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    VIL1 villin 1 [ Gallus gallus (chicken) ]

    Gene ID: 396423, updated on 17-Aug-2024

    Summary

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    Symbol
    VIL1provided by CGNC
    Full Name
    villin 1provided by CGNC
    Primary source
    CGNC:49795
    See related
    Ensembl:ENSGALG00010019011
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Gallus gallus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae; Phasianinae; Gallus
    Also known as
    VIL
    Orthologs
    human mouse all
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    Genomic context

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    See VIL1 in Genome Data Viewer
    Location:
    chromosome: 7
    Exon count:
    21
    Annotation release Status Assembly Chr Location
    106 current bGalGal1.mat.broiler.GRCg7b (GCF_016699485.2) 7 NC_052538.1 (22157465..22164464, complement)
    106 current bGalGal1.pat.whiteleghornlayer.GRCg7w (GCF_016700215.2) 7 NC_052579.1 (22077205..22084205, complement)

    Chromosome 7 - NC_052538.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC112532794 Neighboring gene CCR4-NOT transcription complex subunit 9 Neighboring gene ubiquitin specific peptidase 37 Neighboring gene CTD small phosphatase 1 Neighboring gene microRNA mir-26a-2 Neighboring gene solute carrier family 11 member 1

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Multistate folding of the villin headpiece domain. Tang Y, et al. J Mol Biol, 2006 Feb 3. PMID 16337228
    2. Villin sequence and peptide map identify six homologous domains. Bazari WL, et al. Proc Natl Acad Sci U S A, 1988 Jul. PMID 2839826, Free PMC Article
    3. Demonstration of at least two different actin-binding sites in villin, a calcium-regulated modulator of F-actin organization. Glenney JR Jr, et al. J Biol Chem, 1981 Aug 10. PMID 6790532
    4. Demonstration of three distinct calcium-binding sites in villin, a modulator of actin assembly. Hesterberg LK, et al. J Biol Chem, 1983 Jan 10. PMID 6848508
    5. Solution structure of villin 14T, a domain conserved among actin-severing proteins. Markus MA, et al. Protein Sci, 1994 Jan. PMID 8142900, Free PMC Article

    See all (20) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. This study computes the free-energy landscape in the space of all villin C-alpha carbons. This landscape has the shape of a 12-dimensional funnel with the free energy decreasing monotonically as a function of the native contacts. There are no significant folding barriers.
      Title: Explicit Characterization of the Free-Energy Landscape of a Protein in the Space of All Its C(α) Carbons.
    2. The thermostable 36-residue subdomain of the villin headpiece (HP36) is the smallest known cooperatively folding protein. The side chain methyl dynamics of villin HP36 has been measured across a wide range of temperatures.
      Title: The unusual internal motion of the villin headpiece subdomain.
    3. A compact native 24-residues-long supersecondary structure derived from the hyperstable villin headpiece subdomain consisting of helices 2 and 3, is described.
      Title: A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.
    4. side-chain dynamics of several key hydrophobic methyl groups in chicken villin headpiece subdomain (HP36)
      Title: Slow motions in the hydrophobic core of chicken villin headpiece subdomain and their contributions to configurational entropy and heat capacity from solid-state deuteron NMR measurements.
    5. a buried salt bridge is essential for villin headpiece folding and actin binding
      Title: Competition between intradomain and interdomain interactions: a buried salt bridge is essential for villin headpiece folding and actin binding.
    6. Villin headpiece domain HP67 & its mutant (H41Y) are resolved in different crystal form & space groups. 2 molecules occur in each asymmetric unit in the new space group P6(1) differing in harmonic motions.
      Title: Heterogeneity and dynamics in villin headpiece crystal structures.
    7. a crucial role for this proline residue in structural stability and folding potential of HP (sub)domains consistent with Pro-Trp stacking as a more general determinant of protein stability
      Title: Identification of the PXW sequence as a structural gatekeeper of the headpiece C-terminal subdomain fold.
    8. Results indicate that reduced conformational flexibility of the N-terminal subdomain in wild-type villin HP67 is due to intramolecular interactions with the His41 imidazole ring.
      Title: Characterizing a partially folded intermediate of the villin headpiece domain under non-denaturing conditions: contribution of His41 to the pH-dependent stability of the N-terminal subdomain.
    9. Results presented here demonstrate that unfolding of the villin headpiece is a multistate process.
      Title: Multistate folding of the villin headpiece domain.
    10. detailed comparison of these crystal structures with each other and to our previously determined NMR structures of HP67
      Title: High-resolution crystal structures of villin headpiece and mutants with reduced F-actin binding activity.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RefSeq

