ID   COFI_DEBHA              Reviewed;         143 AA.
AC   Q6BWX4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Cofilin;
DE   AltName: Full=Actin-depolymerizing factor 1;
GN   Name=COF1; OrderedLocusNames=DEHA2B07722g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382134; CAG85296.1; -; Genomic_DNA.
DR   RefSeq; XP_457295.1; XM_457295.1.
DR   AlphaFoldDB; Q6BWX4; -.
DR   SMR; Q6BWX4; -.
DR   STRING; 4959.XP_457295.1; -.
DR   EnsemblFungi; CAG85296; CAG85296; DEHA2B07722g.
DR   GeneID; 2913059; -.
DR   KEGG; dha:DEHA2B07722g; -.
DR   VEuPathDB; FungiDB:DEHA2B07722g; -.
DR   eggNOG; KOG1735; Eukaryota.
DR   HOGENOM; CLU_094004_3_2_1; -.
DR   InParanoid; Q6BWX4; -.
DR   OMA; ECKYAIY; -.
DR   OrthoDB; 1370477at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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_0000255624"
FT   DOMAIN          5..137
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ   SEQUENCE   143 AA;  15860 MW;  52E51DD112CB7703 CRC64;
     MSRSGVAVAD ESLTAFNDLK LGKKYKFIIF ALNDQKTEIV VEETSNNSDY DAFLEKLPEN
     ECKYAIYDFE YEIGGGEGKR SKIVFFTWSP DTAPIKSKMI YASSKDALRR ALNGVSSDVQ
     GTDFSEVAYE SVLDRVSKGA GSH