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Protein

Villin-1

Gene

Vil1

Organism
Mus musculus (Mouse)
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. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi25 – 9369By similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Villin-1
Gene namesi
Name:Vil1
Synonyms:Vil
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:98930. Vil1.

Subcellular locationi

GO - Cellular componenti

  • actin filament bundle Source: UniProtKB
  • brush border Source: UniProtKB
  • cytoplasm Source: UniProtKB-KW
  • extracellular exosome Source: MGI
  • filopodium Source: UniProtKB
  • filopodium tip Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • microvillus Source: UniProtKB
  • nucleoplasm Source: MGI
  • plasma membrane Source: MGI
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile. The ultrastructure of the intestinal brush border is normal. Show increase epithelial cell apoptosis and are more sensitive to extran sodium sulfate-induced colitis. Newborn mice inoculated with S.flexneri are not susceptible to infection; cell invasion and intestinal inflammation were not observed, even though bacteria were seen in large number in the intestinal lumen, close to the intestinal epithelial cells (IEC) brush border.4 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 827826Villin-1PRO_0000218728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei88 – 881PhosphotyrosineBy similarity
Modified residuei366 – 3661PhosphoserineBy similarity
Modified residuei735 – 7351PhosphoserineCombined sources
Modified residuei776 – 7761PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on tyrosine residues by SRC. 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 via interaction with PLCG1 (By similarity). Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ62468.
PaxDbiQ62468.
PRIDEiQ62468.

PTM databases

iPTMnetiQ62468.
PhosphoSiteiQ62468.

Expressioni

Tissue specificityi

Expressed in small intestin, colon, kidney and enterocytes (at protein level).2 Publications

Gene expression databases

BgeeiQ62468.
CleanExiMM_VIL1.
ExpressionAtlasiQ62468. baseline and differential.
GenevisibleiQ62468. MM.

Interactioni

Subunit structurei

Monomer. Homodimer; homodimerization is necessary for actin-bundling. Associates with F-actin; phosphorylation at tyrosines residues decreases the association with F-actin. Interacts (phosphorylated at C-terminus tyrosine phosphorylation sites) with PLCG1 (via the SH2 domains) (By similarity). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ62468. 8 interactions.
MINTiMINT-1852352.
STRINGi10090.ENSMUSP00000027366.

Structurei

3D structure databases

ProteinModelPortaliQ62468.
SMRiQ62468. Positions 3-720, 764-827.
ModBaseiSearch...
MobiDBiSearch...

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
Repeati407 – 45751Gelsolin-like 4Add
BLAST
Repeati528 – 56841Gelsolin-like 5Add
BLAST
Repeati631 – 67242Gelsolin-like 6Add
BLAST
Domaini761 – 82767HPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 734733CoreAdd
BLAST
Regioni2 – 126125Necessary for homodimerizationBy similarityAdd
BLAST
Regioni112 – 1198LPA/PIP2-binding site 1By similarity
Regioni138 – 1469LPA/PIP2-binding site 2By similarity
Regioni735 – 82793HeadpieceAdd
BLAST
Regioni816 – 8249LPA/PIP2-binding site 3By similarity

