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Protein

Villin-1

Gene

VIL1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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). Its actin-bundling activity is inhibited by tropomyosin.By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActin capping, Actin-binding
LigandCalcium

Names & Taxonomyi

Protein namesi
Recommended name:
Villin-1
Gene namesi
Name:VIL1
Synonyms:VIL
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002187301 – 826Villin-1Add BLAST826

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

PaxDbiP02640
PRIDEiP02640

Expressioni

Tissue specificityi

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

Interactioni

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

DIPiDIP-48339N
IntActiP02640, 1 interactor
STRINGi9031.ENSGALP00000037398

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP02640
SMRiP02640
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02640

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
Repeati408 – 457Gelsolin-like 4Add BLAST50
Repeati528 – 568Gelsolin-like 5Add BLAST41
Repeati631 – 672Gelsolin-like 6Add BLAST42
Domaini760 – 826HPPROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

Sequence similaritiesi

Belongs to the villin/gelsolin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0443 Eukaryota
ENOG410XR0A LUCA
HOGENOMiHOG000233630
HOVERGENiHBG004183
InParanoidiP02640
KOiK05761
PhylomeDBiP02640

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

Sequencei

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
Checksum:i6A8898F7DF947389
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J03781 mRNA Translation: AAA49133.1
PIRiA31822
RefSeqiNP_990773.1, NM_205442.1
UniGeneiGga.816

Genome annotation databases

GeneIDi396423
KEGGigga:396423

Similar proteinsi

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
UniGeneiGga.816

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP02640
SMRiP02640
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48339N
IntActiP02640, 1 interactor
STRINGi9031.ENSGALP00000037398

Proteomic databases

PaxDbiP02640
PRIDEiP02640

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396423
KEGGigga:396423

Organism-specific databases

CTDi7429

Phylogenomic databases

eggNOGiKOG0443 Eukaryota
ENOG410XR0A LUCA
HOGENOMiHOG000233630
HOVERGENiHBG004183
InParanoidiP02640
KOiK05761
PhylomeDBiP02640

Miscellaneous databases

EvolutionaryTraceiP02640
PROiPR: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
ProtoNetiSearch...

Entry informationi

Entry nameiVILI_CHICK
AccessioniPrimary (citable) accession number: P02640
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: May 23, 2018
This is version 139 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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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Main funding by: National Institutes of Health

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