TRPM8

TRPM8
Identifiers
Aliases	TRPM8, LTRPC6, TRPP8, transient receptor potential cation channel subfamily M member 8
External IDs	OMIM: 606678 MGI: 2181435 HomoloGene: 23433 GeneCards: TRPM8
Genetically Related Diseases
amyotrophic lateral sclerosis, migraine, ,
Targeted by Drug
(-)-menthol, 5-benzyloxytryptamine, anandamide, cannabidiol, clotrimazole, dronabinol, linoleic acid, NADA
Gene ontology Molecular function • protein homodimerization activity • ion channel activity • protein binding • calcium channel activity Cellular component • integral component of membrane • endoplasmic reticulum membrane • membrane • endoplasmic reticulum • membrane raft • external side of plasma membrane • plasma membrane Biological process • response to stimulus • sensory perception of temperature stimulus • cellular calcium ion homeostasis • cation transport • ion transport • protein homotrimerization • transport • response to cold • detection of temperature stimulus • protein homotetramerization • thermoception • calcium ion transport • response to temperature stimulus • transmembrane transport • calcium ion transmembrane transport Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	79054	171382
Ensembl	ENSG00000144481	ENSMUSG00000036251
UniProt	Q7Z2W7	Q8R4D5
RefSeq (mRNA)	NM_024080	NM_134252
RefSeq (protein)	NP_076985	NP_599013.1
Location (UCSC)	Chr 2: 233.92 – 234.02 Mb	Chr 1: 88.28 – 88.39 Mb
PubMed search

79054

171382

ENSG00000144481

ENSMUSG00000036251

Q7Z2W7

Q8R4D5

NM_024080

NM_134252

NP_076985

NP_599013.1

Transient receptor potential cation channel subfamily M member 8 (TRPM8), also known as the cold and menthol receptor 1 (CMR1), is a protein that in humans is encoded by the TRPM8 gene. The TRPM8 channel is the primary molecular transducer of cold somatosensation in humans.

The TRPM8 channel is a homotetramer, composed of four identical subunits with a transmembrane domain with six helices (S1-S6). The first four, S1-S4, act as the voltage sensor and allow binding of menthol, icilin and similar channel agonists. S5 and S6 and a connecting loop, also part of the structure, make up the pore, a non-selective cation channel which consists of a highly conserved hydrophobic region, A range of diverse components are required for the high level of specificity in responding to result in ion flow to cold and menthol stimuli.

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Wikipedia