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Protein

Villin-1

Gene

VIL1

Organism
Homo sapiens (Human)
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.13 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: UniProtKB
  • identical protein binding Source: IntAct
  • lysophosphatidic acid binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • actin filament capping Source: UniProtKB
  • actin filament depolymerization Source: UniProtKB
  • actin filament polymerization Source: UniProtKB
  • actin filament severing Source: UniProtKB
  • actin nucleation Source: InterPro
  • barbed-end actin filament capping Source: UniProtKB
  • cellular response to epidermal growth factor stimulus Source: UniProtKB
  • cellular response to hepatocyte growth factor stimulus Source: Ensembl
  • cytoplasmic actin-based contraction involved in cell motility Source: UniProtKB
  • epidermal growth factor receptor signaling pathway Source: UniProtKB
  • epithelial cell differentiation Source: UniProtKB
  • intestinal D-glucose absorption Source: Ensembl
  • positive regulation of actin filament bundle assembly Source: UniProtKB
  • positive regulation of actin filament depolymerization Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of epithelial cell migration Source: UniProtKB
  • positive regulation of establishment of protein localization to plasma membrane Source: Ensembl
  • positive regulation of lamellipodium morphogenesis Source: UniProtKB
  • positive regulation of multicellular organism growth Source: Ensembl
  • protein complex assembly Source: ProtInc
  • regulation of actin nucleation Source: UniProtKB
  • regulation of cell shape Source: UniProtKB
  • regulation of lamellipodium morphogenesis Source: UniProtKB
  • regulation of microvillus length Source: Ensembl
  • regulation of wound healing Source: UniProtKB
  • response to bacterium Source: UniProtKB
  • terminal web assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Actin-binding, Calcium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000127831-MONOMER.
SIGNORiP09327.

Names & Taxonomyi

Protein namesi
Recommended name:
Villin-1
Gene namesi
Name:VIL1
Synonyms:VIL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12690. VIL1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Biliary atresia is a chronic and progressive cholestatic liver disease of chilhood characterized by an abnormal villin gene expression and severe malformation of canalicular microvillus structure.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi25E → Q: Inhibits activities regarding actin capping, actin severing and actin bundling. 1 Publication1
Mutagenesisi44D → L: Inhibits activities regarding actin capping and actin severing. 1 Publication1
Mutagenesisi46Y → F: Reduces activities regarding actin capping and actin severing. Does not reduce lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-60; F-81; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-60; F-81 and F-256. 5 Publications1
Mutagenesisi60Y → F: Reduces activities regarding actin capping and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-81; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-81 and F-256. 5 Publications1
Mutagenesisi61D → N: Inhibits actin-severing activity. Does not inhibit actin-nucleation and actin-capping activities. 2 Publications1
Mutagenesisi74E → L: Inhibits activities regarding actin capping and actin severing. 2 Publications1
Mutagenesisi81Y → F: Reduces activities regarding actin nucleating and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-256; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-60 and F-256. 5 Publications1
Mutagenesisi86 – 91DDFLKG → NTLLKE: Inhibits actin-severing activity and motility of the S.flexneri, does not inhibit activities regarding actin nucleation, actin capping and actin bundling, lamellipodium or ruffle localization and cell morphology; when associated with 125-A--S-129. 1 Publication6
Mutagenesisi86D → L: Inhibits actin-severing activity. Does not inhibit actin-capping activity. 1 Publication1
Mutagenesisi93A → G: Inhibits actin-severing activity. Does not inhibit actin-capping activity. 1 Publication1
Mutagenesisi125 – 129GMKHV → AMHKTS: Inhibits actin-severing activity and motility of the S.flexneri, does not inhibit activities regarding actin nucleation, actin capping and actin bundling, lamellipodium or ruffle localization and cell morphology; when associated with 86-N--E-91. 1 Publication5
Mutagenesisi138R → A: Reduces binding to PIP2. 1 Publication1
Mutagenesisi145K → A: Does not reduce binding to PIP2. 1 Publication1
Mutagenesisi146R → A: Does not reduce binding to PIP2. 1 Publication1
Mutagenesisi256Y → F: Reduces activities regarding actin nucleation and actin severing, lamellipodium or ruffle localization and cell migration. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-286; F-324; F-461; F-555; F-604 and F-725. Inhibits lamellipodia localization but does not reduce interaction with PLCG1; when associated with F-46; F-60 and F-81. 5 Publications1
Mutagenesisi286Y → F: Reduces actin-severing activity and interaction with PLCG1. Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-324; F-461; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-324; F-461; F-555; F-604 and F-725. 3 Publications1
Mutagenesisi324Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-461; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-461; F-555; F-604 and F-725. 3 Publications1
Mutagenesisi461Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-555; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-555; F-604 and F-725. 3 Publications1
Mutagenesisi467D → L: Reduces the Ca(2+)-dependent actin-severing activity. 1 Publication1
Mutagenesisi555Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-604 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-604 and F-725. 3 Publications1
Mutagenesisi604Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-555 and F-725. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-555 and F-725. 3 Publications1
Mutagenesisi715D → L: Reduces the Ca(2+)-dependent actin-severing activity. 1 Publication1
Mutagenesisi725Y → F: Complete loss of phosphorylation and interaction with PLCG1, does not reduce lamellipodium or ruffle localization, inhibits cell migration; when associated with F-46; F-60; F-81; F-256; F-286; F-324; F-461; F-555 and F-604. Inhibits interaction with PLCG1 and lamellipodia localization; when associated with F-286; F-324; F-461; F-555 and F-604. 3 Publications1
Mutagenesisi815W → A: Reduces interaction with F-actin. 1 Publication1
Mutagenesisi822K → A: Does not reduce binding to PIP2. 1 Publication1
Mutagenesisi824K → A: Does not reduce binding to PIP2. 1 Publication1

