CDC27_YEAST
ID CDC27_YEAST Reviewed; 758 AA.
AC P38042; D6VPS0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Anaphase-promoting complex subunit CDC27;
DE AltName: Full=Anaphase-promoting complex subunit 3;
DE AltName: Full=Cell division control protein 27;
GN Name=CDC27; Synonyms=APC3, SNB1; OrderedLocusNames=YBL084C;
GN ORFNames=YBL0718;
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 204508 / S288c;
RX PubMed=7502586; DOI=10.1002/yea.320111112;
RA Obermaier B., Gassenhuber J., Piravandi E., Domdey H.;
RT "Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces
RT cerevisiae chromosome II.";
RL Yeast 11:1103-1112(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 430.
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 [4]
RP PARTIAL NUCLEOTIDE SEQUENCE, AND MUTAGENESIS OF GLY-613.
RX PubMed=1819514; DOI=10.1101/sqb.1991.056.01.075;
RA Sikorski R.S., Michaud W.A., Wootton J.C., Boguski M.S., Connelly C.,
RA Hieter P.A.;
RT "TPR proteins as essential components of the yeast cell cycle.";
RL Cold Spring Harb. Symp. Quant. Biol. 56:663-673(1991).
RN [5]
RP FUNCTION, SUBUNIT, DOMAINS TPR REPEATS, AND MUTAGENESIS OF LEU-614.
RX PubMed=7925276; DOI=10.1002/j.1460-2075.1994.tb06752.x;
RA Lamb J.R., Michaud W.A., Sikorski R.S., Hieter P.A.;
RT "Cdc16p, Cdc23p and Cdc27p form a complex essential for mitosis.";
RL EMBO J. 13:4321-4328(1994).
RN [6]
RP FUNCTION, PHOSPHORYLATION BY CDC28, AND MUTAGENESIS OF SER-267; THR-304;
RP SER-328; THR-351 AND THR-397.
RX PubMed=10871279; DOI=10.1083/jcb.149.7.1377;
RA Rudner A.D., Murray A.W.;
RT "Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the
RT anaphase-promoting complex.";
RL J. Cell Biol. 149:1377-1390(2000).
RN [7]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15060174; DOI=10.1128/mcb.24.8.3562-3576.2004;
RA Schwickart M., Havlis J., Habermann B., Bogdanova A., Camasses A.,
RA Oelschlaegel T., Shevchenko A., Zachariae W.;
RT "Swm1/Apc13 is an evolutionarily conserved subunit of the anaphase-
RT promoting complex stabilizing the association of Cdc16 and Cdc27.";
RL Mol. Cell. Biol. 24:3562-3576(2004).
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).
CC -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex
CC that controls progression through mitosis and the G1 phase of the cell
CC cycle. The APC/C is thought to confer substrate specificity and, in the
CC presence of ubiquitin-conjugating E2 enzymes, it catalyzes the
CC formation of protein-ubiquitin conjugates that are subsequently
CC degraded by the 26S proteasome. In early mitosis, the APC/C is
CC activated by CDC20 and targets securin PDS1, the B-type cyclin CLB5,
CC and other anaphase inhibitory proteins for proteolysis, thereby
CC triggering the separation of sister chromatids at the metaphase-to-
CC anaphase transition. In late mitosis and in G1, degradation of CLB5
CC allows activation of the APC/C by CDH1, which is needed to destroy
CC CDC20 and the B-type cyclin CLB2 to allow exit from mitosis and
CC creating the low CDK state necessary for cytokinesis and for reforming
CC prereplicative complexes in G1 prior to another round of replication.
CC {ECO:0000269|PubMed:10871279, ECO:0000269|PubMed:15060174,
CC ECO:0000269|PubMed:7925276}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: The APC/C is composed of at least 13 subunits that stay
CC tightly associated throughout the cell cycle: APC1, APC2, APC4, APC5,
CC APC9, APC11, CDC16, CDC23, CDC26, CDC27, DOC1, MND2 and SWM1.
CC {ECO:0000269|PubMed:15060174, ECO:0000269|PubMed:7925276}.
CC -!- INTERACTION:
CC P38042; P53068: DOC1; NbExp=4; IntAct=EBI-4249, EBI-2603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by CDC28, which is required for the early mitotic
CC activity of the APC/C in its CDC20-bound form.
CC {ECO:0000269|PubMed:10871279}.
CC -!- MISCELLANEOUS: Present with 593 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the APC3/CDC27 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X79489; CAA56022.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z35845; CAA84905.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07040.2; -; Genomic_DNA.
DR PIR; S45825; S45825.
DR RefSeq; NP_009469.2; NM_001178324.2.
DR AlphaFoldDB; P38042; -.
DR SMR; P38042; -.
DR BioGRID; 32620; 406.
