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Protein

Transient receptor potential cation channel subfamily V member 1

Gene

TRPV1

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

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.By similarity4 Publications

Miscellaneous

Responses evoked by low pH and heat, and capsaicin can be antagonized by capsazepine.

<p>This subsection of the ‘Function’ 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 (By similarity). 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 similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei116ATPBy similarity1
Binding sitei156ATPBy similarity1
Binding sitei161ATPBy similarity1
Binding sitei165ATPBy similarity1
Binding sitei512AgonistBy similarity1
Binding sitei550AgonistBy 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>Sitei557Important for agonist bindingBy similarity1
<p>This subsection of the ‘Function’ 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 bindingi647Calcium; shared with neighboring subunitsBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi200 – 203ATPBy similarity4
Nucleotide bindingi211 – 212ATPBy similarity2

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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q8NER1

Protein family/group databases

Transport Classification Database

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TCDBi
1.A.4.2.13 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_and_taxonomy_section">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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 17

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000196689.11

Human Gene Nomenclature Database

More...
HGNCi
HGNC:12716 TRPV1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
602076 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q8NER1

<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; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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 – 433CytoplasmicBy similarityAdd BLAST433
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Transmembranei434 – 454HelicalBy similarityAdd BLAST21
Topological domaini455 – 471ExtracellularBy similarityAdd BLAST17
Transmembranei472 – 497HelicalBy similarityAdd BLAST26
Topological domaini498 – 510CytoplasmicBy similarityAdd BLAST13
Transmembranei511 – 531HelicalBy similarityAdd BLAST21
Topological domaini532 – 535ExtracellularBy similarity4
Transmembranei536 – 556HelicalBy similarityAdd BLAST21
Topological domaini557 – 571CytoplasmicBy similarityAdd BLAST15
Transmembranei572 – 599HelicalBy similarityAdd BLAST28
Topological domaini600 – 658ExtracellularBy similarityAdd BLAST59
Transmembranei659 – 687HelicalBy similarityAdd BLAST29
Topological domaini688 – 839CytoplasmicBy similarityAdd 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_and_biotech_section">'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>Mutagenesisi511Y → A: Loss of sensitivity to capsaicin. 1 Publication1
Mutagenesisi550T → I: Reduces sensitivity to capsaicin 40-fold. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
7442

Open Targets

More...
OpenTargetsi
ENSG00000196689

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA37329

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4794

Drug and drug target database

More...
DrugBanki
DB00316 Acetaminophen
DB00132 Alpha-Linolenic Acid
DB00168 Aspartame
DB06774 Capsaicin
DB00159 Icosapent

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
507

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
TRPV1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
296452849

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002153381 – 839Transient receptor potential cation channel subfamily V member 1Add BLAST839

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 residuei117Phosphoserine; by PKA and PKDBy similarity1
Modified residuei145Phosphothreonine; by PKA; in vitroBy similarity1
Modified residuei371Phosphothreonine; by PKA; in vitroBy similarity1
Modified residuei502Phosphoserine; by PKC/PRKCEBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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...) asparagineBy similarity1
Modified residuei705PhosphothreonineBy similarity1
Modified residuei775PhosphoserineBy similarity1
Modified residuei801Phosphoserine; by PKC/PRKCE and PKC/PRKCZBy similarity1
Modified residuei821PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-117 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.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

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

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PaxDbi
Q8NER1

PeptideAtlas

More...
PeptideAtlasi
Q8NER1

PRoteomics IDEntifications database

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PRIDEi
Q8NER1

ProteomicsDB human proteome resource

More...
ProteomicsDBi
73202

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8NER1

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

More...
PhosphoSitePlusi
Q8NER1

<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

Widely expressed at low levels. Expression is elevated in dorsal root ganglia. In skin, expressed in cutaneous sensory nerve fibers, mast cells, epidermal keratinocytes, dermal blood vessels, the inner root sheet and the infundibulum of hair follicles, differentiated sebocytes, sweat gland ducts, and the secretory portion of eccrine sweat glands (at protein level).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000196689 Expressed in 140 organ(s), highest expression level in brain

