ID   COFI_OGAPD              Reviewed;         143 AA.
AC   Q96VU9; E7R9G4; W1Q9F7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Cofilin;
DE   AltName: Full=Actin-depolymerizing factor 1;
GN   Name=COF1; ORFNames=HPODL_02643;
OS   Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS   Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Pichiaceae; Ogataea.
OX   NCBI_TaxID=871575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1;
RA   Agaphonov M.O., Deev A.V., Kim S.-Y., Sohn J.-H., Choi E.-S.,
RA   Ter-Avanesyan M.D.;
RT   "Novel reporter and strategy for the isolation and functional
RT   characterization of transcriptionally active sequences in the
RT   methylotrophic yeast Hansenula polymorpha.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1;
RX   PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA   Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA   Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA   Skryabin K.G.;
RT   "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT   DL1.";
RL   BMC Genomics 14:837-837(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; AF399639; AAK85273.1; -; mRNA.
DR   EMBL; AEOI02000010; ESW96000.1; -; Genomic_DNA.
DR   RefSeq; XP_013932430.1; XM_014076955.1.
DR   AlphaFoldDB; Q96VU9; -.
DR   SMR; Q96VU9; -.
DR   STRING; 1005962.Q96VU9; -.
DR   EnsemblFungi; ESW96000; ESW96000; HPODL_02643.
DR   GeneID; 25772095; -.
DR   eggNOG; KOG1735; Eukaryota.
DR   HOGENOM; CLU_094004_3_2_1; -.
DR   OMA; ECKYAIY; -.
DR   OrthoDB; 1370477at2759; -.
DR   Proteomes; UP000008673; Chromosome VII.
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   2: Evidence at transcript level;
KW   Actin-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..143
FT                   /note="Cofilin"
FT                   /id="PRO_0000255627"
FT   DOMAIN          5..137
FT                   /note="ADF-H"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ   SEQUENCE   143 AA;  15971 MW;  0AE01CA7C52D15C4 CRC64;
     MSRSGVAVSD EALKAFNDLK LGKKFKSIIY KLNDAKTEIV VDSTSTEDAY DAFVEDLPEN
     DCRYAVYDFE YEVGQGDGKR NKIVFYQWSP DTASVRAKMV YASSKDALRR ALNGIGTEIQ
     GTDFSEVAYE SVLEKISRTT GLH