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Protein

Cofilin-1

Gene

Cfl1

Organism
Rattus norvegicus (Rat)
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. 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. Required for neural tube morphogenesis and neural crest cell migration (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: RGD
  • phosphatidylinositol bisphosphate binding Source: RGD
  • protein phosphatase binding Source: RGD

GO - Biological processi

  • actin filament depolymerization Source: Ensembl
  • cell projection organization Source: MGI
  • cellular response to epidermal growth factor stimulus Source: RGD
  • cellular response to ether Source: RGD
  • cellular response to hydrogen peroxide Source: RGD
  • cellular response to insulin-like growth factor stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to interleukin-6 Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • cytoskeleton organization Source: UniProtKB
  • hippocampus development Source: RGD
  • negative regulation of actin filament bundle assembly Source: RGD
  • negative regulation of actin filament depolymerization Source: RGD
  • negative regulation of cell adhesion Source: RGD
  • negative regulation of cell motility Source: RGD
  • negative regulation of cell size Source: MGI
  • negative regulation of dendritic spine maintenance Source: RGD
  • negative regulation of lamellipodium assembly Source: RGD
  • negative regulation of postsynaptic density organization Source: RGD
  • negative regulation of unidimensional cell growth Source: RGD
  • positive regulation by host of viral process Source: Ensembl
  • positive regulation of barbed-end actin filament capping Source: RGD
  • positive regulation of cell growth Source: RGD
  • positive regulation of cell motility Source: RGD
  • positive regulation of dendritic spine development Source: RGD
  • positive regulation of establishment of cell polarity regulating cell shape Source: RGD
  • positive regulation of focal adhesion assembly Source: RGD
  • positive regulation of lamellipodium assembly Source: RGD
  • positive regulation of NMDA glutamate receptor activity Source: RGD
  • positive regulation of protein localization to cell leading edge Source: RGD
  • positive regulation of proteolysis Source: RGD
  • positive regulation of synaptic plasticity Source: RGD
  • protein import into nucleus Source: RGD
  • regulation of cell morphogenesis Source: UniProtKB
  • regulation of dendritic spine morphogenesis Source: ParkinsonsUK-UCL
  • response to activity Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to virus Source: Ensembl

Keywordsi

Molecular functionActin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cofilin-1
Alternative name(s):
Cofilin, non-muscle isoform
Gene namesi
Name:Cfl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi69285. 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 leading edge Source: RGD
  • cofilin-actin rod Source: RGD
  • cytoplasm Source: RGD
  • dendritic spine Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular matrix Source: Ensembl
  • extracellular space Source: Ensembl
  • filopodium Source: RGD
  • focal adhesion Source: Ensembl
  • growth cone Source: RGD
  • lamellipodium Source: RGD
  • lamellipodium membrane Source: UniProtKB-SubCell
  • mitochondrial membrane Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: RGD
  • nuclear matrix Source: UniProtKB-SubCell
  • ruffle membrane Source: UniProtKB-SubCell
  • synaptic membrane Source: RGD

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00002149022 – 166Cofilin-1Add BLAST165

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine2 Publications1
Modified residuei3Phosphoserine2 Publications1
Modified residuei8PhosphoserineBy similarity1
Modified residuei13N6-acetyllysineBy similarity1
Modified residuei25PhosphothreonineBy similarity1
Modified residuei41PhosphoserineBy similarity1
Modified residuei68PhosphotyrosineBy similarity1
Modified residuei73N6-acetyllysineBy similarity1
Modified residuei140PhosphotyrosineBy similarity1
Modified residuei144N6-acetyllysineBy similarity1
Modified residuei156PhosphoserineBy similarity1

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP45592.
PRIDEiP45592.

2D gel databases

World-2DPAGEi0004:P45592.

PTM databases

iPTMnetiP45592.
PhosphoSitePlusiP45592.

Expressioni

Gene expression databases

BgeeiENSRNOG00000020660.
GenevisibleiP45592. RN.

