TRPM8
entrez
79054
canonical
uniprot
Q7Z2W7
canonical
ensembl
ENSG00000144481
resolver
ensp
ENSP00000323926
resolver
ensp
ENSP00000347956
resolver
ensp
ENSP00000386771
resolver
ensp
ENSP00000414198
resolver
ensp
ENSP00000766282
resolver
enst
ENST00000355722
resolver
genesymbol
TRPM8
resolver
genesymbol_syn
LTRPC6
resolver
genesymbol_syn
TRPP8
resolver
hgnc
HGNC:17961
resolver
uniprot
A0A0C4DFT0
resolver
uniprot
A0A1L1Z822
resolver
uniprot
A0A1L1Z836
resolver
uniprot
A0A1L1Z853
resolver
uniprot
A0A1L1Z856
resolver
uniprot
A0A1L1Z857
resolver
uniprot
A0A1L1Z860
resolver
uniprot
A0A1L1Z866
resolver
uniprot
A0A1L1Z878
resolver
uniprot
A0AVG2
resolver
uniprot
Q3YFM7
resolver
uniprot
Q6QNH9
resolver
uniprot
Q8TAC3
resolver
uniprot
Q8TDX8
resolver
uniprot
Q9BVK1
resolver
uniprot
W8DTH1
resolver
uniprot_entry
A0A0C4DFT0_HUMAN
resolver
uniprot_entry
A0A1L1Z822_HUMAN
resolver
uniprot_entry
A0A1L1Z836_HUMAN
resolver
uniprot_entry
A0A1L1Z853_HUMAN
resolver
uniprot_entry
A0A1L1Z856_HUMAN
resolver
uniprot_entry
A0A1L1Z857_HUMAN
resolver
uniprot_entry
A0A1L1Z860_HUMAN
resolver
uniprot_entry
A0A1L1Z866_HUMAN
resolver
uniprot_entry
A0A1L1Z878_HUMAN
resolver
uniprot_entry
TRPM8_HUMAN
resolver
uniprot_entry
W8DTH1_HUMAN
resolver
uniprot_sec
A0AVG2
resolver
uniprot_sec
Q3YFM7
resolver
uniprot_sec
Q6QNH9
resolver
uniprot_sec
Q8TAC3
resolver
uniprot_sec
Q8TDX8
resolver
uniprot_sec
Q9BVK1
resolver
activity_regulation
ACTIVITY REGULATION: Activated by cold temperatures and by both natural and synthetic cooling compounds such as menthol and icilin (PubMed:15306801, PubMed:16174775). Activation of the channel requires the presence of PI(4,5)P2. PI(4,5)P2 regulates the activation and desensitization of TRPM8 channels (PubMed:15852009). Activated by intracellular Ca(2+) (PubMed:15852009). {ECO:0000269|PubMed:15306801, ECO:0000269|PubMed:15852009, ECO:0000269|PubMed:16174775}.
uniprot
proteins
amino_acid_sequence
MSFRAARLSMRNRRNDTLDSTRTLYSSASRSTDLSYSESDLVNFIQANFKKRECVFFTKDSKATENVCKCGYAQSQHMEGTQINQSEKWNYKKHTKEFPTDAFGDIQFETLGKKGKYIRLSCDTDAEILYELLTQHWHLKTPNLVISVTGGAKNFALKPRMRKIFSRLIYIAQSKGAWILTGGTHYGLMKYIGEVVRDNTISRSSEENIVAIGIAAWGMVSNRDTLIRNCDAEGYFLAQYLMDDFTRDPLYILDNNHTHLLLVDNGCHGHPTVEAKLRNQLEKYISERTIQDSNYGGKIPIVCFAQGGGKETLKAINTSIKNKIPCVVVEGSGQIADVIASLVEVEDALTSSAVKEKLVRFLPRTVSRLPEEETESWIKWLKEILECSHLLTVIKMEEAGDEIVSNAISYALYKAFSTSEQDKDNWNGQLKLLLEWNQLDLANDEIFTNDRRWESADLQEVMFTALIKDRPKFVRLFLENGLNLRKFLTHDVLTELFSNHFSTLVYRNLQIAKNSYNDALLTFVWKLVANFRRGFRKEDRNGRDEMDIELHDVSPITRHPLQALFIWAILQNKKELSKVIWEQTRGCTLAALGASKLLKTLAKVKNDINAAGESEELANEYETRAVELFTECYSSDEDLAEQLLVYSCEAWGGSNCLELAVEATDQHFIAQPGVQNFLSKQWYGEISRDTKNWKIILCLFIIPLVGCGFVSFRKKPVDKHKKLLWYYVAFFTSPFVVFSWNVVFYIAFLLLFAYVLLMDFHSVPHPPELVLYSLVFVLFCDEVRQWYVNGVNYFTDLWNVMDTLGLFYFIAGIVFRLHSSNKSSLYSGRVIFCLDYIIFTLRLIHIFTVSRNLGPKIIMLQRMLIDVFFFLFLFAVWMVAFGVARQGILRQNEQRWRWIFRSVIYEPYLAMFGQVPSDVDGTTYDFAHCTFTGNESKPLCVELDEHNLPRFPEWITIPLVCIYMLSTNILLVNLLVAMFGYTVGTVQENNDQVWKFQRYFLVQEYCSRLNIPFPFIVFAYFYMVVKKCFKCCCKEKNMESSVCCFKNEDNETLAWEGVMKENYLVKINTKANDTSEEMRHRFRQLDTKLNDLKGLLKEIANKIK
uniprot
proteins
function
FUNCTION: Non-selective ion channel permeable to monovalent and divalent cations, including Na(+), K(+), and Ca(2+), with higher permeability for Ca(2+). Activated by multiple factors, such as temperature, voltage, pressure, and changes in osmolality. Activated by cool temperatures (<23-28 degrees Celsius) and by chemical ligands evoking a sensation of coolness, such as menthol and icilin therefore plays a central role in the detection of environmental cold temperatures (PubMed:15306801, PubMed:15852009, PubMed:16174775, PubMed:25559186, PubMed:37857704). TRPM8 is a voltage-dependent channel; its activation by cold or chemical ligands shifts its voltage thresholds towards physiological membrane potentials, leading to the opening of the channel (PubMed:15306801). In addition to its critical role in temperature sensing, regulates basal tear secretion by sensing