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Protein

Transient receptor potential cation channel subfamily M member 8

Gene

Trpm8

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor-activated non-selective cation channel involved in detection of sensations such as coolness, by being activated by cold temperature below 25 degrees Celsius. Activated by icilin, eucalyptol, menthol, cold and modulation of intracellular pH. Involved in menthol sensation. Permeable for monovalent cations sodium, potassium, and cesium and divalent cation calcium. Temperature sensing is tightly linked to voltage-dependent gating. Activated upon depolarization, changes in temperature resulting in graded shifts of its voltage-dependent activation curves. The chemical agonists menthol functions as a gating modifier, shifting activation curves towards physiological membrane potentials. Temperature sensitivity arises from a tenfold difference in the activation energies associated with voltage-dependent opening and closing.1 Publication

GO - Molecular functioni

  • calcium channel activity Source: Ensembl
  • ion channel activity Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Sensory transduction, Transport

Enzyme and pathway databases

ReactomeiR-RNO-3295583. TRP channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily M member 8
Alternative name(s):
Cold menthol receptor 1
Gene namesi
Name:Trpm8
Synonyms:Cmr1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi620762. Trpm8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 691691CytoplasmicSequence analysisAdd
BLAST
Transmembranei692 – 71221Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini713 – 73422ExtracellularSequence analysisAdd
BLAST
Transmembranei735 – 75521Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini756 – 7594CytoplasmicSequence analysis
Transmembranei760 – 78021Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini781 – 79313ExtracellularSequence analysisAdd
BLAST
Transmembranei794 – 81421Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini815 – 82915CytoplasmicSequence analysisAdd
BLAST
Transmembranei830 – 85021Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini851 – 958108ExtracellularSequence analysisAdd
BLAST
Transmembranei959 – 97921Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini980 – 1104125CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL5011.
GuidetoPHARMACOLOGYi500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11041104Transient receptor potential cation channel subfamily M member 8PRO_0000215335Add
BLAST

Proteomic databases

PaxDbiQ8R455.
PRIDEiQ8R455.

Expressioni

Tissue specificityi

Expressed in dorsal root and trigeminal ganglia. Specifically expressed in a subset of sensory neurons, including cold-sensitive neurons in trigeminal neurons.2 Publications

Gene expression databases

GenevisibleiQ8R455. RN.

Interactioni

Subunit structurei

Interacts (via N-terminus and C-terminus domains) with TCAF1; the interaction stimulates TRPM8 channel activity. Interacts (via N-terminus and C-terminus domains) with TCAF2; the interaction inhibits TRPM8 channel activity (By similarity). Homotetramer.By similarity1 Publication

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025879.

Chemistry

BindingDBiQ8R455.

Structurei

3D structure databases

ProteinModelPortaliQ8R455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1067 – 110438Sequence analysisAdd
BLAST

Domaini

The coiled coil region is required for multimerization.By similarity

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410KCTC. Eukaryota.
ENOG4110YBY. LUCA.
GeneTreeiENSGT00760000119127.
HOGENOMiHOG000236350.
HOVERGENiHBG100888.
InParanoidiQ8R455.
KOiK04983.
OMAiYIMDDFT.
OrthoDBiEOG725DH1.
PhylomeDBiQ8R455.
TreeFamiTF314204.

