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Protein

Cofilin

Gene

COF1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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
Complete GO annotation...

Keywords - Ligandi

Actin-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

  • Cytoplasm 1 Publication
  • Cytoplasmcytoskeleton 1 Publication
  • Nucleus matrix 1 Publication

  • Note: Throughout the cytoplasm (but not on the cytoplasmic cables) and major component of the cortical actin cytoskeleton.

GO - Cellular componenti

  • actin cortical patch Source: SGD
  • actin cytoskeleton Source: UniProtKB
  • nuclear matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1062KD → AA: Reduced interaction with PIP2. 1 Publication
Mutagenesisi109 – 1102RR → AA: Defects in actin monomer interaction. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 143143CofilinPRO_0000214915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei4 – 41PhosphoserineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ03048.
PeptideAtlasiQ03048.
TopDownProteomicsiQ03048.

PTM databases

iPTMnetiQ03048.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • actin filament binding Source: SGD

Protein-protein interaction databases

BioGridi31265. 83 interactions.
DIPiDIP-197N.
IntActiQ03048. 3 interactions.
MINTiMINT-396753.

Structurei

Secondary structure

1
143
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2213Combined sources
Beta strandi26 – 327Combined sources
Beta strandi36 – 4510Combined sources
Helixi50 – 545Combined sources
Beta strandi63 – 719Combined sources
Beta strandi74 – 763Combined sources
Beta strandi80 – 889Combined sources
Beta strandi91 – 933Combined sources
Helixi95 – 11117Combined sources
Beta strandi117 – 1237Combined sources
Helixi125 – 1273Combined sources
Helixi129 – 1379Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-140.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03048.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 137133ADF-HPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
InParanoidiQ03048.
KOiK05765.
OMAiVTNENCQ.
OrthoDBiEOG7X3R3K.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 55MSRSG → MWGKKFIRSQENVKFLCS in CAA88007 (Ref. 3) Curated

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31265. 83 interactions.
DIPiDIP-197N.
IntActiQ03048. 3 interactions.
MINTiMINT-396753.

PTM databases

iPTMnetiQ03048.

Proteomic databases

MaxQBiQ03048.
PeptideAtlasiQ03048.
TopDownProteomicsiQ03048.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLL050C; YLL050C; YLL050C.
GeneIDi850676.
KEGGisce:YLL050C.

Organism-specific databases

EuPathDBiFungiDB:YLL050C.
SGDiS000003973. COF1.

Phylogenomic databases

GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
InParanoidiQ03048.
KOiK05765.
OMAiVTNENCQ.
OrthoDBiEOG7X3R3K.

Enzyme and pathway databases

BioCyciYEAST:G3O-32149-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ03048.
PROiQ03048.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cofilin is an essential component of the yeast cortical cytoskeleton."
    Moon A.L., Janmey P.A., Louie K.A., Drubin D.G.
    J. Cell Biol. 120:421-435(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 43-56; 83-98 AND 106-141.
  2. "Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein."
    Iida K., Moriyama K., Matsumoto S., Kawasaki H., Nishida E., Yahara I.
    Gene 124:115-120(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces cerevisiae including the subtelomeric region of the left arm."
    Wedler H., Wambutt R.
    Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "Cooperation of two actin-binding proteins, cofilin and Aip1, in Saccharomyces cerevisiae."
    Iida K., Yahara I.
    Genes Cells 4:21-32(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Aip1p interacts with cofilin to disassemble actin filaments."
    Rodal A.A., Tetreault J.W., Lappalainen P., Drubin D.G., Amberg D.C.
    J. Cell Biol. 145:1251-1264(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AIP1.
  8. "Identification of yeast cofilin residues specific for actin monomer and PIP2 binding."
    Ojala P.J., Paavilainen V., Lappalainen P.
    Biochemistry 40:15562-15569(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF 105-LYS-ASP-106 AND 109-ARG-ARG-110.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiCOFI_YEAST
AccessioniPrimary (citable) accession number: Q03048
Secondary accession number(s): D6VXV8, Q05307, Q2XN65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 8, 2016
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.