CleanEx database of gene expression profiles

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CleanExi
HS_TRPV1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q8NER1 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8NER1 HS

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with PIRT (By similarity). Homotetramer (By similarity). Interacts with TRPV3 and may also form a heteromeric channel with TRPV3 (PubMed:12077606). Interacts with CALM, PRKCM and CSK. Interacts with PRKCG and NTRK1, probably by forming a trimeric complex (By similarity). Interacts with the Scolopendra mutilans RhTx toxin (By similarity). Interacts with TMEM100 (By similarity).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113281, 8 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000459962

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q8NER1

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q8NER1

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

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SMRi
Q8NER1

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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>Repeati111 – 153ANK 1Add BLAST43
Repeati154 – 200ANK 2Add BLAST47
Repeati201 – 247ANK 3Add BLAST47
Repeati248 – 283ANK 4Add BLAST36
Repeati284 – 332ANK 5Add BLAST49
Repeati333 – 359ANK 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>Regioni115 – 116Important for channel activation by agonists and heatBy similarity2
Regioni685 – 713ADBy similarityAdd BLAST29
Regioni768 – 802Interaction with calmodulinBy similarityAdd BLAST35
Regioni778 – 793Required for PIP2-mediated channel inhibitionBy similarityAdd 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>Motifi644 – 647Selectivity filterBy similarity4

<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.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, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3676 Eukaryota
ENOG4110DG4 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000160870

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234630

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG054085

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8NER1

KEGG Orthology (KO)

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KOi
K05222

Database for complete collections of gene phylogenies

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PhylomeDBi
Q8NER1

TreeFam database of animal gene trees

More...
TreeFami
TF314711

Family and domain databases

Conserved Domains Database

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CDDi
cd00204 ANK, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.40.20, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
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

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PRINTSi
PR01768 TRPVRECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00248 ANK, 4 hits

Superfamily database of structural and functional annotation

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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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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 2 <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

This entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q8NER1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MKKWSSTDLG AAADPLQKDT CPDPLDGDPN SRPPPAKPQL STAKSRTRLF
60 70 80 90 100
GKGDSEEAFP VDCPHEEGEL DSCPTITVSP VITIQRPGDG PTGARLLSQD
110 120 130 140 150
SVAASTEKTL RLYDRRSIFE AVAQNNCQDL ESLLLFLQKS KKHLTDNEFK
160 170 180 190 200
DPETGKTCLL KAMLNLHDGQ NTTIPLLLEI ARQTDSLKEL VNASYTDSYY
210 220 230 240 250
KGQTALHIAI ERRNMALVTL LVENGADVQA AAHGDFFKKT KGRPGFYFGE
260 270 280 290 300
LPLSLAACTN QLGIVKFLLQ NSWQTADISA RDSVGNTVLH ALVEVADNTA
310 320 330 340 350
DNTKFVTSMY NEILMLGAKL HPTLKLEELT NKKGMTPLAL AAGTGKIGVL
360 370 380 390 400
AYILQREIQE PECRHLSRKF TEWAYGPVHS SLYDLSCIDT CEKNSVLEVI
410 420 430 440 450
AYSSSETPNR HDMLLVEPLN RLLQDKWDRF VKRIFYFNFL VYCLYMIIFT
460 470 480 490 500
MAAYYRPVDG LPPFKMEKTG DYFRVTGEIL SVLGGVYFFF RGIQYFLQRR
510 520 530 540 550
PSMKTLFVDS YSEMLFFLQS LFMLATVVLY FSHLKEYVAS MVFSLALGWT
560 570 580 590 600
NMLYYTRGFQ QMGIYAVMIE KMILRDLCRF MFVYIVFLFG FSTAVVTLIE
610 620 630 640 650
DGKNDSLPSE STSHRWRGPA CRPPDSSYNS LYSTCLELFK FTIGMGDLEF
660 670 680 690 700
TENYDFKAVF IILLLAYVIL TYILLLNMLI ALMGETVNKI AQESKNIWKL
710 720 730 740 750
QRAITILDTE KSFLKCMRKA FRSGKLLQVG YTPDGKDDYR WCFRVDEVNW
760 770 780 790 800
TTWNTNVGII NEDPGNCEGV KRTLSFSLRS SRVSGRHWKN FALVPLLREA
810 820 830
SARDRQSAQP EEVYLRQFSG SLKPEDAEVF KSPAASGEK
Length:839
Mass (Da):94,956
Last modified:May 18, 2010 - v2
<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:i7142F59D428827FB
GO
Isoform 2 (identifier: Q8NER1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-150: MKKWSSTDLG...KKHLTDNEFK → METLTPGHLQ...ACPDPPLCLS

