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Entry version 106 (26 Feb 2020)
Sequence version 1 (05 Jul 2004)
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Protein

Transient receptor potential cation channel subfamily A member 1

Gene

Trpa1

Organism
Rattus norvegicus (Rat)
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 transcript 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. Shows 8-fold preference for divalent over monovalent cations. Has a central role in the pain response to endogenous inflammatory mediators and to a diverse array of irritants, such as allylthiocyanate (AITC) found in mustard oil or wasabi, cinnamaldehyde, diallyl disulfide (DADS) from garlic, and acrolein, an irritant from tears gas and vehicule exhaust fumes. Acts also as an ionotropic cannabinoid receptor by being activated by delta9-tetrahydrocannabinol (THC), the psychoactive component of marijuana (PubMed:14712238). 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 Publication

<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

Inhibited by ruthenium red, a potent blocker of TRPV channels (PubMed:14712238). Selectively inhibited by A-967079 (PubMed:21402443).2 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 sitei415Agonist (covalent)By similarity1
Binding sitei422Agonist (covalent)By similarity1
Binding sitei622Agonist (covalent); Cys highly reactiveBy 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>Sitei623Key residue for activation by the scorpion wasabi receptor toxinBy similarity1
Sitei635Important residue for activation by the scorpion wasabi receptor toxinBy similarity1
Binding sitei642Agonist (covalent)By similarity1
Sitei647Important residue for activation by the scorpion wasabi receptor toxinBy similarity1
Binding sitei666Agonist (covalent)By similarity1
Binding sitei712Agonist (covalent)By similarity1
Binding sitei912Non-reactive agonists and antagonists that can be structurally distinctBy similarity1
Binding sitei947Non-reactive agonists and antagonists that can be structurally distinctBy similarity1

<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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-3295583 TRP channels

<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
Wasabi receptorBy similarity
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
1303284 Trpa1

<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 – 721CytoplasmicBy similarityAdd BLAST721
<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>Transmembranei722 – 742Helical; Name=1By similarityAdd BLAST21
Topological domaini743 – 767ExtracellularBy similarityAdd BLAST25
Transmembranei768 – 788Helical; Name=2By similarityAdd BLAST21
Topological domaini789 – 806CytoplasmicBy similarityAdd BLAST18
Transmembranei807 – 827Helical; Name=3By similarityAdd BLAST21
Topological domaini828 – 832ExtracellularBy similarity5
Transmembranei833 – 853Helical;Name=4By similarityAdd BLAST21
Topological domaini854 – 876CytoplasmicBy similarityAdd BLAST23
Transmembranei877 – 897Helical; Name=5By similarityAdd BLAST21
Topological domaini898 – 904ExtracellularBy similarity7
<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>Intramembranei905 – 925Pore-formingBy similarityAdd BLAST21
Topological domaini926 – 937ExtracellularBy similarityAdd BLAST12
Transmembranei938 – 959Helical; Name=6By similarityAdd BLAST22
Topological domaini960 – 1125CytoplasmicBy similarityAdd BLAST166

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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5160

DrugCentral

More...
DrugCentrali
Q6RI86

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
485

<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_00002153711 – 1125Transient receptor potential cation channel subfamily A member 1Add BLAST1125

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 bondi193 ↔ 666AlternateBy 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 residuei3954-hydroxyproline; transientBy similarity1
Disulfide bondi463 ↔ 666AlternateBy similarity
Disulfide bondi609 ↔ 622AlternateBy similarity
Disulfide bondi622 ↔ 666AlternateBy similarity
Disulfide bondi634 ↔ 859Alternate; transient; in hyperoxia; unknown whether inter- or intrachainBy similarity
Modified residuei634Cysteine sulfenic acid (-SOH); transient; in hyperoxiaBy similarity1
<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>Glycosylationi749N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi755N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei859Cysteine sulfenic acid (-SOH); transient; in hyperoxiaBy similarity1

<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 (By similarity).By similarity
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.By similarity
Oxidation of Cys-634 and Cys-859 in hyperoxia may override the hydroxylase EGLN1-mediated inhibition, causing TRPA1 activation.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Oxidation

Proteomic databases

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

More...
PaxDbi
Q6RI86

PRoteomics IDEntifications database

More...
PRIDEi
Q6RI86

<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

Specifically expressed in a subset of nociceptive neurons. Expressed in dorsal root ganglia.1 Publication

<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 (By similarity).

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 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-61522N

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000009874

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q6RI86

<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

3D structure databases

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

More...
SMRi
Q6RI86

Database of comparative protein structure models

More...
ModBasei
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>Repeati63 – 94ANK 1Add BLAST32
Repeati98 – 127ANK 2Add BLAST30
Repeati131 – 161ANK 3Add BLAST31
Repeati165 – 194ANK 4Add BLAST30
Repeati198 – 227ANK 5Add BLAST30
Repeati239 – 268ANK 6Add BLAST30
Repeati272 – 301ANK 7Add BLAST30
Repeati309 – 338ANK 8Add BLAST30
Repeati342 – 371ANK 9Add BLAST30
Repeati413 – 442ANK 10Add BLAST30
Repeati446 – 475ANK 11Add BLAST30
Repeati482 – 511ANK 12Add BLAST30
Repeati514 – 543ANK 13Add BLAST30
Repeati548 – 577ANK 14Add BLAST30

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>Regioni1048 – 1054Inositolphosphate bindingBy similarity7

