signals. Is a key player in sensing sweet, umami and bitter stimuli (Probable) (PubMed:16436689, PubMed:16935556). May also be involved in sensing semiochemicals (PubMed:17267604). Involved in insulin secretion by pancreatic beta cells (PubMed:20194741, PubMed:20393858). {ECO:0000269|PubMed:12842017, ECO:0000269|PubMed:14657398, ECO:0000269|PubMed:16436689, ECO:0000269|PubMed:16935556, ECO:0000269|PubMed:17267604, ECO:0000269|PubMed:17522321, ECO:0000269|PubMed:20194741, ECO:0000269|PubMed:20393858, ECO:0000269|PubMed:38538847, ECO:0000305|PubMed:15731110, ECO:0000305|PubMed:16355226}.
uniprot
proteins
mass_dalton
130844
uniprot
proteins
mutagenesis
MUTAGEN 129; /note="S->A: Abolishes the Gq-dependent modulation of TRPM5."; /evidence="ECO:0000269|PubMed:38538847"; MUTAGEN 129; /note="S->D: Increases of the Ca(2+)-evoked TRPM5 current in both positive and negative voltages; mimicking the PKC-dependent phosphorylated form of TRPM5."; /evidence="ECO:0000269|PubMed:38538847"; MUTAGEN 129; /note="S->E: Does not change the Ca(2+)-evoked current of TRPM5."; /evidence="ECO:0000269|PubMed:38538847"; MUTAGEN 831; /note="E->Q: Reduces sensitivity to block by extracellular acidification. Sensitivity to block by low extracellular pH is nearly abolished; when associated with N-935."; /evidence="ECO:0000269|PubMed:15731110"; MUTAGEN 897; /note="H->N: Shows normal sensitivity to acid block and significant recovery from acid-enhanced inactivation."; /evidence="ECO:0000269|PubMed:15731110"; MUTAGEN 935; /note="H->N: Reduces sensitivity to block by extracellular acidification. Sensitivity to block by low extracellular pH is nearly abolished; when associated with Q-831."; /evidence="ECO:0000269|PubMed:15731110
uniprot
proteins
post_translational_modification
PTM: Multiple phosphorylation sites regulate the Gq/ TRPM5 modulation axis, with the Ser-129 playing a substantial role in this positive modulation. {ECO:0000269|PubMed:38538847}.
uniprot
proteins
protein_family
LTrpC subfamily
uniprot
proteins
protein_family
TRPM5 sub-subfamily
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
pubmed
10903843
uniprot
proteins
pubmed
10907850
uniprot
proteins
pubmed
10915772
uniprot
proteins
pubmed
12368808
uniprot
proteins
pubmed
12842017
uniprot
proteins
pubmed
14657398
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15670874
uniprot
proteins
pubmed
15731110
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16355226
uniprot
proteins
pubmed
16436689
uniprot
proteins
pubmed
16935556
uniprot
proteins
pubmed
17267604
uniprot
proteins
pubmed
17522321
uniprot
proteins
pubmed
17610722
uniprot
proteins
pubmed
20194741
uniprot
proteins
pubmed
20393858
uniprot
proteins
pubmed
38538847
uniprot
proteins
sequence_length
1158
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TD43}.
uniprot
proteins
transmembrane_region
TRANSMEM 730..754; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:S5UH55"; TRANSMEM 765..784; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:S5UH55"; TRANSMEM 806..824; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:S5UH55"; TRANSMEM 832..854; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:S5UH55"; TRANSMEM 864..893; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:S5UH55"; TRANSMEM 951..985; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:S5UH55
uniprot
proteins