CDC10_YEAST
ID CDC10_YEAST Reviewed; 322 AA.
AC P25342; D6VR12;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Cell division control protein 10;
GN Name=CDC10; OrderedLocusNames=YCR002C; ORFNames=YCR022, YCR2C;
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].
RC STRAIN=ATCC 26109 / X2180;
RX PubMed=8791410; DOI=10.1016/s0955-0674(96)80054-8;
RA Longtine M.S., DeMarini D.J., Valencik M.L., Al-Awar O.S., Fares H.,
RA De Virgilio C., Pringle J.R.;
RT "The septins: roles in cytokinesis and other processes.";
RL Curr. Opin. Cell Biol. 8:106-119(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1872033; DOI=10.1002/yea.320070412;
RA Steensma H.Y., van der Aart Q.J.M.;
RT "Sequence of the CDC10 region at chromosome III of Saccharomyces
RT cerevisiae.";
RL Yeast 7:425-429(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1574125; DOI=10.1038/357038a0;
RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA Sgouros J.G.;
RT "The complete DNA sequence of yeast chromosome III.";
RL Nature 357:38-46(1992).
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 IDENTIFICATION IN THE SEPTIN COMPLEX.
RX PubMed=9813094; DOI=10.1083/jcb.143.3.737;
RA Frazier J.A., Wong M.L., Longtine M.S., Pringle J.R., Mann M.,
RA Mitchison T.J., Field C.;
RT "Polymerization of purified yeast septins: evidence that organized filament
RT arrays may not be required for septin function.";
RL J. Cell Biol. 143:737-749(1998).
RN [6]
RP IDENTIFICATION IN THE GIN4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12058072; DOI=10.1091/mbc.01-10-0500;
RA Mortensen E.M., McDonald H., Yates J. III, Kellogg D.R.;
RT "Cell cycle-dependent assembly of a Gin4-septin complex.";
RL Mol. Biol. Cell 13:2091-2105(2002).
RN [7]
RP ASSOCIATION WITH PHOSPHOINOSIDES LIPIDS, AND INTERACTION WITH CDC11.
RX PubMed=12665577; DOI=10.1128/mcb.23.8.2762-2777.2003;
RA Casamayor A., Snyder M.;
RT "Molecular dissection of a yeast septin: distinct domains are required for
RT septin interaction, localization, and function.";
RL Mol. Cell. Biol. 23:2762-2777(2003).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [9]
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 [10]
RP SELF-ASSOCIATION, AND ASSEMBLY OF THE SEPTIN FILAMENTS.
RX PubMed=15282341; DOI=10.1091/mbc.e04-04-0330;
RA Versele M., Gullbrand B., Shulewitz M.J., Cid V.J., Bahmanyar S.,
RA Chen R.E., Barth P., Alber T., Thorner J.;
RT "Protein-protein interactions governing septin heteropentamer assembly and
RT septin filament organization in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 15:4568-4583(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [13]
RP INTERACTION WITH SYP1.
RX PubMed=18791237; DOI=10.1534/genetics.108.091900;
RA Qiu W., Neo S.P., Yu X., Cai M.;
RT "A novel septin-associated protein, Syp1p, is required for normal cell
RT cycle-dependent septin cytoskeleton dynamics in yeast.";
RL Genetics 180:1445-1457(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, 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 [15]
RP IDENTIFICATION BY MASS 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).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Septins are GTPases involved in cytokinesis that assemble
CC early in the cell cycle as a patch at the incipient bud site and form a
CC ring approximate 15 minutes before bud emergence, which transforms into
CC an hour-glass shaped collar of cortical filaments that spans both sides
CC of the mother-bud neck. This collar persists until just before
CC cytokinesis, when it splits into two rings that occupy opposite sides
CC of the neck. The septins at the bud neck serve as a structural scaffold
CC that recruits different components involved in diverse processes at
CC specific stages during the cell cycle. Many proteins bind
CC asymmetrically to the septin collar. The septin assembly is regulated
CC by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and
CC HOF1, a protein involved in septation, to the site of cleavage. Septins
CC are also involved in cell morphogenesis, bud site selection, chitin
CC deposition, cell cycle regulation, cell compartmentalization and spore
CC wall formation.
CC -!- SUBUNIT: Component of the septin complex which consists of CDC3, CDC10,
CC CDC11, CDC12 and probably SHS1 and rearranges to a cortical collar of
CC highly ordered filaments at the mother-bud-neck. A complex formed by
CC CDC3, CDC10, CDC11 and CDC12 is capable of forming long filaments in
CC vitro and the components seem to be present in a 2:2:2:2 arrangement in
CC vivo. The filaments are proposed to be formed by the end-to-end
CC polymerization of CDC3-CDC12-CDC11 complexes with CDC10 serving as a
CC bridge to bundle the polymers into paired filaments. Component of the
CC GIN4 complex composed of at least BNI5, CDC3, CDC10, CDC11, CDC12,
CC GIN4, NAP1 and SHS1. Self-associates. Interacts with SYP1.