evaporation-induced cooling and changes in osmolality (By similarity). May play a role in prostate cancer cell migration (PubMed:16174775, PubMed:25559186). {ECO:0000250|UniProtKB:Q8R4D5, ECO:0000269|PubMed:15306801, ECO:0000269|PubMed:15852009, ECO:0000269|PubMed:16174775, ECO:0000269|PubMed:25559186, ECO:0000269|PubMed:37857704}.; FUNCTION: [Isoform 2]: Negatively regulates menthol- and cold-induced channel activity by stabilizing the closed state of the channel. {ECO:0000269|PubMed:22128173}.; FUNCTION: [Isoform 3]: Negatively regulates menthol- and cold-induced channel activity by stabilizing the closed state of the channel. {ECO:0000269|PubMed:22128173}.
uniprot
proteins
mass_dalton
127685
uniprot
proteins
mutagenesis
MUTAGEN 745; /note="Y->A: Abolishes ion channel activity to cold stimulis."; /evidence="ECO:0000269|PubMed:37857704"; MUTAGEN 746; /note="I->A: Does not affect ion channel activity to cold stimulis."; /evidence="ECO:0000269|PubMed:37857704"; MUTAGEN 799; /note="N->A: Abolishes ion channel activity activation by icilin. Does not affect ion channel activity activation by menthol or cooling agent-10."; /evidence="ECO:0000269|PubMed:37857704"; MUTAGEN 802; /note="D->A: Decreases ion channel sensitivity to cold stimulis."; /evidence="ECO:0000269|PubMed:37857704"; MUTAGEN 821; /note="N->Q: No effect on glycosylation or ability to form functional channels."; /evidence="ECO:0000269|PubMed:17065148"; MUTAGEN 934; /note="N->Q: Abolishes glycosylation."; /evidence="ECO:0000269|PubMed:17065148"; MUTAGEN 946; /note="H->N: No effect on glycosylation or channel activity."; /evidence="ECO:0000269|PubMed:17065148"; MUTAGEN 995; /note="K->Q: Decreases in sensitivity to PI(4,5)P2."; /evidence="ECO:0000269|PubMed:15852009"; MUTAGEN 998; /note="R->Q: Decreases in sensitivity to PI(4,5)P2. Insensitive to icilin."; /evidence="ECO:0000269|PubMed:15852009"; MUTAGEN 1008; /note="R->Q: Decreases in sensitivity to PI(4,5)P2. Reduced the sensitivity of the channel to menthol stimulation. Insensitive to icilin."; /evidence="ECO:0000269|PubMed:15852009"; MUTAGEN 1089; /note="L->P: Abolishes multimerization and channel activity. Reduces cell surface expression."; /evidence="ECO:0000269|PubMed:17065148
uniprot
proteins
protein_family
LTrpC subfamily
uniprot
proteins
protein_family
TRPM8 sub-subfamily
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
pubmed
11325849
uniprot
proteins
pubmed
12858355
uniprot
proteins
pubmed
15306801
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15852009
uniprot
proteins
pubmed
16174775
uniprot
proteins
pubmed
17065148
uniprot
proteins
pubmed
22128173
uniprot
proteins
pubmed
25559186
uniprot
proteins
pubmed
37857704
uniprot
proteins
sequence_length
1104
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16174775}; Multi-pass membrane protein {ECO:0000269|PubMed:37857704}. Membrane raft {ECO:0000250|UniProtKB:Q8R4D5}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11325849, ECO:0000269|PubMed:16174775}. Note=Lipid raft association modulates TRPM8 channel activity (By similarity). Located in the endoplasmic reticulum in prostate cancer cells (PubMed:11325849, PubMed:16174775). {ECO:0000250|UniProtKB:Q8R4D5, ECO:0000269|PubMed:11325849, ECO:0000269|PubMed:16174775}.
uniprot
proteins
transmembrane_region
TRANSMEM 734..758; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:37857704, ECO:0007744|PDB:8BDC"; TRANSMEM 766..789; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:37857704, ECO:0007744|PDB:8BDC"; TRANSMEM 797..817; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:37857704, ECO:0007744|PDB:8BDC"; TRANSMEM 823..848; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:37857704, ECO:0007744|PDB:8BDC"; TRANSMEM 854..890; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:37857704, ECO:0007744|PDB:8BDC"; TRANSMEM 955..983; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:37857704, ECO:0007744|PDB:8BDC
uniprot
proteins