Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 164 (07 Oct 2020)
Sequence version 3 (30 Nov 2010)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Transient receptor potential cation channel subfamily A member 1

Gene

TRPA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Receptor-activated non-selective cation channel involved in pain detection and possibly also in cold perception, oxygen concentration perception, cough, itch, and inner ear function (PubMed:21873995, PubMed:23199233, PubMed:25389312, PubMed:25855297). Shows 8-fold preference for divalent over monovalent cations (PubMed:31447178). Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of irritants, such as allylthiocyanate (AITC) from mustard oil or wasabi, cinnamaldehyde, diallyl disulfide (DADS) from garlic, and acrolein, an irritant from tears gas and vehicule exhaust fumes (PubMed:25389312, PubMed:27241698, PubMed:30878828, PubMed:20547126). Acts also as an ionotropic cannabinoid receptor by being activated by delta9-tetrahydrocannabinol (THC), the psychoactive component of marijuana (PubMed:25389312). Is activated by a large variety of structurally unrelated electrophilic and non-electrophilic chemical compounds. Electrophilic ligands activate TRPA1 by interacting with critical N-terminal Cys residues in a covalent manner, whereas mechanisms of non-electrophilic ligands are not well determined. May be a component for the mechanosensitive transduction channel of hair cells in inner ear, thereby participating in the perception of sounds. Probably operated by a phosphatidylinositol second messenger system (By similarity).By similarity1 Publication7 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

A cytosolic factor (probably pyrophosphate, polytriphosphate, polyP4, polyP25, polyP45, and/or polyP65) is necessary for TRPA1 activation by irritants (PubMed:17567811). Such factor acts by keeping TRPA1 in a agonist-sensitive state (PubMed:17567811). Inhibited by the potent blocker of TRPV channels ruthenium red, A-967079, AP-18, HC-030031, and aryl sulfonamide derivative (S)-N-(4-chlorobenzyl)-1-((4-fluorophenyl)sulfonyl)pyrrolidine-2-carboxamide (ASD) (PubMed:17567811, PubMed:21873995, PubMed:21402443, PubMed:30878828, PubMed:20547126). Non-covalently activated by the scorpion wasabi receptor toxin (PubMed:31447178). Activated by benzyl isothiocyanate (BITC), iodoacetamide, sulfhydryl reactive agent MTSEA, N-methyl maleimide (NMM), N-ethylmaleimide (NEM), and 2-aminoethyldiphenylborinate (2-APB) (PubMed:17164327, PubMed:17567811, PubMed:21873995, PubMed:27241698). Also activated by hyperoxia (PubMed:21873995).8 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei414Agonist (covalent)By similarity1
Binding sitei421Agonist (covalent)By similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei620Required for C-621 reactivity1 Publication1
Binding sitei621Agonist (covalent); Cys highly reactiveBy similarity2 Publications1
Sitei622Key residue for activation by the scorpion wasabi receptor toxin1 Publication1
Sitei634Important residue for activation by the scorpion wasabi receptor toxin1 Publication1
Binding sitei641Agonist (covalent)1 Publication1
Sitei646Important residue for activation by the scorpion wasabi receptor toxin1 Publication1
Binding sitei665Agonist (covalent)2 Publications1
Binding sitei710Agonist (covalent)1 Publication1
Binding sitei909Non-reactive agonists and antagonists that can be structurally distinct1 Publication1
Binding sitei944Non-reactive agonists and antagonists that can be structurally distinct1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionIon channel
Biological processIon transport, Sensory transduction, Transport

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
O75762

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-3295583, TRP channels

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.A.4.6.3, the transient receptor potential ca(2+) channel (trp-cc) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Transient receptor potential cation channel subfamily A member 1
Alternative name(s):
Ankyrin-like with transmembrane domains protein 1
Transformation-sensitive protein p120
Wasabi receptor2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TRPA1
Synonyms:ANKTM1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000104321.10

Human Gene Nomenclature Database

More...
HGNCi
HGNC:497, TRPA1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
604775, gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_O75762

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 719Cytoplasmic1 PublicationAdd BLAST719
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei720 – 740Helical; Name=11 PublicationAdd BLAST21
Topological domaini741 – 764Extracellular1 PublicationAdd BLAST24
Transmembranei765 – 785Helical; Name=21 PublicationAdd BLAST21
Topological domaini786 – 803Cytoplasmic1 PublicationAdd BLAST18
Transmembranei804 – 824Helical; Name=31 PublicationAdd BLAST21
Topological domaini825 – 829Extracellular1 Publication5
Transmembranei830 – 850Helical; Name=41 PublicationAdd BLAST21
Topological domaini851 – 873Cytoplasmic1 PublicationAdd BLAST23
Transmembranei874 – 894Helical; Name=51 PublicationAdd BLAST21
Topological domaini895 – 901Extracellular1 Publication7
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei902 – 922Pore-forming1 PublicationAdd BLAST21
Topological domaini923 – 934Extracellular1 PublicationAdd BLAST12
Transmembranei935 – 956Helical; Name=61 PublicationAdd BLAST22
Topological domaini957 – 1119Cytoplasmic1 PublicationAdd BLAST163

