Protein detail
VILI
Villin-1
Entry name VILI | UniProt ID | EVMP confidence score 0.28 |
Supporting publications (n) 2 | Transmembrane count | Protein classification Cancer-related genesDisease related genesPlasma proteinsPredicted intracellular proteins |
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.70High >= 0.60Medium >= 0.40Low >= 0.30Basic Information
Protein Names
Villin-1
Protein Class (4)
Cancer-related genesDisease related genesPlasma proteinsPredicted intracellular proteins
Protein Function (3)
- Disease related genes
- Cancer-related genes:Candidate cancer biomarkers
- Predicted intracellular proteins
Ensembl
Entrez Gene Symbol
Gene Synonym (2)
D2S1471VIL
Gene Description
Villin 1
Chromosome
2
Position
218419121-218453295
Supporting publications (n)
2
EVMP confidence score
0.28
Fluorescence & Localization
Cell SpecificAlveolar cells type 2
Function & Pathway
Protein Function (3)
- Disease related genes
- Cancer-related genes:Candidate cancer biomarkers
- Predicted intracellular proteins
Cellular Component (11)
- GO:0001726 ruffle
- GO:0005737 cytoplasm
- GO:0005886 plasma membrane
- GO:0005902 microvillus
- GO:0005903 brush border
- GO:0015629 actin cytoskeleton
- GO:0030027 lamellipodium
- GO:0030175 filopodium
- GO:0032432 actin filament bundle
- GO:0032433 filopodium tip
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Molecular Function (8)
- GO:0005509 calcium ion binding
- GO:0005515 protein binding
- GO:0005546 phosphatidylinositol-4,5-bisphosphate binding
- GO:0035727 lysophosphatidic acid binding
- GO:0042802 identical protein binding
- GO:0042803 protein homodimerization activity
- GO:0043027 cysteine-type endopeptidase inhibitor activity involved in apoptotic process
- GO:0051015 actin filament binding
Biological Process (3)
Canonical Pathways (3)
- M138 Pid thrombin par4 pathway
- M252 Pid il8 cxcr1 pathway
- M213 Pid ar nongenomic pathway
Mediation Categories (2)
Fusion and delivery mediationReceptor-signaling mediation
Relations & Evidence14
Enzyme-Mediated Modification (5)
5 records.
| Substrate Gene Symbol | Enzyme Gene Symbol | Enzyme UniProt ID | Residue Type | Residue Offset | Modification | Database | References |
|---|---|---|---|---|---|---|---|
| VIL1 | SRC | P12931 | Y | 81 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | KEA:15342783SIGNOR:15342783ProtMapper:15342783 |
| VIL1 | SRC | P12931 | Y | 256 | phosphorylation | PhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | KEA:15342783SIGNOR:15342783ProtMapper:15342783 |
| VIL1 | SRC | P12931 | Y | 60 | phosphorylation | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | KEA:15342783SIGNOR:15342783ProtMapper:15342783 |
| VIL1 | SRC | P12931 | Y | 64 | phosphorylation | PhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper | |
| VIL1 | SRC | P12931 | Y | 46 | phosphorylation | PhosphoSite_MIMPMIMPProtMapperPhosphoSitePhosphoSite_ProtMapper |
Ligand-Receptor Signaling (5)
5 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | LOCATE | |||||
| intracellular | intracellular | ComPPI | |||||
| intracellular | intracellular | GO_Intercell | |||||
