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UniProtKB - O35433 (TRPV1_RAT)

Entry version 182 (23 Feb 2022)
Sequence version 1 (01 Jan 1998)
Previous versions | rss
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Protein

Transient receptor potential cation channel subfamily V member 1

Gene

Trpv1

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 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

Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca2+-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis.

16 Publications

Does not display channel activity in response to noxious chemical compounds, such as capsaicin and the vanilloid resiniferatoxin. Channel activity is not elicited by mildly acidic extracellular pH, and only slight channel activity is observed in response to noxiuos heat stimuli.

1 Publication

Miscellaneous

Responses evoked by capsaicin, but not by low pH and heat, can be antagonized by capsazepine.

<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

Channel activity is activated via the interaction with PIRT and phosphatidylinositol 4,5-bisphosphate (PIP2). Both PIRT and PIP2 are required to activate channel activity (By similarity). The channel is sensitized by ATP binding. Repeated stimulation with capsaicin gives rise to progressively smaller responses, due to desensitization. This desensitization is triggered by the influx of calcium ions and is inhibited by elevated ATP levels. Ca2+ and CALM displace ATP from its binding site and trigger a conformation change that leads to a closed, desensitized channel. Intracellular PIP2 inhibits desensitization. The double-knot toxin (DkTx) from the Chinese earth tiger tarantula activates the channel and traps it in an open conformation. The Scolopendra mutilans RhTx toxin potentiates the heat activation pathway mediated by this channel by binding to the charge-rich outer pore region (in an activated state) (By similarity).By similarity3 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 sitei115ATPCombined sources1
Binding sitei155ATPCombined sources1
Binding sitei160ATPCombined sources1
Binding sitei164ATPCombined sources1
Binding sitei550Resiniferatoxin; agonistCombined sources1 Publication1
Binding sitei557Resiniferatoxin; agonistCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi646Calcium; shared with neighboring subunitsBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi199 – 202ATPCombined sources4
Nucleotide bindingi210 – 211ATPCombined sources2

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionCalcium channel, Calmodulin-binding, Ion channel
Biological processCalcium transport, Ion transport, Transport
LigandATP-binding, Calcium, Lipid-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

Protein family/group databases

Transport Classification Database

More...TCDBi		1.A.4.2.1, 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 V member 1
Short name:
TrpV1
Alternative name(s):
Capsaicin receptor
Osm-9-like TRP channel 1
Short name:
OTRPC1
Vanilloid receptor 1
Vanilloid receptor type 1-like
<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:Trpv1
Synonyms:Vr1, Vr1l
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
<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: Chromosome 10

Organism-specific databases

Rat genome database

More...RGDi		628841, Trpv1

<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

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 – 432Cytoplasmic2 PublicationsAdd BLAST432
<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>Transmembranei433 – 453Helical2 PublicationsAdd BLAST21
Topological domaini454 – 471Extracellular2 PublicationsAdd BLAST18
Transmembranei472 – 497Helical2 PublicationsAdd BLAST26
Topological domaini498 – 510Cytoplasmic2 PublicationsAdd BLAST13
Transmembranei511 – 531Helical2 PublicationsAdd BLAST21
Topological domaini532 – 535Extracellular2 Publications4
Transmembranei536 – 556Helical2 PublicationsAdd BLAST21
Topological domaini557 – 571Cytoplasmic2 PublicationsAdd BLAST15
Transmembranei572 – 599Helical2 PublicationsAdd BLAST28
Topological domaini600 – 626Extracellular2 PublicationsAdd BLAST27
<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>Intramembranei627 – 649Pore-forming1 Publication2 PublicationsAdd BLAST23
Transmembranei658 – 686Helical2 PublicationsAdd BLAST29
Topological domaini687 – 838Cytoplasmic2 PublicationsAdd BLAST152

