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Protein

Cofilin-1

Gene

Cfl1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11809832). 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). Required for neural tube morphogenesis and neural crest cell migration (PubMed:15649475).By similarity2 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB

GO - Biological processi

  • actin filament depolymerization Source: UniProtKB
  • actin filament fragmentation Source: UniProtKB
  • actin filament organization Source: MGI
  • cell projection organization Source: MGI
  • cytoskeleton organization Source: UniProtKB
  • establishment of cell polarity Source: MGI
  • mitotic cytokinesis Source: MGI
  • negative regulation of cell size Source: MGI
  • neural crest cell migration Source: MGI
  • neural fold formation Source: MGI
  • platelet degranulation Source: Reactome
  • positive regulation by host of viral process Source: MGI
  • positive regulation of actin filament depolymerization Source: CACAO
  • protein phosphorylation Source: MGI
  • regulation of cell morphogenesis Source: UniProtKB
  • regulation of dendritic spine morphogenesis Source: ParkinsonsUK-UCL
  • response to amino acid Source: MGI
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Cofilin-1
Alternative name(s):
Cofilin, non-muscle isoform
Gene namesi
Name:Cfl1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:101757. Cfl1.

Subcellular locationi

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

GO - Cellular componenti

  • cell-cell junction Source: MGI
  • cortical actin cytoskeleton Source: MGI
  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • extracellular exosome Source: MGI
  • extracellular matrix Source: MGI
  • extracellular region Source: Reactome
  • extracellular space Source: MGI
  • focal adhesion Source: MGI
  • lamellipodium membrane Source: UniProtKB-SubCell
  • membrane Source: MGI
  • nuclear matrix Source: UniProtKB-SubCell
  • ruffle membrane Source: UniProtKB-SubCell
  • vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002149002 – 166Cofilin-1Add BLAST165

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei3PhosphoserineCombined sources1
Modified residuei8PhosphoserineCombined sources1
Modified residuei13N6-acetyllysineBy similarity1
Modified residuei25PhosphothreonineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei68PhosphotyrosineCombined sources1
Modified residuei73N6-acetyllysineBy similarity1
Modified residuei140PhosphotyrosineCombined sources1
Modified residuei144N6-acetyllysineBy similarity1
Modified residuei156PhosphoserineCombined sources1

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP18760.
PaxDbiP18760.
PeptideAtlasiP18760.
PRIDEiP18760.
TopDownProteomicsiP18760.

2D gel databases

REPRODUCTION-2DPAGEP18760.
SWISS-2DPAGEP18760.

PTM databases

iPTMnetiP18760.
PhosphoSitePlusiP18760.
SwissPalmiP18760.

Expressioni

Tissue specificityi

Widely distributed in various tissues. Not found in skeletal muscle.1 Publication

Developmental stagei

In E10.5 embryo somites is expressed in a ventral cell layer (myotome).1 Publication

Gene expression databases

BgeeiENSMUSG00000056201.
CleanExiMM_CFL1.
ExpressionAtlasiP18760. baseline and differential.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • actin filament binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198684. 8 interactors.
DIPiDIP-38073N.
IntActiP18760. 10 interactors.
MINTiMINT-1862314.
STRINGi10090.ENSMUSP00000112259.

Structurei

3D structure databases

ProteinModelPortaliP18760.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 153ADF-HPROSITE-ProRule annotationAdd BLAST150

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi30 – 34Nuclear localization signalSequence analysis5

Sequence similaritiesi

Belongs to the actin-binding proteins ADF family.Curated
Contains 1 ADF-H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1735. Eukaryota.
ENOG41122P5. LUCA.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiP18760.
KOiK05765.
PhylomeDBiP18760.

Family and domain databases

CDDicd11286. ADF_cofilin_like. 1 hit.
Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin.
IPR027234. Cofilin_1.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18760-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE
60 70 80 90 100
EGKEILVGDV GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV
110 120 130 140 150
FIFWAPENAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA
160
EKLGGSAVIS LEGKPL
Length:166
Mass (Da):18,560
Last modified:January 23, 2007 - v3
Checksum:i19834E8CA80747B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00472 mRNA. Translation: BAA00364.1.
BC046225 mRNA. Translation: AAH46225.1.
BC058726 mRNA. Translation: AAH58726.1.
PIRiS12584.
RefSeqiNP_031713.1. NM_007687.5.
UniGeneiMm.329655.

Genome annotation databases

EnsembliENSMUST00000209469; ENSMUSP00000147514; ENSMUSG00000056201.
GeneIDi12631.
KEGGimmu:12631.
UCSCiuc008gdq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00472 mRNA. Translation: BAA00364.1.
BC046225 mRNA. Translation: AAH46225.1.
BC058726 mRNA. Translation: AAH58726.1.
PIRiS12584.
RefSeqiNP_031713.1. NM_007687.5.
UniGeneiMm.329655.

3D structure databases

ProteinModelPortaliP18760.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198684. 8 interactors.
DIPiDIP-38073N.
IntActiP18760. 10 interactors.
MINTiMINT-1862314.
STRINGi10090.ENSMUSP00000112259.

PTM databases

iPTMnetiP18760.
PhosphoSitePlusiP18760.
SwissPalmiP18760.

2D gel databases

REPRODUCTION-2DPAGEP18760.
SWISS-2DPAGEP18760.

Proteomic databases

EPDiP18760.
PaxDbiP18760.
PeptideAtlasiP18760.
PRIDEiP18760.
TopDownProteomicsiP18760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000209469; ENSMUSP00000147514; ENSMUSG00000056201.
GeneIDi12631.
KEGGimmu:12631.
UCSCiuc008gdq.2. mouse.

Organism-specific databases

CTDi1072.
MGIiMGI:101757. Cfl1.

Phylogenomic databases

eggNOGiKOG1735. Eukaryota.
ENOG41122P5. LUCA.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiP18760.
KOiK05765.
PhylomeDBiP18760.

Enzyme and pathway databases

ReactomeiR-MMU-114608. Platelet degranulation.

Miscellaneous databases

PROiP18760.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000056201.
CleanExiMM_CFL1.
ExpressionAtlasiP18760. baseline and differential.

Family and domain databases

CDDicd11286. ADF_cofilin_like. 1 hit.
Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin.
IPR027234. Cofilin_1.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOF1_MOUSE
AccessioniPrimary (citable) accession number: P18760
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 171 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.