Protein detail

VILI

Villin-1

Entry name VILI	UniProt ID P09327	EVMP confidence score 0.38
Supporting publications (n) 2	Transmembrane count	Protein classification Cancer-related genesDisease related genesPlasma proteinsPredicted intracellular proteins

EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40

Basic Information11

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

ENSG00000127831

Entrez Gene Symbol

VIL1

Gene Synonym (2)

D2S1471VIL

Gene Description

Villin 1

Chromosome

Position

218419121-218453295

Supporting publications (n)

EVMP confidence score

0.38

Fluorescence & Localization1

Cell SpecificAlveolar cells type 2

Function & Pathway6

Protein Function (3)

Disease related genes
Cancer-related genes:Candidate cancer biomarkers
Predicted intracellular proteins

Cellular Component (11)

Page 1 of 2

Molecular Function (8)

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:15342783 SIGNOR:15342783 ProtMapper:15342783
VIL1	SRC	P12931	Y	256	phosphorylation	PhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper	KEA:15342783 SIGNOR:15342783 ProtMapper:15342783
VIL1	SRC	P12931	Y	60	phosphorylation	phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEASIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper	KEA:15342783 SIGNOR:15342783 ProtMapper: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	No	No	No	No	No
intracellular	intracellular	ComPPI	No	No	No	No	No
intracellular	intracellular	GO_Intercell	No	No	No	No	No
intracellular	intracellular	UniProt_location	No	No	No	No	No
intracellular	intracellular	OmniPath	No	No	No	No	No

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	No	phosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPPhosphoSite_norefPhosphoPointSIGNORProtMapperiPTMnetHPRDPhosphoSite_KEAKEAHPRD_KEAInnateDBSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapper	SIGNOR:15342783 ProtMapper:15342783 HPRD:15342783 PhosphoSite:12269817 InnateDB:17537734 PhosphoSite:16921170 KEA:15342783 PhosphoSite:15342783

Protein Complex Composition (2)

2 records.

Component Name	Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs	References
	AVIL VIL1	O75366 P09327	0:0	hu.MAP2
	VIL1	P09327	2	PDB	PDB:3fg7

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential UltracentrifugationUltrafiltration / Tangential Flow Filtration	Mass spectrometry	2	37786918 38321535

Sequence, Structure & Domains14

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.

Clinical Relevance2

Disease Involvement

Cancer-related genes

Antibody (3)

CAB002452 HPA006884 HPA006885

Supporting Publications2

PMID	Title	Abstract
31805958	Proteomic analysis of cerebrospinal fluid extracellular vesicles reveals synaptic injury, inflammation, and stress response markers in HIV patients with cognitive impairment.	No abstract available
37670049	Proteomic and functional characterisation of extracellular vesicles from collagen VI deficient human fibroblasts reveals a role in cell motility.	No abstract available