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
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

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).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin capping, Actin-binding
Biological processApoptosis
LigandCalcium

Names & Taxonomyi

Protein namesi
Recommended name:
Villin-1
Gene namesi
Name:VIL1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002713931 – 827Villin-1Add BLAST827

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei366PhosphoserineBy similarity1
Modified residuei735PhosphoserineBy similarity1

Post-translational modificationi

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. Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ3SZP7
PeptideAtlasiQ3SZP7
PRIDEiQ3SZP7

Interactioni

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000024683

Structurei

3D structure databases

ProteinModelPortaliQ3SZP7
SMRiQ3SZP7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Domaini761 – 827HPPROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 734CoreAdd BLAST734
Regioni1 – 126Necessary for homodimerizationBy similarityAdd BLAST126
Regioni112 – 119LPA/PIP2-binding site 1By similarity8
Regioni138 – 146LPA/PIP2-binding site 2By similarity9
Regioni735 – 827HeadpieceAdd BLAST93
Regioni816 – 824LPA/PIP2-binding site 3By similarity9

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0443 Eukaryota
ENOG410XR0A LUCA
HOGENOMiHOG000233630
HOVERGENiHBG004183
InParanoidiQ3SZP7

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

Sequence (1+)i

Sequence statusi: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.iShow all

Q3SZP7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKLSAQVKG SLNITTPGVQ IWRIEAMQMV PVPSNSFGSF FDGDCYVIQA
60 70 80 90 100
IHKTGSNLSY DIHYWIGQAS SQDEQGAAAI YTTQMDDFLK GRAVQHREVQ
110 120 130 140 150
GNESDTFRGY FKKGIVIRKG GVASGMKQVE TNSYDIQRLL HVKGKRNVVA
160 170 180 190 200
GEVEMSWKSF NRGDVFLLDL GKLIIQWNGP ESNHMERLRG MNLAKEIRDQ
210 220 230 240 250
ERGGRTYVGV VDGEDEKASP QLMEIMNHVL GQRKELKAAV ADTVVEPALK
260 270 280 290 300
AALKLYHVSD SEGKVVVREI ATQPLTQDLL SHEDCYILDQ GGLKIYVWKG
310 320 330 340 350
KNANAQEKKE AMNQALNFIK AKQYPPSTQV ELQNDGAESA VFQQLFQKWT
360 370 380 390 400
VPNRTTGLGK THTVGSVAKV EQVKFDAMSM HVQPQVAAQQ KMVDDGSGEV
410 420 430 440 450
QMWRIENLEL VPVNTKWLGH FFGGDCYLLL YTYFINEKPH YLLYIWQGSQ
460 470 480 490 500
ASQDEITASA YQAVILDQEY NNEPVQIRVP MGKEPPHLMS IFKGCMVVYQ
510 520 530 540 550
GGTSRANSVE PVPSTRLFQV RGTSANNTKA FEVSPRAASL NSNDVFILKT
560 570 580 590 600
QSCCYLWCGK GCSGDEREMA KMVADTVSRT EKQVVVEGQE PANFWLALGG
610 620 630 640 650
KAPYASTKRL QEENLVITPR LFECSNQTGR FLATEIPDFN QDDLEEDDVF
660 670 680 690 700
LLDVWDQVFF WIGKNANEDE KKAAATTVQE YLKTHPGGRD LETPIIVVKQ
710 720 730 740 750
GHEPPTFTGW FLAWDPFKWN NSKSYEDLKA ELGNSGDWSQ ITAELTSSKP
760 770 780 790 800
EAFNANSNLS SGPLPIFPLE QLVNKPTEEL PEGVDPSRRE EHLSIEDFTR
810 820
ALGMTPSAFW ALPRWKQQNL KKEKGLF
Length:827
Mass (Da):92,802
Last modified:January 23, 2007 - v3
Checksum:iF760711EB6334755
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5E9Z3Q5E9Z3_BOVIN
Villin-1
VIL1
827Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102759 mRNA Translation: AAI02760.1
UniGeneiBt.24710

Similar proteinsi

Entry informationi

Entry nameiVILI_BOVIN
AccessioniPrimary (citable) accession number: Q3SZP7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 23, 2007
Last modified: November 22, 2017
This is version 78 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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