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P45592

- COF1_RAT

UniProt

P45592 - COF1_RAT

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Protein

Cofilin-1

Gene
Cfl1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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 By similarity. 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.

GO - Molecular functioni

  1. actin binding Source: RGD
  2. protein binding Source: IntAct

GO - Biological processi

  1. actin filament depolymerization Source: InterPro
  2. cell projection organization Source: MGI
  3. cytoskeleton organization Source: UniProtKB
  4. establishment of cell polarity Source: Ensembl
  5. negative regulation of cell size Source: MGI
  6. neural crest cell migration Source: Ensembl
  7. neural fold formation Source: Ensembl
  8. positive regulation of actin filament depolymerization Source: Ensembl
  9. protein import into nucleus Source: RGD
  10. protein phosphorylation Source: Ensembl
  11. regulation of cell morphogenesis Source: UniProtKB
  12. response to amino acid Source: Ensembl
  13. response to virus Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Actin-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 1

Organism-specific databases

RGDi69285. Cfl1.

Subcellular locationi

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

GO - Cellular componenti

  1. cell leading edge Source: RGD
  2. cortical actin cytoskeleton Source: Ensembl
  3. cytoplasm Source: RGD
  4. lamellipodium Source: RGD
  5. lamellipodium membrane Source: UniProtKB-SubCell
  6. nuclear matrix Source: UniProtKB-SubCell
  7. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 166165Cofilin-1PRO_0000214902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei3 – 31Phosphoserine2 Publications
Modified residuei8 – 81Phosphoserine By similarity
Modified residuei13 – 131N6-acetyllysine By similarity
Modified residuei25 – 251Phosphothreonine By similarity
Modified residuei68 – 681Phosphotyrosine By similarity
Modified residuei73 – 731N6-acetyllysine By similarity
Modified residuei140 – 1401Phosphotyrosine By similarity
Modified residuei144 – 1441N6-acetyllysine By similarity
Modified residuei156 – 1561Phosphoserine By similarity

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.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP45592.
PRIDEiP45592.

2D gel databases

World-2DPAGE0004:P45592.

PTM databases

PhosphoSiteiP45592.

Expressioni

Gene expression databases

GenevestigatoriP45592.

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
CttnQ605982EBI-917556,EBI-397955From a different organism.
CttnQ66HL24EBI-917556,EBI-6273816

Protein-protein interaction databases

BioGridi247942. 5 interactions.
IntActiP45592. 4 interactions.
MINTiMINT-247733.
STRINGi10116.ENSRNOP00000028041.

Structurei

3D structure databases

ProteinModelPortaliP45592.
SMRiP45592. Positions 1-166.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 153150ADF-HAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 345Nuclear localization signal Reviewed prediction

Sequence similaritiesi

Contains 1 ADF-H domain.

Phylogenomic databases

eggNOGiNOG286948.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiP45592.
KOiK05765.
OMAiPPSCQTG.
OrthoDBiEOG7353Z9.
PhylomeDBiP45592.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
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.

P45592-1 [UniParc]FASTAAdd to Basket

« Hide

MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE    50
EGKEILVGDV GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV 100
FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA 150
EKLGGSAVIS LEGKPL 166
Length:166
Mass (Da):18,533
Last modified:January 23, 2007 - v3
Checksum:i19835391A81A5AB2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
X62908 mRNA. Translation: CAA44694.1 .
BC059143 mRNA. Translation: AAH59143.1 .
BC086533 mRNA. Translation: AAH86533.1 .
PIRi S49101.
RefSeqi NP_058843.1. NM_017147.2.
UniGenei Rn.11675.

3D structure databases

ProteinModelPortali P45592.
SMRi P45592. Positions 1-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 247942. 5 interactions.
IntActi P45592. 4 interactions.
MINTi MINT-247733.
STRINGi 10116.ENSRNOP00000028041.

PTM databases

PhosphoSitei P45592.

2D gel databases

World-2DPAGE 0004:P45592.

Proteomic databases

PaxDbi P45592.
PRIDEi P45592.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000015962 ; ENSRNOP00000059624 ; ENSRNOG00000020660 .
GeneIDi 29271.
KEGGi rno:29271.
UCSCi RGD:69285. rat.

Organism-specific databases

CTDi 1072.
RGDi 69285. Cfl1.

Phylogenomic databases

eggNOGi NOG286948.
GeneTreei ENSGT00440000033289.
HOGENOMi HOG000039697.
HOVERGENi HBG000381.
InParanoidi P45592.
KOi K05765.
OMAi PPSCQTG.
OrthoDBi EOG7353Z9.
PhylomeDBi P45592.

Miscellaneous databases

NextBioi 608622.

Gene expression databases

Genevestigatori P45592.

Family and domain databases

Gene3Di 3.40.20.10. 1 hit.
InterProi IPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
IPR027234. Cofilin_1.
[Graphical view ]
PANTHERi PTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
Pfami PF00241. Cofilin_ADF. 1 hit.
[Graphical view ]
PRINTSi PR00006. COFILIN.
SMARTi SM00102. ADF. 1 hit.
[Graphical view ]
PROSITEi PS51263. ADF_H. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiCOF1_RAT
AccessioniPrimary (citable) accession number: P45592
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 121 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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