Show »
Length:837
Mass (Da):94,211
Checksum:iD662DD6094BDCA56
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 are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EQ78E7EQ78_HUMAN
Transient receptor potential cation...
TRPV1
850Annotation 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>
I3L1R6I3L1R6_HUMAN
Transient receptor potential cation...
TRPV1
829Annotation 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>
E7ESJ2E7ESJ2_HUMAN
Transient receptor potential cation...
TRPV1
779Annotation 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>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAG43467 differs from that shown. Reason: Frameshift at position 498.Curated

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 conflicti336T → M in CAB89866 (PubMed:11226139).Curated1
Sequence conflicti552M → V in ABA06605 (Ref. 5) 1 Publication1

Natural variant

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_05730791P → S1 PublicationCorresponds to variant dbSNP:rs222749Ensembl.1
Natural variantiVAR_071244315M → I8 PublicationsCorresponds to variant dbSNP:rs222747Ensembl.1
Natural variantiVAR_057308469T → I2 PublicationsCorresponds to variant dbSNP:rs224534Ensembl.1
Natural variantiVAR_057309505T → A. Corresponds to variant dbSNP:rs17633288Ensembl.1
Natural variantiVAR_022246585I → V2 PublicationsCorresponds to variant dbSNP:rs8065080Ensembl.1

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. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0568621 – 150MKKWS…DNEFK → METLTPGHLQPSPSSPRPRA APGSLGRVTRRRLSRWIALT RKVSWTPARPSQSALLSPSR GQETAPPVPGCCPRTLSPPA PRRPSGSMIAGVSLKPLLRI TARIWRACCSSCRRARSTSQ TTSSKVAPALGSGRAPALAC PDPPLCLS in isoform 2. 1 PublicationAdd BLAST150

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ277028 mRNA Translation: CAB95729.1
AF196175 mRNA Translation: AAG43466.1
AF196176 mRNA Translation: AAG43467.1 Frameshift.
AJ272063 mRNA Translation: CAB89866.2
AY131289 mRNA Translation: AAM89472.1
DQ177332 mRNA Translation: ABA06605.1
AL136801 mRNA Translation: CAB66735.1
AC027796 Genomic DNA No translation available.
CH471108 Genomic DNA Translation: EAW90497.1
BC132820 mRNA Translation: AAI32821.1
BC136633 mRNA Translation: AAI36634.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS45576.1 [Q8NER1-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
JC7621

NCBI Reference Sequences

More...
RefSeqi
NP_061197.4, NM_018727.5 [Q8NER1-1]
NP_542435.2, NM_080704.3 [Q8NER1-1]
NP_542436.2, NM_080705.3 [Q8NER1-1]
NP_542437.2, NM_080706.3 [Q8NER1-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.579217
Hs.655380

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000399756; ENSP00000382659; ENSG00000196689 [Q8NER1-1]
ENST00000399759; ENSP00000382661; ENSG00000196689 [Q8NER1-1]
ENST00000571088; ENSP00000461007; ENSG00000196689 [Q8NER1-1]
ENST00000572705; ENSP00000459962; ENSG00000196689 [Q8NER1-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7442

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7442

UCSC genome browser

More...
UCSCi
uc010vrr.3 human [Q8NER1-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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_references_section">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

