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Protein

Cofilin

Gene

COF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton. In effect, yeast cofilin increases the rate of actin polymerization by making new ends available for actin subunit addition. Such a protein complex is important for the polarized growth of yeast cells.2 Publications

Miscellaneous

Present with 19600 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • actin filament binding Source: SGD

GO - Biological processi

  • actin filament depolymerization Source: SGD
  • actin filament organization Source: SGD
  • actin filament severing Source: SGD
  • endocytosis Source: SGD
  • Golgi to plasma membrane protein transport Source: SGD

Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-32149-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
Cofilin
Alternative name(s):
Actin-depolymerizing factor 1
Gene namesi
Name:COF1
Ordered Locus Names:YLL050C
ORF Names:L0596
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLL050C
SGDiS000003973 COF1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105 – 106KD → AA: Reduced interaction with PIP2. 1 Publication2
Mutagenesisi109 – 110RR → AA: Defects in actin monomer interaction. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002149151 – 143CofilinAdd BLAST143

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei4PhosphoserineCombined sources1

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03048
PaxDbiQ03048
PRIDEiQ03048
TopDownProteomicsiQ03048

PTM databases

iPTMnetiQ03048

Interactioni

Subunit structurei

Interacts with actin and AIP1 in a ternary complex.1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin filament binding Source: SGD

Protein-protein interaction databases

BioGridi31265, 475 interactors
DIPiDIP-197N
IntActiQ03048, 24 interactors
MINTiQ03048
STRINGi4932.YLL050C

Structurei

Secondary structure

1143
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 22Combined sources13
Beta strandi26 – 32Combined sources7
Beta strandi36 – 45Combined sources10
Helixi50 – 54Combined sources5
Beta strandi63 – 71Combined sources9
Beta strandi74 – 76Combined sources3
Beta strandi80 – 88Combined sources9
Beta strandi91 – 93Combined sources3
Helixi95 – 111Combined sources17
Beta strandi117 – 123Combined sources7
Helixi125 – 127Combined sources3
Helixi129 – 137Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CFYX-ray2.30A/B1-143[»]
1COFX-ray2.30A1-143[»]
1QPVX-ray3.00A1-143[»]
4KEDX-ray1.90A/B2-143[»]
4KEEX-ray1.45A2-143[»]
4KEFX-ray1.10A2-143[»]
ProteinModelPortaliQ03048
SMRiQ03048
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03048

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 137ADF-HPROSITE-ProRule annotationAdd BLAST133

Sequence similaritiesi

Belongs to the actin-binding proteins ADF family.Curated

Phylogenomic databases

GeneTreeiENSGT00440000033289
HOGENOMiHOG000039697
InParanoidiQ03048
KOiK05765
OMAiGLYDATY
OrthoDBiEOG092C589Z

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_sf
IPR017904 ADF/Cofilin
PANTHERiPTHR11913 PTHR11913, 1 hit
PfamiView protein in Pfam
PF00241 Cofilin_ADF, 1 hit
SMARTiView protein in SMART
SM00102 ADF, 1 hit
PROSITEiView protein in PROSITE
PS51263 ADF_H, 1 hit

Sequencei

Sequence statusi: Complete.

Q03048-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRSGVAVAD ESLTAFNDLK LGKKYKFILF GLNDAKTEIV VKETSTDPSY
60 70 80 90 100
DAFLEKLPEN DCLYAIYDFE YEINGNEGKR SKIVFFTWSP DTAPVRSKMV
110 120 130 140
YASSKDALRR ALNGVSTDVQ GTDFSEVSYD SVLERVSRGA GSH
Length:143
Mass (Da):15,901
Last modified:July 1, 1993 - v1
Checksum:i7A03747B0F21F22D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1 – 5MSRSG → MWGKKFIRSQENVKFLCS in CAA88007 (Ref. 3) Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z14971 Genomic DNA Translation: CAA78694.1
S52662 Genomic DNA Translation: AAA13256.1
D13230 Genomic DNA Translation: BAA02514.1
Z47973 Genomic DNA Translation: CAA88007.1
Z73155 Genomic DNA Translation: CAA97502.1
BK006945 Genomic DNA Translation: DAA09274.1
PIRiA44397
RefSeqiNP_013050.1, NM_001181870.1

Genome annotation databases

EnsemblFungiiYLL050C; YLL050C; YLL050C
GeneIDi850676
KEGGisce:YLL050C

Similar proteinsi

Entry informationi

Entry nameiCOFI_YEAST
AccessioniPrimary (citable) accession number: Q03048
Secondary accession number(s): D6VXV8, Q05307, Q2XN65
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: May 23, 2018
This is version 166 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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