Organism-specific databases

DisGeNETi7429.
OpenTargetsiENSG00000127831.
PharmGKBiPA37309.

Polymorphism and mutation databases

BioMutaiVIL1.
DMDMi224471905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002187272 – 827Villin-1Add BLAST826

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei366PhosphoserineCombined sources1
Modified residuei735PhosphoserineBy similarity1

Post-translational modificationi

Tyrosine phosphorylation is induced by epidermal growth factor (EGF) and stimulates cell migration (By similarity). 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 similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP09327.
MaxQBiP09327.
PaxDbiP09327.
PeptideAtlasiP09327.
PRIDEiP09327.

PTM databases

iPTMnetiP09327.
PhosphoSitePlusiP09327.

Expressioni

Tissue specificityi

Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes (at protein level).2 Publications

Gene expression databases

BgeeiENSG00000127831.
CleanExiHS_VIL1.
ExpressionAtlasiP09327. baseline and differential.
GenevisibleiP09327. HS.

Organism-specific databases

HPAiCAB002452.
HPA006884.
HPA006885.

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). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-746958,EBI-746958
PLCG1P191745EBI-746958,EBI-79387

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi113270. 6 interactors.
IntActiP09327. 2 interactors.
MINTiMINT-1484088.
STRINGi9606.ENSP00000248444.

Structurei

Secondary structure

1827
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi620 – 625Combined sources6
Beta strandi632 – 635Combined sources4
Helixi641 – 643Combined sources3
Beta strandi648 – 653Combined sources6
Beta strandi658 – 662Combined sources5
Helixi668 – 684Combined sources17
Beta strandi685 – 688Combined sources4
Beta strandi695 – 699Combined sources5
Helixi705 – 708Combined sources4
Helixi795 – 800Combined sources6
Helixi806 – 811Combined sources6
Helixi814 – 823Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UNCNMR-A793-827[»]
3FG7X-ray2.00A/B360-720[»]
ProteinModelPortaliP09327.
SMRiP09327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09327.

