Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Villin-1

Gene

VIL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.13 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
Biological processApoptosis
LigandCalcium

Enzyme and pathway databases

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P09327

<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:
Villin-1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:VIL1
Synonyms:VIL
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000127831.10

Human Gene Nomenclature Database

More...
HGNCi
HGNC:12690 VIL1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
193040 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P09327

<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

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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.

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>Mutagenesisi25E → Q: Inhibits activities regarding actin capping, actin severing and actin bundling. 1 Publication1
Mutagenesisi44D → L: Inhibits activities regarding actin capping and actin severing. 1 Publication1
Mutagenesisi46Y → F: Reduces activities regarding actin capping and actin severing. Does not reduce lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-60; F-81; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-60; F-81 and F-256. 5 Publications1
Mutagenesisi60Y → F: Reduces activities regarding actin capping and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-81; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-81 and F-256. 5 Publications1
Mutagenesisi61D → N: Inhibits actin-severing activity. Does not inhibit actin-nucleation and actin-capping activities. 2 Publications1
Mutagenesisi74E → L: Inhibits activities regarding actin capping and actin severing. 2 Publications1
Mutagenesisi81Y → F: Reduces activities regarding actin nucleating and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-60 and F-256. 5 Publications1
Mutagenesisi86 – 91DDFLKG → NTLLKE: Inhibits actin-severing activity and motility of the S.flexneri, does not inhibit activities regarding actin nucleation, actin capping and actin bundling, lamellipodium or ruffle localization and cell morphology; when associated with 125-A--S-129. 1 Publication6
Mutagenesisi86D → L: Inhibits actin-severing activity. Does not inhibit actin-capping activity. 1 Publication1
Mutagenesisi93A → G: Inhibits actin-severing activity. Does not inhibit actin-capping activity. 1 Publication1
Mutagenesisi125 – 129GMKHV → AMHKTS: Inhibits actin-severing activity and motility of the S.flexneri, does not inhibit activities regarding actin nucleation, actin capping and actin bundling, lamellipodium or ruffle localization and cell morphology; when associated with 86-N--E-91. 1 Publication5
Mutagenesisi138R → A: Reduces binding to PIP2. 1 Publication1
Mutagenesisi145K → A: Does not reduce binding to PIP2. 1 Publication1
Mutagenesisi146R → A: Does not reduce binding to PIP2. 1 Publication1
Mutagenesisi256Y → F: Reduces activities regarding actin nucleation and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-60 and F-81. 5 Publications1
Mutagenesisi286Y → F: Reduces actin-severing activity and interaction with PLCG1. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-324; F-461; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-324; F-461; F-555; F-604 and F-725. 3 Publications1
Mutagenesisi324Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-461; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-461; F-555; F-604 and F-725. 3 Publications1
Mutagenesisi461Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-555; F-604 and F-725. 3 Publications1
Mutagenesisi467D → L: Reduces the Ca(2+)-dependent actin-severing activity. 1 Publication1
Mutagenesisi555Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-604 and F-725. 3 Publications1
Mutagenesisi604Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-555 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-555 and F-725. 3 Publications1
Mutagenesisi715D → L: Reduces the Ca(2+)-dependent actin-severing activity. 1 Publication1
Mutagenesisi725Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-555 and F-604. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-555 and F-604. 3 Publications1
Mutagenesisi815W → A: Reduces interaction with F-actin. 1 Publication1
Mutagenesisi822K → A: Does not reduce binding to PIP2. 1 Publication1
Mutagenesisi824K → A: Does not reduce binding to PIP2. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
7429

Open Targets

More...
OpenTargetsi
ENSG00000127831

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA37309

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
VIL1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
224471905

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00002187272 – 827Villin-1Add BLAST826

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 residuei366PhosphoserineCombined sources1
Modified residuei735PhosphoserineBy similarity1

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

Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity). Phosphorylated on tyrosine residues by SRC. 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 via interaction with PLCG1.By similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P09327

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P09327

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P09327

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

More...
PaxDbi
P09327

PeptideAtlas

More...
PeptideAtlasi
P09327

PRoteomics IDEntifications database

More...
PRIDEi
P09327

ProteomicsDB human proteome resource

More...
ProteomicsDBi
52213

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1893

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P09327

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

More...
PhosphoSitePlusi
P09327

<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. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes (at protein level).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000127831 Expressed in 94 organ(s), highest expression level in duodenum

CleanEx database of gene expression profiles

More...
CleanExi
HS_VIL1

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P09327 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P09327 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB002452
HPA006884
HPA006885

