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P09327

- VILI_HUMAN

UniProt

P09327 - VILI_HUMAN

Protein

Villin-1

Gene

VIL1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 4 (03 Mar 2009)
      Previous versions | rss
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    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 binding Source: UniProtKB
    8. 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

    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

    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.
    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

    ArrayExpressiP09327.
    BgeeiP09327.
    CleanExiHS_VIL1.
    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. 3 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.
    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

    MTKLSAQVKG SLNITTPGLQ IWRIEAMQMV PVPSSTFGSF FDGDCYIILA    50
    IHKTASSLSY DIHYWIGQDS SLDEQGAAAI YTTQMDDFLK GRAVQHREVQ 100
    GNESEAFRGY FKQGLVIRKG GVASGMKHVE TNSYDVQRLL HVKGKRNVVA 150
    GEVEMSWKSF NRGDVFLLDL GKLIIQWNGP ESTRMERLRG MTLAKEIRDQ 200
    ERGGRTYVGV VDGENELASP KLMEVMNHVL GKRRELKAAV PDTVVEPALK 250
    AALKLYHVSD SEGNLVVREV ATRPLTQDLL SHEDCYILDQ GGLKIYVWKG 300
    KKANEQEKKG AMSHALNFIK AKQYPPSTQV EVQNDGAESA VFQQLFQKWT 350
    ASNRTSGLGK THTVGSVAKV EQVKFDATSM HVKPQVAAQQ KMVDDGSGEV 400
    QVWRIENLEL VPVDSKWLGH FYGGDCYLLL YTYLIGEKQH YLLYVWQGSQ 450
    ASQDEITASA YQAVILDQKY NGEPVQIRVP MGKEPPHLMS IFKGRMVVYQ 500
    GGTSRTNNLE TGPSTRLFQV QGTGANNTKA FEVPARANFL NSNDVFVLKT 550
    QSCCYLWCGK GCSGDEREMA KMVADTISRT EKQVVVEGQE PANFWMALGG 600
    KAPYANTKRL QEENLVITPR LFECSNKTGR FLATEIPDFN QDDLEEDDVF 650
    LLDVWDQVFF WIGKHANEEE KKAAATTAQE YLKTHPSGRD PETPIIVVKQ 700
    GHEPPTFTGW FLAWDPFKWS NTKSYEDLKA ELGNSRDWSQ ITAEVTSPKV 750
    DVFNANSNLS SGPLPIFPLE QLVNKPVEEL PEGVDPSRKE EHLSIEDFTQ 800
    AFGMTPAAFS ALPRWKQQNL KKEKGLF 827
    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. 3 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.
    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

    ArrayExpressi P09327.
    Bgeei P09327.
    CleanExi HS_VIL1.
    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

    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 1, 2014
    This is version 148 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