COFI_YEAST
ID COFI_YEAST Reviewed; 143 AA.
AC Q03048; D6VXV8; Q05307; Q2XN65;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Cofilin;
DE AltName: Full=Actin-depolymerizing factor 1;
GN Name=COF1; OrderedLocusNames=YLL050C; ORFNames=L0596;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 43-56; 83-98 AND
RP 106-141.
RX PubMed=8421056; DOI=10.1083/jcb.120.2.421;
RA Moon A.L., Janmey P.A., Louie K.A., Drubin D.G.;
RT "Cofilin is an essential component of the yeast cortical cytoskeleton.";
RL J. Cell Biol. 120:421-435(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8440472; DOI=10.1016/0378-1119(93)90770-4;
RA Iida K., Moriyama K., Matsumoto S., Kawasaki H., Nishida E., Yahara I.;
RT "Isolation of a yeast essential gene, COF1, that encodes a homologue of
RT mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein.";
RL Gene 124:115-120(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA Wedler H., Wambutt R.;
RT "Sequence of a 37 kb DNA fragment from chromosome XII of Saccharomyces
RT cerevisiae including the subtelomeric region of the left arm.";
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10231390; DOI=10.1046/j.1365-2443.1999.00235.x;
RA Iida K., Yahara I.;
RT "Cooperation of two actin-binding proteins, cofilin and Aip1, in
RT Saccharomyces cerevisiae.";
RL Genes Cells 4:21-32(1999).
RN [7]
RP INTERACTION WITH AIP1.
RX PubMed=10366597; DOI=10.1083/jcb.145.6.1251;
RA Rodal A.A., Tetreault J.W., Lappalainen P., Drubin D.G., Amberg D.C.;
RT "Aip1p interacts with cofilin to disassemble actin filaments.";
RL J. Cell Biol. 145:1251-1264(1999).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF 105-LYS-ASP-106 AND 109-ARG-ARG-110.
RX PubMed=11747431; DOI=10.1021/bi0117697;
RA Ojala P.J., Paavilainen V., Lappalainen P.;
RT "Identification of yeast cofilin residues specific for actin monomer and
RT PIP2 binding.";
RL Biochemistry 40:15562-15569(2001).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9145106; DOI=10.1038/nsb0597-366;
RA Fedorov A.A., Lappalainen P., Fedorov E.V., Drubin D.G., Almo S.C.;
RT "Structure determination of yeast cofilin.";
RL Nat. Struct. Biol. 4:366-369(1997).
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. In effect, yeast cofilin increases the rate of actin
CC polymerization by making new ends available for actin subunit addition.
CC Such a protein complex is important for the polarized growth of yeast
CC cells. {ECO:0000269|PubMed:10231390, ECO:0000269|PubMed:11747431}.
CC -!- SUBUNIT: Interacts with actin and AIP1 in a ternary complex.
CC {ECO:0000269|PubMed:10366597}.
CC -!- INTERACTION:
CC Q03048; P60010: ACT1; NbExp=3; IntAct=EBI-4853, EBI-2169;
CC Q03048; P39109: YCF1; NbExp=2; IntAct=EBI-4853, EBI-21779;
CC Q03048; P68135: ACTA1; Xeno; NbExp=3; IntAct=EBI-4853, EBI-367540;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10231390}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10231390}. Nucleus matrix
CC {ECO:0000269|PubMed:10231390}. Note=Throughout the cytoplasm (but not
CC on the cytoplasmic cables) and major component of the cortical actin
CC cytoskeleton.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: Present with 19600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; Z14971; CAA78694.1; -; Genomic_DNA.
DR EMBL; S52662; AAA13256.1; -; Genomic_DNA.
DR EMBL; D13230; BAA02514.1; -; Genomic_DNA.
DR EMBL; Z47973; CAA88007.1; -; Genomic_DNA.
DR EMBL; Z73155; CAA97502.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09274.1; -; Genomic_DNA.
DR PIR; A44397; A44397.
DR RefSeq; NP_013050.1; NM_001181870.1.
DR PDB; 1CFY; X-ray; 2.30 A; A/B=1-143.
DR PDB; 1COF; X-ray; 2.30 A; A=1-143.
DR PDB; 1QPV; X-ray; 3.00 A; A=1-143.
DR PDB; 4KED; X-ray; 1.90 A; A/B=2-143.
DR PDB; 4KEE; X-ray; 1.45 A; A=2-143.
DR PDB; 4KEF; X-ray; 1.10 A; A=2-143.
DR PDBsum; 1CFY; -.
DR PDBsum; 1COF; -.
DR PDBsum; 1QPV; -.
DR PDBsum; 4KED; -.
DR PDBsum; 4KEE; -.
DR PDBsum; 4KEF; -.
DR AlphaFoldDB; Q03048; -.
DR SMR; Q03048; -.
DR BioGRID; 31265; 498.
DR DIP; DIP-197N; -.
DR IntAct; Q03048; 28.
DR MINT; Q03048; -.
DR STRING; 4932.YLL050C; -.
DR iPTMnet; Q03048; -.
DR MaxQB; Q03048; -.
DR PaxDb; Q03048; -.
DR PRIDE; Q03048; -.
DR TopDownProteomics; Q03048; -.
DR EnsemblFungi; YLL050C_mRNA; YLL050C; YLL050C.
DR GeneID; 850676; -.
DR KEGG; sce:YLL050C; -.
DR SGD; S000003973; COF1.
DR VEuPathDB; FungiDB:YLL050C; -.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_3_2_1; -.
DR InParanoid; Q03048; -.
DR OMA; ECKYAIY; -.
DR BioCyc; YEAST:G3O-32149-MON; -.
DR EvolutionaryTrace; Q03048; -.
DR PRO; PR:Q03048; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q03048; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0051015; F:actin filament binding; IDA:SGD.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:SGD.
DR GO; GO:0007015; P:actin filament organization; IDA:SGD.
DR GO; GO:0051014; P:actin filament severing; IDA:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..143
FT /note="Cofilin"
FT /id="PRO_0000214915"
FT DOMAIN 5..137
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 105..106
FT /note="KD->AA: Reduced interaction with PIP2."
FT /evidence="ECO:0000269|PubMed:11747431"
FT MUTAGEN 109..110
FT /note="RR->AA: Defects in actin monomer interaction."
FT /evidence="ECO:0000269|PubMed:11747431"
FT CONFLICT 1..5
FT /note="MSRSG -> MWGKKFIRSQENVKFLCS (in Ref. 3; CAA88007)"
FT /evidence="ECO:0000305"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:4KEF"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:4KEF"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:4KEF"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:4KEF"
FT STRAND 63..71
FT /evidence="ECO:0007829|PDB:4KEF"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1CFY"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:4KEF"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1QPV"
FT HELIX 95..111
FT /evidence="ECO:0007829|PDB:4KEF"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:4KEF"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4KEF"
FT HELIX 129..137
FT /evidence="ECO:0007829|PDB:4KEF"
SQ SEQUENCE 143 AA; 15901 MW; 7A03747B0F21F22D CRC64;
MSRSGVAVAD ESLTAFNDLK LGKKYKFILF GLNDAKTEIV VKETSTDPSY DAFLEKLPEN
DCLYAIYDFE YEINGNEGKR SKIVFFTWSP DTAPVRSKMV YASSKDALRR ALNGVSTDVQ
GTDFSEVSYD SVLERVSRGA GSH
