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Entry version 143 (26 Feb 2020)
Sequence version 2 (01 Jul 1989)
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Protein

Villin-1

Gene

VIL1

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

Epithelial cell-specific Ca2+-regulated actin-modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair (By similarity). Its actin-bundling activity is inhibited by tropomyosin.By similarity2 Publications

<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 functionActin capping, Actin-binding
LigandCalcium

<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:
Villin-1
<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:VIL1
Synonyms:VIL
<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)
<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

<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>Mutagenesisi138R → A: Reduces the actin-severing activity. Does not affect actin-capping activity. 1 Publication1
Mutagenesisi141H → A: Does not reduce the actin-severing activity. Does not affect actin-capping activity. 1 Publication1
Mutagenesisi144G → A: Reduces the actin-severing activity. Does not affect actin-capping activity. 1 Publication1
Mutagenesisi145K → A: Reduces the actin-severing activity. Does not affect actin-capping activity. 1 Publication1
Mutagenesisi146K → A: Reduces the actin-severing activity. Does not affect actin-capping activity. 1 Publication1
Mutagenesisi787R → A: Reduces affinity for F-actin. 1 Publication1
Mutagenesisi814W → A: Loss of F-actin binding. 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_00002187301 – 826Villin-1Add BLAST826

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated on tyrosine residues. The unphosphorylated form increases the initial rate of actin-nucleating activity, whereas the tyrosine-phosphorylated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca2+ requirements. The tyrosine-phosphorylated form does not regulate actin-capping activity. Tyrosine phosphorylation is essential for cell migration: tyrosine phosphorylation sites in the N-terminus half regulate actin reorganization and cell morphology, whereas tyrosine phosphorylation sites in the C-terminus half regulate cell migration. Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity).By similarity

Proteomic databases

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

More...
PaxDbi
P02640

PRoteomics IDEntifications database

More...
PRIDEi
P02640

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Specifically expressed in epithelial cells. Component of brush border microvilli.1 Publication

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

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

Monomer. Homodimer (By similarity). Associates with F-actin; the association with F-actin is inhibited by tropomyosin.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-48339N

Protein interaction database and analysis system

More...
IntActi
P02640, 1 interactor

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000037398

<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

1826
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P02640

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P02640

<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>Repeati27 – 76Gelsolin-like 1Add BLAST50
Repeati148 – 188Gelsolin-like 2Add BLAST41
Repeati265 – 309Gelsolin-like 3Add BLAST45
Repeati408 – 457Gelsolin-like 4Add BLAST50
Repeati528 – 568Gelsolin-like 5Add BLAST41
Repeati631 – 672Gelsolin-like 6Add BLAST42
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini760 – 826HPPROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 734CoreAdd BLAST734
Regioni112 – 119Polyphosphoinositide bindingBy similarity8
Regioni129 – 137Crucial for binding an actin filament9
Regioni138 – 146Polyphosphoinositide bindingBy similarity9
Regioni735 – 826HeadpieceAdd BLAST92
Regioni820 – 823Absolutely required for activity4

<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

Consists of a large core fragment in the N-terminal portion and a small headpiece (HP) in the C-terminal portion. The core fragment is necessary for both actin-nucleating and -severing activities, whereas the HP binds F-actin strongly in both the presence and absence of calcium and is necessary in actin-bundling activity. The Gelsolin-like 1 repeat is necessary for the actin-capping activity. The entire core fragment is necessary for the actin-severing activity (By similarity).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

Belongs to the villin/gelsolin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0443 Eukaryota
ENOG410XR0A LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P02640

KEGG Orthology (KO)

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KOi
K05761

Database of Orthologous Groups

More...
OrthoDBi
1376537at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P02640

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.950.10, 1 hit
3.40.20.10, 6 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR007123 Gelsolin-like_dom
IPR036180 Gelsolin-like_dom_sf
IPR030007 Villin
IPR007122 Villin/Gelsolin
IPR003128 Villin_headpiece
IPR036886 Villin_headpiece_dom_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11977 PTHR11977, 1 hit
PTHR11977:SF35 PTHR11977:SF35, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00626 Gelsolin, 6 hits
PF02209 VHP, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00597 GELSOLIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00262 GEL, 6 hits
SM00153 VHP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47050 SSF47050, 1 hit
SSF82754 SSF82754, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51089 HP, 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.

