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P09327

- VILI_HUMAN

UniProt

P09327 - VILI_HUMAN

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Protein

Villin-1

Gene

VIL1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

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

GO - Biological processi

  1. actin filament capping Source: UniProtKB
  2. actin filament depolymerization Source: UniProtKB
  3. actin filament polymerization Source: UniProtKB
  4. actin filament severing Source: UniProtKB
  5. cellular response to epidermal growth factor stimulus Source: UniProtKB
  6. cellular response to hepatocyte growth factor stimulus Source: Ensembl
  7. cytoplasmic actin-based contraction involved in cell motility Source: UniProtKB
  8. epidermal growth factor receptor signaling pathway Source: UniProtKB
  9. epithelial cell differentiation Source: UniProt
  10. positive regulation of actin filament bundle assembly Source: UniProtKB
  11. positive regulation of cell migration Source: UniProtKB
  12. positive regulation of epithelial cell migration Source: UniProtKB
  13. protein complex assembly Source: ProtInc
  14. regulation of actin nucleation Source: UniProtKB
  15. regulation of cell shape Source: UniProtKB
  16. regulation of lamellipodium morphogenesis Source: UniProtKB
  17. regulation of wound healing Source: UniProtKB
  18. response to bacterium Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Actin capping

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Actin-binding, Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Villin-1
Gene namesi
Name:VIL1
Synonyms:VIL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:12690. VIL1.

Subcellular locationi

Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cell projectionruffle. Cell projectionmicrovillus. Cell projectionfilopodium tip By similarity. Cell projectionfilopodium By similarity
Note: Relocalized in the tip of cellular protrusions and filipodial extensions upon infection with S.flexneri in primary intestinal epithelial cells (IEC) and in the tail-like structures forming the actin comets of S.flexneri. Redistributed to the leading edge of hepatocyte growth factor (HGF)-induced lamellipodia (By similarity). Rapidly redistributed to ruffles and lamellipodia structures in response to autotaxin, lysophosphatidic acid (LPA) and epidermal growth factor (EGF) treatment.By similarity

GO - Cellular componenti

  1. actin filament bundle Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. extracellular vesicular exosome Source: UniProt
  4. filopodium Source: UniProtKB
  5. filopodium tip Source: UniProtKB
  6. lamellipodium Source: UniProtKB
  7. microvillus Source: UniProtKB
  8. 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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi25 – 251E → Q: Inhibits activities regarding actin capping, actin severing and actin bundling. 1 Publication
Mutagenesisi44 – 441D → L: Inhibits activities regarding actin capping and actin severing. 1 Publication
Mutagenesisi46 – 461Y → 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 Publications
Mutagenesisi60 – 601Y → 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 Publications
Mutagenesisi61 – 611D → N: Inhibits actin-severing activity. Does not inhibit actin-nucleation and actin-capping activities. 2 Publications
Mutagenesisi74 – 741E → L: Inhibits activities regarding actin capping and actin severing. 2 Publications
Mutagenesisi81 – 811Y → 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 Publications
Mutagenesisi86 – 916DDFLKG → 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 Publication
Mutagenesisi86 – 861D → L: Inhibits actin-severing activity. Does not inhibit actin-capping activity. 1 Publication
Mutagenesisi93 – 931A → G: Inhibits actin-severing activity. Does not inhibit actin-capping activity. 1 Publication
Mutagenesisi125 – 1295GMKHV → 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 Publication
Mutagenesisi138 – 1381R → A: Reduces binding to PIP2. 1 Publication
Mutagenesisi145 – 1451K → A: Does not reduce binding to PIP2. 1 Publication
Mutagenesisi146 – 1461R → A: Does not reduce binding to PIP2. 1 Publication
Mutagenesisi256 – 2561Y → 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 Publications
Mutagenesisi286 – 2861Y → 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 Publications
Mutagenesisi324 – 3241Y → 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 Publications
Mutagenesisi461 – 4611Y → 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 Publications
Mutagenesisi467 – 4671D → L: Reduces the Ca(2+)-dependent actin-severing activity. 1 Publication
Mutagenesisi555 – 5551Y → 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 Publications
Mutagenesisi604 – 6041Y → 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 Publications
Mutagenesisi715 – 7151D → L: Reduces the Ca(2+)-dependent actin-severing activity. 1 Publication
Mutagenesisi725 – 7251Y → 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 Publications
Mutagenesisi815 – 8151W → A: Reduces interaction with F-actin. 1 Publication
Mutagenesisi822 – 8221K → A: Does not reduce binding to PIP2. 1 Publication
Mutagenesisi824 – 8241K → A: Does not reduce binding to PIP2. 1 Publication

