ID   COFI_CANGA              Reviewed;         143 AA.
AC   Q6FV81;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Cofilin;
DE   AltName: Full=Actin-depolymerizing factor 1;
GN   Name=COF1; OrderedLocusNames=CAGL0E04048g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380951; CAG58782.1; -; Genomic_DNA.
DR   RefSeq; XP_445863.1; XM_445863.1.
DR   AlphaFoldDB; Q6FV81; -.
DR   SMR; Q6FV81; -.
DR   STRING; 5478.XP_445863.1; -.
DR   EnsemblFungi; CAG58782; CAG58782; CAGL0E04048g.
DR   GeneID; 2887320; -.
DR   KEGG; cgr:CAGL0E04048g; -.
DR   CGD; CAL0128806; COF1.
DR   VEuPathDB; FungiDB:CAGL0E04048g; -.
DR   eggNOG; KOG1735; Eukaryota.
DR   HOGENOM; CLU_094004_3_2_1; -.
DR   InParanoid; Q6FV81; -.
DR   OMA; ITFYSWS; -.
DR   Proteomes; UP000002428; Chromosome E.
DR   GO; GO:0030479; C:actin cortical patch; IEA:EnsemblFungi.
DR   GO; GO:0005829; C:cytosol; IDA:CGD.
DR   GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IEA:EnsemblFungi.
DR   GO; GO:0030042; P:actin filament depolymerization; IEA:EnsemblFungi.
DR   GO; GO:0051014; P:actin filament severing; IEA:EnsemblFungi.
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_0000255622"
FT   DOMAIN          5..137
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ   SEQUENCE   143 AA;  15902 MW;  AC7B029F62CCFBFB CRC64;
     MSRSGVAVAD ESIQAFNDLK LGMKYKFVLF SLNDAKTEIV VKETSSDPSY DAFLEKLPEN
     DCLYAVYDFE YQISESEGKR SKIVFFTWSP DTASVRPKMV YASSKDALKR ALNGVAIEIQ
     GTDFSEVSYE AVLEKVSRGA GSH