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Episodic pain syndrome, familial, 1 (FEPS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant neurologic disorder characterized by onset in infancy of episodic debilitating upper body pain triggered by fasting, cold, and physical stress. The period of intense pain is accompanied by breathing difficulties, tachycardia, sweating, generalized pallor, peribuccal cyanosis, and stiffness of the abdominal wall. Affected individuals do not manifest altered pain sensitivity outside the episodes.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_069737855N → S in FEPS1; 5-fold increase in inward current when stimulated by the agonist cinnamaldehyde compared to wild-type at normal neuronal resting potential; consistent with a gain of function mutation. 1 PublicationCorresponds to variant dbSNP:rs398123010EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi173C → S: Decrease in activation by hyperoxia and diallyl disulfide. 1 Publication1
Mutagenesisi192C → S: Decrease in activation by hyperoxia and diallyl disulfide. 1 Publication1
Mutagenesisi394P → A: Loss of answer to hypoxia and hydroxylase inhibitor DMOG, but not to AITC and hyperoxia. 1 Publication1
Mutagenesisi620K → A: Important decrease in electrophile-evoked response. 1 Publication1
Mutagenesisi621C → A or S: Decrease in electrophile-evoked response. No change in answer to hyperoxia and diallyl disulfide. In TRPA1-3C-K708R/Q; loss in irritant-evoked response. 4 Publications1
Mutagenesisi622P → A: Loss of activation by the scorpion wasabi receptor toxin. 1 Publication1
Mutagenesisi633C → S: Decrease in activation by hyperoxia and diallyl disulfide. Important decrease in activation by hyperoxia and diallyl disulfide; when associated with S-856. 1 Publication1
Mutagenesisi634M → L: Loss of activation by the scorpion wasabi receptor toxin. 1 Publication1
Mutagenesisi641C → A or S: Decrease in electrophile-evoked and hyperoxia response. In TRPA1-3C-K708R/Q; loss in irritant-evoked response. 2 Publications1
Mutagenesisi646T → P: Loss of activation by the scorpion wasabi receptor toxin. 1 Publication1
Mutagenesisi665C → A, L or S: Decrease in electrophile-evoked and hyperoxia response. In TRPA1-3C-K708R/Q; loss in irritant-evoked response. 3 Publications1
Mutagenesisi710K → R or Q: No change in electrophile sensitivity. In TRPA1-3C-K708R/Q; loss in irritant-evoked response. 1
Mutagenesisi856C → S: Decrease in activation by hyperoxia and diallyl disulfide. Important decrease in activation by hyperoxia and diallyl disulfide; when associated with S-633. 1 Publication1
Mutagenesisi909F → A or T: Loss of inhibition by A-967079, AP-18, and ASD. Increase in activation by cinnamaldehyde, AITC and acrolein. 2 Publications1
Mutagenesisi944F → A: Loss of inhibition by A-967079, AP-18, and ASD. Weak or no change in activation by cinnamaldehyde, AITC and acrolein. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
8989

MalaCards human disease database

More...
MalaCardsi
TRPA1
MIMi615040, phenotype

Open Targets

More...
OpenTargetsi
ENSG00000104321

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
391389, Familial episodic pain syndrome with predominantly upper body involvement

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
O75762, Tclin

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL6007

Drug and drug target database

More...
DrugBanki
DB11345, (S)-camphor
DB11148, Butamben
DB01744, Camphor
DB09061, Cannabidiol
DB14050, Cannabidivarin
DB00825, Levomenthol
DB14009, Medical Cannabis
DB14011, Nabiximols
DB11755, Tetrahydrocannabivarin

DrugCentral

More...
DrugCentrali
O75762

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
485

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
TRPA1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002153691 – 1119Transient receptor potential cation channel subfamily A member 1Add BLAST1119

