COFI_GIBZE
ID COFI_GIBZE Reviewed; 153 AA.
AC Q4I963; A0A098E4Q7; A0A0E0SP10; A0A1I9FVL7; I1RQA4; V6REA7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Cofilin;
DE AltName: Full=Actin-depolymerizing factor 1;
GN Name=COF1; ORFNames=FGRAMPH1_01T19853, FGRRES_06245, FGSG_06245;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CEF88173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS231665; ESU12317.1; -; Genomic_DNA.
DR EMBL; HG970334; CEF88173.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_011324893.1; XM_011326591.1.
DR AlphaFoldDB; Q4I963; -.
DR SMR; Q4I963; -.
DR STRING; 5518.FGSG_06245P0; -.
DR EnsemblFungi; ESU12317; ESU12317; FGSG_06245.
DR GeneID; 23553381; -.
DR KEGG; fgr:FGSG_06245; -.
DR eggNOG; KOG1735; Eukaryota.
DR HOGENOM; CLU_094004_4_0_1; -.
DR InParanoid; Q4I963; -.
DR Proteomes; UP000070720; Chromosome 3.
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 PRINTS; PR00006; COFILIN.
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_0000255625"
FT DOMAIN 4..148
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ SEQUENCE 153 AA; 16969 MW; 3711C4C9D8718DFA CRC64;
MSQSGATVSQ DCITAFNDLK LNKKYKFIVY KLSDDYKEIV IDKASESRDW EDFRETLVNA
TAKSRTGAVG KGPRYAVYDF EYNLASGDGI RNKITFIAWS PDDAGIQPKM IYASSKEALK
RSLTGIATEL QANDTDDIEY DSILKTVSKG LAA
