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P45592

- COF1_RAT

UniProt

P45592 - COF1_RAT

Protein

Cofilin-1

Gene

Cfl1

Organism
Rattus norvegicus (Rat)
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 By similarity. 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 - Molecular functioni

    1. actin binding Source: RGD
    2. protein binding Source: IntAct

    GO - Biological processi

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

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cofilin-1
    Alternative name(s):
    Cofilin, non-muscle isoform
    Gene namesi
    Name:Cfl1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 1

    Organism-specific databases

    RGDi69285. Cfl1.

    Subcellular locationi

    Nucleus matrix By similarity. Cytoplasmcytoskeleton By similarity. 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 leading edge Source: RGD
    2. cortical actin cytoskeleton Source: Ensembl
    3. cytoplasm Source: RGD
    4. lamellipodium Source: RGD
    5. lamellipodium membrane Source: UniProtKB-SubCell
    6. nuclear matrix Source: UniProtKB-SubCell
    7. 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_0000214902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei3 – 31Phosphoserine2 Publications
    Modified residuei8 – 81PhosphoserineBy similarity
    Modified residuei13 – 131N6-acetyllysineBy similarity
    Modified residuei25 – 251PhosphothreonineBy similarity
    Modified residuei68 – 681PhosphotyrosineBy similarity
    Modified residuei73 – 731N6-acetyllysineBy similarity
    Modified residuei140 – 1401PhosphotyrosineBy similarity
    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. 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

    PaxDbiP45592.
    PRIDEiP45592.

    2D gel databases

    World-2DPAGE0004:P45592.

    PTM databases

    PhosphoSiteiP45592.

    Expressioni

    Gene expression databases

    GenevestigatoriP45592.

    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 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CttnQ605982EBI-917556,EBI-397955From a different organism.
    CttnQ66HL24EBI-917556,EBI-6273816

    Protein-protein interaction databases

    BioGridi247942. 5 interactions.
    IntActiP45592. 4 interactions.
    MINTiMINT-247733.
    STRINGi10116.ENSRNOP00000028041.

    Structurei

    3D structure databases

    ProteinModelPortaliP45592.
    SMRiP45592. 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.
    GeneTreeiENSGT00440000033289.
    HOGENOMiHOG000039697.
    HOVERGENiHBG000381.
    InParanoidiP45592.
    KOiK05765.
    OMAiPPSCQTG.
    OrthoDBiEOG7353Z9.
    PhylomeDBiP45592.

    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.

    P45592-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE    50
    EGKEILVGDV GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV 100
    FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA 150
    EKLGGSAVIS LEGKPL 166
    Length:166
    Mass (Da):18,533
    Last modified:January 23, 2007 - v3
    Checksum:i19835391A81A5AB2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62908 mRNA. Translation: CAA44694.1.
    BC059143 mRNA. Translation: AAH59143.1.
    BC086533 mRNA. Translation: AAH86533.1.
    PIRiS49101.
    RefSeqiNP_058843.1. NM_017147.2.
    UniGeneiRn.11675.

    Genome annotation databases

    EnsembliENSRNOT00000015962; ENSRNOP00000059624; ENSRNOG00000020660.
    GeneIDi29271.
    KEGGirno:29271.
    UCSCiRGD:69285. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X62908 mRNA. Translation: CAA44694.1 .
    BC059143 mRNA. Translation: AAH59143.1 .
    BC086533 mRNA. Translation: AAH86533.1 .
    PIRi S49101.
    RefSeqi NP_058843.1. NM_017147.2.
    UniGenei Rn.11675.

    3D structure databases

    ProteinModelPortali P45592.
    SMRi P45592. Positions 1-166.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247942. 5 interactions.
    IntActi P45592. 4 interactions.
    MINTi MINT-247733.
    STRINGi 10116.ENSRNOP00000028041.

    PTM databases

    PhosphoSitei P45592.

    2D gel databases

    World-2DPAGE 0004:P45592.

    Proteomic databases

    PaxDbi P45592.
    PRIDEi P45592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000015962 ; ENSRNOP00000059624 ; ENSRNOG00000020660 .
    GeneIDi 29271.
    KEGGi rno:29271.
    UCSCi RGD:69285. rat.

    Organism-specific databases

    CTDi 1072.
    RGDi 69285. Cfl1.

    Phylogenomic databases

    eggNOGi NOG286948.
    GeneTreei ENSGT00440000033289.
    HOGENOMi HOG000039697.
    HOVERGENi HBG000381.
    InParanoidi P45592.
    KOi K05765.
    OMAi PPSCQTG.
    OrthoDBi EOG7353Z9.
    PhylomeDBi P45592.

    Miscellaneous databases

    NextBioi 608622.

    Gene expression databases

    Genevestigatori P45592.

    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. Shirasawa T., Takahashi H., Sakamoto K., Kawashima A., Akashi T.
      Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Wistar.
      Tissue: Brain.
    2. "Complete amino acid sequences and phosphorylation sites, determined by Edman degradation and mass spectrometry, of rat parotid destrin- and cofilin-like proteins."
      Kanamori T., Suzuki M., Titani K.
      Arch. Oral Biol. 43:955-967(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-166, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Parotid gland.
    3. "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].
      Tissue: Ovary and Pituitary.
    4. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 35-73; 82-92; 96-112; 133-146 AND 153-166, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain, Hippocampus and Spinal cord.
    5. Lubec G., Chen W.-Q.
      Submitted (FEB-2007) to UniProtKB
      Cited for: ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiCOF1_RAT
    AccessioniPrimary (citable) accession number: P45592
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 122 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3