DR ComplexPortal; CPX-756; Anaphase-Promoting core complex.
DR ComplexPortal; CPX-760; Anaphase-Promoting Complex, CDC20 variant.
DR ComplexPortal; CPX-761; Anaphase-Promoting Complex, CDH1 variant.
DR ComplexPortal; CPX-762; Anaphase-Promoting complex AMA1 variant.
DR DIP; DIP-796N; -.
DR ELM; P38042; -.
DR IntAct; P38042; 41.
DR MINT; P38042; -.
DR STRING; 4932.YBL084C; -.
DR iPTMnet; P38042; -.
DR MaxQB; P38042; -.
DR PaxDb; P38042; -.
DR PRIDE; P38042; -.
DR EnsemblFungi; YBL084C_mRNA; YBL084C; YBL084C.
DR GeneID; 852194; -.
DR KEGG; sce:YBL084C; -.
DR SGD; S000000180; CDC27.
DR VEuPathDB; FungiDB:YBL084C; -.
DR eggNOG; KOG1126; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_008850_2_0_1; -.
DR InParanoid; P38042; -.
DR OMA; ADKRHYN; -.
DR BioCyc; YEAST:G3O-28973-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P38042; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38042; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:SGD.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR Gene3D; 1.25.40.10; -; 4.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00515; TPR_1; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..758
FT /note="Anaphase-promoting complex subunit CDC27"
FT /id="PRO_0000106274"
FT REPEAT 154..187
FT /note="TPR 1"
FT REPEAT 472..505
FT /note="TPR 2"
FT REPEAT 540..573
FT /note="TPR 3"
FT REPEAT 574..607
FT /note="TPR 4"
FT REPEAT 608..641
FT /note="TPR 5"
FT REPEAT 642..675
FT /note="TPR 6"
FT REPEAT 676..709
FT /note="TPR 7"
FT REPEAT 710..743
FT /note="TPR 8"
FT REGION 218..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 267
FT /note="S->A: Abolishes phosphorylation; when associated
FT with A-304; A-328; A-351 and A-397."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 304
FT /note="T->A: Abolishes phosphorylation; when associated
FT with A-267; A-304; A-351 and A-397."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 328
FT /note="S->A: Abolishes phosphorylation; when associated
FT with A-267; A-304; A-328 and A-397."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 351
FT /note="T->A: Abolishes phosphorylation; when associated
FT with A-267; A-304; A-328 and A-304."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 397
FT /note="T->A: Abolishes phosphorylation; when associated
FT with A-304; A-328; A-351 and A-397."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 613
FT /note="G->D: In CDC27-633; G2/M cell cycle arrest at 35
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:1819514"
FT MUTAGEN 614
FT /note="L->GL: Abolishes interaction with CDC23."
FT /evidence="ECO:0000269|PubMed:7925276"
FT CONFLICT 430
FT /note="S -> Q (in Ref. 1; CAA56022 and 2; CAA84905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 85396 MW; A1ECA067AF8784E3 CRC64;
MAVNPELAPF TLSRGIPSFD DQALSTIIQL QDCIQQAIQQ LNYSTAEFLA ELLYAECSIL
DKSSVYWSDA VYLYALSLFL NKSYHTAFQI SKEFKEYHLG IAYIFGRCAL QLSQGVNEAI
LTLLSIINVF SSNSSNTRIN MVLNSNLVHI PDLATLNCLL GNLYMKLDHS KEGAFYHSEA
LAINPYLWES YEAICKMRAT VDLKRVFFDI AGKKSNSHNN NAASSFPSTS LSHFEPRSQP
SLYSKTNKNG NNNINNNVNT LFQSSNSPPS TSASSFSSIQ HFSRSQQQQA NTSIRTCQNK
NTQTPKNPAI NSKTSSALPN NISMNLVSPS SKQPTISSLA KVYNRNKLLT TPPSKLLNND
RNHQNNNNNN NNNNNNNNNN NNNNNNNNII NKTTFKTPRN LYSSTGRLTT SKKNPRSLII
SNSILTSDYS ITLPEIMYNF ALILRSSSQY NSFKAIRLFE SQIPSHIKDT MPWCLVQLGK
LHFEIINYDM SLKYFNRLKD LQPARVKDME IFSTLLWHLH DKVKSSNLAN GLMDTMPNKP
ETWCCIGNLL SLQKDHDAAI KAFEKATQLD PNFAYAYTLQ GHEHSSNDSS DSAKTCYRKA
LACDPQHYNA YYGLGTSAMK LGQYEEALLY FEKARSINPV NVVLICCCGG SLEKLGYKEK
ALQYYELACH LQPTSSLSKY KMGQLLYSMT RYNVALQTFE ELVKLVPDDA TAHYLLGQTY
RIVGRKKDAI KELTVAMNLD PKGNQVIIDE LQKCHMQE