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi192 ↔ 665AlternateBy similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3944-hydroxyproline; by EGLN1; transient; in normoxia and hyperoxia1 Publication1
Disulfide bondi462 ↔ 665AlternateBy similarity
Disulfide bondi608 ↔ 621AlternateBy similarity
Disulfide bondi621 ↔ 665AlternateBy similarity
Disulfide bondi633 ↔ 856Alternate; transient; in hyperoxia; unknown whether inter- or intrachain1 Publication
Modified residuei633Cysteine sulfenic acid (-SOH); transient; in hyperoxia1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi747N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi753N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei856Cysteine sulfenic acid (-SOH); transient; in hyperoxia1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

TRPA1 activation by electrophiles occurs though covalent modification of specific cysteine residues in the N-terminal cytoplasmic domain (PubMed:25389312).1 Publication
Hydroxylation is required for TRPA1 activity inhibition in normoxia. In hypoxia, the decrease in oxygene concentration diminishes the activity of the hydroxylase EGLN1, thus relieving TRPA1 from inhibition and ultimately leading to channel activation.1 Publication
Oxidation of Cys-633 and Cys-856 in hyperoxia may override the hydroxylase EGLN1-mediated inhibition, causing TRPA1 activation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Oxidation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
O75762

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
O75762

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O75762

PeptideAtlas

More...
PeptideAtlasi
O75762

PRoteomics IDEntifications database

More...
PRIDEi
O75762

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
50181

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
O75762, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O75762

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
O75762

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed at very low level in human fibroblasts and at a moderate level in liposarcoma cells (PubMed:10066796).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000104321, Expressed in oocyte and 122 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O75762, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O75762, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000104321, Tissue enhanced (intestine, urinary bladder, vagina)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer (PubMed:25389312, PubMed:25855297).

Interacts with TMEM100 (By similarity).

Interacts with EGLN1 (By similarity).

Interacts with the scorpion wasabi receptor toxin at the same site that electrophiles but in a non-covalent manner (PubMed:31447178).

By similarity3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

O75762
With#Exp.IntAct
itself2EBI-11722999,EBI-11722999

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
114471, 2 interactors

Database of interacting proteins

More...
DIPi
DIP-61520N

Protein interaction database and analysis system

More...
IntActi
O75762, 3 interactors

Molecular INTeraction database

More...
MINTi
O75762

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000262209

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
O75762

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
O75762, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11119
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
O75762

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati62 – 92ANK 1Sequence analysis1 PublicationAdd BLAST31
Repeati97 – 126ANK 2Sequence analysis1 PublicationAdd BLAST30
Repeati130 – 160ANK 3Sequence analysis1 PublicationAdd BLAST31
Repeati164 – 193ANK 4Sequence analysis1 PublicationAdd BLAST30
Repeati197 – 226ANK 5Sequence analysis1 PublicationAdd BLAST30
Repeati238 – 267ANK 6Sequence analysis1 PublicationAdd BLAST30
Repeati271 – 301ANK 7Sequence analysis1 PublicationAdd BLAST31
Repeati308 – 337ANK 8Sequence analysis1 PublicationAdd BLAST30
Repeati341 – 370ANK 9Sequence analysis1 PublicationAdd BLAST30
Repeati374 – 403ANK 101 PublicationAdd BLAST30
Repeati412 – 441ANK 11Sequence analysis1 PublicationAdd BLAST30
Repeati445 – 474ANK 12Sequence analysis1 PublicationAdd BLAST30
Repeati481 – 510ANK 13Sequence analysis1 PublicationAdd BLAST30
Repeati513 – 542ANK 14Sequence analysis1 PublicationAdd BLAST30
Repeati547 – 576ANK 15Sequence analysis1 PublicationAdd BLAST30
Repeati579 – 609ANK 16Sequence analysis1 PublicationAdd BLAST31

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1046 – 1052Inositolphosphate binding1 Publication7

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili1042 – 10711 PublicationAdd BLAST30

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

C-terminal helices from the four subunits associate to form atypical coiled coil structure; this region is probably involved in binding the inositol polyphosphates that are required for optimal channel activity (in vitro).1 Publication
The ANK repeat domain consists of a convex stem structure formed by five ANK repeats and 11 additional ANK repeats that form a crescent-shaped structure that surrounds the protein core.1 Publication

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

ANK repeat, Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0510, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156118

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O75762

KEGG Orthology (KO)

More...
KOi
K04984

Identification of Orthologs from Complete Genome Data

More...
OMAi
QDYHIEY

Database of Orthologous Groups

More...
OrthoDBi
361612at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
O75762

