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Entry version 36 (25 May 2022)
Sequence version 1 (30 Nov 2016)
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Protein

Transient receptor potential cation channel subfamily V member 4

Gene

TRPV4

Organism
Gallus gallus (Chicken)
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:11081638).

Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification (PubMed:11081638).

Also activated by phorbol esters (PubMed:19864432).

Channel activity seems to be regulated by a calmodulin-dependent mechanism (By similarity).

By similarity2 Publications

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

ATP binding enhances channel sensitivity to agonists. Ca2+-calmodulin prevents the ATP-mediated increased sensitivity to agonists.1 Publication

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 sitei178ATPBy similarity1
Binding sitei183ATPBy similarity1
Binding sitei187ATPBy similarity1
Binding sitei234ATPBy similarity1
Binding sitei330Phosphatidylinositol 4,5-bisphosphateCombined 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 bindingi668Calcium; 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 bindingi222 – 225ATPBy 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

<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 4
Short name:
TrpV4
Alternative name(s):
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%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:TRPV4
<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>OrganismiGallus gallus (Chicken)Imported
<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 identifieri9031 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<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
  • UP000000539 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<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 – 455CytoplasmicBy similarityAdd BLAST455
<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>Transmembranei456 – 476HelicalBy similarityAdd BLAST21
Topological domaini477 – 493ExtracellularBy similarityAdd BLAST17
Transmembranei494 – 520HelicalBy similarityAdd BLAST27
Topological domaini521 – 533CytoplasmicBy similarityAdd BLAST13
Transmembranei534 – 554HelicalBy similarityAdd BLAST21
Topological domaini555 – 558ExtracellularBy similarity4
Transmembranei559 – 579HelicalBy similarityAdd BLAST21
Topological domaini580 – 594CytoplasmicBy similarityAdd BLAST15
Transmembranei595 – 622HelicalBy similarityAdd BLAST28
Topological domaini623 – 651ExtracellularBy similarityAdd BLAST29
<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>Intramembranei652 – 671Pore-formingBy similarityAdd BLAST20
Topological domaini672 – 679ExtracellularBy similarity8
Transmembranei680 – 708HelicalBy similarityAdd BLAST29
Topological domaini709 – 852CytoplasmicBy similarityAdd BLAST144

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane

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

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>Mutagenesisi178K → A: Strongly decreased affinity for ATP and Ca(2+)-calmodulin. Abolishes ATP-mediated increase in channel sensitivity to agonists. 1 Publication1
Mutagenesisi183K → A: Strongly decreased affinity for ATP and slightly decreased affinity for Ca(2+)-calmodulin. 1 Publication1
Mutagenesisi205K → A: No significant effect on affinity for ATP and Ca(2+)-calmodulin. 1 Publication1

<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_00004434811 – 852Transient receptor potential cation channel subfamily V member 4Add BLAST852

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

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

Homotetramer (By similarity).

Interacts with Ca2+-calmodulin (PubMed:19864432).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000008256

<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

1852
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
A0A1D5PXA5

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

More...
SMRi
A0A1D5PXA5

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati223 – 252ANK 1Sequence analysisAdd BLAST30
Repeati270 – 299ANK 2Sequence analysisAdd BLAST30
Repeati355 – 387ANK 3Sequence analysisAdd BLAST33

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>Regioni30 – 51DisorderedSequence analysisAdd BLAST22
Regioni235 – 237Phosphatidylinositol 4,5-bisphosphate bindingCombined sources1 Publication3
Regioni282 – 285Phosphatidylinositol 4,5-bisphosphate bindingCombined sources1 Publication4

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>Motifi665 – 668Selectivity 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 ANK repeat region mediates interaction with Ca2+-calmodulin and ATP binding (PubMed:19864432). The ANK repeat region mediates interaction with phosphatidylinositol-4,5-bisphosphate and related phosphatidylinositides (PubMed:25256292).2 Publications

<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

Database of Orthologous Groups

More...
OrthoDBi
693004at2759

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
IPR008347, TrpV1-4
IPR008348, TrpV4

The PANTHER Classification System

More...
PANTHERi
PTHR10582, PTHR10582, 1 hit
PTHR10582:SF4, PTHR10582:SF4, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01768, TRPVRECEPTOR
PR01769, VRL2RECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00248, ANK, 3 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>Sequencei

<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.