<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

Monomer. Homodimer; homodimerization is necessary for actin-bundling. Associates with F-actin; phosphorylation at tyrosine residues decreases the association with F-actin. Interacts (phosphorylated at C-terminus tyrosine phosphorylation sites) with PLCG1 (via the SH2 domains). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF) (By similarity).By similarity

<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

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113270, 7 interactors

Protein interaction database and analysis system

More...
IntActi
P09327, 3 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000248444

<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

1827
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1UNCNMR-A793-827[»]
3FG7X-ray2.00A/B360-720[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P09327

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

More...
SMRi
P09327

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P09327

<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
Repeati407 – 457Gelsolin-like 4Add BLAST51
Repeati528 – 568Gelsolin-like 5Add BLAST41
Repeati631 – 672Gelsolin-like 6Add BLAST42
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">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>Domaini761 – 827HPPROSITE-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>Regioni2 – 734CoreAdd BLAST733
Regioni2 – 126Necessary for homodimerizationAdd BLAST125
Regioni112 – 119LPA/PIP2-binding site 18
Regioni138 – 146LPA/PIP2-binding site 29
Regioni735 – 827HeadpieceAdd BLAST93
Regioni816 – 824LPA/PIP2-binding site 39

<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. Two major calcium-sensitive sites are involved in conformational changes and determine separate functional properties: the first site (Glu-25, Asp-44 and Glu-74) regulates the actin-capping and actin-severing activities; while the second site (Asp-61, Asp-86 and Ala-93) regulates only the actin-severing activity.

<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

More...
eggNOGi
KOG0443 Eukaryota
ENOG410XR0A LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160544

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000233630

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG001093

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P09327

KEGG Orthology (KO)

More...
KOi
K05761

Identification of Orthologs from Complete Genome Data

More...
OMAi
KFDATSM

Database of Orthologous Groups

More...
OrthoDBi
1376537at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P09327

TreeFam database of animal gene trees

More...
TreeFami
TF313468

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

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

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

Isoform 1 (identifier: P09327-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MTKLSAQVKG SLNITTPGLQ IWRIEAMQMV PVPSSTFGSF FDGDCYIILA
60 70 80 90 100
IHKTASSLSY DIHYWIGQDS SLDEQGAAAI YTTQMDDFLK GRAVQHREVQ
110 120 130 140 150
GNESEAFRGY FKQGLVIRKG GVASGMKHVE TNSYDVQRLL HVKGKRNVVA
160 170 180 190 200
GEVEMSWKSF NRGDVFLLDL GKLIIQWNGP ESTRMERLRG MTLAKEIRDQ
210 220 230 240 250
ERGGRTYVGV VDGENELASP KLMEVMNHVL GKRRELKAAV PDTVVEPALK
260 270 280 290 300
AALKLYHVSD SEGNLVVREV ATRPLTQDLL SHEDCYILDQ GGLKIYVWKG
310 320 330 340 350
KKANEQEKKG AMSHALNFIK AKQYPPSTQV EVQNDGAESA VFQQLFQKWT
360 370 380 390 400
ASNRTSGLGK THTVGSVAKV EQVKFDATSM HVKPQVAAQQ KMVDDGSGEV
410 420 430 440 450
QVWRIENLEL VPVDSKWLGH FYGGDCYLLL YTYLIGEKQH YLLYVWQGSQ
460 470 480 490 500
ASQDEITASA YQAVILDQKY NGEPVQIRVP MGKEPPHLMS IFKGRMVVYQ
510 520 530 540 550
GGTSRTNNLE TGPSTRLFQV QGTGANNTKA FEVPARANFL NSNDVFVLKT
560 570 580 590 600
QSCCYLWCGK GCSGDEREMA KMVADTISRT EKQVVVEGQE PANFWMALGG
610 620 630 640 650
KAPYANTKRL QEENLVITPR LFECSNKTGR FLATEIPDFN QDDLEEDDVF
660 670 680 690 700
LLDVWDQVFF WIGKHANEEE KKAAATTAQE YLKTHPSGRD PETPIIVVKQ
710 720 730 740 750
GHEPPTFTGW FLAWDPFKWS NTKSYEDLKA ELGNSRDWSQ ITAEVTSPKV
760 770 780 790 800
DVFNANSNLS SGPLPIFPLE QLVNKPVEEL PEGVDPSRKE EHLSIEDFTQ
810 820
AFGMTPAAFS ALPRWKQQNL KKEKGLF
Length:827
Mass (Da):92,695
Last modified:March 3, 2009 - v4
<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:i96439B33B81E5F19
GO
Isoform 2 (identifier: P09327-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     368-421: AKVEQVKFDA...PVDSKWLGHF → GEGQAGAVRE...VLADGDVDKL
     422-827: Missing.