    Function Evidence Code Pubs
    enables actin filament binding IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    enables phosphatidylinositol-4,5-bisphosphate binding IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in actin filament severing IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in actin polymerization or depolymerization IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in barbed-end actin filament capping IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in cytoskeleton organization IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    involved_in regulation of lamellipodium morphogenesis IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in actin cytoskeleton IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 
    located_in lamellipodium IEA
    Inferred from Electronic Annotation
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    villin-1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001396564.1 → NP_001383493.1  villin-1 isoform 2

      Status: VALIDATED

      Source sequence(s)
      JAENSK010000236
      UniProtKB/Swiss-Prot
      P02640
      Conserved Domains (7) summary
      smart00153
      Location:785 → 820
      VHP; Villin headpiece domain
      cd11288
      Location:513 → 597
      gelsolin_S5_like; Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins
      cd11289
      Location:136 → 227
      gelsolin_S2_like; Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins
      cd11290
      Location:17 → 121
      gelsolin_S1_like; Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins
      cd11291
      Location:612 → 709
      gelsolin_S6_like; Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins
      cd11292
      Location:250 → 348
      gelsolin_S3_like; Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins
      cd11293
      Location:392 → 492
      gelsolin_S4_like; Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins

    2. NM_001396565.1 → NP_001383494.1  villin-1 isoform 1

      Status: VALIDATED

      Source sequence(s)
      JAENSK010000236
      UniProtKB/Swiss-Prot
      P02640
      Related
      ENSGALP00010027417.1, ENSGALT00010046020.1
      Conserved Domains (7) summary
      smart00153
      Location:791 → 826
      VHP; Villin headpiece domain
      cd11288
      Location:513 → 603
      gelsolin_S5_like; Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins
      cd11289
      Location:136 → 227
      gelsolin_S2_like; Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins
      cd11290
      Location:17 → 121
      gelsolin_S1_like; Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins
      cd11291
      Location:618 → 715
      gelsolin_S6_like; Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins
      cd11292
      Location:250 → 348
      gelsolin_S3_like; Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins
      cd11293
      Location:392 → 492
      gelsolin_S4_like; Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins

    3. NM_205442.2 → NP_990773.2  villin-1 isoform 1

      Status: VALIDATED

      Source sequence(s)
      JAENSK010000236
      UniProtKB/Swiss-Prot
      P02640
      Related
      ENSGALP00010027414.1, ENSGALT00010046014.1
      Conserved Domains (7) summary
      smart00153
      Location:791 → 826
      VHP; Villin headpiece domain
      cd11288
      Location:513 → 603
      gelsolin_S5_like; Gelsolin sub-domain 5-like domain found in gelsolin, severin, villin, and related proteins
      cd11289
      Location:136 → 227
      gelsolin_S2_like; Gelsolin sub-domain 2-like domain found in gelsolin, severin, villin, and related proteins
      cd11290
      Location:17 → 121
      gelsolin_S1_like; Gelsolin sub-domain 1-like domain found in gelsolin, severin, villin, and related proteins
      cd11291
      Location:618 → 715
      gelsolin_S6_like; Gelsolin sub-domain 6-like domain found in gelsolin, severin, villin, and related proteins
      cd11292
      Location:250 → 348
      gelsolin_S3_like; Gelsolin sub-domain 3-like domain found in gelsolin, severin, villin, and related proteins
      cd11293
      Location:392 → 492
      gelsolin_S4_like; Gelsolin sub-domain 4-like domain found in gelsolin, severin, villin, and related proteins

    RefSeqs of Annotated Genomes: Gallus gallus Annotation Release 106 details...Open this link in a new tab

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference bGalGal1.mat.broiler.GRCg7b Primary Assembly

    Genomic

    1. NC_052538.1 Reference bGalGal1.mat.broiler.GRCg7b Primary Assembly

      Range
      22157465..22164464 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    Alternate bGalGal1.pat.whiteleghornlayer.GRCg7w

    Genomic

    1. NC_052579.1 Alternate bGalGal1.pat.whiteleghornlayer.GRCg7w

      Range
      22077205..22084205 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P02640.2 GenPept UniProtKB/Swiss-Prot:P02640

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

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    Research Materials