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Protein

Transient receptor potential cation channel subfamily V member 4

Gene

Trpv4

Organism
Mus musculus (Mouse)
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

Non-selective calcium permeant cation channel involved in osmotic sensitivity and mechanosensitivity (PubMed:11094154). Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:12093812, PubMed:14691263, PubMed:16368742, PubMed:16571723). Also activated by heat, low pH, citrate and phorbol esters (PubMed:14691263). Increase of intracellular Ca2+ potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism (By similarity). Acts as a regulator of intracellular Ca2+ in synoviocytes (By similarity). Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8 (By similarity). Together with PKD2, forms mechano- and thermosensitive channels in cilium (PubMed:18695040). Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers (PubMed:20413591). Negatively regulates expression of PPARGC1A, UCP1, oxidative metabolism and respiration in adipocytes (PubMed:23021218). Regulates expression of chemokines and cytokines related to proinflammatory pathway in adipocytes (PubMed:23021218). Together with AQP5, controls regulatory volume decrease in salivary epithelial cells (PubMed:16571723). Required for normal development and maintenance of bone and cartilage (By similarity).By similarity9 Publications

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 sitei192ATPBy similarity1
Binding sitei197ATPBy similarity1
Binding sitei201ATPBy similarity1
Binding sitei248ATPBy similarity1
Binding sitei344Phosphatidylinositol-1,4,5-trisphosphateBy 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 bindingi682Calcium; 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 bindingi236 – 239ATPBy similarity4

<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, Lipid-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-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_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 4
Short name:
TrpV4
Alternative name(s):
Osm-9-like TRP channel 4
Short name:
OTRPC4
Transient receptor potential protein 12
Short name:
TRP12
Vanilloid receptor-like channel 2
Vanilloid receptor-like protein 2
Vanilloid receptor-related osmotically-activated channel1 Publication
Short name:
VR-OAC1 Publication
<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:Trpv4
Synonyms:Trp12, Vrl2, Vroac
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1926945 Trpv4

<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 – 469CytoplasmicBy similarityAdd BLAST469
<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>Transmembranei470 – 490HelicalBy similarityAdd BLAST21
Topological domaini491 – 507ExtracellularBy similarityAdd BLAST17
Transmembranei508 – 534HelicalBy similarityAdd BLAST27
Topological domaini535 – 547CytoplasmicBy similarityAdd BLAST13
Transmembranei548 – 568HelicalBy similarityAdd BLAST21
Topological domaini569 – 572ExtracellularBy similarity4
Transmembranei573 – 593HelicalBy similarityAdd BLAST21
Topological domaini594 – 608CytoplasmicBy similarityAdd BLAST15
Transmembranei609 – 636HelicalBy similarityAdd BLAST28
Topological domaini637 – 665ExtracellularBy similarityAdd BLAST29
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'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>Intramembranei666 – 685Pore-formingBy similarityAdd BLAST20
Topological domaini686 – 693ExtracellularBy similarity8
Transmembranei694 – 722HelicalBy similarityAdd BLAST29
Topological domaini723 – 871CytoplasmicBy similarityAdd BLAST149

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cilium, Membrane

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

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mice display impairment of the intercellular junction-dependent barrier function in the skin (PubMed:20413591). Increased energy expenditure and improved insulin sensitivity in white adipose tissues (PubMed:23021218). Reduced Ca2+ entry and loss of regulatory volume decrease in response to hypotonicity in acinar cells (PubMed:16571723).3 Publications

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>Mutagenesisi110Y → F: Increases protein abundance at plasma membrane. Greatly reduces channel activity. 1 Publication1
Mutagenesisi142 – 143PP → AL: Strongly reduced interaction with PACSIN3. 1 Publication2
Mutagenesisi253Y → F: Results are conflicting as to whether hypotonicity-dependent channel activity is abolished. 2 Publications1
Mutagenesisi556Y → A: Reduces channel activation by 4-alpha-PDD and heat but not hypo-osmotic cell swelling. 1 Publication1
Mutagenesisi556Y → F: No changes in channel activation by 4-alpha-PDD or heat. 1 Publication1
Mutagenesisi557S → A: No changes in channel activity. 1 Publication1
Mutagenesisi651N → Q: Loss of a probable N-glycosylation site. Increased expression at the cell membrane, leading to increased ion currents. 1 Publication1
Mutagenesisi672D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-682. 1 Publication1
Mutagenesisi675K → A: No effect on channel pore properties. 1 Publication1
Mutagenesisi680M → A: Impairs Ca(2+) permeation. 1 Publication1
Mutagenesisi682D → A: Greatly reduces Ca(2+) permeation and channel rectification; when associated with A-672. 1 Publication1
Mutagenesisi805Y → F: No changes in channel activity. 1 Publication1
Mutagenesisi824S → A: Loss of phosphorylation but no significant effect on channel activity. 1 Publication1
Mutagenesisi824S → D: Phosphomimetic mutant which enhances channel function. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL6126

