Trpa1
entrez
312896
canonical
uniprot
Q6RI86
canonical
ensembl
ENSRNOG00000007354
resolver
ensembl
ENSRNOG00055011060
resolver
ensembl
ENSRNOG00060001872
resolver
ensembl
ENSRNOG00065010758
resolver
ensp
ENSRNOP00000009874
resolver
ensp
ENSRNOP00055015102
resolver
ensp
ENSRNOP00060001899
resolver
ensp
ENSRNOP00065013360
resolver
enst
ENSRNOT00000009874
resolver
enst
ENSRNOT00055018742
resolver
enst
ENSRNOT00060002897
resolver
enst
ENSRNOT00065017425
resolver
genesymbol
Trpa1
resolver
genesymbol_syn
Anktm1
resolver
uniprot
F1LRH9
resolver
uniprot_entry
TRPA1_RAT
resolver
uniprot_sec
F1LRH9
resolver
activity_regulation
ACTIVITY REGULATION: Electrophilic ligands activate the channel by covalent modification of intracellular cysteines; Cys-622 plays a key role in covalent binding of electrophiles (By similarity). Extracellular Ca(2+) both potentiates and inactivates TRPA1; a rapid potentiation follows by slow desensitization (PubMed:18775987). Activated by increase in intracellular Ca(2+) concentration (By similarity). Inhibited by ruthenium red, a potent blocker of TRPV channels and selectively by A-967079 (PubMed:14712238, PubMed:21402443). Activated by benzyl isothiocyanate (BITC), iodoacetamide, sulfhydryl reactive agent MTSEA, N-methyl maleimide (NMM), N-ethylmaleimide (NEM), and 2-aminoethyldiphenylborinate (2-APB). Also activated by hyperoxia. Activated by intracellular Zn(2+). TRPA1 activation may critically depend on the presence of small intracellular compounds such as polyphosphates (By similarity). {ECO:0000250|UniProtKB:O75762, ECO:0000269|PubMed:14712238, ECO:0000269|PubMed:18775987, ECO:0000269|PubMed:21402443}.
uniprot
proteins
amino_acid_sequence
MKRSLRRVLRPEERKEVQGVVYRGVGEDMDCSKESFKVDIEGDMCRLEAFIKNRRKLSKYEDENLCLLHHAAAEGQVELMQLIINGSSCEALNVMDDYGNTPLHWAAEKNQVESVKFLLSQGANPNLRNRNMMAPLHIAVQGMYNEVIKVLTEHKATNINLEGENGNTALMSTCAKDNSEALQILLEKGAKLCKSNKWGDYPVHQAAFSGAKRCMELILAYGEKTGYSREAHINFVNHKKASPLHLAVQSGDLDMIKMCLDSGAHIDMMENAKCMALHFAATQGATDIVKLMISSYTGSSDIVNAVDGNQETLLHRASLFDHHDLADYLISVGADINSTDSEGRSPLILATASASWNIVNLLLSKGAKVDIKDHLGRNFLHLTVQQPYGLRNLRPEFLQMQHIKELVMDEDNDGCTPLHYACRQGAPVSVNNLLRFNVSVHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRLDEEGNTALHFAAREGHAKAVAMLLSYNADILLNKKQASFLHIALHNKRKEVVLTTIRSKRWDECLQVFTHDSPSNRCPIMEMVEYLPECMKVLLDFCMIPSTEDKSCQDYHIEYNFKYLQCPLSMTKKVTPTQDVIYEPLTILNVMVQHNRIELLNHPVCREYLLMKWCAYGFRAHMMNLGSYCLGLIPMTLLVVKIQPGMAFNSTGIINETISTHEERINTLNSFPLKICMILVFLSSIFGYCKEVVQIFQQKRNYFLDYNNALEWVIYTTSMIFVLPLFLDIPAYMQWQCGAIAIFFYWMNFLLYLQRFENCGIFIVMLEVIFKTLLRSTGVFIFLLLAFGLSFYVLLNFQDAFSTPLLSLIQTFSMMLGDINYRDAFLEPLFRNELAYPVLTFGQLIAFTMFVPIVLMNLLIGLAVGDIAEVQKHASLKRIAMQVELHTNLEKKLPFWYLRKVDQRSTIVYPNRPRHGRMLRFFHYFLSMQETRQEAPNIDTCLEMEILKQKYRLKDLTSLLEKQHELIKLIIQKMEIISETEDEDNHCSFQDRFKKERLEQMHSKWNFVLNAVKTKTHCSISHPDI
uniprot
proteins
function