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 coili1044 – 1073By similarityAdd 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).By similarity
The ANK repeat domain consists of a convex stem structure followed by a crescent-shaped structure that surrounds the protein core.By similarity

<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
COG0666 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q6RI86

KEGG Orthology (KO)

More...
KOi
K04984

Database of Orthologous Groups

More...
OrthoDBi
361612at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q6RI86

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
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

Q6RI86-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKRSLRRVLR PEERKEVQGV VYRGVGKDMD CSKESFKVDI EGDMCRLEAF
60 70 80 90 100
IKNRRKLSKY EDENLCLLHH AAAEGQVELM QLIINGSSCE ALNVMDDYGN
110 120 130 140 150
TPLHWAAEKN QVESVKFLLS QGANPNLRNR NMMAPLHIAV QGMYNEVIKV
160 170 180 190 200
LTEHKATNIN LEGENGNTAL MSTCAKDNSE ALQILLEKGA KLCKSNKWGD
210 220 230 240 250
YPVHQAAFSG AKRCMELILA YGEKTGYSRE AHINFVNHKK ASPLHLAVQS
260 270 280 290 300
GDLDMIKMCL DSGAHIDMME NAKCMALHFA ATQGATDIVK LMISSYTGSS
310 320 330 340 350
DIVNAVDGNQ ETLLHRASLF DHHDLADYLI SVGADINSTD SEGRSPLILA
360 370 380 390 400
TASASWNIVN LLLSKGAKVD IKDHLGRNFL HLTVQQPYGL RNLRPEFLQM
410 420 430 440 450
QHIKELVMDE DNDGCTPLHY ACRQGAPVSV NNLLRFNVSV HSKSKDKKSP
460 470 480 490 500
LHFAASYGRI NTCQRLLQDI SDTRLLNEGD LHGMTPLHLA AKNGHDKVVQ
510 520 530 540 550
LLLKKGALFL SDHNGWTALH HASMGGYTQT MKVILDTNLK CTDRLDEEGN
560 570 580 590 600
TALHFAAREG HAKAVAMLLS YNADILLNKK QASFLHIALH NKRKEVVLTT
610 620 630 640 650
IRSKRWDECL QVFTHDSPSN RCPIMEMVEY LPECMKVLLD FCMIPSTEDK
660 670 680 690 700
SCQDYHIEYN FKYLQCPLSM TKKVTPTQDV IYEPLTILNV MVQHNRIELL
710 720 730 740 750
NHPVCREYLL MKWCAYGFRA HMMNLGSYCL GLIPMTLLVV KIQPGMAFNS
760 770 780 790 800
TGIINETIST HEERINTLNS FPLKICMILV FLSSIFGYCK EVVQIFQQKR
810 820 830 840 850
NYFLDYNNAL EWVIYTTSMI FVLPLFLDIP AYMQWQCGAI AIFFYWMNFL
860 870 880 890 900
LYLQRFENCG IFIVMLEVIF KTLLRSTGVF IFLLLAFGLS FYVLLNFQDA
910 920 930 940 950
FSTPLLSLIQ TFSMMLGDIN YRDAFLEPLF RNELAYPVLT FGQLIAFTMF
960 970 980 990 1000
VPIVLMNLLI GLAVGDIAEV QKHASLKRIA MQVELHTNLE KKLPFWYLRK
1010 1020 1030 1040 1050
VDQRSTIVYP NRPRHGRMLR FFHYFLSMQE TRQEAPNIDT CLEMEILKQK
1060 1070 1080 1090 1100
YRLKDLTSLL EKQHELIKLI IQKMEIISET EDEDNHCSFQ DRFKKERLEQ
1110 1120
MHSKWNFVLN AVKTKTHCSI SHPDI
Length:1,125
Mass (Da):128,602
Last modified:July 5, 2004 - v1
<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:i32A6FB51EDCBB4B5
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
F1LRH9F1LRH9_RAT
Transient receptor potential cation...
Trpa1
1,125Annotation score:

Annotation score:3 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AY496961 mRNA Translation: AAS78661.1

NCBI Reference Sequences

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RefSeqi
NP_997491.1, NM_207608.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
312896

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:312896

UCSC genome browser

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UCSCi
RGD:1303284 rat

<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
AY496961 mRNA Translation: AAS78661.1
RefSeqiNP_997491.1, NM_207608.1

3D structure databases

SMRiQ6RI86
ModBaseiSearch...

Protein-protein interaction databases

DIPiDIP-61522N
STRINGi10116.ENSRNOP00000009874

Chemistry databases

BindingDBiQ6RI86
ChEMBLiCHEMBL5160
DrugCentraliQ6RI86
GuidetoPHARMACOLOGYi485

Proteomic databases

PaxDbiQ6RI86
PRIDEiQ6RI86

Genome annotation databases

GeneIDi312896
KEGGirno:312896
UCSCiRGD:1303284 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8989
RGDi1303284 Trpa1

Phylogenomic databases

eggNOGiKOG0510 Eukaryota
COG0666 LUCA
InParanoidiQ6RI86
KOiK04984
OrthoDBi361612at2759
PhylomeDBiQ6RI86

Enzyme and pathway databases

ReactomeiR-RNO-3295583 TRP channels

Miscellaneous databases

Protein Ontology

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PROi
PR:Q6RI86

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
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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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_RAT
<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: Q6RI86
<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: July 5, 2004
Last modified: February 26, 2020
This is version 106 of the entry and version 1 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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