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

<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

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>Mutagenesisi114R → E: Abolishes capsaicin-evoked current and binding to resiniferatoxin. 1 Publication1
Mutagenesisi114Missing : Abolishes sensitivity to acid. 1 Publication1
Mutagenesisi115R → D: Abolishes capsaicin-evoked current and binding to resiniferatoxin. 1 Publication1
Mutagenesisi116S → A: Abolishes phosphorylation by PKCM and enhances channel response to capsaicin by PKCM. 1 Publication1
Mutagenesisi155K → A: Abolishes ATP binding. Abolishes CALM binding. Impairs normal desensitization by repeated exposure to capsaicin. 2 Publications1
Mutagenesisi160K → A: Abolishes ATP binding. Abolishes CALM binding. 1 Publication1
Mutagenesisi199Y → A: Strongly reduces affinity for ATP; when associated with A-202. 1 Publication1
Mutagenesisi202Q → A: Strongly reduces affinity for ATP; when associated with A-199. 1 Publication1
Mutagenesisi502S → A: Largely reduces PMA enhancement of capsaicin-evoked currents, but no effect on direct activation by PMA. Loss of activation by capsaicin and loss of vanilloid binding; when associated with I-704. 3 Publications1
Mutagenesisi511Y → A: Loss of sensitivity to capsaicin. 1 Publication1
Mutagenesisi547M → L: Reduces binding to resiniferatoxin. 1 Publication1
Mutagenesisi550T → I: Reduces sensitivity to capsaicin 10-fold; no effect on sensitivity to resiniferatoxin. Reduces binding to resiniferatoxin. 1 Publication1
Mutagenesisi636E → K: Abolishes channel activity. Restored channel activity; when associated with E-639. 1 Publication1
Mutagenesisi636E → Q: Slight modification of pore attributes. 1 Publication1
Mutagenesisi639K → E: Restored channel activity; when associated with K-636. 1 Publication1
Mutagenesisi644M → Y: Slightly modifies channel permeability. 1 Publication1
Mutagenesisi646D → N: Strongly reduces the affinity for pore blocker ruthenium red and lowered channel permeability for Mg(2+). 1 Publication1
Mutagenesisi648E → Q: Minor modification of pore attributes. 1 Publication1
Mutagenesisi651E → Q: Minor modification of pore attributes. 1 Publication1
Mutagenesisi704T → A: No effect on PMA-induced enhancement of capsaicin-evoked currents but reduces direct activation by PMA. 2 Publications1
Mutagenesisi704T → I: Loss of activation by capsaicin and loss of vanilloid binding; when associated with A-502. 2 Publications1
Mutagenesisi761E → K or Q: Abolishes capsaiin-evoked current and binding to resiniferatoxin. 1 Publication1
Mutagenesisi761Missing : Abolishes sensitivity to acid. 1 Publication1
Mutagenesisi785R → Q: Strongly reduces CALM-binding and abolishes PLC-mediated channel activity; when associated with Q-788. 2 Publications1
Mutagenesisi787W → R: Reduces CALM-binding. Reduces desensitization by repeated exposure to capsaicin. 1 Publication1
Mutagenesisi788K → Q: Strongly reduces CALM-binding and abolishes PLC-mediated channel activity; when associated with Q-785 or Q-797. 2 Publications1
Mutagenesisi797R → Q: Abolishes PLC-mediated channel activity; when associated with Q-788. 1 Publication1
Mutagenesisi800S → A: Largely reduces direct activation of by PMA and PMA-induced currents; no effect on receptor kinase-induced currents. 3 Publications1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL5102

DrugCentral

More...DrugCentrali		O35433

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		507

<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_00002153411 – 838Transient receptor potential cation channel subfamily V member 1Add BLAST838

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei116Phosphoserine; by PKA and PKD2 Publications1
Modified residuei144Phosphothreonine; by PKA; in vitro1 Publication1
Modified residuei370Phosphothreonine; by PKA; in vitro1 Publication1
Modified residuei502Phosphoserine; by PKC/PRKCE3 Publications1
<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>Glycosylationi604N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei704Phosphothreonine1 Publication1
Modified residuei774Phosphoserine; by PKA; in vitro1 Publication1
Modified residuei800Phosphoserine; by PKC/PRKCE and PKC/PRKCZ1 Publication1
Modified residuei820Phosphoserine; by PKA; in vitro1 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

Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-116 as a major phosphorylation site. Phosphorylation by CAMKII seems to regulate binding to vanilloids. Phosphorylated and modulated by PRKCE, PRKCM and probably PRKCZ. Dephosphorylation by calcineurin seems to lead to receptor desensitization and phosphorylation by CAMKII recovers activity.4 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

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

More...PaxDbi		O35433

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		O35433, 1 site

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		O35433

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

More...PhosphoSitePlusi		O35433

<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

Predominantly expressed in trigeminal and dorsal root sensory ganglia. Expressed also in hippocampus, cortex, cerebellum, olfactory bulb, mesencephalon and hindbrain. High expression in the cell bodies and dendrites of neurons in the hippocampus and in the cortex. In the brain detected also in astrocytes and pericytes (at protein level) (PubMed:15857679). Isoform 1 and isoform 3 are expressed in brain and peripheral blood mononuclear cells.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSRNOG00000019486, Expressed in adult mammalian kidney and 19 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		O35433, RN

<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

Interacts with PIRT (By similarity). Homotetramer (PubMed:15190102, PubMed:24305160, PubMed:24305161, PubMed:27281200). May also form a heteromeric channel with TRPV3 (By similarity).

