ID   CDC10_SCHPO             Reviewed;         767 AA.
AC   P01129; Q9UU04;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 191.
DE   RecName: Full=Start control protein cdc10;
GN   Name=cdc10; ORFNames=SPBC336.12c;
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].
RX   PubMed=4018034; DOI=10.1002/j.1460-2075.1985.tb03651.x;
RA   Aves S.J., Durkacz B.W., Carr A., Nurse P.;
RT   "Cloning, sequencing and transcriptional control of the Schizosaccharomyces
RT   pombe cdc10 'start' gene.";
RL   EMBO J. 4:457-463(1985).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 76-310, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=8532516; DOI=10.1093/nar/23.23.4761;
RA   McInerny C.J., Kersey P.J., Creanor J., Fantes P.A.;
RT   "Positive and negative roles for cdc10 in cell cycle gene expression.";
RL   Nucleic Acids Res. 23:4761-4768(1995).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH POL5.
RX   PubMed=16816948; DOI=10.1007/s00438-006-0144-6;
RA   Nadeem F.K., Blair D., McInerny C.J.;
RT   "Pol5p, a novel binding partner to Cdc10p in fission yeast involved in rRNA
RT   production.";
RL   Mol. Genet. Genomics 276:391-401(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, 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: Major component of the cell cycle transcription factor
CC       complex MBF (MCB binding factor, also known as DSC1), that controls G1-
CC       S phase specific gene expression. Involved in the control of rRNA
CC       production, via interaction with pol5. May be involved in the
CC       transcriptional regulation of the cdc22 and cdt1 genes. In fission
CC       yeast, two genes, cdc10 and cdc2, are required for the cell cycle
CC       control called start, the point early in the G1 phase at which cells
CC       become committed to the mitotic cycle. {ECO:0000269|PubMed:16816948,
CC       ECO:0000269|PubMed:8532516}.
CC   -!- SUBUNIT: DSC1 contains cdc10 and sct1/res1. Interacts with pol5.
CC       {ECO:0000269|PubMed:16816948}.
CC   -!- INTERACTION:
CC       P01129; O60094: pol5; NbExp=2; IntAct=EBI-1009350, EBI-1009362;
CC       P01129; P41412: res2; NbExp=3; IntAct=EBI-1009350, EBI-1149177;
CC       P01129; P40923: yox1; NbExp=4; IntAct=EBI-1009350, EBI-8530485;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00630,
CC       ECO:0000269|PubMed:10759889}.
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DR   EMBL; X02175; CAA26116.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB58164.1; -; Genomic_DNA.
DR   EMBL; AB027889; BAA87193.1; -; Genomic_DNA.
DR   PIR; A01382; COZPCD.
DR   RefSeq; NP_596132.1; NM_001022050.2.
DR   AlphaFoldDB; P01129; -.
DR   SMR; P01129; -.
DR   BioGRID; 276766; 71.
DR   DIP; DIP-353N; -.
DR   IntAct; P01129; 5.
DR   MINT; P01129; -.
DR   STRING; 284812.P01129; -.
DR   iPTMnet; P01129; -.
DR   MaxQB; P01129; -.
DR   PaxDb; 4896-SPBC336-12c-1; -.
DR   EnsemblFungi; SPBC336.12c.1; SPBC336.12c.1:pep; SPBC336.12c.
DR   GeneID; 2540234; -.
DR   KEGG; spo:SPBC336.12c; -.
DR   PomBase; SPBC336.12c; cdc10.
DR   VEuPathDB; FungiDB:SPBC336.12c; -.
DR   eggNOG; ENOG502QPWC; Eukaryota.
DR   HOGENOM; CLU_009666_1_1_1; -.
DR   InParanoid; P01129; -.
DR   OMA; WIPYDKA; -.
DR   PhylomeDB; P01129; -.
DR   PRO; PR:P01129; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR   GO; GO:0030907; C:MBF transcription complex; IDA:PomBase.
DR   GO; GO:0005634; C:nucleus; EXP:PomBase.
DR   GO; GO:0033309; C:SBF transcription complex; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:PomBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:PomBase.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:PomBase.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; EXP:PomBase.
DR   GO; GO:0009303; P:rRNA transcription; IDA:UniProtKB.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.10.260.10; Transcription regulator HTH, APSES-type DNA-binding domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR036887; HTH_APSES_sf.
DR   InterPro; IPR018004; KilA/APSES_HTH.
DR   InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR   PANTHER; PTHR43828; ASPARAGINASE; 1.
DR   PANTHER; PTHR43828:SF3; REGULATORY PROTEIN SWI6; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF04383; KilA-N; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM01252; KilA-N; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF54616; DNA-binding domain of Mlu1-box binding protein MBP1; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS51299; HTH_APSES; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           1..767
FT                   /note="Start control protein cdc10"
FT                   /id="PRO_0000067060"
FT   DOMAIN          66..173
FT                   /note="HTH APSES-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   REPEAT          356..385
FT                   /note="ANK 1"
FT   REPEAT          483..512
FT                   /note="ANK 2"
FT   DNA_BIND        98..119
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT   REGION          17..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          542..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           261..264
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        23..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   767 AA;  85513 MW;  0E514EE1BE218EFA CRC64;
     MASANFIRQF ELGNDSFSYQ KRPEDEPSQP LSNRNINKLN DSSTLKDSSS RIFINSQVLR
     DGRPVELYAV ECSGMKYMEL SCGDNVALRR CPDSYFNISQ ILRLAGTSSS ENAKELDDII
     ESGDYENVDS KHPQIDGVWV PYDRAISIAK RYGVYEILQP LISFNLDLFP KFSKQQQIES
     SSISKNLNTS SFNTRSPLRN HNFSNPSKSS KNGVHTINNM QSSPSPSSSF LLPLTQIDSQ
     NVKRSNNYLS TSPPILEQRL KRHRIDVSDE DLHPSSQLND NEASSLFPDT PRLNHSLSFV
     SLVSSLPPLD QNIMQDYHTS KDILTSIFLD VNFADSSALE AKLSDSLDLD VPIDELGHAA
     LHWAAAVAKM PLLQALIHKG ANPLRGNLTG ETALMRSVLV TNHLNQNSFG DLLDLLYASL
     PCTDRAGRTV VHHICLTAGI KGRGSASRYY LETLLNWAKK HASGNNGYML KDFINYLNHQ
     DKNGDTALNI AARIGNKNIV EVLMQAGASA YIPNRAGLSV ANFGIFVENA LKQPEDSKQT
     KVSLMSENLS SKEKTAVPPR QKSRDIIASV TDVISSLDKD FQDEMAAKQS MIDSAYTQLR
     ESTKKLSDLR EQLHVSETQR TLFLELRQRC KNLMTSIEEQ KSELSNLYES FDPNGIHDSL
     SLDADAPFTV NENNNKNLSI AELKFQVAAY ERNEARLNEL ANKLWQRNSN IKSKCRRVVS
     LCTGVDESRV DSLLESLLQA VESDGQQGEV DMGRVAGFLR VVKEHQA
//