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P45591 (COF2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 102. 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-2
Alternative name(s):
Cofilin, muscle isoform
Gene names
Name:Cfl2
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

Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods.

Subcellular location

Nucleus matrix. Cytoplasmcytoskeleton.

Tissue specificity

Predominantly expressed in skeletal muscle.

Post-translational modification

The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal.

Sequence similarities

Belongs to the actin-binding proteins ADF family.

Contains 1 ADF-H domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 166165Cofilin-2
PRO_0000214908

Regions

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

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue31Phosphoserine Ref.5
Modified residue61Phosphothreonine Ref.5
Modified residue891Phosphotyrosine Ref.3 Ref.4

Sequences

Sequence LengthMass (Da)Tools
P45591 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 48B6D7E5AE9FE1CC

FASTA16618,710
        10         20         30         40         50         60 
MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI 

        70         80         90        100        110        120 
GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS 

       130        140        150        160 
KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGSVVVS LEGKPL 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a novel cofilin isoform that is predominantly expressed in mammalian skeletal muscle."
Ono S., Minami N., Abe H., Obinata T.
J. Biol. Chem. 269:15280-15286(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H.
Tissue: Skeletal muscle.
[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].
[3]"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-89, MASS SPECTROMETRY.
Tissue: Mast cell.
[4]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, MASS SPECTROMETRY.
Tissue: Brain.
[5]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND THR-6, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L29468 mRNA. Translation: AAA37433.1.
BC007138 mRNA. Translation: AAH07138.1.
IPIIPI00266188.
PIRA53812.
RefSeqNP_031714.1. NM_007688.2.
UniGeneMm.276826.

3D structure databases

ProteinModelPortalP45591.
SMRP45591. Positions 1-166.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000077262.

PTM databases

PhosphoSiteP45591.

2D gel databases

REPRODUCTION-2DPAGEP45591.

Proteomic databases

PaxDbP45591.
PRIDEP45591.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000078124; ENSMUSP00000077262; ENSMUSG00000062929.
GeneID12632.
KEGGmmu:12632.

Organism-specific databases

CTD1073.
MGIMGI:101763. Cfl2.

Phylogenomic databases

eggNOGNOG303866.
HOGENOMHOG000039697.
HOVERGENHBG000381.
InParanoidP45591.
KOK05765.
OMAGLYDATY.
OrthoDBEOG4WSWBP.

Gene expression databases

ArrayExpressP45591.
BgeeP45591.
CleanExMM_CFL2.
GenevestigatorP45591.
GermOnlineENSMUSG00000062929. Mus musculus.

Family and domain databases

InterProIPR002108. Actin-bd_cofilin/tropomyosin.
IPR017904. ADF/Cofilin/Destrin.
IPR027234. Cofilin_1/2.
[Graphical view]
PANTHERPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF2. PTHR11913:SF2. 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

ChiTaRSCFL2. mouse.
NextBio281820.
SOURCESearch...

Entry information

Entry nameCOF2_MOUSE
AccessionPrimary (citable) accession number: P45591
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 1, 2013
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families