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
Repeati407 – 457Gelsolin-like 4Add BLAST51
Repeati528 – 568Gelsolin-like 5Add BLAST41
Repeati631 – 672Gelsolin-like 6Add BLAST42
Domaini761 – 827HPPROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 734CoreAdd BLAST733
Regioni2 – 126Necessary for homodimerizationAdd BLAST125
Regioni112 – 119LPA/PIP2-binding site 18
Regioni138 – 146LPA/PIP2-binding site 29
Regioni735 – 827HeadpieceAdd BLAST93
Regioni816 – 824LPA/PIP2-binding site 39

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.

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.
InParanoidiP09327.
KOiK05761.
OMAiVPVESKW.
OrthoDBiEOG091G05SC.
PhylomeDBiP09327.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P09327-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTKLSAQVKG SLNITTPGLQ IWRIEAMQMV PVPSSTFGSF FDGDCYIILA
60 70 80 90 100
IHKTASSLSY DIHYWIGQDS SLDEQGAAAI YTTQMDDFLK GRAVQHREVQ
110 120 130 140 150
GNESEAFRGY FKQGLVIRKG GVASGMKHVE TNSYDVQRLL HVKGKRNVVA
160 170 180 190 200
GEVEMSWKSF NRGDVFLLDL GKLIIQWNGP ESTRMERLRG MTLAKEIRDQ
210 220 230 240 250
ERGGRTYVGV VDGENELASP KLMEVMNHVL GKRRELKAAV PDTVVEPALK
260 270 280 290 300
AALKLYHVSD SEGNLVVREV ATRPLTQDLL SHEDCYILDQ GGLKIYVWKG
310 320 330 340 350
KKANEQEKKG AMSHALNFIK AKQYPPSTQV EVQNDGAESA VFQQLFQKWT
360 370 380 390 400
ASNRTSGLGK THTVGSVAKV EQVKFDATSM HVKPQVAAQQ KMVDDGSGEV
410 420 430 440 450
QVWRIENLEL VPVDSKWLGH FYGGDCYLLL YTYLIGEKQH YLLYVWQGSQ
460 470 480 490 500
ASQDEITASA YQAVILDQKY NGEPVQIRVP MGKEPPHLMS IFKGRMVVYQ
510 520 530 540 550
GGTSRTNNLE TGPSTRLFQV QGTGANNTKA FEVPARANFL NSNDVFVLKT
560 570 580 590 600
QSCCYLWCGK GCSGDEREMA KMVADTISRT EKQVVVEGQE PANFWMALGG
610 620 630 640 650
KAPYANTKRL QEENLVITPR LFECSNKTGR FLATEIPDFN QDDLEEDDVF
660 670 680 690 700
LLDVWDQVFF WIGKHANEEE KKAAATTAQE YLKTHPSGRD PETPIIVVKQ
710 720 730 740 750
GHEPPTFTGW FLAWDPFKWS NTKSYEDLKA ELGNSRDWSQ ITAEVTSPKV
760 770 780 790 800
DVFNANSNLS SGPLPIFPLE QLVNKPVEEL PEGVDPSRKE EHLSIEDFTQ
810 820
AFGMTPAAFS ALPRWKQQNL KKEKGLF
Length:827
Mass (Da):92,695
Last modified:March 3, 2009 - v4
Checksum:i96439B33B81E5F19
GO
Isoform 2 (identifier: P09327-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     368-421: AKVEQVKFDA...PVDSKWLGHF → GEGQAGAVRE...VLADGDVDKL
     422-827: Missing.

