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P18760

- COF1_MOUSE

UniProt

P18760 - COF1_MOUSE

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Protein

Cofilin-1

Gene

Cfl1

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

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
Complete GO annotation...

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. extracellular space Source: Ensembl
  7. extracellular vesicular exosome Source: Ensembl
  8. lamellipodium Source: Ensembl
  9. nucleus Source: UniProtKB-KW
  10. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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.
ExpressionAtlasiP18760. baseline.
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.
InParanoidiP18760.
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

        10         20         30         40         50
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE
60 70 80 90 100
EGKEILVGDV GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV
110 120 130 140 150
FIFWAPENAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA
160
EKLGGSAVIS LEGKPL
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.
InParanoidi P18760.
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.
ExpressionAtlasi P18760. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 147 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