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
510

<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_00002153481 – 871Transient receptor potential cation channel subfamily V member 4Add BLAST871

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 residuei110Phosphotyrosine; by SRC-type Tyr-kinases1 Publication1
Modified residuei253Phosphotyrosine; by LYN1 Publication1
<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>Glycosylationi651N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei805Phosphotyrosine; by SRC-type Tyr-kinases1 Publication1
Modified residuei824Phosphoserine; by PKC and PKA1 Publication1

<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

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9EPK8

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9EPK8

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

More...
PaxDbi
Q9EPK8

PRoteomics IDEntifications database

More...
PRIDEi
Q9EPK8

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9EPK8

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

More...
PhosphoSitePlusi
Q9EPK8

<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

Detected in liver, kidney, heart, brain cortex, cerebellum and brainstem (at protein level). Expressed in salivary glands (at protein level) (PubMed:16571723). Expressed in heart, lung, spleen, liver, kidney, brain, skeletal muscle and testis. In the central nervous system, expressed in the lamina terminalis (arched vascular organ and neurons of the subfornical organ), median preoptic area, ventral hippocampal commissure, and ependymal cells of the choroid plexus. In the cochlea, expressed in both inner and outer hair cells, and in marginal cells of the cochlear stria vascularis. Expressed in large neurons of the trigeminal ganglion. In the kidney cortex, strongly expressed by epithelial cells of tubules and much weaker in glomeruli.6 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000014158 Expressed in 141 organ(s), highest expression level in intervertebral disk of lumbar vertebra

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9EPK8 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9EPK8 MM

<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

Homotetramer. Interacts with calmodulin (By similarity). Interacts with CTNNB1 (PubMed:20413591). The TRPV4 and CTNNB1 complex can interact with CDH1 (PubMed:20413591). Part of a complex containing MLC1, AQP4, HEPACAM and ATP1B1 (By similarity). Interacts with MAP7 and Src family Tyr protein kinases LYN, SRC, FYN, HCK, LCK and YES (PubMed:14517216, PubMed:12538589). Interacts with PACSIN1, PACSIN2 and PACSIN3 (via SH3 domain) (PubMed:16627472, PubMed:18174177). Interacts with ITPR3 (By similarity). Interacts with AQP5; the interaction is probably indirect and regulates TRPV4 activation by hypotonicity (PubMed:16571723). Interacts with ANO1 (PubMed:24509911). Interacts (via C-terminus) with PKD2 (via C-terminus) (PubMed:18695040).By similarity8 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

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DIPi
DIP-44011N

Protein interaction database and analysis system

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IntActi
Q9EPK8, 3 interactors

Molecular INTeraction database

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MINTi
Q9EPK8

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000071859

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q9EPK8

<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

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ProteinModelPortali
Q9EPK8

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

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SMRi
Q9EPK8

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>Repeati237 – 266ANK 1Add BLAST30
Repeati284 – 313ANK 2Add BLAST30
Repeati369 – 398ANK 3Add 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>Regioni249 – 251Phosphatidylinositol-1,4,5-trisphosphate bindingBy similarity3
Regioni296 – 299Phosphatidylinositol-1,4,5-trisphosphate bindingBy similarity4
Regioni812 – 831Interaction with calmodulin and ITPR3By similarityAdd BLAST20

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>Motifi679 – 682Selectivity filter1 Publication4

<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 ANK repeat region mediates interaction with Ca2+-calmodulin and ATP binding. The ANK repeat region mediates interaction with phosphatidylinositol-4,5-bisphosphate and related phosphatidylinositides.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