FUNCTION: Ligand-activated Ca(2+)-permeable, nonselective cation channel (PubMed:14712238, PubMed:18775987). Involved in pain detection and possibly also in cold perception, oxygen concentration perception, cough, itch, and inner ear function (By similarity). Has a relatively high Ca(2+) selectivity, with a preference for divalent over monovalent cations (Ca(2+) > Ba(2+) > Mg(2+) > NH4(+) > Li(+) > K(+)), the influx of cation into the cytoplasm, leads to membrane depolarization. Has a central role in the pain response to endogenous inflammatory mediators, such as bradykinin and to a diverse array of irritants. Activated by a large variety of structurally unrelated electrophilic and non-electrophilic chemical compounds, such as allylthiocyanate (AITC) from mustard oil or wasabi, cinnamaldehyde, diallyl disulfide (DADS) from garlic, and acrolein, an environmental irritant. Electrophilic ligands activate TRPA1 by interacting with critical N-terminal Cys residues in a covalent manner. Non-electrophile agonists bind at distinct sites in the transmembrane domain to promote channel activation. Also acts as an ionotropic cannabinoid receptor by being activated by delta(9)-tetrahydrocannabinol (THC), the psychoactive component of marijuana. May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds (By similarity). {ECO:0000250|UniProtKB:O75762, ECO:0000250|UniProtKB:Q8BLA8, ECO:0000269|PubMed:14712238, ECO:0000269|PubMed:18775987}.
uniprot
proteins
mass_dalton
128603
uniprot
proteins
mutagenesis
MUTAGEN 918; /note="D->A: Ca(2+) permeability is greatly reduced."; /evidence="ECO:0000269|PubMed:18775987"; MUTAGEN 918; /note="D->E: Ca(2+) permeability is greatly increased."; /evidence="ECO:0000269|PubMed:18775987
uniprot
proteins
post_translational_modification
PTM: TRPA1 activation by electrophiles occurs though covalent modification of specific cysteine residues in the N-terminal cytoplasmic domain (By similarity). {ECO:0000250|UniProtKB:Q8BLA8}.; PTM: Hydroxylation is required for TRPA1 activity inhibition in normoxia. In hypoxia, the decrease in oxygen concentration diminishes the activity of the hydroxylase EGLN1, thus relieving TRPA1 from inhibition and ultimately leading to channel activation. {ECO:0000250|UniProtKB:O75762}.; PTM: Oxidation of Cys-634 and Cys-859 in hyperoxia may override the hydroxylase EGLN1-mediated inhibition, causing TRPA1 activation. {ECO:0000250|UniProtKB:O75762}.
uniprot
proteins
protein_family
Transient receptor (TC 1.A.4) family
uniprot
proteins
pubmed
12654248
uniprot
proteins
pubmed
14712238
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
18775987
uniprot
proteins
pubmed
21402443
uniprot
proteins
sequence_length
1125
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BLA8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O75762}.
uniprot
proteins
transmembrane_region
TRANSMEM 722..742; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:O75762"; TRANSMEM 768..788; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:O75762"; TRANSMEM 807..827; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:O75762"; TRANSMEM 833..853; /note="Helical;Name=4"; /evidence="ECO:0000250|UniProtKB:O75762"; TRANSMEM 877..897; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:O75762"; TRANSMEM 938..959; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:O75762
uniprot
proteins