TreeFam database of animal gene trees

More...
TreeFami
TF317264

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.20, 4 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR005821, Ion_trans_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00023, Ank, 1 hit
PF12796, Ank_2, 5 hits
PF00520, Ion_trans, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01415, ANKYRIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248, ANK, 14 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48403, SSF48403, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 9 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O75762-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRSLRKMWR PGEKKEPQGV VYEDVPDDTE DFKESLKVVF EGSAYGLQNF
60 70 80 90 100
NKQKKLKRCD DMDTFFLHYA AAEGQIELME KITRDSSLEV LHEMDDYGNT
110 120 130 140 150
PLHCAVEKNQ IESVKFLLSR GANPNLRNFN MMAPLHIAVQ GMNNEVMKVL
160 170 180 190 200
LEHRTIDVNL EGENGNTAVI IACTTNNSEA LQILLKKGAK PCKSNKWGCF
210 220 230 240 250
PIHQAAFSGS KECMEIILRF GEEHGYSRQL HINFMNNGKA TPLHLAVQNG
260 270 280 290 300
DLEMIKMCLD NGAQIDPVEK GRCTAIHFAA TQGATEIVKL MISSYSGSVD
310 320 330 340 350
IVNTTDGCHE TMLHRASLFD HHELADYLIS VGADINKIDS EGRSPLILAT
360 370 380 390 400
ASASWNIVNL LLSKGAQVDI KDNFGRNFLH LTVQQPYGLK NLRPEFMQMQ
410 420 430 440 450
QIKELVMDED NDGCTPLHYA CRQGGPGSVN NLLGFNVSIH SKSKDKKSPL
460 470 480 490 500
HFAASYGRIN TCQRLLQDIS DTRLLNEGDL HGMTPLHLAA KNGHDKVVQL
510 520 530 540 550
LLKKGALFLS DHNGWTALHH ASMGGYTQTM KVILDTNLKC TDRLDEDGNT
560 570 580 590 600
ALHFAAREGH AKAVALLLSH NADIVLNKQQ ASFLHLALHN KRKEVVLTII
610 620 630 640 650
RSKRWDECLK IFSHNSPGNK CPITEMIEYL PECMKVLLDF CMLHSTEDKS
660 670 680 690 700
CRDYYIEYNF KYLQCPLEFT KKTPTQDVIY EPLTALNAMV QNNRIELLNH
710 720 730 740 750
PVCKEYLLMK WLAYGFRAHM MNLGSYCLGL IPMTILVVNI KPGMAFNSTG
760 770 780 790 800
IINETSDHSE ILDTTNSYLI KTCMILVFLS SIFGYCKEAG QIFQQKRNYF
810 820 830 840 850
MDISNVLEWI IYTTGIIFVL PLFVEIPAHL QWQCGAIAVY FYWMNFLLYL
860 870 880 890 900
QRFENCGIFI VMLEVILKTL LRSTVVFIFL LLAFGLSFYI LLNLQDPFSS
910 920 930 940 950
PLLSIIQTFS MMLGDINYRE SFLEPYLRNE LAHPVLSFAQ LVSFTIFVPI
960 970 980 990 1000
VLMNLLIGLA VGDIAEVQKH ASLKRIAMQV ELHTSLEKKL PLWFLRKVDQ
1010 1020 1030 1040 1050
KSTIVYPNKP RSGGMLFHIF CFLFCTGEIR QEIPNADKSL EMEILKQKYR
1060 1070 1080 1090 1100
LKDLTFLLEK QHELIKLIIQ KMEIISETED DDSHCSFQDR FKKEQMEQRN
1110
SRWNTVLRAV KAKTHHLEP
Length:1,119
Mass (Da):127,501
Last modified:November 30, 2010 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i283BF31BC77CF71B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
H0YAW0H0YAW0_HUMAN
Transient receptor potential cation...
TRPA1
916Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0206603R → C1 PublicationCorresponds to variant dbSNP:rs13268757Ensembl.1
Natural variantiVAR_04747158R → T1 PublicationCorresponds to variant dbSNP:rs16937976Ensembl.1
Natural variantiVAR_020661179E → K. Corresponds to variant dbSNP:rs920829Ensembl.1
Natural variantiVAR_020662186K → N1 PublicationCorresponds to variant dbSNP:rs7819749Ensembl.1
Natural variantiVAR_069737855N → S in FEPS1; 5-fold increase in inward current when stimulated by the agonist cinnamaldehyde compared to wild-type at normal neuronal resting potential; consistent with a gain of function mutation. 1 PublicationCorresponds to variant dbSNP:rs398123010EnsemblClinVar.1
Natural variantiVAR_0206631018H → R. Corresponds to variant dbSNP:rs959976Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y10601 mRNA Translation: CAA71610.1
AC022867 Genomic DNA No translation available.

