ID   COFI_CRYNJ              Reviewed;         138 AA.
AC   P0CM06; Q55WM0; Q5KJM6;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Cofilin;
DE   AltName: Full=Actin-depolymerizing factor 1;
GN   Name=COF1; OrderedLocusNames=CNC05990;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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; AE017343; AAW42673.1; -; Genomic_DNA.
DR   RefSeq; XP_569980.1; XM_569980.1.
DR   AlphaFoldDB; P0CM06; -.
DR   SMR; P0CM06; -.
DR   STRING; 5207.AAW42673; -.
DR   PaxDb; P0CM06; -.
DR   EnsemblFungi; AAW42673; AAW42673; CNC05990.
DR   GeneID; 3256627; -.
DR   KEGG; cne:CNC05990; -.
DR   VEuPathDB; FungiDB:CNC05990; -.
DR   eggNOG; KOG1735; Eukaryota.
DR   HOGENOM; CLU_094004_3_2_1; -.
DR   InParanoid; P0CM06; -.
DR   OMA; ECKYAIY; -.
DR   OrthoDB; 1370477at2759; -.
DR   Proteomes; UP000002149; Chromosome 3.
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   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..138
FT                   /note="Cofilin"
FT                   /id="PRO_0000255623"
FT   DOMAIN          2..136
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ   SEQUENCE   138 AA;  15738 MW;  C618F8A0B437928B CRC64;
     MSSGVQPTQE CLEKFQELKT GKKLTYVIYG LSEDKRSIVV LKASEDKDFD SFVAELPEKD
     CRWAVYDFEF TLPGGEGVRN KLCFIVWSPD DASVKNKMIF ASSKEAIRRR LDGIHTEIQA
     TDFSEITKDA LFEKATRK