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).By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: RGD
  • actin filament binding Source: RGD
  • protein phosphatase binding Source: RGD

Protein-protein interaction databases

BioGridi247942. 5 interactors.
IntActiP45592. 4 interactors.
MINTiMINT-247733.
STRINGi10116.ENSRNOP00000059624.

Structurei

3D structure databases

ProteinModelPortaliP45592.
SMRiP45592.
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

Phylogenomic databases

eggNOGiKOG1735. Eukaryota.
ENOG41122P5. LUCA.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiP45592.
KOiK05765.
OMAiPTFVIYR.
OrthoDBiEOG091G0PWC.
PhylomeDBiP45592.

Family and domain databases

CDDicd11286. ADF_cofilin_like. 1 hit.
Gene3Di3.40.20.10. 1 hit.
InterProiView protein in InterPro
IPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin.
IPR027234. Cofilin_1.
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF37. PTHR11913:SF37. 1 hit.
PfamiView protein in Pfam
PF00241. Cofilin_ADF. 1 hit.
PRINTSiPR00006. COFILIN.
SMARTiView protein in SMART
SM00102. ADF. 1 hit.
PROSITEiView protein in PROSITE
PS51263. ADF_H. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P45592-1 [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
FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA
160
EKLGGSAVIS LEGKPL
Length:166
Mass (Da):18,533
Last modified:January 23, 2007 - v3
Checksum:i19835391A81A5AB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62908 mRNA. Translation: CAA44694.1.
BC059143 mRNA. Translation: AAH59143.1.
BC086533 mRNA. Translation: AAH86533.1.
PIRiS49101.
RefSeqiNP_058843.1. NM_017147.2.
UniGeneiRn.11675.

Genome annotation databases

EnsembliENSRNOT00000015962; ENSRNOP00000059624; ENSRNOG00000020660.
GeneIDi29271.
KEGGirno:29271.
UCSCiRGD:69285. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62908 mRNA. Translation: CAA44694.1.
BC059143 mRNA. Translation: AAH59143.1.
BC086533 mRNA. Translation: AAH86533.1.
PIRiS49101.
RefSeqiNP_058843.1. NM_017147.2.
UniGeneiRn.11675.

3D structure databases

ProteinModelPortaliP45592.
SMRiP45592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247942. 5 interactors.
IntActiP45592. 4 interactors.
MINTiMINT-247733.
STRINGi10116.ENSRNOP00000059624.

PTM databases

iPTMnetiP45592.
PhosphoSitePlusiP45592.

2D gel databases

World-2DPAGEi0004:P45592.

Proteomic databases

PaxDbiP45592.
PRIDEiP45592.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015962; ENSRNOP00000059624; ENSRNOG00000020660.
GeneIDi29271.
KEGGirno:29271.
UCSCiRGD:69285. rat.

Organism-specific databases

CTDi1072.
RGDi69285. Cfl1.

Phylogenomic databases

eggNOGiKOG1735. Eukaryota.
ENOG41122P5. LUCA.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiP45592.
KOiK05765.
OMAiPTFVIYR.
OrthoDBiEOG091G0PWC.
PhylomeDBiP45592.

Miscellaneous databases

PROiPR:P45592.

Gene expression databases

BgeeiENSRNOG00000020660.
GenevisibleiP45592. RN.

Family and domain databases

CDDicd11286. ADF_cofilin_like. 1 hit.
Gene3Di3.40.20.10. 1 hit.
InterProiView protein in InterPro
IPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin.
IPR027234. Cofilin_1.
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF37. PTHR11913:SF37. 1 hit.
PfamiView protein in Pfam
PF00241. Cofilin_ADF. 1 hit.
PRINTSiPR00006. COFILIN.
SMARTiView protein in SMART
SM00102. ADF. 1 hit.
PROSITEiView protein in PROSITE
PS51263. ADF_H. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCOF1_RAT
AccessioniPrimary (citable) accession number: P45592
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 7, 2017
This is version 149 of the entry and version 3 of the sequence. See 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. 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.