COFI_SCHPO
ID COFI_SCHPO Reviewed; 137 AA.
AC P78929;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Cofilin;
DE AltName: Full=Actin-depolymerizing factor 1;
GN Name=cof1; Synonyms=adf1; ORFNames=SPAC20G4.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Kawamukai M.;
RT "S. pombe cDNA for actin depolymerizing factor.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16467379; DOI=10.1091/mbc.e05-09-0900;
RA Nakano K., Mabuchi I.;
RT "Actin-depolymerizing protein Adf1 is required for formation and
RT maintenance of the contractile ring during cytokinesis in fission yeast.";
RL Mol. Biol. Cell 17:1933-1945(2006).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. {ECO:0000269|PubMed:16467379}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus
CC matrix. Note=Septum. Throughout the cytoplasm (but not on the
CC cytoplasmic cables) and major component of the cortical actin
CC cytoskeleton.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; D89939; BAA14039.1; -; mRNA.
DR EMBL; CU329670; CAB11258.1; -; Genomic_DNA.
DR PIR; T43245; T43245.
DR RefSeq; NP_594741.1; NM_001020169.2.
DR PDB; 2I2Q; X-ray; 1.72 A; A=1-137.
DR PDBsum; 2I2Q; -.
DR AlphaFoldDB; P78929; -.
DR SMR; P78929; -.
DR BioGRID; 278232; 17.
DR STRING; 4896.SPAC20G4.06c.1; -.
DR iPTMnet; P78929; -.
DR SwissPalm; P78929; -.
DR MaxQB; P78929; -.
DR PaxDb; P78929; -.
DR PRIDE; P78929; -.
DR EnsemblFungi; SPAC20G4.06c.1; SPAC20G4.06c.1:pep; SPAC20G4.06c.
DR GeneID; 2541738; -.
DR KEGG; spo:SPAC20G4.06c; -.
DR PomBase; SPAC20G4.06c; -.
DR VEuPathDB; FungiDB:SPAC20G4.06c; -.
DR eggNOG; KOG1735; Eukaryota.
DR HOGENOM; CLU_094004_3_2_1; -.
DR InParanoid; P78929; -.
DR OMA; ECKYAIY; -.
DR PhylomeDB; P78929; -.
DR EvolutionaryTrace; P78929; -.
DR PRO; PR:P78929; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0003785; F:actin monomer binding; IDA:PomBase.
DR GO; GO:0071846; P:actin filament debranching; IDA:PomBase.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IDA:PomBase.
DR GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IDA:PomBase.
DR GO; GO:1904530; P:negative regulation of actin filament binding; IDA:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Nucleus; Reference proteome.
FT CHAIN 1..137
FT /note="Cofilin"
FT /id="PRO_0000214914"
FT DOMAIN 5..135
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:2I2Q"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2I2Q"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:2I2Q"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:2I2Q"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:2I2Q"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:2I2Q"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2I2Q"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:2I2Q"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:2I2Q"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:2I2Q"
SQ SEQUENCE 137 AA; 15620 MW; ECC6D3354C959E04 CRC64;
MSFSGVKVSP ECLEAFQELK LGKSLRYVVF KMNDTKTEIV VEKKSTDKDF DTFLGDLPEK
DCRYAIYDFE FNLGEGVRNK IIFISWSPDV APIKSKMVYS SSKDTLRRAF TGIGTDIQAT
DFSEVAYETV LEKVTRK