Organism-specific databases

PharmGKBiPA37309.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 827826Villin-1PRO_0000218727Add
BLAST

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

Proteomic databases

MaxQBiP09327.
PaxDbiP09327.
PRIDEiP09327.

PTM databases

PhosphoSiteiP09327.

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

BgeeiP09327.
CleanExiHS_VIL1.
ExpressionAtlasiP09327. baseline and differential.
GenevestigatoriP09327.

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

Protein-protein interaction databases

BioGridi113270. 4 interactions.
IntActiP09327. 2 interactions.
MINTiMINT-1484088.
STRINGi9606.ENSP00000248444.

Structurei

Secondary structure

1
827
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi620 – 6256
Beta strandi632 – 6354
Helixi641 – 6433
Beta strandi648 – 6536
Beta strandi658 – 6625
Helixi668 – 68417
Beta strandi685 – 6884
Beta strandi695 – 6995
Helixi705 – 7084
Helixi795 – 8006
Helixi806 – 8116
Helixi814 – 82310

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UNCNMR-A793-827[»]
3FG7X-ray2.00A/B360-720[»]
ProteinModelPortaliP09327.
SMRiP09327. Positions 3-720, 767-827.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09327.

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 homodimerizationAdd
BLAST
Regioni112 – 1198LPA/PIP2-binding site 1
Regioni138 – 1469LPA/PIP2-binding site 2
Regioni735 – 82793HeadpieceAdd
BLAST
Regioni816 – 8249LPA/PIP2-binding site 3

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

eggNOGiNOG304849.
GeneTreeiENSGT00760000119111.
HOGENOMiHOG000233630.
HOVERGENiHBG004183.
InParanoidiP09327.
KOiK05761.
OMAiVPVESKW.
OrthoDBiEOG7288RJ.
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.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view]
PANTHERiPTHR11977. PTHR11977. 1 hit.
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.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461R → K in BAG36454. (PubMed:14702039)Curated
Sequence conflicti732 – 7321L → S in CAA31386. (PubMed:2846586)Curated
Sequence conflicti732 – 7321L → S in CAA28355. 1 PublicationCurated
Sequence conflicti735 – 7351S → L in CAA31386. (PubMed:2846586)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti254 – 2541K → R.
Corresponds to variant rs35305540 [ dbSNP | Ensembl ].
VAR_054502

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei368 – 42154AKVEQ…WLGHF → GEGQAGAVREPGSRSWARRA TWSTTHPPSLTCIFNEDFYA GSGLVLADGDVDKL in isoform 2. 1 PublicationVSP_054436Add
BLAST
Alternative sequencei422 – 827406Missing in isoform 2. 1 PublicationVSP_054437Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human. [P09327-1]
uc002vic.1. human.

Polymorphism databases

DMDMi224471905.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2417.1. [P09327-1 ]
PIRi A31642.
RefSeqi NP_009058.2. NM_007127.2. [P09327-1 ]
UniGenei Hs.654595.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UNC NMR - A 793-827 [» ]
3FG7 X-ray 2.00 A/B 360-720 [» ]
ProteinModelPortali P09327.
SMRi P09327. Positions 3-720, 767-827.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113270. 4 interactions.
IntActi P09327. 2 interactions.
MINTi MINT-1484088.
STRINGi 9606.ENSP00000248444.

PTM databases

PhosphoSitei P09327.

Polymorphism databases

DMDMi 224471905.

Proteomic databases

MaxQBi P09327.
PaxDbi P09327.
PRIDEi P09327.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248444 ; ENSP00000248444 ; ENSG00000127831 . [P09327-1 ]
ENST00000440053 ; ENSP00000409270 ; ENSG00000127831 . [P09327-2 ]
GeneIDi 7429.
KEGGi hsa:7429.
UCSCi uc002via.3. human. [P09327-1 ]
uc002vic.1. human.

