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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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi138 – 1381R → A: Reduces the actin-severing activity. Does not affect actin-capping activity. 1 Publication
Mutagenesisi141 – 1411H → A: Does not reduce the actin-severing activity. Does not affect actin-capping activity. 1 Publication
Mutagenesisi144 – 1441G → A: Reduces the actin-severing activity. Does not affect actin-capping activity. 1 Publication
Mutagenesisi145 – 1451K → A: Reduces the actin-severing activity. Does not affect actin-capping activity. 1 Publication
Mutagenesisi146 – 1461K → A: Reduces the actin-severing activity. Does not affect actin-capping activity. 1 Publication
Mutagenesisi787 – 7871R → A: Reduces affinity for F-actin. 1 Publication
Mutagenesisi814 – 8141W → A: Loss of F-actin binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 826826Villin-1PRO_0000218730Add
BLAST

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

1
826
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84Combined sources
Helixi9 – 113Combined sources
Beta strandi18 – 236Combined sources
Helixi25 – 273Combined sources
Turni34 – 385Combined sources
Beta strandi42 – 443Combined sources
Beta strandi46 – 538Combined sources
Beta strandi55 – 6612Combined sources
Helixi72 – 8817Combined sources
Beta strandi95 – 995Combined sources
Turni100 – 1023Combined sources
Helixi104 – 1107Combined sources
Beta strandi621 – 63616Combined sources
Beta strandi649 – 6535Combined sources
Beta strandi658 – 6625Combined sources
Beta strandi664 – 6663Combined sources
Helixi668 – 68215Combined sources
Helixi690 – 6923Combined sources
Beta strandi696 – 6983Combined sources
Helixi705 – 7084Combined sources
Beta strandi711 – 7133Combined sources
Helixi716 – 7205Combined sources
Turni721 – 7233Combined sources
Helixi768 – 7725Combined sources
Helixi776 – 7783Combined sources
Beta strandi785 – 7873Combined sources
Helixi788 – 7914Combined sources
Helixi794 – 8018Combined sources
Helixi805 – 8106Combined sources
Helixi813 – 82311Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-127, 760-826.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02640.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati27 – 7650Gelsolin-like 1Add
BLAST
Repeati148 – 18841Gelsolin-like 2Add
BLAST
Repeati265 – 30945Gelsolin-like 3Add
BLAST
Repeati408 – 45750Gelsolin-like 4Add
BLAST
Repeati528 – 56841Gelsolin-like 5Add
BLAST
Repeati631 – 67242Gelsolin-like 6Add
BLAST
Domaini760 – 82667HPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 734734CoreAdd
BLAST
Regioni112 – 1198Polyphosphoinositide bindingBy similarity
Regioni129 – 1379Crucial for binding an actin filament
Regioni138 – 1469Polyphosphoinositide bindingBy similarity
Regioni735 – 82692HeadpieceAdd
BLAST
Regioni820 – 8234Absolutely required for activity

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
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. Positions 2-127, 760-826.
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: July 6, 2016
This is version 131 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.