P45592 (COF1_RAT) 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

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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 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. Cytoplasm › cytoskeleton By similarity. 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.
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. Ref.2 Ref.5
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 depolymerization Inferred from electronic annotation. Source: InterPro cell projection organization Inferred from direct assay PubMed 16286931. Source: MGI cytokinesis Inferred from electronic annotation. Source: Compara cytoskeleton organization Inferred from sequence or structural similarity. Source: UniProtKB establishment of cell polarity Inferred from electronic annotation. Source: Compara negative regulation of cell size Inferred from direct assay PubMed 16286931. Source: MGI neural crest cell migration Inferred from electronic annotation. Source: Compara neural fold formation Inferred from electronic annotation. Source: Compara positive regulation of actin filament depolymerization Inferred from electronic annotation. Source: Compara protein import into nucleus Inferred from mutant phenotype PubMed 12566455. Source: RGD protein phosphorylation Inferred from electronic annotation. Source: Compara regulation of cell morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB response to amino acid stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cortical actin cytoskeleton Inferred from electronic annotation. Source: Compara 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_function	actin binding Inferred from mutant phenotype PubMed 12566455. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cttn	Q60598	2	EBI-917556,EBI-397955	From a different organism.
Cttn	Q66HL2	4	EBI-917556,EBI-6273816

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 166	165	Cofilin-1		PRO_0000214902
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.2 Ref.5
	Modified residue	3	1	Phosphoserine Ref.2 Ref.5
	Modified residue	8	1	Phosphoserine By similarity
	Modified residue	13	1	N6-acetyllysine By similarity
	Modified residue	25	1	Phosphothreonine By similarity
	Modified residue	68	1	Phosphotyrosine By similarity
	Modified residue	73	1	N6-acetyllysine By similarity
	Modified residue	140	1	Phosphotyrosine By similarity
	Modified residue	144	1	N6-acetyllysine By similarity
	Modified residue	156	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P45592 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 19835391A81A5AB2	FASTA	166	18,533
	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

References

	« Hide 'large scale' referencesShow '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, 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, 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, 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.
IPI	IPI00327144.
PIR	S49101.
RefSeq	NP_058843.1. NM_017147.2.
UniGene	Rn.11675.
3D structure databases
ProteinModelPortal	P45592.
SMR	P45592. Positions 1-166.
ModBase	Search...
Protein-protein interaction databases
IntAct	P45592. 4 interactions.
MINT	MINT-247733.
STRING	10116.ENSRNOP00000028041.
PTM databases
PhosphoSite	P45592.
2D gel databases
World-2DPAGE	0004:P45592.
Proteomic databases
PaxDb	P45592.
PRIDE	P45592.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000015962; ENSRNOP00000059624; ENSRNOG00000020660.
GeneID	29271.
KEGG	rno:29271.
UCSC	RGD:69285. rat.
Organism-specific databases
CTD	1072.
RGD	69285. Cfl1.
Phylogenomic databases
eggNOG	NOG286948.
GeneTree	ENSGT00440000033289.
HOGENOM	HOG000039697.
HOVERGEN	HBG000381.
InParanoid	P45592.
KO	K05765.
OrthoDB	EOG4WSWBP.
Gene expression databases
ArrayExpress	P45592.
Genevestigator	P45592.
GermOnline	ENSRNOG00000020660. Rattus norvegicus.
Family and domain databases
InterPro	IPR002108. Actin-bd_cofilin/tropomyosin. IPR017904. ADF/Cofilin/Destrin. IPR027234. Cofilin_1/2. [Graphical view]
PANTHER	PTHR11913. PTHR11913. 1 hit. PTHR11913:SF2. PTHR11913:SF2. 1 hit.
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	608622.

Entry information

Entry name

COF1_RAT

Accession

Primary (citable) accession number: P45592

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program