Organism-specific databases

CTDi 7429.
GeneCardsi GC02P219285.
HGNCi HGNC:12690. VIL1.
HPAi CAB002452.
HPA006884.
HPA006885.
MIMi 193040. gene.
neXtProti NX_P09327.
PharmGKBi PA37309.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG304849.
GeneTreei ENSGT00760000119111.
HOGENOMi HOG000233630.
HOVERGENi HBG004183.
InParanoidi P09327.
KOi K05761.
OMAi VPVESKW.
OrthoDBi EOG7288RJ.
PhylomeDBi P09327.
TreeFami TF313468.

Miscellaneous databases

EvolutionaryTracei P09327.
GenomeRNAii 7429.
NextBioi 29096.
PROi P09327.
SOURCEi Search...

Gene expression databases

Bgeei P09327.
CleanExi HS_VIL1.
ExpressionAtlasi P09327. baseline and differential.
Genevestigatori P09327.

Family and domain databases

Gene3Di 1.10.950.10. 1 hit.
3.40.20.10. 6 hits.
InterProi IPR029006. ADF-H/Gelsolin-like_dom.
IPR007123. Gelsolin-like_dom.
IPR007122. Villin/Gelsolin.
IPR003128. Villin_headpiece.
[Graphical view ]
PANTHERi PTHR11977. PTHR11977. 1 hit.
Pfami PF00626. Gelsolin. 6 hits.
PF02209. VHP. 1 hit.
[Graphical view ]
PRINTSi PR00597. GELSOLIN.
SMARTi SM00262. GEL. 6 hits.
SM00153. VHP. 1 hit.
[Graphical view ]
SUPFAMi SSF47050. SSF47050. 1 hit.
PROSITEi PS51089. HP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity."
    Arpin M., Pringault E., Finidori J., Garcia A., Jeltsch J.-M., Louvard D., van de Kerckhove B.
    J. Cell Biol. 107:1759-1766(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 2-13.
    Tissue: Intestine.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Liver.
  6. "A human villin cDNA clone to investigate the differentiation of intestinal and kidney cells in vivo and in culture."
    Pringault E., Arpin M., Garcia A., Finidori J., Louvard D.
    EMBO J. 5:3119-3124(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 718-827 (ISOFORM 1), TISSUE SPECIFICITY.
  7. "Different calcium dependence of the capping and cutting activities of villin."
    Northrop J., Weber A., Mooseker M.S., Franzini-Armstrong C., Bishop M.F., Dubyak G.R., Tucker M., Walsh T.P.
    J. Biol. Chem. 261:9274-9281(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton."
    Zhai L., Zhao P., Panebra A., Guerrerio A.L., Khurana S.
    J. Biol. Chem. 276:36163-36167(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH F-ACTIN, PHOSPHORYLATION.
  9. "Regulation of actin dynamics by tyrosine phosphorylation: identification of tyrosine phosphorylation sites within the actin-severing domain of villin."
    Zhai L., Kumar N., Panebra A., Zhao P., Parrill A.L., Khurana S.
    Biochemistry 41:11750-11760(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY SRC, PHOSPHORYLATION AT TYROSINE RESIDUES, MUTAGENESIS OF TYR-46; TYR-60; TYR-81 AND TYR-256.
  10. "Abnormalities in villin gene expression and canalicular microvillus structure in progressive cholestatic liver disease of childhood."
    Phillips M.J., Azuma T., Meredith S.L., Squire J.A., Ackerley C.A., Pluthero F.G., Roberts E.A., Superina R.A., Levy G.A., Marsden P.A.
    Lancet 362:1112-1119(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INVOLVEMENT IN BILIARY ATRESIA, TISSUE SPECIFICITY.
  11. "Association of villin with phosphatidylinositol 4,5-bisphosphate regulates the actin cytoskeleton."
    Kumar N., Zhao P., Tomar A., Galea C.A., Khurana S.
    J. Biol. Chem. 279:3096-3110(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PHOSPHATIDYLINOSITOL, MUTAGENESIS OF ARG-138; LYS-145; ARG-146; LYS-822 AND LYS-824.
  12. "Identification of a functional switch for actin severing by cytoskeletal proteins."
    Kumar N., Khurana S.
