COFI_ASHGO
ID COFI_ASHGO Reviewed; 143 AA.
AC Q759P0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Cofilin;
DE AltName: Full=Actin-depolymerizing factor 1;
GN Name=COF1; OrderedLocusNames=ADR235W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Controls reversibly actin polymerization and depolymerization
CC in a pH-sensitive manner. It has the ability to bind G- and F-actin in
CC a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by
CC tropomyosin. It is the major component of intranuclear and cytoplasmic
CC actin rods. Required for accumulation of actin at the cell division
CC site via depolymerizing actin at the cell ends. In association with
CC myosin II has a role in the assembly of the contractile ring via
CC severing actin filaments. Involved in the maintenance of the
CC contractile ring once formed. In association with profilin and capping
CC protein, has a role in the mitotic reorganization of the actin
CC cytoskeleton (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Nucleus matrix {ECO:0000250}. Note=Throughout the
CC cytoplasm (but not on the cytoplasmic cables) and major component of
CC the cortical actin cytoskeleton. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; AE016817; AAS52155.1; -; Genomic_DNA.
DR RefSeq; NP_984331.1; NM_209684.1.
DR AlphaFoldDB; Q759P0; -.
DR SMR; Q759P0; -.
DR STRING; 33169.AAS52155; -.
DR EnsemblFungi; AAS52155; AAS52155; AGOS_ADR235W.
DR GeneID; 4620493; -.
DR KEGG; ago:AGOS_ADR235W; -.
DR eggNOG; KOG1735; Eukaryota.
DR HOGENOM; CLU_094004_3_2_1; -.
DR InParanoid; Q759P0; -.
DR OMA; ECKYAIY; -.
DR Proteomes; UP000000591; Chromosome IV.
DR GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IEA:EnsemblFungi.
DR CDD; cd11286; ADF_cofilin_like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR017904; ADF/Cofilin.
DR PANTHER; PTHR11913; PTHR11913; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 3: Inferred from homology;
KW Actin-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Nucleus;
KW Reference proteome.
FT CHAIN 1..143
FT /note="Cofilin"
FT /id="PRO_0000255621"
FT DOMAIN 5..137
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ SEQUENCE 143 AA; 15902 MW; FACEAF9CB221F146 CRC64;
MSRSGVAVAD ESLTAFNDLK LGKKYKFVLF GLNADKTSII VKETSNERDY DVFLEKLPED
DCLYAVYDFE YEISGAEGKR SKIVFFTWSP DTAPIRSKMV YASSKDALRR ALNGVSSDIQ
GTDFSEVAYE SVLEKVSRGA GSH