Interacts with CALM, PRKCM and CSK (PubMed:12808128, PubMed:15084474, PubMed:15471852, PubMed:17582331).

Interacts with PRKCG and NTRK1, probably by forming a trimeric complex (PubMed:11418861).

Interacts with the Scolopendra mutilans RhTx toxin (By similarity).

Interacts with the spider Tau-theraphotoxin-Hs1a (PubMed:27281200).

Interacts with TMEM100 (By similarity).

Interacts with PACS2 (By similarity).

By similarity9 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

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		249845, 3 interactors

Database of interacting proteins

More...DIPi		DIP-56949N

Protein interaction database and analysis system

More...IntActi		O35433, 3 interactors

Molecular INTeraction database

More...MINTi		O35433

STRING: functional protein association networks

More...STRINGi		10116.ENSRNOP00000026493

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		O35433

<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

1838
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		O35433

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		O35433

<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>Repeati110 – 152ANK 1Add BLAST43
Repeati153 – 199ANK 2Add BLAST47
Repeati200 – 246ANK 3Add BLAST47
Repeati247 – 282ANK 4Add BLAST36
Repeati283 – 331ANK 5Add BLAST49
Repeati332 – 358ANK 6Add BLAST27

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>Regioni1 – 63DisorderedSequence analysisAdd BLAST63
Regioni86 – 109DisorderedSequence analysisAdd BLAST24
Regioni511 – 512Resiniferatoxin binding; agonistCombined sources1 Publication2
Regioni684 – 712ADAdd BLAST29
Regioni767 – 801Interaction with calmodulin1 PublicationAdd BLAST35
Regioni777 – 792Required for PIP2-mediated channel inhibitionAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi643 – 646Selectivity filter1 Publication4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi86 – 104Polar residuesSequence analysisAdd BLAST19

<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

The association domain (AD) is necessary for self-association.

<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

Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV1 sub-subfamily. [View classification]Curated

Keywords - Domaini

ANK repeat, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3676, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000160870

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_012795_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		O35433

Identification of Orthologs from Complete Genome Data

More...OMAi		YLHQNMK

Database of Orthologous Groups

More...OrthoDBi		693004at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		O35433

TreeFam database of animal gene trees

More...TreeFami		TF314711

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.25.40.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002110, Ankyrin_rpt
IPR036770, Ankyrin_rpt-contain_sf
IPR005821, Ion_trans_dom
IPR024862, TRPV
IPR024863, TRPV1
IPR008347, TRPV1-4_channel

The PANTHER Classification System

More...PANTHERi		PTHR10582, PTHR10582, 1 hit
PTHR10582:SF17, PTHR10582:SF17, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF12796, Ank_2, 1 hit
PF00520, Ion_trans, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01768, TRPVRECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00248, ANK, 4 hits

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48403, SSF48403, 1 hit

PROSITE; a protein domain and family database

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

<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>Sequences (3)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 describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: O35433-1) [UniParc]FASTAAdd to basket
Also known as: VR1L1

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEQRASLDSE ESESPPQENS CLDPPDRDPN CKPPPVKPHI FTTRSRTRLF 
        60         70         80         90        100
GKGDSEEASP LDCPYEEGGL ASCPIITVSS VLTIQRPGDG PASVRPSSQD 
       110        120        130        140        150
SVSAGEKPPR LYDRRSIFDA VAQSNCQELE SLLPFLQRSK KRLTDSEFKD 
       160        170        180        190        200
PETGKTCLLK AMLNLHNGQN DTIALLLDVA RKTDSLKQFV NASYTDSYYK 
       210        220        230        240        250
GQTALHIAIE RRNMTLVTLL VENGADVQAA ANGDFFKKTK GRPGFYFGEL 
       260        270        280        290        300
PLSLAACTNQ LAIVKFLLQN SWQPADISAR DSVGNTVLHA LVEVADNTVD 
       310        320        330        340        350
NTKFVTSMYN EILILGAKLH PTLKLEEITN RKGLTPLALA ASSGKIGVLA 
       360        370        380        390        400
YILQREIHEP ECRHLSRKFT EWAYGPVHSS LYDLSCIDTC EKNSVLEVIA 
       410        420        430        440        450
YSSSETPNRH DMLLVEPLNR LLQDKWDRFV KRIFYFNFFV YCLYMIIFTA 
       460        470        480        490        500
AAYYRPVEGL PPYKLKNTVG DYFRVTGEIL SVSGGVYFFF RGIQYFLQRR 
       510        520        530        540        550
PSLKSLFVDS YSEILFFVQS LFMLVSVVLY FSQRKEYVAS MVFSLAMGWT 
       560        570        580        590        600
NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYLVFLFG FSTAVVTLIE 
       610        620        630        640        650
DGKNNSLPME STPHKCRGSA CKPGNSYNSL YSTCLELFKF TIGMGDLEFT 
       660        670        680        690        700
ENYDFKAVFI ILLLAYVILT YILLLNMLIA LMGETVNKIA QESKNIWKLQ 
       710        720        730        740        750
RAITILDTEK SFLKCMRKAF RSGKLLQVGF TPDGKDDYRW CFRVDEVNWT 
       760        770        780        790        800
TWNTNVGIIN EDPGNCEGVK RTLSFSLRSG RVSGRNWKNF ALVPLLRDAS 
       810        820        830 
TRDRHATQQE EVQLKHYTGS LKPEDAEVFK DSMVPGEK
Length:838
Mass (Da):94,948
Last modified:January 1, 1998 - 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:iDAFC80B12BDF71BF
GO
Isoform 2 (identifier: O35433-2) [UniParc]FASTAAdd to basket
Also known as: VR1L2