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiQ62468.
KOiK05761.
OMAiVPVESKW.
OrthoDBiEOG7288RJ.
TreeFamiTF313468.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q62468-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKLNAQVKG SLNITTPGIQ IWRIEAMQMV PVPSSTFGSF FDGDCYVVLA
60 70 80 90 100
IHKTSSTLSY DIHYWIGQDS SQDEQGAAAI YTTQMDDYLK GRAVQHREVQ
110 120 130 140 150
GNESETFRSY FKQGLVIRKG GVASGMKHVE TNSCDVQRLL HVKGKRNVLA
160 170 180 190 200
GEVEMSWKSF NRGDVFLLDL GKLIIQWNGP ESNRMERLRG MALAKEIRDQ
210 220 230 240 250
ERGGRTYVGV VDGEKEGDSP QLMAIMNHVL GPRKELKAAI SDSVVEPAAK
260 270 280 290 300
AALKLYHVSD SEGKLVVREV ATRPLTQDLL KHEDCYILDQ GGLKIFVWKG
310 320 330 340 350
KNANAQERSG AMSQALNFIK AKQYPPSTQV EVQNDGAESP IFQQLFQKWT
360 370 380 390 400
VPNRTSGLGK THTVGSVAKV EQVKFDALTM HVQPQVAAQQ KMVDDGSGEV
410 420 430 440 450
QVWRIEDLEL VPVESKWLGH FYGGDCYLLL YTYLIGEKQH YLLYIWQGSQ
460 470 480 490 500
ASQDEIAASA YQAVLLDQKY NDEPVQIRVT MGKEPPHLMS IFKGRMVVYQ
510 520 530 540 550
GGTSRKNNLE PVPSTRLFQV RGTNADNTKA FEVTARATSL NSNDVFILKT
560 570 580 590 600
PSCCYLWCGK GCSGDEREMA KMVADTISRT EKQVVVEGQE PANFWMALGG
610 620 630 640 650
KAPYANTKRL QEENQVITPR LFECSNQTGR FLATEIFDFN QDDLEEEDVF
660 670 680 690 700
LLDVWDQVFF WIGKHANEEE KKAAATTVQE YLKTHPGNRD LETPIIVVKQ
710 720 730 740 750
GHEPPTFTGW FLAWDPFKWS NTKSYDDLKA ELGNSGDWSQ IADEVMSPKV
760 770 780 790 800
DVFTANTSLS SGPLPTFPLE QLVNKSVEDL PEGVDPSRKE EHLSTEDFTR
810 820
ALGMTPAAFS ALPRWKQQNI KKEKGLF
Length:827
Mass (Da):92,775
Last modified:July 27, 2011 - v3
Checksum:i15601DFBA04B500E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti192 – 1921A → P in AAA40554 (PubMed:1601186).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98454 mRNA. Translation: AAA40554.1.
BC117875 mRNA. Translation: AAI17876.1.
BC145671 mRNA. Translation: AAI45672.1.
BC015267 mRNA. Translation: AAH15267.1.
CCDSiCCDS15049.1.
RefSeqiNP_033535.2. NM_009509.2.
UniGeneiMm.471601.

Genome annotation databases

EnsembliENSMUST00000027366; ENSMUSP00000027366; ENSMUSG00000026175.
GeneIDi22349.
KEGGimmu:22349.
UCSCiuc007bmb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M98454 mRNA. Translation: AAA40554.1.
BC117875 mRNA. Translation: AAI17876.1.
BC145671 mRNA. Translation: AAI45672.1.
BC015267 mRNA. Translation: AAH15267.1.
CCDSiCCDS15049.1.
RefSeqiNP_033535.2. NM_009509.2.
UniGeneiMm.471601.

3D structure databases

ProteinModelPortaliQ62468.
SMRiQ62468. Positions 3-720, 764-827.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ62468. 8 interactions.
MINTiMINT-1852352.
STRINGi10090.ENSMUSP00000027366.

PTM databases

iPTMnetiQ62468.
PhosphoSiteiQ62468.

Proteomic databases

MaxQBiQ62468.
PaxDbiQ62468.
PRIDEiQ62468.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027366; ENSMUSP00000027366; ENSMUSG00000026175.
GeneIDi22349.
KEGGimmu:22349.
UCSCiuc007bmb.2. mouse.

Organism-specific databases

CTDi7429.
MGIiMGI:98930. Vil1.

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiQ62468.
KOiK05761.
OMAiVPVESKW.
OrthoDBiEOG7288RJ.
TreeFamiTF313468.

Miscellaneous databases

PROiQ62468.
SOURCEiSearch...

Gene expression databases

BgeeiQ62468.
CleanExiMM_VIL1.
ExpressionAtlasiQ62468. baseline and differential.
GenevisibleiQ62468. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Expression and localization of villin, fimbrin, and myosin I in differentiating mouse F9 teratocarcinoma cells."
    Ezzell R.M., Leung J., Collins K., Chafel M.M., Cardozo T.J., Matsudaira P.T.
    Dev. Biol. 151:575-585(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Brain and Kidney.
  3. Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "Villin enhances hepatocyte growth factor-induced actin cytoskeleton remodeling in epithelial cells."
    Athman R., Louvard D., Robine S.
    Mol. Biol. Cell 14:4641-4653(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TYROSINE PHOSPHORYLATION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
  5. "Shigella flexneri infection is dependent on villin in the mouse intestine and in primary cultures of intestinal epithelial cells."
    Athman R., Fernandez M.I., Gounon P., Sansonetti P., Louvard D., Philpott D., Robine S.
    Cell. Microbiol. 7:1109-1116(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SHIGELLA FLEXNERI INFECTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "A novel role for villin in intestinal epithelial cell survival and homeostasis."
    Wang Y., Srinivasan K., Siddiqui M.R., George S.P., Tomar A., Khurana S.
    J. Biol. Chem. 283:9454-9464(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735 AND SER-776, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney.

Entry informationi

Entry nameiVILI_MOUSE
AccessioniPrimary (citable) accession number: Q62468
Secondary accession number(s): Q149B6, Q91WH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.