ID   COFI_YARLI              Reviewed;         153 AA.
AC   Q6C0Y0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Cofilin;
DE   AltName: Full=Actin-depolymerizing factor 1;
GN   Name=COF1; OrderedLocusNames=YALI0F20856g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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; CR382132; CAG78491.1; -; Genomic_DNA.
DR   RefSeq; XP_505682.1; XM_505682.1.
DR   AlphaFoldDB; Q6C0Y0; -.
DR   SMR; Q6C0Y0; -.
DR   STRING; 4952.CAG78491; -.
DR   EnsemblFungi; CAG78491; CAG78491; YALI0_F20856g.
DR   GeneID; 2908953; -.
DR   KEGG; yli:YALI0F20856g; -.
DR   VEuPathDB; FungiDB:YALI0_F20856g; -.
DR   HOGENOM; CLU_094004_3_2_1; -.
DR   InParanoid; Q6C0Y0; -.
DR   OMA; ECKYAIY; -.
DR   Proteomes; UP000001300; Chromosome F.
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..153
FT                   /note="Cofilin"
FT                   /id="PRO_0000255629"
FT   DOMAIN          15..147
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ   SEQUENCE   153 AA;  17029 MW;  017ACADE7FBD2E8A CRC64;
     MFQPCCSKST MSRSGVAVND SALQAFNELK LGKKVTFIIY KINDAKTEIV VEEEGTTDSY
     DTFLGKLPEN DCRYAVYDFE YEISSGEGKR SKLVFFTWSP DTAPVRSKMI YASSKDSLRR
     ALTGISTEIQ GTDFSEVAYE SVLERVSRGA GSH