Note: No experimental confirmation available.
Show »
Length:421
Mass (Da):46,567
Checksum:i897332F5D0ECFC02
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
B4DV78B4DV78_HUMAN
cDNA FLJ57609, highly similar to Vi...
VIL1
516Annotation score:

Annotation score:2 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>
H7C0B6H7C0B6_HUMAN
Villin-1
VIL1
213Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
C9J2B5C9J2B5_HUMAN
Villin-1
VIL1
157Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

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 conflicti146R → K in BAG36454 (PubMed:14702039).Curated1
Sequence conflicti732L → S in CAA31386 (PubMed:2846586).Curated1
Sequence conflicti732L → S in CAA28355 (Ref. 4) Curated1
Sequence conflicti735S → L in CAA31386 (PubMed:2846586).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_054502254K → R. Corresponds to variant dbSNP:rs35305540Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_054436368 – 421AKVEQ…WLGHF → GEGQAGAVREPGSRSWARRA TWSTTHPPSLTCIFNEDFYA GSGLVLADGDVDKL in isoform 2. 1 PublicationAdd BLAST54
Alternative sequenceiVSP_054437422 – 827Missing in isoform 2. 1 PublicationAdd BLAST406

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
X12901 mRNA Translation: CAA31386.1
AK313709 mRNA Translation: BAG36454.1
AC021016 Genomic DNA No translation available.
AC073838 Genomic DNA Translation: AAY14886.1
CH471063 Genomic DNA Translation: EAW70619.1
BC017303 mRNA Translation: AAH17303.1
X04657 mRNA Translation: CAA28355.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2417.1 [P09327-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A31642

NCBI Reference Sequences

More...
RefSeqi
NP_009058.2, NM_007127.2 [P09327-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.654595

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000248444; ENSP00000248444; ENSG00000127831 [P09327-1]
ENST00000440053; ENSP00000409270; ENSG00000127831 [P09327-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7429

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7429

UCSC genome browser

More...
UCSCi
uc002via.4 human [P09327-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12901 mRNA Translation: CAA31386.1
AK313709 mRNA Translation: BAG36454.1
AC021016 Genomic DNA No translation available.
AC073838 Genomic DNA Translation: AAY14886.1
CH471063 Genomic DNA Translation: EAW70619.1
BC017303 mRNA Translation: AAH17303.1
X04657 mRNA Translation: CAA28355.1
CCDSiCCDS2417.1 [P09327-1]
PIRiA31642
RefSeqiNP_009058.2, NM_007127.2 [P09327-1]
UniGeneiHs.654595

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UNCNMR-A793-827[»]
3FG7X-ray2.00A/B360-720[»]
ProteinModelPortaliP09327
SMRiP09327
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113270, 7 interactors
IntActiP09327, 3 interactors
STRINGi9606.ENSP00000248444

PTM databases

GlyConnecti1893
iPTMnetiP09327
PhosphoSitePlusiP09327

Polymorphism and mutation databases

BioMutaiVIL1
DMDMi224471905

Proteomic databases

EPDiP09327
jPOSTiP09327
MaxQBiP09327
PaxDbiP09327
PeptideAtlasiP09327
PRIDEiP09327
ProteomicsDBi52213

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248444; ENSP00000248444; ENSG00000127831 [P09327-1]
ENST00000440053; ENSP00000409270; ENSG00000127831 [P09327-2]
GeneIDi7429
KEGGihsa:7429
UCSCiuc002via.4 human [P09327-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7429
DisGeNETi7429
EuPathDBiHostDB:ENSG00000127831.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
VIL1
HGNCiHGNC:12690 VIL1
HPAiCAB002452
HPA006884
HPA006885
MIMi193040 gene
neXtProtiNX_P09327
OpenTargetsiENSG00000127831
PharmGKBiPA37309

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0443 Eukaryota
ENOG410XR0A LUCA
GeneTreeiENSGT00940000160544
HOGENOMiHOG000233630
HOVERGENiHBG001093
InParanoidiP09327
KOiK05761
OMAiKFDATSM
OrthoDBi1376537at2759
PhylomeDBiP09327
TreeFamiTF313468

Enzyme and pathway databases

SIGNORiP09327

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
VIL1 human
EvolutionaryTraceiP09327

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

More...
GenomeRNAii
7429

Protein Ontology

More...
PROi
PR:P09327

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000127831 Expressed in 94 organ(s), highest expression level in duodenum
CleanExiHS_VIL1
ExpressionAtlasiP09327 baseline and differential
GenevisibleiP09327 HS

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...

<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_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09327
Secondary accession number(s): B2R9A7, Q53S11, Q96AC8
<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: July 1, 1989
Last sequence update: March 3, 2009
Last modified: January 16, 2019
This is version 185 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again