Note: No experimental confirmation available.
Show »
Length:421
Mass (Da):46,567
Checksum:i897332F5D0ECFC02
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti146R → K in BAG36454 (PubMed:14702039).Curated1
Sequence conflicti732L → S in CAA31386 (PubMed:2846586).Curated1
Sequence conflicti732L → S in CAA28355 (Ref. 4) Curated1
Sequence conflicti735S → L in CAA31386 (PubMed:2846586).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_054502254K → R.Corresponds to variant rs35305540dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054436368 – 421AKVEQ…WLGHF → GEGQAGAVREPGSRSWARRA TWSTTHPPSLTCIFNEDFYA GSGLVLADGDVDKL in isoform 2. 1 PublicationAdd BLAST54
Alternative sequenceiVSP_054437422 – 827Missing in isoform 2. 1 PublicationAdd BLAST406

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12901 mRNA. Translation: CAA31386.1.
AK313709 mRNA. Translation: BAG36454.1.
AC021016 Genomic DNA. No translation available.
AC073838 Genomic DNA. Translation: AAY14886.1.
CH471063 Genomic DNA. Translation: EAW70619.1.
BC017303 mRNA. Translation: AAH17303.1.
X04657 mRNA. Translation: CAA28355.1.
CCDSiCCDS2417.1. [P09327-1]
PIRiA31642.
RefSeqiNP_009058.2. NM_007127.2. [P09327-1]
UniGeneiHs.654595.

Genome annotation databases

EnsembliENST00000248444; ENSP00000248444; ENSG00000127831. [P09327-1]
ENST00000440053; ENSP00000409270; ENSG00000127831. [P09327-2]
GeneIDi7429.
KEGGihsa:7429.
UCSCiuc002via.4. human. [P09327-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12901 mRNA. Translation: CAA31386.1.
AK313709 mRNA. Translation: BAG36454.1.
AC021016 Genomic DNA. No translation available.
AC073838 Genomic DNA. Translation: AAY14886.1.
CH471063 Genomic DNA. Translation: EAW70619.1.
BC017303 mRNA. Translation: AAH17303.1.
X04657 mRNA. Translation: CAA28355.1.
CCDSiCCDS2417.1. [P09327-1]
PIRiA31642.
RefSeqiNP_009058.2. NM_007127.2. [P09327-1]
UniGeneiHs.654595.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UNCNMR-A793-827[»]
3FG7X-ray2.00A/B360-720[»]
ProteinModelPortaliP09327.
SMRiP09327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113270. 6 interactors.
IntActiP09327. 2 interactors.
MINTiMINT-1484088.
STRINGi9606.ENSP00000248444.

PTM databases

iPTMnetiP09327.
PhosphoSitePlusiP09327.

Polymorphism and mutation databases

BioMutaiVIL1.
DMDMi224471905.

Proteomic databases

EPDiP09327.
MaxQBiP09327.
PaxDbiP09327.
PeptideAtlasiP09327.
PRIDEiP09327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000248444; ENSP00000248444; ENSG00000127831. [P09327-1]
ENST00000440053; ENSP00000409270; ENSG00000127831. [P09327-2]
GeneIDi7429.
KEGGihsa:7429.
UCSCiuc002via.4. human. [P09327-1]

Organism-specific databases

CTDi7429.
DisGeNETi7429.
GeneCardsiVIL1.
HGNCiHGNC:12690. VIL1.
HPAiCAB002452.
HPA006884.
HPA006885.
MIMi193040. gene.
neXtProtiNX_P09327.
OpenTargetsiENSG00000127831.
PharmGKBiPA37309.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0443. Eukaryota.
ENOG410XR0A. LUCA.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiP09327.
KOiK05761.
OMAiVPVESKW.
OrthoDBiEOG091G05SC.
PhylomeDBiP09327.
TreeFamiTF313468.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000127831-MONOMER.
SIGNORiP09327.

Miscellaneous databases

ChiTaRSiVIL1. human.
EvolutionaryTraceiP09327.
GenomeRNAii7429.
PROiP09327.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000127831.
CleanExiHS_VIL1.
ExpressionAtlasiP09327. baseline and differential.
GenevisibleiP09327. HS.

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_HUMAN
AccessioniPrimary (citable) accession number: P09327
Secondary accession number(s): B2R9A7, Q53S11, Q96AC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 3, 2009
Last modified: November 2, 2016
This is version 169 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.