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eggNOGi
KOG3676 Eukaryota
ENOG4110DG4 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000158615

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000234630

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG054085

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9EPK8

KEGG Orthology (KO)

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KOi
K04973

Identification of Orthologs from Complete Genome Data

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OMAi
GDLEMIN

Database of Orthologous Groups

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OrthoDBi
693004at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9EPK8

TreeFam database of animal gene trees

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TreeFami
TF314711

Family and domain databases

Conserved Domains Database

More...
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
IPR008347 TRPV1-4_channel
IPR008348 TRPV4_channel

The PANTHER Classification System

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PANTHERi
PTHR10582 PTHR10582, 1 hit
PTHR10582:SF4 PTHR10582:SF4, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00023 Ank, 1 hit
PF00520 Ion_trans, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01768 TRPVRECEPTOR
PR01769 VRL2RECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00248 ANK, 3 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48403 SSF48403, 1 hit

PROSITE; a protein domain and family database

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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>Sequence (1+)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 has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All

Q9EPK8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADPGDGPRA APGEVAEPPG DESGTSGGEA FPLSSLANLF EGEEGSSSLS
60 70 80 90 100
PVDASRPAGP GDGRPNLRMK FQGAFRKGVP NPIDLLESTL YESSVVPGPK
110 120 130 140 150
KAPMDSLFDY GTYRHHPSDN KRWRRKVVEK QPQSPKAPAP QPPPILKVFN
160 170 180 190 200
RPILFDIVSR GSTADLDGLL SFLLTHKKRL TDEEFREPST GKTCLPKALL
210 220 230 240 250
NLSNGRNDTI PVLLDIAERT GNMREFINSP FRDIYYRGQT SLHIAIERRC
260 270 280 290 300
KHYVELLVAQ GADVHAQARG RFFQPKDEGG YFYFGELPLS LAACTNQPHI
310 320 330 340 350
VNYLTENPHK KADMRRQDSR GNTVLHALVA IADNTRENTK FVTKMYDLLL
360 370 380 390 400
LKCSRLFPDS NLETVLNNDG LSPLMMAAKT GKIGVFQHII RREVTDEDTR
410 420 430 440 450
HLSRKFKDWA YGPVYSSLYD LSSLDTCGEE VSVLEILVYN SKIENRHEML
460 470 480 490 500
AVEPINELLR DKWRKFGAVS FYINVVSYLC AMVIFTLTAY YQPLEGTPPY
510 520 530 540 550
PYRTTVDYLR LAGEVITLFT GVLFFFTSIK DLFTKKCPGV NSLFVDGSFQ
560 570 580 590 600
LLYFIYSVLV VVSAALYLAG IEAYLAVMVF ALVLGWMNAL YFTRGLKLTG
610 620 630 640 650
TYSIMIQKIL FKDLFRFLLV YLLFMIGYAS ALVTLLNPCT NMKVCDEDQS
660 670 680 690 700
NCTVPTYPAC RDSETFSAFL LDLFKLTIGM GDLEMLSSAK YPVVFILLLV
710 720 730 740 750
TYIILTFVLL LNMLIALMGE TVGQVSKESK HIWKLQWATT ILDIERSFPV
760 770 780 790 800
FLRKAFRSGE MVTVGKSSDG TPDRRWCFRV DEVNWSHWNQ NLGIINEDPG
810 820 830 840 850
KSEIYQYYGF SHTVGRLRRD RWSSVVPRVV ELNKNSSADE VVVPLDNLGN
860 870
PNCDGHQQGY APKWRTDDAP L
Length:871
Mass (Da):98,027
Last modified:March 1, 2001 - 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:i5BAC6E33F89CEA05
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
D3Z1H7D3Z1H7_MOUSE
Transient receptor potential cation...
Trpv4
811Annotation 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>
D3Z1H6D3Z1H6_MOUSE
Transient receptor potential cation...
Trpv4
764Annotation 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>
E9Q7L7E9Q7L7_MOUSE
Transient receptor potential cation...
Trpv4
824Annotation 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>