| intracellular | intracellular | UniProt_location | |||||
| intracellular | intracellular | OmniPath |
Regulatory Interaction Network (1)
1 record.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| SRC | P12931 | VILI | P09327 | Yes | Yes | phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPPhosphoSite_norefPhosphoPointSIGNORProtMapperiPTMnetHPRDPhosphoSite_KEAKEAHPRD_KEAInnateDBSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper | SIGNOR:15342783ProtMapper:15342783HPRD:15342783PhosphoSite:12269817InnateDB:17537734PhosphoSite:16921170KEA:15342783PhosphoSite:15342783 |
Protein Complex Composition (2)
Sequence, Structure & Domains
Sequences
Length
827
Mass
92,695
Sequence
MTKLSAQVKGSLNITTPGLQIWRIEAMQMVPVPSSTFGSFFDGDCYIILAIHKTASSLSYDIHYWIGQDSSLDEQGAAAIYTTQMDDFLKGRAVQHREVQGNESEAFRGYFKQGLVIRKGGVASGMKHVETNSYDVQRLLHVKGKRNVVAGEVEMSWKSFNRGDVFLLDLGKLIIQWNGPESTRMERLRGMTLAKEIRDQERGGRTYVGVVDGENELASPKLMEVMNHVLGKRRELKAAVPDTVVEPALKAALKLYHVSDSEGNLVVREVATRPLTQDLLSHEDCYILDQGGLKIYVWKGKKANEQEKKGAMSHALNFIKAKQYPPSTQVEVQNDGAESAVFQQLFQKWTASNRTSGLGKTHTVGSVAKVEQVKFDATSMHVKPQVAAQQKMVDDGSGEVQVWRIENLELVPVDSKWLGHFYGGDCYLLLYTYLIGEKQHYLLYVWQGSQASQDEITASAYQAVILDQKYNGEPVQIRVPMGKEPPHLMSIFKGRMVVYQGGTSRTNNLETGPSTRLFQVQGTGANNTKAFEVPARANFLNSNDVFVLKTQSCCYLWCGKGCSGDEREMAKMVADTISRTEKQVVVEGQEPANFWMALGGKAPYANTKRLQEENLVITPRLFECSNKTGRFLATEIPDFNQDDLEEDDVFLLDVWDQVFFWIGKHANEEEKKAAATTAQEYLKTHPSGRDPETPIIVVKQGHEPPTFTGWFLAWDPFKWSNTKSYEDLKAELGNSRDWSQITAEVTSPKVDVFNANSNLSSGPLPIFPLEQLVNKPVEELPEGVDPSRKEEHLSIEDFTQAFGMTPAAFSALPRWKQQNLKKEKGLF
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=P09327-1; Sequence=Displayed; Name=2; IsoId=P09327-2; Sequence=VSP_054436, VSP_054437
Alternative Sequence
368..421; AKVEQVKFDATSMHVKPQVAAQQKMVDDGSGEVQVWRIENLELVPVDSKWLGHF -> GEGQAGAVREPGSRSWARRATWSTTHPPSLTCIFNEDFYAGSGLVLADGDVDKL (in isoform 2); 422..827; Missing (in isoform 2)
3D Structural Models
Helix
641..643; 668..684; 705..708; 795..800; 806..811; 814..823
Beta Strand
620..625; 632..635; 648..653; 658..662; 685..688; 695..699
3D Structure
NMR spectroscopy (1); X-ray crystallography (1)
Domain & Motif Annotations
Repeat
27..76; Gelsolin-like 1; 148..188; Gelsolin-like 2; 265..309; Gelsolin-like 3; 407..457; Gelsolin-like 4; 528..568; Gelsolin-like 5; 631..672; Gelsolin-like 6
Domain (CC)
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.
Domain (FT)
761..827; HP
Region
2..734; Core; 2..126; Necessary for homodimerization; 112..119; LPA/PIP2-binding site 1; 138..146; LPA/PIP2-binding site 2; 735..827; Headpiece; 816..824; LPA/PIP2-binding site 3
Protein Families
Villin/gelsolin family
Sequence Similarities
Belongs to the villin/gelsolin family.
Supporting Publications2
| PMID | Title | Related sentences |
|---|---|---|
| 31805958 | Proteomic analysis of cerebrospinal fluid extracellular vesicles reveals synaptic injury, inflammation, and stress response markers in HIV patients with cognitive impairment. | No related sentences available |
| 37670049 | Proteomic and functional characterisation of extracellular vesicles from collagen VI deficient human fibroblasts reveals a role in cell motility. | No related sentences available |