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ277028 mRNA Translation: CAB95729.1
AF196175 mRNA Translation: AAG43466.1
AF196176 mRNA Translation: AAG43467.1 Frameshift.
AJ272063 mRNA Translation: CAB89866.2
AY131289 mRNA Translation: AAM89472.1
DQ177332 mRNA Translation: ABA06605.1
AL136801 mRNA Translation: CAB66735.1
AC027796 Genomic DNA No translation available.
CH471108 Genomic DNA Translation: EAW90497.1
BC132820 mRNA Translation: AAI32821.1
BC136633 mRNA Translation: AAI36634.1
CCDSiCCDS45576.1 [Q8NER1-1]
PIRiJC7621
RefSeqiNP_061197.4, NM_018727.5 [Q8NER1-1]
NP_542435.2, NM_080704.3 [Q8NER1-1]
NP_542436.2, NM_080705.3 [Q8NER1-1]
NP_542437.2, NM_080706.3 [Q8NER1-1]
UniGeneiHs.579217
Hs.655380

3D structure databases

ProteinModelPortaliQ8NER1
SMRiQ8NER1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113281, 8 interactors
STRINGi9606.ENSP00000459962

Chemistry databases

BindingDBiQ8NER1
ChEMBLiCHEMBL4794
DrugBankiDB00316 Acetaminophen
DB00132 Alpha-Linolenic Acid
DB00168 Aspartame
DB06774 Capsaicin
DB00159 Icosapent
GuidetoPHARMACOLOGYi507

Protein family/group databases

TCDBi1.A.4.2.13 the transient receptor potential ca(2+) channel (trp-cc) family

PTM databases

iPTMnetiQ8NER1
PhosphoSitePlusiQ8NER1

Polymorphism and mutation databases

BioMutaiTRPV1
DMDMi296452849

Proteomic databases

PaxDbiQ8NER1
PeptideAtlasiQ8NER1
PRIDEiQ8NER1
ProteomicsDBi73202

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7442
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000399756; ENSP00000382659; ENSG00000196689 [Q8NER1-1]
ENST00000399759; ENSP00000382661; ENSG00000196689 [Q8NER1-1]
ENST00000571088; ENSP00000461007; ENSG00000196689 [Q8NER1-1]
ENST00000572705; ENSP00000459962; ENSG00000196689 [Q8NER1-1]
GeneIDi7442
KEGGihsa:7442
UCSCiuc010vrr.3 human [Q8NER1-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7442
DisGeNETi7442
EuPathDBiHostDB:ENSG00000196689.11

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TRPV1

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0013428
HIX0079948
HGNCiHGNC:12716 TRPV1
MIMi602076 gene
neXtProtiNX_Q8NER1
OpenTargetsiENSG00000196689
PharmGKBiPA37329

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3676 Eukaryota
ENOG4110DG4 LUCA
GeneTreeiENSGT00940000160870
HOGENOMiHOG000234630
HOVERGENiHBG054085
InParanoidiQ8NER1
KOiK05222
PhylomeDBiQ8NER1
TreeFamiTF314711

Enzyme and pathway databases

ReactomeiR-HSA-3295583 TRP channels
SIGNORiQ8NER1

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
TRPV1

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

More...
GenomeRNAii
7442

Protein Ontology

More...
PROi
PR:Q8NER1

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000196689 Expressed in 140 organ(s), highest expression level in brain
CleanExiHS_TRPV1
ExpressionAtlasiQ8NER1 baseline and differential
GenevisibleiQ8NER1 HS

Family and domain databases

CDDicd00204 ANK, 1 hit
Gene3Di1.25.40.20, 1 hit
InterProiView protein in InterPro
IPR002110 Ankyrin_rpt
IPR020683 Ankyrin_rpt-contain_dom
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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_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: Q8NER1
Secondary accession number(s): A2RUA9
, Q3LU47, Q9H0G9, Q9H303, Q9H304, Q9NQ74, Q9NY22
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: May 18, 2010
Last modified: December 5, 2018
This is version 149 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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