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    TWF1 twinfilin TWF1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852971, updated on 17-Dec-2024

    Summary

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    Official Symbol
    TWF1
    Official Full Name
    twinfilin TWF1
    Primary source
    SGD:S000003312
    Locus tag
    YGR080W
    See related
    AllianceGenome:SGD:S000003312; FungiDB:YGR080W; VEuPathDB:YGR080W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables actin filament binding activity and actin monomer binding activity. Involved in actin cytoskeleton organization; actin filament severing; and regulation of actin polymerization or depolymerization. Located in actin filament. Orthologous to several human genes including TWF2 (twinfilin actin binding protein 2). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See TWF1 in Genome Data Viewer
    Location:
    chromosome: VII
    Exon count:
    1
    Sequence:
    Chromosome: VII; NC_001139.9 (642010..643008)

    Chromosome VII - NC_001139.9Genomic Context describing neighboring genes Neighboring gene tubulin-binding prefolding complex subunit PAC10 Neighboring gene uncharacterized protein Neighboring gene Slx9p Neighboring gene Tom20p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001139.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The ADF homology (ADF-H) domain: a highly exploited actin-binding module. Lappalainen P, et al. Mol Biol Cell, 1998 Aug. PMID 9693358, Free PMC Article
    2. Species-Specific Functions of Twinfilin in Actin Filament Depolymerization. Hilton DM, et al. J Mol Biol, 2018 Sep 14. PMID 29928893, Free PMC Article
    3. Regulation of the cortical actin cytoskeleton in budding yeast by twinfilin, a ubiquitous actin monomer-sequestering protein. Goode BL, et al. J Cell Biol, 1998 Aug 10. PMID 9700161, Free PMC Article
    4. High-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP. Johnston AB, et al. Nat Cell Biol, 2015 Nov. PMID 26458246, Free PMC Article
    5. Biological role and structural mechanism of twinfilin-capping protein interaction. Falck S, et al. EMBO J, 2004 Aug 4. PMID 15282541, Free PMC Article

    See all (45) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Data show that Twinfilin and Srv2 proteins accelerate depolymerization from actin filament ends.
      Title: High-speed depolymerization at actin filament ends jointly catalysed by Twinfilin and Srv2/CAP.
    2. Together, our data suggest that twinfilin coordinates filament severing and monomer sequestering at sites of rapid actin turnover and is controlled by multiple regulatory inputs.
      Title: Twinfilin is an actin-filament-severing protein and promotes rapid turnover of actin structures in vivo.
    3. binding of twinfilin to capping protein does not affect the binding of either protein to actin
      Title: Biological role and structural mechanism of twinfilin-capping protein interaction.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables actin binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables actin filament binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables actin filament binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables actin monomer binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables actin monomer binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in actin cortical patch organization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in actin filament depolymerization IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in actin filament depolymerization IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in actin filament organization IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in actin filament organization IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in actin filament severing IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in actin filament severing IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in barbed-end actin filament capping IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in negative regulation of actin filament polymerization IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in positive regulation of actin filament depolymerization IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in sequestering of actin monomers IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in sequestering of actin monomers IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in actin filament IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in actin filament IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytoskeleton IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mating projection tip HDA PubMed 

    General protein information

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    Preferred Names
    twinfilin TWF1
    NP_011594.3
    • Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, stimulates actin depolymerization as does the mouse homolog, mTwf1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

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

    Reference assembly

    Genomic

    1. NC_001139.9 Reference assembly

      Range
      642010..643008
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181209.3 → NP_011594.3  TPA: twinfilin TWF1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011594.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VUL2, P53250
      UniProtKB/TrEMBL
      A6ZV62, B3LIE6, B5VJ24, C7GXQ9, C8Z8X4, G2WEG4, N1P3X8
      Conserved Domains (2) summary
      cd11284
      Location:175 → 297
      ADF_Twf-C_like; C-terminal ADF domain of twinfilin and related proteins
      cd11285
      Location:4 → 124
      ADF_Twf-N_like; N-terminal ADF domain of twinfilin and related proteins
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P53250.1

    Gene LinkOut

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