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS34908.1

NCBI Reference Sequences

More...
RefSeqi
NP_015628.2, NM_007332.2
XP_011515927.1, XM_011517625.2
XP_016869435.1, XM_017013946.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000262209; ENSP00000262209; ENSG00000104321

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
8989

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:8989

UCSC genome browser

More...
UCSCi
uc003xza.4, human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Protein Spotlight

The power behind pain - Issue 82 of May 2007

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y10601 mRNA Translation: CAA71610.1
AC022867 Genomic DNA No translation available.
CCDSiCCDS34908.1
RefSeqiNP_015628.2, NM_007332.2
XP_011515927.1, XM_011517625.2
XP_016869435.1, XM_017013946.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J9Pelectron microscopy4.24A/B/C/D2-1119[»]
6HC8X-ray1.90E313-339[»]
6PQOelectron microscopy2.88A/B/C/D2-1119[»]
6PQPelectron microscopy3.06A/B/C/D2-1119[»]
6PQQelectron microscopy2.81A/B/C/D2-1119[»]
6V9Velectron microscopy2.60A/B/C/D1-1119[»]
6V9Welectron microscopy3.10A/B/C/D1-1119[»]
6V9Xelectron microscopy3.30A/B/C/D1-1119[»]
6V9Yelectron microscopy3.60A/B/C/D1-1119[»]
SMRiO75762
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi114471, 2 interactors
DIPiDIP-61520N
IntActiO75762, 3 interactors
MINTiO75762
STRINGi9606.ENSP00000262209

Chemistry databases

BindingDBiO75762
ChEMBLiCHEMBL6007
DrugBankiDB11345, (S)-camphor
DB11148, Butamben
DB01744, Camphor
DB09061, Cannabidiol
DB14050, Cannabidivarin
DB00825, Levomenthol
DB14009, Medical Cannabis
DB14011, Nabiximols
DB11755, Tetrahydrocannabivarin
DrugCentraliO75762
GuidetoPHARMACOLOGYi485

Protein family/group databases

TCDBi1.A.4.6.3, the transient receptor potential ca(2+) channel (trp-cc) family

PTM databases

GlyGeniO75762, 2 sites
iPTMnetiO75762
PhosphoSitePlusiO75762

Polymorphism and mutation databases

BioMutaiTRPA1

Proteomic databases

jPOSTiO75762
MassIVEiO75762
PaxDbiO75762
PeptideAtlasiO75762
PRIDEiO75762
ProteomicsDBi50181

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
12262, 274 antibodies

The DNASU plasmid repository

More...
DNASUi
8989

Genome annotation databases

EnsembliENST00000262209; ENSP00000262209; ENSG00000104321
GeneIDi8989
KEGGihsa:8989
UCSCiuc003xza.4, human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
8989
DisGeNETi8989
EuPathDBiHostDB:ENSG00000104321.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TRPA1
HGNCiHGNC:497, TRPA1
HPAiENSG00000104321, Tissue enhanced (intestine, urinary bladder, vagina)
MalaCardsiTRPA1
MIMi604775, gene
615040, phenotype
neXtProtiNX_O75762
OpenTargetsiENSG00000104321
Orphaneti391389, Familial episodic pain syndrome with predominantly upper body involvement

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0510, Eukaryota
GeneTreeiENSGT00940000156118
InParanoidiO75762
KOiK04984
OMAiQDYHIEY
OrthoDBi361612at2759
PhylomeDBiO75762
TreeFamiTF317264

Enzyme and pathway databases

PathwayCommonsiO75762
ReactomeiR-HSA-3295583, TRP channels

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
8989, 1 hit in 868 CRISPR screens

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
8989
PharosiO75762, Tclin

Protein Ontology

More...
PROi
PR:O75762
RNActiO75762, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000104321, Expressed in oocyte and 122 other tissues
ExpressionAtlasiO75762, baseline and differential
GenevisibleiO75762, HS

Family and domain databases

Gene3Di1.25.40.20, 4 hits
InterProiView protein in InterPro
IPR002110, Ankyrin_rpt
IPR020683, Ankyrin_rpt-contain_dom
IPR036770, Ankyrin_rpt-contain_sf
IPR005821, Ion_trans_dom
PfamiView protein in Pfam
PF00023, Ank, 1 hit
PF12796, Ank_2, 5 hits
PF00520, Ion_trans, 1 hit
PRINTSiPR01415, ANKYRIN
SMARTiView protein in SMART
SM00248, ANK, 14 hits
SUPFAMiSSF48403, SSF48403, 2 hits
PROSITEiView protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 9 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTRPA1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O75762
Secondary accession number(s): A6NIN6
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: November 30, 2010
Last modified: October 7, 2020
This is version 164 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  6. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again