P18760 (COF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cofilin-1

Alternative name(s):
Cofilin, non-muscle isoform

Gene names

Name:

Cfl1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	166 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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. Cytoplasm › cytoskeleton. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection › lamellipodium 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. Ref.5 Ref.6 Ref.7 Ref.8
Sequence similarities	Belongs to the actin-binding proteins ADF family. Contains 1 ADF-H domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane Nucleus
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	actin filament organization Inferred from mutant phenotype. Source: MGI cytokinesis Inferred from mutant phenotype. Source: MGI establishment of cell polarity Inferred from mutant phenotype. Source: MGI neural crest cell migration Inferred from mutant phenotype. Source: MGI neural fold formation Inferred from mutant phenotype. Source: MGI positive regulation of actin filament depolymerization Inferred from mutant phenotype. Source: MGI protein phosphorylation Inferred from direct assay. Source: MGI regulation of cell morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB response to amino acid stimulus Inferred from direct assay. Source: MGI
Cellular component	cortical actin cytoskeleton Inferred from direct assay. 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
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.3
	Chain	2 – 166	165	Cofilin-1		PRO_0000214900
Regions
	Domain	4 – 153	150	ADF-H
	Motif	30 – 34	5	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.3 Ref.5
	Modified residue	3	1	Phosphoserine Ref.5 Ref.7 Ref.8
	Modified residue	8	1	Phosphoserine Ref.8
	Modified residue	13	1	N6-acetyllysine By similarity
	Modified residue	19	1	N6-acetyllysine By similarity
	Modified residue	24	1	Phosphoserine By similarity
	Modified residue	25	1	Phosphothreonine By similarity
	Modified residue	41	1	Phosphoserine By similarity
	Modified residue	68	1	Phosphotyrosine Ref.6
	Modified residue	73	1	N6-acetyllysine By similarity
	Modified residue	89	1	Phosphotyrosine By similarity
	Modified residue	132	1	N6-acetyllysine By similarity
	Modified residue	140	1	Phosphotyrosine Ref.6
	Modified residue	144	1	N6-acetyllysine By similarity
	Modified residue	156	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P18760 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 19834E8CA80747B2	FASTA	166	18,560
	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

References

	« Hide 'large scale' referencesShow '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: 2349104] [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: 15489334] [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, 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, MASS SPECTROMETRY. Tissue: Hippocampus.
[5]	"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: 16452087] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3, MASS SPECTROMETRY. Tissue: Brain.
[6]	"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: 17947660] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND TYR-140, MASS SPECTROMETRY. Tissue: Mast cell.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY. Tissue: Melanoma.
[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: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-8, MASS SPECTROMETRY. 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.
IPI	IPI00407543.
PIR	S12584.
RefSeq	NP_031713.1. NM_007687.5.
UniGene	Mm.329655.
3D structure databases
ProteinModelPortal	P18760.
SMR	P18760. Positions 1-166.
ModBase	Search...
Protein-protein interaction databases
IntAct	P18760. 3 interactions.
STRING	P18760.
PTM databases
PhosphoSite	P18760.
2D gel databases
SWISS-2DPAGE	P18760.
REPRODUCTION-2DPAGE	P18760.
Proteomic databases
PRIDE	P18760.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	12631.
KEGG	mmu:12631.
Organism-specific databases
CTD	1072.
MGI	MGI:101757. Cfl1.
Phylogenomic databases
eggNOG	roNOG07842.
HOVERGEN	HBG000381.
OrthoDB	EOG4WSWBP.
Enzyme and pathway databases
Reactome	REACT_115492. Developmental Biology.
Gene expression databases
ArrayExpress	P18760.
Bgee	P18760.
CleanEx	MM_CFL1.
Genevestigator	P18760.
GermOnline	ENSMUSG00000056201. Mus musculus.
Family and domain databases
InterPro	IPR002108. Actin-bd_cofilin/tropomyosin. IPR017904. ADF/Cofilin/Destrin. [Graphical view]
KO	K05765.
Pfam	PF00241. Cofilin_ADF. 1 hit. [Graphical view]
PRINTS	PR00006. COFILIN.
SMART	SM00102. ADF. 1 hit. [Graphical view]
PROSITE	PS51263. ADF_H. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	281816.
SOURCE	Search...

Entry information

Entry name

COF1_MOUSE

Accession

Primary (citable) accession number: P18760

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 122 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program