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P18760

- COF1_MOUSE

UniProt

P18760 - COF1_MOUSE

Protein

Cofilin-1

Gene

Cfl1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation By similarity.By similarity

    GO - Biological processi

    1. actin filament depolymerization Source: InterPro
    2. actin filament organization Source: MGI
    3. cell projection organization Source: MGI
    4. cellular component movement Source: MGI
    5. cytoskeleton organization Source: UniProtKB
    6. establishment of cell polarity Source: MGI
    7. mitotic cytokinesis Source: MGI
    8. negative regulation of cell size Source: MGI
    9. neural crest cell migration Source: MGI
    10. neural fold formation Source: MGI
    11. positive regulation of actin filament depolymerization Source: MGI
    12. protein import into nucleus Source: Ensembl
    13. protein phosphorylation Source: MGI
    14. regulation of cell morphogenesis Source: UniProtKB
    15. response to amino acid Source: MGI
    16. response to virus Source: Ensembl

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cofilin-1
    Alternative name(s):
    Cofilin, non-muscle isoform
    Gene namesi
    Name:Cfl1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:101757. Cfl1.

    Subcellular locationi

    Nucleus matrix. Cytoplasmcytoskeleton. Cell projectionruffle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projectionlamellipodium membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock By similarity.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cortical actin cytoskeleton Source: MGI
    3. cytoplasm Source: MGI
    4. cytosol Source: Reactome
    5. extracellular region Source: Reactome
    6. lamellipodium membrane Source: UniProtKB-SubCell
    7. nuclear matrix Source: UniProtKB-SubCell
    8. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 166165Cofilin-1PRO_0000214900Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei3 – 31Phosphoserine2 Publications
    Modified residuei8 – 81Phosphoserine1 Publication
    Modified residuei13 – 131N6-acetyllysineBy similarity
    Modified residuei25 – 251PhosphothreonineBy similarity
    Modified residuei68 – 681Phosphotyrosine1 Publication
    Modified residuei73 – 731N6-acetyllysineBy similarity
    Modified residuei140 – 1401Phosphotyrosine2 Publications
    Modified residuei144 – 1441N6-acetyllysineBy similarity
    Modified residuei156 – 1561PhosphoserineBy similarity

    Post-translational modificationi

    Inactivated by phosphorylation on Ser-3. Phosphorylated on Ser-3 in resting cells By similarity. Dephosphorylated by PDXP/chronophin; this restores its activity in promoting actin filament depolymerization. The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal By similarity. Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1 cascade upon active ligand stimulation of atypical chemokine receptor ACKR2 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP18760.
    PaxDbiP18760.
    PRIDEiP18760.

    2D gel databases

    REPRODUCTION-2DPAGEP18760.
    SWISS-2DPAGEP18760.

    PTM databases

    PhosphoSiteiP18760.

    Expressioni

    Tissue specificityi

    Widely distributed in various tissues.

    Gene expression databases

    BgeeiP18760.
    CleanExiMM_CFL1.
    GenevestigatoriP18760.

    Interactioni

    Subunit structurei

    Can bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is a major component of intranuclear and cytoplasmic actin rods.

    Protein-protein interaction databases

    BioGridi198684. 7 interactions.
    DIPiDIP-38073N.
    IntActiP18760. 8 interactions.
    MINTiMINT-1862314.

    Structurei

    3D structure databases

    ProteinModelPortaliP18760.
    SMRiP18760. Positions 1-166.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 153150ADF-HPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi30 – 345Nuclear localization signalSequence Analysis

    Sequence similaritiesi

    Belongs to the actin-binding proteins ADF family.Curated
    Contains 1 ADF-H domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG286948.
    HOGENOMiHOG000039697.
    HOVERGENiHBG000381.
    KOiK05765.
    PhylomeDBiP18760.

    Family and domain databases

    Gene3Di3.40.20.10. 1 hit.
    InterProiIPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR017904. ADF/Cofilin/Destrin.
    IPR027234. Cofilin_1.
    [Graphical view]
    PANTHERiPTHR11913. PTHR11913. 1 hit.
    PTHR11913:SF17. PTHR11913:SF17. 1 hit.
    PfamiPF00241. Cofilin_ADF. 1 hit.
    [Graphical view]
    PRINTSiPR00006. COFILIN.
    SMARTiSM00102. ADF. 1 hit.
    [Graphical view]
    PROSITEiPS51263. ADF_H. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P18760-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE    50
    EGKEILVGDV GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV 100
    FIFWAPENAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA 150
    EKLGGSAVIS LEGKPL 166
    Length:166
    Mass (Da):18,560
    Last modified:January 23, 2007 - v3
    Checksum:i19834E8CA80747B2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00472 mRNA. Translation: BAA00364.1.
    BC046225 mRNA. Translation: AAH46225.1.
    BC058726 mRNA. Translation: AAH58726.1.
    PIRiS12584.
    RefSeqiNP_031713.1. NM_007687.5.
    UniGeneiMm.329655.

    Genome annotation databases

    GeneIDi12631.
    KEGGimmu:12631.
    UCSCiuc008gdq.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D00472 mRNA. Translation: BAA00364.1 .
    BC046225 mRNA. Translation: AAH46225.1 .
    BC058726 mRNA. Translation: AAH58726.1 .
    PIRi S12584.
    RefSeqi NP_031713.1. NM_007687.5.
    UniGenei Mm.329655.

    3D structure databases

    ProteinModelPortali P18760.
    SMRi P18760. Positions 1-166.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198684. 7 interactions.
    DIPi DIP-38073N.
    IntActi P18760. 8 interactions.
    MINTi MINT-1862314.

    PTM databases

    PhosphoSitei P18760.

    2D gel databases

    REPRODUCTION-2DPAGE P18760.
    SWISS-2DPAGE P18760.

    Proteomic databases

    MaxQBi P18760.
    PaxDbi P18760.
    PRIDEi P18760.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 12631.
    KEGGi mmu:12631.
    UCSCi uc008gdq.2. mouse.

    Organism-specific databases

    CTDi 1072.
    MGIi MGI:101757. Cfl1.

    Phylogenomic databases

    eggNOGi NOG286948.
    HOGENOMi HOG000039697.
    HOVERGENi HBG000381.
    KOi K05765.
    PhylomeDBi P18760.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.

    Miscellaneous databases

    NextBioi 281816.
    PROi P18760.
    SOURCEi Search...

    Gene expression databases

    Bgeei P18760.
    CleanExi MM_CFL1.
    Genevestigatori P18760.

    Family and domain databases

    Gene3Di 3.40.20.10. 1 hit.
    InterProi IPR002108. ADF-H.
    IPR029006. ADF-H/Gelsolin-like_dom.
    IPR017904. ADF/Cofilin/Destrin.
    IPR027234. Cofilin_1.
    [Graphical view ]
    PANTHERi PTHR11913. PTHR11913. 1 hit.
    PTHR11913:SF17. PTHR11913:SF17. 1 hit.
    Pfami PF00241. Cofilin_ADF. 1 hit.
    [Graphical view ]
    PRINTSi PR00006. COFILIN.
    SMARTi SM00102. ADF. 1 hit.
    [Graphical view ]
    PROSITEi PS51263. ADF_H. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Swiss Webster.
    2. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    3. Bienvenut W.V.
      Submitted (JUL-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13 AND 153-166, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Liver.
    4. Lubec G., Klug S.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 54-73 AND 96-112, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Hippocampus.
    5. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND TYR-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiCOF1_MOUSE
    AccessioniPrimary (citable) accession number: P18760
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 146 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3