CC {ECO:0000269|PubMed:12058072, ECO:0000269|PubMed:12665577,
CC ECO:0000269|PubMed:18791237, ECO:0000269|PubMed:9813094}.
CC -!- INTERACTION:
CC P25342; P47136: BUD4; NbExp=2; IntAct=EBI-4174, EBI-3848;
CC P25342; P32457: CDC3; NbExp=11; IntAct=EBI-4174, EBI-4429;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:14562095};
CC Peripheral membrane protein {ECO:0000269|PubMed:14562095}. Bud neck
CC {ECO:0000269|PubMed:14562095}. Note=Present at the bud neck during cell
CC division. Probably interacts with phosphoinosides such as
CC phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate.
CC -!- MISCELLANEOUS: Present with 14100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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DR EMBL; L16549; AAB49377.1; -; Genomic_DNA.
DR EMBL; S48552; AAD13856.1; -; Genomic_DNA.
DR EMBL; X59720; CAA42339.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07481.1; -; Genomic_DNA.
DR PIR; S19441; S19441.
DR RefSeq; NP_009928.1; NM_001178715.1.
DR AlphaFoldDB; P25342; -.
DR SMR; P25342; -.
DR BioGRID; 30980; 573.
DR ComplexPortal; CPX-1675; Septin complex.
DR ComplexPortal; CPX-1712; Gin4 serine/threonine kinase complex.
DR DIP; DIP-673N; -.
DR IntAct; P25342; 46.
DR MINT; P25342; -.
DR STRING; 4932.YCR002C; -.
DR iPTMnet; P25342; -.
DR MaxQB; P25342; -.
DR PaxDb; P25342; -.
DR PRIDE; P25342; -.
DR EnsemblFungi; YCR002C_mRNA; YCR002C; YCR002C.
DR GeneID; 850358; -.
DR KEGG; sce:YCR002C; -.
DR SGD; S000000595; CDC10.
DR VEuPathDB; FungiDB:YCR002C; -.
DR eggNOG; KOG1547; Eukaryota.
DR GeneTree; ENSGT00940000175654; -.
DR HOGENOM; CLU_017718_7_1_1; -.
DR InParanoid; P25342; -.
DR OMA; QCEFVYL; -.
DR BioCyc; YEAST:G3O-29321-MON; -.
DR PRO; PR:P25342; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P25342; protein.
DR GO; GO:0005619; C:ascospore wall; IC:ComplexPortal.
DR GO; GO:0042764; C:ascospore-type prospore; IDA:SGD.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:1990317; C:Gin4 complex; IPI:ComplexPortal.
DR GO; GO:0001400; C:mating projection base; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0072687; C:meiotic spindle; IDA:SGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005628; C:prospore membrane; IDA:SGD.
DR GO; GO:0031105; C:septin complex; IDA:SGD.
DR GO; GO:0032160; C:septin filament array; IDA:SGD.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0005876; C:spindle microtubule; IDA:SGD.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:SGD.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IDA:SGD.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IDA:SGD.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:SGD.
DR GO; GO:0032186; P:cellular bud neck septin ring organization; IC:ComplexPortal.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0010458; P:exit from mitosis; IMP:SGD.
DR GO; GO:0030011; P:maintenance of cell polarity; IC:SGD.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:SGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:ComplexPortal.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0000921; P:septin ring assembly; IMP:SGD.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IC:ComplexPortal.
DR GO; GO:0043934; P:sporulation; IDA:SGD.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR PIRSF; PIRSF006698; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; GTP-binding; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..322
FT /note="Cell division control protein 10"
FT /id="PRO_0000173498"
FT DOMAIN 29..302
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 39..46
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 97..100
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 179..182
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT BINDING 39..46
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 180..188
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
SQ SEQUENCE 322 AA; 37025 MW; 672467301D4D2697 CRC64;
MDPLSSVQPA SYVGFDTITN QIEHRLLKKG FQFNIMVVGQ SGLGKSTLIN TLFASHLIDS
ATGDDISALP VTKTTEMKIS THTLVEDRVR LNINVIDTPG FGDFIDNSKA WEPIVKYIKE
QHSQYLRKEL TAQRERFITD TRVHAILYFL QPNGKELSRL DVEALKRLTE IANVIPVIGK
SDTLTLDERT EFRELIQNEF EKYNFKIYPY DSEELTDEEL ELNRSVRSII PFAVVGSENE
IEINGETFRG RKTRWSAINV EDINQCDFVY LREFLIRTHL QDLIETTSYI HYEGFRARQL
IALKENANSR SSAHMSSNAI QR
