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 27-MAR-2024, entry version 217.
DE RecName: Full=Cell division control protein 25;
GN Name=CDC25; Synonyms=CTN1; OrderedLocusNames=YLR310C; 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;
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; 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; 517.
DR DIP; DIP-2261N; -.
DR IntAct; P04821; 70.
DR MINT; P04821; -.
DR STRING; 4932.YLR310C; -.
DR GlyGen; P04821; 23 sites, 1 O-linked glycan (23 sites).
DR iPTMnet; P04821; -.
DR MaxQB; 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; LEISANC; -.
DR OrthoDB; 68574at2759; -.
DR BioCyc; YEAST:G3O-32396-MONOMER; -.
DR Reactome; R-SCE-193648; NRAGE signals death through JNK.
DR Reactome; R-SCE-416482; G alpha (12/13) signalling events.
DR Reactome; R-SCE-9013149; RAC1 GTPase cycle.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 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; GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR PANTHER; PTHR23113:SF99; RAP GUANINE NUCLEOTIDE EXCHANGE FACTOR 1; 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 129..143
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1287
FT /note="Polar 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
//