P02640-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVELSKKVTG KLDKTTPGIQ IWRIENMEMV PVPTKSYGNF YEGDCYVLLS
60 70 80 90 100
TRKTGSGFSY NIHYWLGKNS SQDEQGAAAI YTTQMDEYLG SVAVQHREVQ
110 120 130 140 150
GHESETFRAY FKQGLIYKQG GVASGMKHVE TNTYNVQRLL HVKGKKNVVA
160 170 180 190 200
AEVEMSWKSF NLGDVFLLDL GQLIIQWNGP ESNRAERLRA MTLAKDIRDR
210 220 230 240 250
ERAGRAKVGV VEGENEAASP ELMQALTHVL GEKKNIKAAT PDEQVHQALN
260 270 280 290 300
SALKLYHVSD ASGNLVIQEV AIRPLTQDML QHEDCYILDQ AGLKIFVWKG
310 320 330 340 350
KNANKEEKQQ AMSRALGFIK AKNYLASTSV ETENDGSESA VFRQLFQKWT
360 370 380 390 400
VPNQTSGLGK THTVGKVAKV EQVKFDATTM HVKPEVAAQQ KMVDDGSGEA
410 420 430 440 450
EVWRVENQEL VPVEKRWLGH FYGGDCYLVL YTYYVGPKVN RIIYIWQGRH
460 470 480 490 500
ASTDELAASA YQAVFLDQKY NNEPVQVRVT MGKEPAHLMA IFKGKMVVYE
510 520 530 540 550
NGSSRAGGTE PASSTRLFHV HGTNEYNTKA FEVPVRAASL NSNDVFVLKT
560 570 580 590 600
PSSCYLWYGK GCSGDEREMG KMVADIISKT EKPVVAEGQE PPEFWVALGG
610 620 630 640 650
KTSYANSKRL QEENPSVPPR LFECSNKTGR FLATEIVDFT QDDLDENDVY
660 670 680 690 700
LLDTWDQIFF WIGKGANESE KEAAAETAQE YLRSHPGSRD LDTPIIVVKQ
710 720 730 740 750
GFEPPTFTGW FMAWDPLCWS DRKSYDELKA ELGDNASIGQ LVSGLTSKNE
760 770 780 790 800
VFTATTTLVP TKLETFPLDV LVNTAAEDLP RGVDPSRKEN HLSDEDFKAV
810 820
FGMTRSAFAN LPLWKQQNLK KEKGLF
Length:826
Mass (Da):92,479
Last modified:July 1, 1989 - 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:i6A8898F7DF947389
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J03781 mRNA Translation: AAA49133.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A31822

NCBI Reference Sequences

More...
RefSeqi
NP_990773.1, NM_205442.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
396423

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gga:396423

<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
J03781 mRNA Translation: AAA49133.1
PIRiA31822
RefSeqiNP_990773.1, NM_205442.1

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
1QQVNMR-A760-826[»]
1VIINMR-A792-826[»]
1WY3X-ray0.95A792-826[»]
1WY4X-ray1.55A792-826[»]
1YRFX-ray1.07A792-826[»]
1YRIX-ray1.00A792-826[»]
1YU5X-ray1.40X760-826[»]
1YU7X-ray1.50X760-826[»]
1YU8X-ray1.45X760-826[»]
2F4KX-ray1.05A792-826[»]
2JM0NMR-A792-826[»]
2LLFNMR-A619-725[»]
2PPZNMR-A792-826[»]
2RJVX-ray1.45A760-826[»]
2RJWX-ray1.55A/B760-826[»]
2RJXX-ray1.70A/B760-826[»]
2RJYX-ray1.40A760-826[»]
2VIKNMR-A2-127[»]
2VILNMR-A2-127[»]
3MYAX-ray2.50A/B760-826[»]
3MYCX-ray1.70A760-826[»]
3MYEX-ray1.80X760-826[»]
3NKJX-ray1.60A760-826[»]
3TJWX-ray1.46A/B792-825[»]
3TRVX-ray1.00A/B792-826[»]
3TRWX-ray2.10A/D792-826[»]
3TRYX-ray2.30A792-826[»]
4CZ3NMR-A803-826[»]
4CZ4NMR-A803-826[»]
5I1NX-ray1.30A/B/C/D792-826[»]
5I1OX-ray1.35A/B/C/D792-826[»]
5I1PX-ray1.40A/B/C/D792-826[»]
5I1SX-ray1.12A/B792-826[»]
SMRiP02640
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

DIPiDIP-48339N
IntActiP02640, 1 interactor
STRINGi9031.ENSGALP00000037398

Proteomic databases

PaxDbiP02640
PRIDEiP02640

Genome annotation databases

GeneIDi396423
KEGGigga:396423

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7429

Phylogenomic databases

eggNOGiKOG0443 Eukaryota
ENOG410XR0A LUCA
InParanoidiP02640
KOiK05761
OrthoDBi1376537at2759
PhylomeDBiP02640

Miscellaneous databases

EvolutionaryTraceiP02640

Protein Ontology

More...
PROi
PR:P02640

Family and domain databases

Gene3Di1.10.950.10, 1 hit
3.40.20.10, 6 hits
InterProiView protein in InterPro
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR007123 Gelsolin-like_dom
IPR036180 Gelsolin-like_dom_sf
IPR030007 Villin
IPR007122 Villin/Gelsolin
IPR003128 Villin_headpiece
IPR036886 Villin_headpiece_dom_sf
PANTHERiPTHR11977 PTHR11977, 1 hit
PTHR11977:SF35 PTHR11977:SF35, 1 hit
PfamiView protein in Pfam
PF00626 Gelsolin, 6 hits
PF02209 VHP, 1 hit
PRINTSiPR00597 GELSOLIN
SMARTiView protein in SMART
SM00262 GEL, 6 hits
SM00153 VHP, 1 hit
SUPFAMiSSF47050 SSF47050, 1 hit
SSF82754 SSF82754, 2 hits
PROSITEiView protein in PROSITE
PS51089 HP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiVILI_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: P02640
<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: July 21, 1986
Last sequence update: July 1, 1989
Last modified: February 26, 2020
This is version 143 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

<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, Direct protein sequencing, Reference proteome

Documents

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