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Protein

Villin-1

Gene

VIL1

Organism
Sus scrofa (Pig)
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
Synonyms:VIL
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 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_00002187291 – 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. Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ29261
PeptideAtlasiQ29261
PRIDEiQ29261

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

STRINGi9823.ENSSSCP00000017159

Structurei

3D structure databases

SMRiQ29261
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati28 – 107Gelsolin-like 1Add BLAST80
Repeati148 – 216Gelsolin-like 2Add BLAST69
Repeati269 – 342Gelsolin-like 3Add BLAST74
Repeati409 – 489Gelsolin-like 4Add BLAST81
Repeati528 – 595Gelsolin-like 5Add BLAST68
Repeati634 – 707Gelsolin-like 6Add BLAST74
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
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
HOVERGENiHBG059781
InParanoidiQ29261

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

Q29261-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTKLNAQVKG SLNVTTPGVQ IWRIEAMQMV PVSSSTYGSF FDGDCYIVLA
60 70 80 90 100
IHKTGSNLSY DIHYWIGQDS SQDEQGAAAI YTTLMDDFLK GRAVQHREVQ
110 120 130 140 150
GNESEAFRGY FKQGIVIRKG GVASGMKKVE TNSYDIQRLL HVKGKRNVVA
160 170 180 190 200
GEVEMSWKSF NRGDVFLLDL GKLIIQWNGP ESNRMERLRG MTLAKEIRDQ
210 220 230 240 250
ERGGRTYVGV VDGEDEKASP QLMEIMNYVL GQRKELKAAV PDTVVEPALK
260 270 280 290 300
AALKLYHVSD SEGKVVVREV ATRPLTQDLL SHEDCYILDQ GGLKIYVWKG
310 320 330 340 350
KNANPQEKKE AMNQALNFIK AKQYPPSTQV EVQNDGAESA VFQQLFQKWT
360 370 380 390 400
VPNQTSGLGK THTVGSVAKV EQVKFDATSM HVQPQVAAQQ KMVDDGSGEV
410 420 430 440 450
EIWRIENLDL VPVESKWVGH FYGGDCYLLL YTYLIGEKQH YLLYIWQGSQ
460 470 480 490 500
ASQDEITASA YQAVILDQKY NNEPVQIRVP MGKEPPHLMS IFKGRMVVYQ
510 520 530 540 550
GGTSRANSTE PVPSTRLFQV RGTSVNNTKA FEVPARATSL NSNDIFVLKT
560 570 580 590 600
QSCCYLWCGK GCSGDEREMA KMVADTISRT EKQVVVEGQE PANFWVALGG
610 620 630 640 650
KAPYASSKRL QEETLVITPR LFECSNQTGR FLATEIPDFN QDDLEEDDVF
660 670 680 690 700
LLDVWDQVFF WIGKNANEDE KKAAAVTAQE YLKTHPSGRD PETPIIVVKQ
710 720 730 740 750
GYEPPTFTGW FLAWDPFKWS DSKSYEDLKA ELGNSGDWSQ ITAEIKNPKP
760 770 780 790 800
DVFNANTNLS SGPLPIFPLE QLVNKPAEEL PQGVDPSRRE EHLSIEDFTK
810 820
ALGMTPAAFS ALPRWKQQNL KKEKGLF
Length:827
Mass (Da):92,701
Last modified:May 3, 2011 - v2
Checksum:iB48E433074120A26
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1SRY3F1SRY3_PIG
Villin-1
VIL1
826Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti186E → V in CAA23122 (PubMed:8672129).Curated1
Sequence conflicti198R → P in CAA23122 (PubMed:8672129).Curated1
Sequence conflicti201 – 202ER → GA in CAA23122 (PubMed:8672129).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK231370 mRNA No translation available.
F14554 mRNA Translation: CAA23122.1
UniGeneiSsc.48958

Similar proteinsi

Entry informationi

Entry nameiVILI_PIG
AccessioniPrimary (citable) accession number: Q29261
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: May 3, 2011
Last modified: May 23, 2018
This is version 85 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

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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