<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 AAG28028 differs from that shown. Reason: Frameshift at positions 47, 50, 53, 72 and 73.Curated
The sequence AAK69486 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.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 conflicti45G → S in AAG28028 (PubMed:11081638).Curated1
Sequence conflicti90L → R in AAG17543 (PubMed:11025659).Curated1
Sequence conflicti90L → R in AAK69486 (Ref. 5) Curated1
Sequence conflicti137A → T in BAA83731 (PubMed:12692122).Curated1
Sequence conflicti210 – 211IP → LQ in BAA83731 (PubMed:12692122).Curated2
Sequence conflicti477S → P in AAG28028 (PubMed:11081638).Curated1
Sequence conflicti784N → S in BAA83731 (PubMed:12692122).Curated1

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
AF263522 mRNA Translation: AAG28028.1 Frameshift.
AJ296078 mRNA Translation: CAC20703.1
AF208026 mRNA Translation: AAG17543.1
AB021875 mRNA Translation: BAA83731.2
AF279672 mRNA Translation: AAK69486.1 Different initiation.
BC127052 mRNA Translation: AAI27053.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS19568.1

NCBI Reference Sequences

More...
RefSeqi
NP_071300.2, NM_022017.3
XP_006530495.2, XM_006530432.2

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Mm.266450

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000071968; ENSMUSP00000071859; ENSMUSG00000014158
ENSMUST00000112225; ENSMUSP00000107844; ENSMUSG00000014158

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
63873

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:63873

UCSC genome browser

More...
UCSCi
uc008yzu.1 mouse

<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
AF263522 mRNA Translation: AAG28028.1 Frameshift.
AJ296078 mRNA Translation: CAC20703.1
AF208026 mRNA Translation: AAG17543.1
AB021875 mRNA Translation: BAA83731.2
AF279672 mRNA Translation: AAK69486.1 Different initiation.
BC127052 mRNA Translation: AAI27053.1
CCDSiCCDS19568.1
RefSeqiNP_071300.2, NM_022017.3
XP_006530495.2, XM_006530432.2
UniGeneiMm.266450

3D structure databases

ProteinModelPortaliQ9EPK8
SMRiQ9EPK8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-44011N
IntActiQ9EPK8, 3 interactors
MINTiQ9EPK8
STRINGi10090.ENSMUSP00000071859

Chemistry databases

BindingDBiQ9EPK8
ChEMBLiCHEMBL6126
GuidetoPHARMACOLOGYi510

PTM databases

iPTMnetiQ9EPK8
PhosphoSitePlusiQ9EPK8

Proteomic databases

jPOSTiQ9EPK8
MaxQBiQ9EPK8
PaxDbiQ9EPK8
PRIDEiQ9EPK8

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000071968; ENSMUSP00000071859; ENSMUSG00000014158
ENSMUST00000112225; ENSMUSP00000107844; ENSMUSG00000014158
GeneIDi63873
KEGGimmu:63873
UCSCiuc008yzu.1 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
59341
MGIiMGI:1926945 Trpv4

Phylogenomic databases

eggNOGiKOG3676 Eukaryota
ENOG4110DG4 LUCA
GeneTreeiENSGT00940000158615
HOGENOMiHOG000234630
HOVERGENiHBG054085
InParanoidiQ9EPK8
KOiK04973
OMAiGDLEMIN
OrthoDBi693004at2759
PhylomeDBiQ9EPK8
TreeFamiTF314711

Enzyme and pathway databases

ReactomeiR-MMU-3295583 TRP channels

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q9EPK8

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000014158 Expressed in 141 organ(s), highest expression level in intervertebral disk of lumbar vertebra
ExpressionAtlasiQ9EPK8 baseline and differential
GenevisibleiQ9EPK8 MM

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
IPR008347 TRPV1-4_channel
IPR008348 TRPV4_channel
PANTHERiPTHR10582 PTHR10582, 1 hit
PTHR10582:SF4 PTHR10582:SF4, 1 hit
PfamiView protein in Pfam
PF00023 Ank, 1 hit
PF00520 Ion_trans, 1 hit
PRINTSiPR01768 TRPVRECEPTOR
PR01769 VRL2RECEPTOR
SMARTiView protein in SMART
SM00248 ANK, 3 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 nameiTRPV4_MOUSE
<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: Q9EPK8
Secondary accession number(s): A0JNY0
, Q91XR5, Q9EQZ4, Q9ERZ7, Q9ES76
<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: March 1, 2001
Last modified: January 16, 2019
This is version 147 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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