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
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Ligandi

Actin-binding, Calcium

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

GO - Cellular componenti

Complete GO annotation...

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-phosphorlyated form inhibits actin-nucleating activity, enhances actin-bundling activity and enhances actin-severing activity by reducing high Ca2+ requirements. The tyrosine-phosphorlyated 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.

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.
STRINGi9031.ENSGALP00000037398.

Structurei

Secondary structure

1826
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Helixi9 – 11Combined sources3
Beta strandi18 – 23Combined sources6
Helixi25 – 27Combined sources3
Turni34 – 38Combined sources5
Beta strandi42 – 44Combined sources3
Beta strandi46 – 53Combined sources8
Beta strandi55 – 66Combined sources12
Helixi72 – 88Combined sources17
Beta strandi95 – 99Combined sources5
Turni100 – 102Combined sources3
Helixi104 – 110Combined sources7
Beta strandi621 – 636Combined sources16
Beta strandi649 – 653Combined sources5
Beta strandi658 – 662Combined sources5
Beta strandi664 – 666Combined sources3
Helixi668 – 682Combined sources15
Helixi690 – 692Combined sources3
Beta strandi696 – 698Combined sources3
Helixi705 – 708Combined sources4
Beta strandi711 – 713Combined sources3
Helixi716 – 720Combined sources5
Turni721 – 723Combined sources3
Helixi768 – 772Combined sources5
Helixi776 – 778Combined sources3
Beta strandi785 – 787Combined sources3
Helixi788 – 791Combined sources4
Helixi794 – 801Combined sources8
Helixi805 – 810Combined sources6
Helixi813 – 823Combined sources11

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-ray1.46A802-824[»]
B792-825[»]
3TRVX-ray1.00A792-826[»]
B802-824[»]
3TRWX-ray2.10A/D792-826[»]
3TRYX-ray2.30A802-824[»]
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...

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
Contains 6 gelsolin-like repeats.Curated
Contains 1 HP (headpiece) domain.PROSITE-ProRule annotation

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.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR030007. Villin.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 2 hits.
PTHR11977:SF35. PTHR11977:SF35. 2 hits.
PfamiPF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
SSF82754. SSF82754. 2 hits.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]

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.

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-ray1.46A802-824[»]
B792-825[»]
3TRVX-ray1.00A792-826[»]
B802-824[»]
3TRWX-ray2.10A/D792-826[»]
3TRYX-ray2.30A802-824[»]
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.
STRINGi9031.ENSGALP00000037398.

Proteomic databases

PaxDbiP02640.

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.
PROiP02640.

Family and domain databases

Gene3Di1.10.950.10. 1 hit.
3.40.20.10. 6 hits.
InterProiIPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR030007. Villin.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 2 hits.
PTHR11977:SF35. PTHR11977:SF35. 2 hits.
PfamiPF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view]
PRINTSiPR00597. GELSOLIN.
SMARTiSM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view]
SUPFAMiSSF47050. SSF47050. 1 hit.
SSF82754. SSF82754. 2 hits.
PROSITEiPS51089. HP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVILI_CHICK
AccessioniPrimary (citable) accession number: P02640
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 2, 2016
This is version 133 of the entry and version 2 of the sequence. [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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.