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VIL1 villin 1 [ Gallus gallus (chicken) ]

Gene ID: 396423, updated on 5-Mar-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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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. Explicit Characterization of the Free-Energy Landscape of a Protein in the Space of All Its C(α) Carbons. Sormani G, et al. J Chem Theory Comput, 2020 Jan 14. PMID 31809040
  2. The unusual internal motion of the villin headpiece subdomain. Harpole KW, et al. Protein Sci, 2016 Feb. PMID 26473993, Free PMC Article
  3. A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain. Hocking HG, et al. Biophys J, 2015 Feb 3. PMID 25650934, Free PMC Article
  4. 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. Vugmeyster L, et al. Biochemistry, 2011 Dec 13. PMID 22085262, Free PMC Article
  5. Competition between intradomain and interdomain interactions: a buried salt bridge is essential for villin headpiece folding and actin binding. Packer LE, et al. Biochemistry, 2011 May 10. PMID 21449557, Free PMC Article

See all (18) 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.
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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

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