The sequence of this isoform differs from the canonical sequence as follows:
     348-407: Missing.

Show »
Length:778
Mass (Da):88,050
Checksum:iAB7BC5F1721C9010
GO
Isoform 3 (identifier: O35433-3) [UniParc]FASTAAdd to basket
Also known as: VR.5'sv

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.
     348-407: Missing.

Note: Inactive.Curated
Show »
Length:471
Mass (Da):54,420
Checksum:iDFD8082CA26CA3C6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti18E → D in BAA94307 (PubMed:11578842).Curated1
Sequence conflicti36V → A in AAK83151 (PubMed:11549313).Curated1
Sequence conflicti48R → G in BAA94306 (PubMed:11578842).Curated1
Sequence conflicti51G → W in BAA94306 (PubMed:11578842).Curated1
Sequence conflicti96P → Q in BAA94307 (PubMed:11578842).Curated1
Sequence conflicti179V → I in AAK83151 (PubMed:11549313).Curated1
Sequence conflicti735K → Q in BAA94306 (PubMed:11578842).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0134311 – 307Missing in isoform 3. 1 PublicationAdd BLAST307
Alternative sequenceiVSP_013432348 – 407Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST60

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
AF029310 mRNA Translation: AAC53398.1
AF158248 mRNA Translation: AAF28389.1
AB041029 mRNA Translation: BAA94306.1
AB040873 mRNA Translation: BAA94307.1
AF327067 Genomic DNA Translation: AAK83151.1
AF327067 Genomic DNA Translation: AAK83152.1

Protein sequence database of the Protein Information Resource

More...PIRi		T09054

NCBI Reference Sequences

More...RefSeqi		NP_114188.1, NM_031982.1 [O35433-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486 [O35433-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		83810

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		rno:83810

Keywords - Coding sequence diversityi

Alternative splicing

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029310 mRNA Translation: AAC53398.1
AF158248 mRNA Translation: AAF28389.1
AB041029 mRNA Translation: BAA94306.1
AB040873 mRNA Translation: BAA94307.1
AF327067 Genomic DNA Translation: AAK83151.1
AF327067 Genomic DNA Translation: AAK83152.1
PIRiT09054
RefSeqiNP_114188.1, NM_031982.1 [O35433-1]

