GMF1_SCHPO
ID GMF1_SCHPO Reviewed; 141 AA.
AC O13808;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Actin-depolymerizing factor gmf1;
DE AltName: Full=Glia maturation factor-like protein 1;
GN Name=gmf1; ORFNames=SPAC17H9.11;
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 [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 [2]
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).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE ARP2/3 COMPLEX.
RX PubMed=20517925; DOI=10.1002/cm.20451;
RA Nakano K., Kuwayama H., Kawasaki M., Numata O., Takaine M.;
RT "GMF is an evolutionarily developed Adf/cofilin-super family protein
RT involved in the Arp2/3 complex-mediated organization of the actin
RT cytoskeleton.";
RL Cytoskeleton 67:373-382(2010).
CC -!- FUNCTION: Actin depolymerizing factor involved in the control of the
CC disassembly of actin patches. Binds and suppresses the arp2/3 complex
CC functions such as the promotion of actin polymerisation and branching
CC filaments. {ECO:0000269|PubMed:20517925}.
CC -!- SUBUNIT: Associates with the arp2/3 complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC actin patch.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family. GMF
CC subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB11220.1; -; Genomic_DNA.
DR PIR; T37877; T37877.
DR RefSeq; NP_593581.1; NM_001019013.2.
DR AlphaFoldDB; O13808; -.
DR SMR; O13808; -.
DR BioGRID; 278728; 7.
DR STRING; 4896.SPAC17H9.11.1; -.
DR iPTMnet; O13808; -.
DR MaxQB; O13808; -.
DR PaxDb; O13808; -.
DR PRIDE; O13808; -.
DR EnsemblFungi; SPAC17H9.11.1; SPAC17H9.11.1:pep; SPAC17H9.11.
DR GeneID; 2542259; -.
DR KEGG; spo:SPAC17H9.11; -.
DR PomBase; SPAC17H9.11; gmf1.
DR VEuPathDB; FungiDB:SPAC17H9.11; -.
DR eggNOG; KOG1736; Eukaryota.
DR HOGENOM; CLU_087056_0_0_1; -.
DR InParanoid; O13808; -.
DR OMA; EWKMLYA; -.
DR PhylomeDB; O13808; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:O13808; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:PomBase.
DR GO; GO:0071846; P:actin filament debranching; IMP:PomBase.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR CDD; cd11283; ADF_GMF-beta_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; IPR011171; GMF.
DR PANTHER; PTHR11249; PTHR11249; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR PIRSF; PIRSF001788; GMF-beta; 1.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoskeleton; Nucleus; Reference proteome.
FT CHAIN 1..141
FT /note="Actin-depolymerizing factor gmf1"
FT /id="PRO_0000310308"
FT DOMAIN 6..141
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
SQ SEQUENCE 141 AA; 16282 MW; 96CB544AE4FD9CAD CRC64;
MSSEARMFTI SDTTMKEIDR FRLRLKKSVM YAFILKVDKA TKEIVPDGEI MDLQSIEEVA
DELSETNPRF ILVSYPTKTT DGRLSTPLFM IYWRPSATPN DLSMIYASAK VWFQDVSQVH
KVFEARDSED ITSEAVDEFL H
