EFC25_SCHPO
ID EFC25_SCHPO Reviewed; 987 AA.
AC Q9USU1;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Ras guanine nucleotide exchange factor efc25;
DE AltName: Full=Exchange factor cdc25p-like protein;
GN Name=efc25; ORFNames=SPBC336.03;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=9256078; DOI=10.1016/s0378-1119(97)00115-7;
RA Tratner I., Fourticq-Esqueoute A., Tillit J., Baldacci G.;
RT "Cloning and characterization of the S. pombe gene efc25+, a new putative
RT guanine nucleotide exchange factor.";
RL Gene 193:203-210(1997).
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.
RC STRAIN=SP870;
RX PubMed=12052869; DOI=10.1128/mcb.22.13.4598-4606.2002;
RA Papadaki P., Pizon V., Onken B., Chang E.C.;
RT "Two ras pathways in fission yeast are differentially regulated by two ras
RT guanine nucleotide exchange factors.";
RL Mol. Cell. Biol. 22:4598-4606(2002).
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).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in chromosome segregation and cell morphology
CC upstream of the ras1-scd1 pathway. Promotes the exchange of ras1-bound
CC GDP by GTP leading to its activation. {ECO:0000269|PubMed:12052869,
CC ECO:0000269|PubMed:9256078}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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DR EMBL; CU329671; CAB58155.1; -; Genomic_DNA.
DR PIR; T40241; T40241.
DR RefSeq; NP_596123.1; NM_001022041.2.
DR AlphaFoldDB; Q9USU1; -.
DR SMR; Q9USU1; -.
DR BioGRID; 276780; 41.
DR STRING; 4896.SPBC336.03.1; -.
DR iPTMnet; Q9USU1; -.
DR MaxQB; Q9USU1; -.
DR PaxDb; Q9USU1; -.
DR PRIDE; Q9USU1; -.
DR EnsemblFungi; SPBC336.03.1; SPBC336.03.1:pep; SPBC336.03.
DR GeneID; 2540248; -.
DR KEGG; spo:SPBC336.03; -.
DR PomBase; SPBC336.03; efc25.
DR VEuPathDB; FungiDB:SPBC336.03; -.
DR eggNOG; KOG3417; Eukaryota.
DR HOGENOM; CLU_302305_0_0_1; -.
DR InParanoid; Q9USU1; -.
DR OMA; NFSNCFT; -.
DR Reactome; R-SPO-416482; G alpha (12/13) signalling events.
DR Reactome; R-SPO-8980692; RHOA GTPase cycle.
DR Reactome; R-SPO-9013148; CDC42 GTPase cycle.
DR PRO; PR:Q9USU1; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:PomBase.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0071963; P:establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW Chromosome partition; Cytoplasm; Guanine-nucleotide releasing factor;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..987
FT /note="Ras guanine nucleotide exchange factor efc25"
FT /id="PRO_0000372377"
FT DOMAIN 590..723
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 752..985
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 552
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 987 AA; 112730 MW; 66614B02CAD74422 CRC64;
MRRPNLDRLR LKSRQGFETS VSKPSTPSYS TYSLSPTFSD KSVLSPSTMS DSYALSSTYT
AGSSYQNGES DYFGSLPTPS SDKSSTSPFP YLKGSFDDRF SSTHSLTRQP SPRSPLTPLK
GNTRASPEIR YVSDFTPPSS PFEDMQASVH SLPLSGCSIG PVRTNHSSSL SNSSNSLLQT
ESSLRPNSSF VNSPFFPLPS SDDLFLNDRV INLFLFYEKF SYLFTHLLSA IKSRDALSIP
SLVLSLQEEL FNLCQQTGTF YLLQHNLLQN FEFENPIKLH FDKIIPYFSR LTVLTFSNRA
FIFPDHTFPR LQQSAEDFLY HLQFFFTLCA NNSLYLSRFC YYPSFVPNTP FGGKWTNNGL
SAVSSAYRTR LLEPCLPELD KCVWFLLKNC DEFIENFSDF ADEEYVFEIC STITSHSEQI
FNKLESWDMS IYFDKDLSEC EQATNFAVQS YFVTKQRCYD LLTDLVCSSQ DLMMEHSNDF
STMPTMIASI AVAFQTLFEN VCDFLKVRAA LVDEMQELAT KEFENKFSNA NTAKDDEPAR
QTNKGTTRIS RSSDFTAVSE MSKDTLTLGR NSLQSILMLD NLLTNKVVQS DNNVKGGTLP
ALVHYLVQNV HLNKDFRHSF LLTYKTFTTP QELFTLLVIL FHELPPPGLD ATAYSSWEKG
DNFVTKKNVC TVMNLWVQKY FFEDLKARNT LYLISEMRTF LRDHVVPSFH IGSVILSEID
NLWTEEPPDS LTQRLLSSPM ATFISLNVYA YTPEEFASQM TLLEFDYLKQ IPSREWIFRS
WVSRDSRSAV RNYINFSNCF TYWIINCILE KKNTKARTAV ISFFIQTAYK CLSLQNFSTL
MSIVSALNSA PIYRLHAAYK LVKAEDIICL SGLREIVETK KNFSTYRALL RKAELPCVPF
LGVILSDLTF IDEGNPDVLD SSPHLLSFNK RHRLADVVAD VCRFQSSSYE MQSNTDLQSY
ILHRCRFVNQ DLSYLFDKSL SLEPRSS