Family and domain databases

InterProiIPR029603. TRPM8.
[Graphical view]
PANTHERiPTHR13800:SF9. PTHR13800:SF9. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8R455-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFEGARLSM RSRRNGTLGS TRTLYSSVSR STDVSYSESD LVNFIQANFK
60 70 80 90 100
KRECVFFTRD SKAMESICKC GYAQSQHIEG TQINQNEKWN YKKHTKEFPT
110 120 130 140 150
DAFGDIQFET LGKKGKYLRL SCDTDSETLY ELLTQHWHLK TPNLVISVTG
160 170 180 190 200
GAKNFALKPR MRKIFSRLIY IAQSKGAWIL TGGTHYGLMK YIGEVVRDNT
210 220 230 240 250
ISRNSEENIV AIGIAAWGMV SNRDTLIRNC DDEGHFSAQY IMDDFMRDPL
260 270 280 290 300
YILDNNHTHL LLVDNGCHGH PTVEAKLRNQ LEKYISERTS QDSNYGGKIP
310 320 330 340 350
IVCFAQGGGR ETLKAINTSV KSKIPCVVVE GSGQIADVIA SLVEVEDVLT
360 370 380 390 400
SSMVKEKLVR FLPRTVSRLP EEEIESWIKW LKEILESPHL LTVIKMEEAG
410 420 430 440 450
DEVVSSAISY ALYKAFSTNE QDKDNWNGQL KLLLEWNQLD LASDEIFTND
460 470 480 490 500
RRWESADLQE VMFTALIKDR PKFVRLFLEN GLNLQKFLTN EVLTELFSTH
510 520 530 540 550
FSTLVYRNLQ IAKNSYNDAL LTFVWKLVAN FRRSFWKEDR SSREDLDVEL
560 570 580 590 600
HDASLTTRHP LQALFIWAIL QNKKELSKVI WEQTKGCTLA ALGASKLLKT
610 620 630 640 650
LAKVKNDINA AGESEELANE YETRAVELFT ECYSSDEDLA EQLLVYSCEA
660 670 680 690 700
WGGSNCLELA VEATDQHFIA QPGVQNFLSK QWYGEISRDT KNWKIILCLF
710 720 730 740 750
IIPLVGCGLV SFRKKPIDKH KKLLWYYVAF FTSPFVVFSW NVVFYIAFLL
760 770 780 790 800
LFAYVLLMDF HSVPHTPELI LYALVFVLFC DEVRQWYMNG VNYFTDLWNV
810 820 830 840 850
MDTLGLFYFI AGIVFRLHSS NKSSLYSGRV IFCLDYIIFT LRLIHIFTVS
860 870 880 890 900
RNLGPKIIML QRMLIDVFFF LFLFAVWMVA FGVARQGILR QNEQRWRWIF
910 920 930 940 950
RSVIYEPYLA MFGQVPSDVD STTYDFSHCT FSGNESKPLC VELDEYNLPR
960 970 980 990 1000
FPEWITIPLV CIYMLSTNIL LVNLLVAMFG YTVGIVQENN DQVWKFQRYF
1010 1020 1030 1040 1050
LVQEYCNRLN IPFPFVVFAY FYMVVKKCFK CCCKEKNTES SACCFRNEDN
1060 1070 1080 1090 1100
ETLAWEGVMK ENYLVKINTK ANDNAEEMRH RFRQLDTKLN DLKGLLKEIA

NKIK
Length:1,104
Mass (Da):127,629
Last modified:January 4, 2005 - v4
Checksum:iD07BFF14EB23970A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY072788 mRNA. Translation: AAL68394.2.
RefSeqiNP_599198.2. NM_134371.2.
XP_008765414.1. XM_008767192.1.
UniGeneiRn.81225.

Genome annotation databases

EnsembliENSRNOT00000025879; ENSRNOP00000025879; ENSRNOG00000019035.
GeneIDi171384.
KEGGirno:171384.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY072788 mRNA. Translation: AAL68394.2.
RefSeqiNP_599198.2. NM_134371.2.
XP_008765414.1. XM_008767192.1.
UniGeneiRn.81225.

3D structure databases

ProteinModelPortaliQ8R455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025879.

Chemistry

BindingDBiQ8R455.
ChEMBLiCHEMBL5011.
GuidetoPHARMACOLOGYi500.

Proteomic databases

PaxDbiQ8R455.
PRIDEiQ8R455.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000025879; ENSRNOP00000025879; ENSRNOG00000019035.
GeneIDi171384.
KEGGirno:171384.

Organism-specific databases

CTDi79054.
RGDi620762. Trpm8.

Phylogenomic databases

eggNOGiENOG410KCTC. Eukaryota.
ENOG4110YBY. LUCA.
GeneTreeiENSGT00760000119127.
HOGENOMiHOG000236350.
HOVERGENiHBG100888.
InParanoidiQ8R455.
KOiK04983.
OMAiYIMDDFT.
OrthoDBiEOG725DH1.
PhylomeDBiQ8R455.
TreeFamiTF314204.

Enzyme and pathway databases

ReactomeiR-RNO-3295583. TRP channels.

Miscellaneous databases

NextBioi622214.
PROiQ8R455.

Gene expression databases

GenevisibleiQ8R455. RN.

Family and domain databases

InterProiIPR029603. TRPM8.
[Graphical view]
PANTHERiPTHR13800:SF9. PTHR13800:SF9. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Identification of a cold receptor reveals a general role for TRP channels in thermosensation."
    McKemy D.D., Neuhausser W.M., Julius D.
    Nature 416:52-58(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Tissue: Trigeminal ganglion.
  2. McKemy D.D., Neuhausser W.M., Julius D.
    Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 449.
    Tissue: Trigeminal ganglion.
  3. "TRPM8 mRNA is expressed in a subset of cold-responsive trigeminal neurons from rat."
    Nealen M.L., Gold M.S., Thut P.D., Caterina M.J.
    J. Neurophysiol. 90:515-520(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  4. Cited for: SUBCELLULAR LOCATION.
  5. "AFM imaging reveals the tetrameric structure of the TRPM8 channel."
    Stewart A.P., Egressy K., Lim A., Edwardson J.M.
    Biochem. Biophys. Res. Commun. 394:383-386(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.

Entry informationi

Entry nameiTRPM8_RAT
AccessioniPrimary (citable) accession number: Q8R455
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: January 4, 2005
Last modified: November 11, 2015
This is version 90 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.