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
2NYJX-ray3.20A101-364[»]
2PNNX-ray2.70A101-364[»]
3J5Pelectron microscopy3.28A/B/C/D111-719[»]
3J5Qelectron microscopy3.80B/D/E/G111-719[»]
3J5Relectron microscopy4.20A/B/C/D111-719[»]
3J9Jelectron microscopy-A/B/C/D111-719[»]
3SUIX-ray1.95B767-801[»]
5IRXelectron microscopy2.95A/B/C/D110-764[»]
5IRZelectron microscopy3.28B/C/D/E110-764[»]
5IS0electron microscopy3.43B/C/D/E110-764[»]
7L2Helectron microscopy2.63A/B/C/D2-838[»]
7L2Ielectron microscopy3.70A/B/C/D2-838[»]
7L2Jelectron microscopy3.66A/B/C/D2-838[»]
7L2Kelectron microscopy3.89A/B/C/D2-838[»]
7L2Lelectron microscopy3.42A/B/C/D2-838[»]
7L2Melectron microscopy3.84A/B/C/D2-838[»]
7L2Nelectron microscopy3.09A/B/C/D2-838[»]
7L2Oelectron microscopy3.64A/B/C/D2-838[»]
7L2Pelectron microscopy2.60A/B/C/D110-764[»]
7L2Relectron microscopy3.30A/B/C/D110-764[»]
7L2Selectron microscopy2.71A/B/C/D110-764[»]
7L2Telectron microscopy3.08A/B/C/D110-764[»]
7L2Uelectron microscopy3.47A/B/C/D110-764[»]
7L2Velectron microscopy3.64A/B/C/D110-764[»]
7L2Welectron microscopy3.16A/B/C/D110-764[»]
7L2Xelectron microscopy3.26A/B/C/D110-764[»]
7LP9electron microscopy2.63A/B/C/D1-838[»]
7LPAelectron microscopy3.37A/B/C/D1-838[»]
7LPBelectron microscopy3.54A/B/C/D1-838[»]
7LPCelectron microscopy3.06A/B/C/D1-838[»]
7LPDelectron microscopy3.55A/B/C/D1-838[»]
7LPEelectron microscopy3.72A/B/C/D1-838[»]
7MZ5electron microscopy2.76A/B/C/D2-838[»]
7MZ6electron microscopy2.91A/B/C/D110-764[»]
7MZ7electron microscopy3.35A/B/C/D110-764[»]
7MZ9electron microscopy3.18A/B/C/D110-764[»]
7MZAelectron microscopy3.46A/B/C/D110-764[»]
7MZBelectron microscopy3.72A/B/C/D110-764[»]
7MZCelectron microscopy3.03A/B/C/D110-764[»]
7MZDelectron microscopy2.90A/B/C/D110-764[»]
7MZEelectron microscopy3.42A/B/C/D110-764[»]
SMRiO35433
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi249845, 3 interactors
DIPiDIP-56949N
IntActiO35433, 3 interactors
MINTiO35433
STRINGi10116.ENSRNOP00000026493

Chemistry databases

BindingDBiO35433
ChEMBLiCHEMBL5102
DrugCentraliO35433
GuidetoPHARMACOLOGYi507

Protein family/group databases

TCDBi1.A.4.2.1, the transient receptor potential ca(2+) channel (trp-cc) family

PTM databases

GlyGeniO35433, 1 site
iPTMnetiO35433
PhosphoSitePlusiO35433

Proteomic databases

PaxDbiO35433

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		O35433, 2 sequenced antibodies

Genome annotation databases

EnsembliENSRNOT00000026493; ENSRNOP00000026493; ENSRNOG00000019486 [O35433-1]
GeneIDi83810
KEGGirno:83810

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7442
RGDi628841, Trpv1

Phylogenomic databases

eggNOGiKOG3676, Eukaryota
GeneTreeiENSGT00940000160870
HOGENOMiCLU_012795_1_0_1
InParanoidiO35433
OMAiYLHQNMK
OrthoDBi693004at2759
PhylomeDBiO35433
TreeFamiTF314711

Enzyme and pathway databases

ReactomeiR-RNO-3295583, TRP channels

Miscellaneous databases

EvolutionaryTraceiO35433

Protein Ontology

More...PROi		PR:O35433

Gene expression databases

BgeeiENSRNOG00000019486, Expressed in adult mammalian kidney and 19 other tissues
GenevisibleiO35433, RN

Family and domain databases

Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110, Ankyrin_rpt
IPR036770, Ankyrin_rpt-contain_sf
IPR005821, Ion_trans_dom
IPR024862, TRPV
IPR024863, TRPV1
IPR008347, TRPV1-4_channel
PANTHERiPTHR10582, PTHR10582, 1 hit
PTHR10582:SF17, PTHR10582:SF17, 1 hit
PfamiView protein in Pfam
PF12796, Ank_2, 1 hit
PF00520, Ion_trans, 1 hit
PRINTSiPR01768, TRPVRECEPTOR
SMARTiView protein in SMART
SM00248, ANK, 4 hits
SUPFAMiSSF48403, SSF48403, 1 hit
PROSITEiView protein in PROSITE
PS50297, ANK_REP_REGION, 1 hit
PS50088, ANK_REPEAT, 1 hit

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 nameiTRPV1_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: O35433
Secondary accession number(s): Q920B3
, Q920B4, Q9JLM0, Q9JM56, Q9JM57
<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: May 10, 2005
Last sequence update: January 1, 1998
Last modified: February 23, 2022
This is version 182 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

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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