    J. Biol. Chem. 279:24915-24918(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-467 AND ASP-715.
  13. "Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin."
    Kumar N., Tomar A., Parrill A.L., Khurana S.
    J. Biol. Chem. 279:45036-45046(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CALCIUM-BINDING, MUTAGENESIS OF GLU-25; ASP-44; ASP-61; GLU-74; ASP-86 AND ALA-93.
  14. Cited for: FUNCTION, MUTAGENESIS OF TYR-46; TYR-60; TYR-81 AND TYR-256, SUBCELLULAR LOCATION.
  15. "Interaction of phospholipase C-gamma1 with villin regulates epithelial cell migration."
    Tomar A., George S., Kansal P., Wang Y., Khurana S.
    J. Biol. Chem. 281:31972-31986(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYROSINE RESIDUES, MUTAGENESIS OF TYR-46; TYR-60; TYR-81; TYR-256; TYR-286; TYR-324; TYR-461; TYR-555; TYR-604 AND TYR-725, SUBCELLULAR LOCATION.
  16. "Obligatory role for phospholipase C-gamma(1) in villin-induced epithelial cell migration."
    Wang Y., Tomar A., George S.P., Khurana S.
    Am. J. Physiol. 292:C1775-C1786(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYROSINE RESIDUES, MUTAGENESIS OF TYR-46; TYR-60; TYR-81; TYR-256; TYR-286; TYR-324; TYR-461; TYR-555; TYR-604 AND TYR-725, SUBCELLULAR LOCATION.
  17. "Dimerization and actin-bundling properties of villin and its role in the assembly of epithelial cell brush borders."
    George S.P., Wang Y., Mathew S., Srinivasan K., Khurana S.
    J. Biol. Chem. 282:26528-26541(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION.
  18. "Villin severing activity enhances actin-based motility in vivo."
    Revenu C., Courtois M., Michelot A., Sykes C., Louvard D., Robine S.
    Mol. Biol. Cell 18:827-838(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-61; GLU-74; 86-ASP--GLY-91 AND 125-GLY--VAL-129, SUBCELLULAR LOCATION.
  19. "Autotaxin and lysophosphatidic acid stimulate intestinal cell motility by redistribution of the actin modifying protein villin to the developing lamellipodia."
    Khurana S., Tomar A., George S.P., Wang Y., Siddiqui M.R., Guo H., Tigyi G., Mathew S.
    Exp. Cell Res. 314:530-542(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-46; TYR-60; TYR-81; TYR-256; TYR-286; TYR-324; TYR-461; TYR-555; TYR-604 AND TYR-725, SUBCELLULAR LOCATION.
  20. "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, SUBCELLULAR LOCATION.
  21. "Differential effects of lysophosphatidic acid and phosphatidylinositol 4,5-bisphosphate on actin dynamics by direct association with the actin-binding protein villin."
    Tomar A., George S.P., Mathew S., Khurana S.
    J. Biol. Chem. 284:35278-35282(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LYSOPHOSPHATIDIC ACID, ASSOCIATION WITH F-ACTIN, SUBCELLULAR LOCATION.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements."
    Vermeulen W., Vanhaesebrouck P., Van Troys M., Verschueren M., Fant F., Goethals M., Ampe C., Martins J.C., Borremans F.A.
    Protein Sci. 13:1276-1287(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 793-827, ASSOCIATION WITH F-ACTIN, MUTAGENESIS OF TRP-815.
  24. "Helix straightening as an activation mechanism in the gelsolin superfamily of actin regulatory proteins."
    Wang H., Chumnarnsilpa S., Loonchanta A., Li Q., Kuan Y.M., Robine S., Larsson M., Mihalek I., Burtnick L.D., Robinson R.C.
    J. Biol. Chem. 284:21265-21269(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 360-720.

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: October 29, 2014
This is version 149 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

External Data

Dasty 3