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P18760 (COF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cofilin-1
Alternative name(s):
Cofilin, non-muscle isoform
Gene names
Name:Cfl1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

Nucleus matrix. Cytoplasmcytoskeleton. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionlamellipodium membrane; Peripheral membrane protein; 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.

Tissue specificity

Widely distributed in various tissues.

Post-translational modification

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.

Sequence similarities

Belongs to the actin-binding proteins ADF family.

Contains 1 ADF-H domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
Nucleus
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament depolymerization

Inferred from electronic annotation. Source: InterPro

actin filament organization

Inferred from mutant phenotype PubMed 15606898. Source: MGI

cell projection organization

Inferred from sequence orthology PubMed 16286931. Source: MGI

cellular component movement

Inferred from mutant phenotype PubMed 15548599. Source: MGI

cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of cell polarity

Inferred from mutant phenotype PubMed 15606898. Source: MGI

mitotic cytokinesis

Inferred from mutant phenotype PubMed 15548599. Source: MGI

negative regulation of cell size

Inferred from sequence orthology PubMed 16286931. Source: MGI

neural crest cell migration

Inferred from mutant phenotype PubMed 15649475. Source: MGI

neural fold formation

Inferred from mutant phenotype PubMed 15649475. Source: MGI

positive regulation of actin filament depolymerization

Inferred from mutant phenotype PubMed 15548599. Source: MGI

protein import into nucleus

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay PubMed 17018287. Source: MGI

regulation of cell morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

response to amino acid

Inferred from direct assay PubMed 17018287. Source: MGI

response to virus

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell-cell junction

Inferred from direct assay PubMed 23793062. Source: MGI

cortical actin cytoskeleton

Inferred from direct assay PubMed 15004221PubMed 15548599. Source: MGI

cytoplasm

Inferred from direct assay PubMed 15548599. Source: MGI

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

lamellipodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 166165Cofilin-1
PRO_0000214900

Regions

Domain4 – 153150ADF-H
Motif30 – 345Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.8
Modified residue31Phosphoserine Ref.6 Ref.8
Modified residue81Phosphoserine Ref.8
Modified residue131N6-acetyllysine By similarity
Modified residue251Phosphothreonine By similarity
Modified residue681Phosphotyrosine Ref.7
Modified residue731N6-acetyllysine By similarity
Modified residue1401Phosphotyrosine Ref.5 Ref.7
Modified residue1441N6-acetyllysine By similarity
Modified residue1561Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P18760 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 19834E8CA80747B2

FASTA16618,560
        10         20         30         40         50         60 
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV 

        70         80         90        100        110        120 
GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPENAP LKSKMIYASS 

       130        140        150        160 
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of mouse cofilin cDNA."
Moriyama K., Matsumoto S., Nishida E., Sakai H., Yahara I.
Nucleic Acids Res. 18:3053-3053(1990) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00472 mRNA. Translation: BAA00364.1.
BC046225 mRNA. Translation: AAH46225.1.
BC058726 mRNA. Translation: AAH58726.1.
PIRS12584.
RefSeqNP_031713.1. NM_007687.5.
UniGeneMm.329655.

3D structure databases

ProteinModelPortalP18760.
SMRP18760. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198684. 7 interactions.
DIPDIP-38073N.
IntActP18760. 8 interactions.
MINTMINT-1862314.

PTM databases

PhosphoSiteP18760.

2D gel databases

REPRODUCTION-2DPAGEP18760.
SWISS-2DPAGEP18760.

Proteomic databases

MaxQBP18760.
PaxDbP18760.
PRIDEP18760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID12631.
KEGGmmu:12631.
UCSCuc008gdq.2. mouse.

Organism-specific databases

CTD1072.
MGIMGI:101757. Cfl1.

Phylogenomic databases

eggNOGNOG286948.
HOGENOMHOG000039697.
HOVERGENHBG000381.
KOK05765.
PhylomeDBP18760.

Enzyme and pathway databases

ReactomeREACT_224553. Hemostasis.

Gene expression databases

BgeeP18760.
CleanExMM_CFL1.
GenevestigatorP18760.

Family and domain databases

Gene3D3.40.20.10. 1 hit.
InterProIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
IPR027234. Cofilin_1.
[Graphical view]
PANTHERPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
PfamPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSPR00006. COFILIN.
SMARTSM00102. ADF. 1 hit.
[Graphical view]
PROSITEPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio281816.
PROP18760.
SOURCESearch...

Entry information

Entry nameCOF1_MOUSE
AccessionPrimary (citable) accession number: P18760
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot