ID   CDC25_YEAST             Reviewed;        1589 AA.
AC   P04821; D6VYV4;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   02-SEP-2026, entry version 227.
DE   RecName: Full=Cell division control protein 25;
GN   Name=CDC25; Synonyms=CTN1; OrderedLocusNames=YLR310C;
GN   ORFNames=L2142.6;
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].
RX   PubMed=3545497; DOI=10.1016/0092-8674(87)90076-6;
RA   Broek D., Toda T., Michaeli T., Levin L., Birchmeier C., Zoller M.,
RA   Powers S., Wigler M.;
RT   "The S. cerevisiae CDC25 gene product regulates the RAS/adenylate cyclase
RT   pathway.";
RL   Cell 48:789-799(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3011405; DOI=10.1002/j.1460-2075.1986.tb04222.x;
RA   Camonis J.H., Kalekine M., Gondre B., Garreau H., Boy-Marcotte E.,
RA   Jacquet M.;
RT   "Characterization, cloning and sequence analysis of the CDC25 gene which
RT   controls the cyclic AMP level of Saccharomyces cerevisiae.";
RL   EMBO J. 5:375-380(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871; DOI=10.1038/387s087;
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 877-1589.
RX   PubMed=3329037; DOI=10.1007/bf00398284;
RA   Daniel J.H.;
RT   "The CDC25 'Start' gene of Saccharomyces cerevisiae: sequencing of the
RT   active C-terminal fragment and regional homologies with rhodopsin and
RT   cytochrome P450.";
RL   Curr. Genet. 10:879-885(1986).
RN   [6]
RP   DOMAINS.
RX   PubMed=3070351; DOI=10.1007/bf00337721;
RA   Munder T., Mink M., Kuentzel H.;
RT   "Domains of the Saccharomyces cerevisiae CDC25 gene controlling mitosis and
RT   meiosis.";
RL   Mol. Gen. Genet. 214:271-277(1988).
RN   [7]
RP   FUNCTION.
RX   PubMed=2017169; DOI=10.1128/mcb.11.5.2641-2646.1991;
RA   Jones S., Vignais M.L., Broach J.R.;
RT   "The CDC25 protein of Saccharomyces cerevisiae promotes exchange of guanine
RT   nucleotides bound to ras.";
RL   Mol. Cell. Biol. 11:2641-2646(1991).
RN   [8]
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP   MASS 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-151; SER-154; SER-580;
RP   SER-596; SER-632; THR-635 AND SER-649, 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).
CC   -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP. This protein
CC       positively controls the level of cellular cAMP at start, the stage at
CC       which the yeast cell division cycle is triggered.
CC       {ECO:0000269|PubMed:2017169}.
CC   -!- INTERACTION:
CC       P04821; P53094: MDS3; NbExp=3; IntAct=EBI-4237, EBI-10651;
CC       P04821; P01120: RAS2; NbExp=2; IntAct=EBI-4237, EBI-14838;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X03579; CAA27259.1; -; Genomic_DNA.
DR   EMBL; M15458; AAA34478.1; -; Genomic_DNA.
DR   EMBL; U17247; AAB67360.1; -; Genomic_DNA.
DR   EMBL; U20618; AAB64528.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09620.1; -; Genomic_DNA.
DR   PIR; A26596; RGBYC5.
DR   RefSeq; NP_013413.1; NM_001182198.1.
DR   AlphaFoldDB; P04821; -.
DR   SMR; P04821; -.
DR   BioGRID; 31575; 519.
DR   DIP; DIP-2261N; -.
DR   FunCoup; P04821; 371.
DR   IntAct; P04821; 77.
DR   MINT; P04821; -.
DR   STRING; 4932.YLR310C; -.
DR   GlyGen; P04821; 25 sites, 1 O-linked glycan (24 sites).
DR   iPTMnet; P04821; -.
DR   PaxDb; 4932-YLR310C; -.
DR   PeptideAtlas; P04821; -.
DR   EnsemblFungi; YLR310C_mRNA; YLR310C; YLR310C.
DR   GeneID; 851019; -.
DR   KEGG; sce:YLR310C; -.
DR   AGR; SGD:S000004301; -.
DR   SGD; S000004301; CDC25.
DR   VEuPathDB; FungiDB:YLR310C; -.
DR   eggNOG; KOG3417; Eukaryota.
DR   HOGENOM; CLU_002171_1_0_1; -.
DR   InParanoid; P04821; -.
DR   OMA; SEHEYSL; -.
DR   OrthoDB; 546434at2759; -.
DR   BioCyc; YEAST:G3O-32396-MONOMER; -.
DR   Reactome; R-SCE-354192; Integrin signaling.
DR   Reactome; R-SCE-392517; Rap1 signalling.
DR   SABIO-RK; P04821; -.
DR   BioGRID-ORCS; 851019; 4 hits in 10 CRISPR screens.
DR   PRO; PR:P04821; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P04821; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR   GO; GO:0007265; P:Ras protein signal transduction; IDA:SGD.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR   GO; GO:0007089; P:traversing start control point of mitotic cell cycle; IMP:SGD.
DR   CDD; cd00155; RasGEF; 1.
DR   CDD; cd06224; REM; 1.
DR   CDD; cd11883; SH3_Sdc25; 1.
DR   FunFam; 1.20.870.10:FF:000020; Cell division control protein 25; 1.
DR   FunFam; 2.30.30.40:FF:000343; Cell division cycle-related protein; 1.
DR   Gene3D; 1.10.840.10; Ras guanine-nucleotide exchange factors catalytic domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.20.870.10; Son of sevenless (SoS) protein Chain: S domain 1; 1.
DR   InterPro; IPR008937; Ras-like_GEF.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23113:SF368; CELL DIVISION CONTROL PROTEIN 25; 1.
DR   PANTHER; PTHR23113; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48366; Ras GEF; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Guanine-nucleotide releasing factor; Membrane;
KW   Mitosis; Phosphoprotein; Reference proteome; SH3 domain; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1589
FT                   /note="Cell division control protein 25"
FT                   /id="PRO_0000068863"
FT   TRANSMEM        1452..1473
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          58..128
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          1117..1247
FT                   /note="N-terminal Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT   DOMAIN          1305..1542
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          121..243
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..424
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1249..1287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1570..1589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..14
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        20..53
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..139
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..158
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..238
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1249..1259
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1578..1589
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         154
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         580
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         596
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         632
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         635
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         649
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        497
FT                   /note="I -> Y (in Ref. 2; CAA27259)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        954..963
FT                   /note="PVGHHEPFKN -> LSVIMNLSR (in Ref. 2; CAA27259)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1589 AA;  179092 MW;  CA90053435C85465 CRC64;
     MSDTNTSIPN TSSAREAGNA SQTPSISSSS NTSTTTNTES SSASLSSSPS TSELTSIRPI
     GIVVAAYDFN YPIKKDSSSQ LLSVQQGETI YILNKNSSGW WDGLVIDDSN GKVNRGWFPQ
     NFGRPLRDSH LRKHSHPMKK YSSSKSSRRS SLNSLGNSAY LHVPRNPSKS RRGSSTLSAS
     LSNAHNAETS SGHNNTVSMN NSPFSAPNDA SHITPQSSNF NSNASLSQDM TKSADGSSEM
     NTNAIMNNNE TNLQTSGEKA GPPLVAEETI KILPLEEIEM IINGIRSNIA STWSPIPLIT
     KTSDYKLVYY NKDLDIYCSE LPLISNSIME SDDICDSEPK FPPNDHLVNL YTRDLRKNAN
     IEDSSTRSKQ SESEQNRSSL LMEKQDSKET DGNNNSINDD DNNNENNKNE FNEAGPSSLN
     SLSAPDLTQN IQSRVVAPSR SSILAKSDIF YHYSRDIKLW TELQDLTVYY TKTAHKMFLK
     ENRLNFTKYF DLISDSIVFT QLGCRLMQHE IKAKSCSKEI KKIFKGLISS LSRISINSHL
     YFDSAFHRKK MDTMNDKDND NQENNCSRTE GDDGKIEVDS VHDLVSVPLS GKRNVSTSTT
     DTLTPMRSSF STVNENDMEN FSVLGPRNSV NSVVTPRTSI QNSTLEDFSP SNKNFKSAKS
     IYEMVDVEFS KFLRHVQLLY FVLQSSVFSD DNTLPQLLPR FFKGSFSGGS WTNPFSTFIT
     DEFGNATKNK AVTSNEVTAS SSKNSSISRI PPKMADAIAS ASGYSANSET NSQIDLKASS
     AASGSVFTPF NRPSHNRTFS RARVSKRKKK YPLTVDTLNT MKKKSSQIFE KLNNATGEHL
     KIISKPKSRI RNLEINSSTY EQINQNVLLL EILENLDLSI FINLKNLIKT PSILLDLESE
     EFLVHAMSSV SSVLTEFFDI KQAFHDIVIR LIMTTQQTTL DDPYLFSSMR SNFPVGHHEP
     FKNISNTPLV KGPFHKKNEQ LALSLFHVLV SQDVEFNNLE FLNNSDDFKD ACEKYVEISN
     LACIIVDQLI EERENLLNYA ARMMKNNLTA ELLKGEQEKW FDIYSEDYSD DDSENDEAII
     DDELGSEDYI ERKAANIEKN LPWFLTSDYE TSLVYDSRGK IRGGTKEALI EHLTSHELVD
     AAFNVTMLIT FRSILTTREF FYALIYRYNL YPPEGLSYDD YNIWIEKKSN PIKCRVVNIM
     RTFLTQYWTR NYYEPGIPLI LNFAKMVVSE KIPGAEDLLQ KINEKLINEN EKEPVDPKQQ
     DSVSAVVQTT KRDNKSPIHM SSSSLPSSAS SAFFRLKKLK LLDIDPYTYA TQLTVLEHDL
     YLRITMFECL DRAWGTKYCN MGGSPNITKF IANANTLTNF VSHTIVKQAD VKTRSKLTQY
     FVTVAQHCKE LNNFSSMTAI VSALYSSPIY RLKKTWDLVS TESKDLLKNL NNLMDSKRNF
     VKYRELLRSV TDVACVPFFG VYLSDLTFTF VGNPDFLHNS TNIINFSKRT KIANIVEEII
     SFKRFHYKLK RLDDIQTVIE ASLENVPHIE KQYQLSLQVE PRSGNTKGST HASSASGTKT
     AKFLSEFTDD KNGNFLKLGK KKPPSRLFR
//