A0A1D5PXA5-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADPEDPRDA GDVLGDDSFP LSSLANLFEV EDTPSPAEPS RGPPGAVDGK
60 70 80 90 100
QNLRMKFHGA FRKGPPKPME LLESTIYESS VVPAPKKAPM DSLFDYGTYR
110 120 130 140 150
QHPSENKRWR RRVVEKPVAG TKGPAPNPPP ILKVFNRPIL FDIVSRGSPD
160 170 180 190 200
GLEGLLSFLL THKKRLTDEE FREPSTGKTC LPKALLNLSA GRNDTIPILL
210 220 230 240 250
DIAEKTGNMR EFINSPFRDV YYRGQTALHI AIERRCKHYV ELLVEKGADV
260 270 280 290 300
HAQARGRFFQ PKDEGGYFYF GELPLSLAAC TNQPHIVHYL TENGHKQADL
310 320 330 340 350
RRQDSRGNTV LHALVAIADN TRENTKFVTK MYDLLLIKCA KLFPDTNLEA
360 370 380 390 400
LLNNDGLSPL MMAAKTGKIG IFQHIIRREI ADEDVRHLSR KFKDWAYGPV
410 420 430 440 450
YSSLYDLSSL DTCGEEVSVL EILVYNSKIE NRHEMLAVEP INELLRDKWR
460 470 480 490 500
KFGAVSFYIS VVSYLCAMII FTLIAYYRPM EGPPPYPYTT TIDYLRLAGE
510 520 530 540 550
IITLLTGILF FFSNIKDLFM KKCPGVNSFF IDGSFQLLYF IYSVLVIVTA
560 570 580 590 600
GLYLGGVEAY LAVMVFALVL GWMNALYFTR GLKLTGTYSI MIQKILFKDL
610 620 630 640 650
FRFLLVYLLF MIGYASALVS LLNPCPSSES CSEDHSNCTL PTYPSCRDSQ
660 670 680 690 700
TFSTFLLDLF KLTIGMGDLE MLESAKYPGV FIILLVTYII LTFVLLLNML
710 720 730 740 750
IALMGETVGQ VSKESKHIWK LQWATTILDI ERSFPLFLRR VFRSGEMVTV
760 770 780 790 800
GKGTDGTPDR RWCFRVDEVN WSHWNQNLGI ISEDPGKSDT YQYYGFSHTV
810 820 830 840 850
GRLRRDRWST VVPRVVELNK SCPTEDVVVP LGTMGTAEAR ERRHGQTPSS

PL
Length:852
Mass (Da):96,282
Last modified:November 30, 2016 - 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:i0A799C76C6598845
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 conflicti47V → G in AAG28026 (PubMed:11081638).Curated1
Sequence conflicti131I → V in AAG28026 (PubMed:11081638).Curated1
Sequence conflicti741V → A in AAG28026 (PubMed:11081638).Curated1

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
AF261883 mRNA Translation: AAG28026.1
AADN04000193 Genomic DNA No translation available.

NCBI Reference Sequences

More...
RefSeqi
NP_990023.1, NM_204692.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
395427

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gga:395427

<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
AF261883 mRNA Translation: AAG28026.1
AADN04000193 Genomic DNA No translation available.
RefSeqiNP_990023.1, NM_204692.1

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
3JXIX-ray2.30A/B/C/D133-382[»]
3JXJX-ray2.80A/B133-382[»]
3W9FX-ray1.90A/B/C/D133-382[»]
3W9GX-ray2.00A/B/C/D133-382[»]
6F55NMR-B121-135[»]
AlphaFoldDBiA0A1D5PXA5
SMRiA0A1D5PXA5
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000008256

Genome annotation databases

GeneIDi395427
KEGGigga:395427

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
59341

Phylogenomic databases

eggNOGiKOG3676, Eukaryota
OrthoDBi693004at2759

Miscellaneous databases

Protein Ontology

More...
PROi
PR:A0A1D5PXA5

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
IPR008347, TrpV1-4
IPR008348, TrpV4
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

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 nameiTRPV4_CHICK
<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: A0A1D5PXA5
Secondary accession number(s): Q9DFS3
<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: March 28, 2018
Last sequence update: November 30, 2016
Last modified: May 25, 2022
This is version 36 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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