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P45592 (COF1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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 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.

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 By similarity.

Subcellular location

Nucleus matrix By similarity. Cytoplasmcytoskeleton By similarity. 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.

Post-translational modification

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. Ref.2 Ref.5

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

cell projection organization

Inferred from direct assay PubMed 16286931. Source: MGI

cytoskeleton organization

Inferred from sequence or structural similarity. Source: UniProtKB

establishment of cell polarity

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell size

Inferred from direct assay PubMed 16286931. Source: MGI

neural crest cell migration

Inferred from electronic annotation. Source: Ensembl

neural fold formation

Inferred from electronic annotation. Source: Ensembl

positive regulation of actin filament depolymerization

Inferred from electronic annotation. Source: Ensembl

protein import into nucleus

Inferred from mutant phenotype PubMed 12566455. Source: RGD

protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of cell morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to virus

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell leading edge

Inferred from direct assay PubMed 15252126. Source: RGD

cortical actin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 15252126. Source: RGD

lamellipodium

Inferred from direct assay PubMed 15252126. Source: RGD

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

   Molecular_functionactin binding

Inferred from mutant phenotype PubMed 12566455. Source: RGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CttnQ605982EBI-917556,EBI-397955From a different organism.
CttnQ66HL24EBI-917556,EBI-6273816

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 166165Cofilin-1
PRO_0000214902

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine Ref.2 Ref.5
Modified residue31Phosphoserine Ref.2 Ref.5
Modified residue81Phosphoserine By similarity
Modified residue131N6-acetyllysine By similarity
Modified residue251Phosphothreonine By similarity
Modified residue681Phosphotyrosine By similarity
Modified residue731N6-acetyllysine By similarity
Modified residue1401Phosphotyrosine By similarity
Modified residue1441N6-acetyllysine By similarity
Modified residue1561Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P45592 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 19835391A81A5AB2

FASTA16618,533
        10         20         30         40         50         60 
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV 

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

       130        140        150        160 
KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X62908 mRNA. Translation: CAA44694.1.
BC059143 mRNA. Translation: AAH59143.1.
BC086533 mRNA. Translation: AAH86533.1.
PIRS49101.
RefSeqNP_058843.1. NM_017147.2.
UniGeneRn.11675.

3D structure databases

ProteinModelPortalP45592.
SMRP45592. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247942. 5 interactions.
IntActP45592. 4 interactions.
MINTMINT-247733.
STRING10116.ENSRNOP00000028041.

PTM databases

PhosphoSiteP45592.

2D gel databases

World-2DPAGE0004:P45592.

Proteomic databases

PaxDbP45592.
PRIDEP45592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015962; ENSRNOP00000059624; ENSRNOG00000020660.
GeneID29271.
KEGGrno:29271.
UCSCRGD:69285. rat.

Organism-specific databases

CTD1072.
RGD69285. Cfl1.

Phylogenomic databases

eggNOGNOG286948.
GeneTreeENSGT00440000033289.
HOGENOMHOG000039697.
HOVERGENHBG000381.
InParanoidP45592.
KOK05765.
OMAPPSCQTG.
OrthoDBEOG7353Z9.
PhylomeDBP45592.

Gene expression databases

GenevestigatorP45592.

Family and domain databases

InterProIPR002108. ADF-H.
IPR017904. ADF/Cofilin/Destrin.
[Graphical view]
PANTHERPTHR11913. PTHR11913. 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

NextBio608622.

Entry information

Entry nameCOF1_RAT
AccessionPrimary (citable) accession number: P45592
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 120 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