CDC16_YEAST
ID CDC16_YEAST Reviewed; 840 AA.
AC P09798; D6VXR3;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Anaphase-promoting complex subunit CDC16;
DE AltName: Full=Cell division control protein 16;
GN Name=CDC16; OrderedLocusNames=YKL022C;
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=R.B.Wickner 1385;
RX PubMed=2823230; DOI=10.1093/nar/15.20.8439;
RA Icho T., Wickner R.B.;
RT "Metal-binding, nucleic acid-binding finger sequences in the CDC16 gene of
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 15:8439-8450(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
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 [4]
RP FUNCTION, AND SUBUNIT.
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 [5]
RP FUNCTION, AND MUTAGENESIS OF CYS-482 AND SER-557.
RX PubMed=9660930; DOI=10.1016/s1097-2765(00)80046-5;
RA Heichman K.A., Roberts J.M.;
RT "CDC16 controls initiation at chromosome replication origins.";
RL Mol. Cell 1:457-463(1998).
RN [6]
RP FUNCTION, PHOSPHORYLATION BY CDC28, AND MUTAGENESIS OF SER-44; SER-59;
RP SER-95; SER-103; THR-115 AND THR-406.
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 INTERACTION WITH AMA1.
RX PubMed=11114178; DOI=10.1073/pnas.250351297;
RA Cooper K.F., Mallory M.J., Egeland D.B., Jarnik M., Strich R.;
RT "Ama1p is a meiosis-specific regulator of the anaphase promoting
RT complex/cyclosome in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14548-14553(2000).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF SER-530.
RX PubMed=12928868; DOI=10.1007/s00438-003-0912-5;
RA Lai L.A., Morabito L., Holloway S.L.;
RT "A novel yeast mutant that is defective in regulation of the Anaphase-
RT Promoting Complex by the spindle damage checkpoint.";
RL Mol. Genet. Genomics 270:156-164(2003).
RN [9]
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 [10]
RP DOMAINS TPR REPEATS.
RX PubMed=2404612; DOI=10.1016/0092-8674(90)90745-z;
RA Sikorski R.S., Boguski M.S., Goebl M., Hieter P.A.;
RT "A repeating amino acid motif in CDC23 defines a family of proteins and a
RT new relationship among genes required for mitosis and RNA synthesis.";
RL Cell 60:307-317(1990).
RN [11]
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 [12]
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 [13]
RP IDENTIFICATION BY 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 [14]
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).
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:12928868,
CC ECO:0000269|PubMed:15060174, ECO:0000269|PubMed:7925276,
CC ECO:0000269|PubMed:9660930}.
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. Interacts
CC with AMA1. {ECO:0000269|PubMed:11114178, ECO:0000269|PubMed:15060174,
CC ECO:0000269|PubMed:7925276}.
CC -!- INTERACTION:
CC P09798; P53068: DOC1; NbExp=13; IntAct=EBI-4208, EBI-2603;
CC -!- SUBCELLULAR LOCATION: Nucleus {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 2753 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the APC6/CDC16 family. {ECO:0000305}.
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DR EMBL; X06165; CAA29521.1; -; Genomic_DNA.
DR EMBL; Z28022; CAA81857.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09133.1; -; Genomic_DNA.
DR PIR; A27832; A27832.
DR RefSeq; NP_012903.1; NM_001179588.1.
DR AlphaFoldDB; P09798; -.
DR SMR; P09798; -.
DR BioGRID; 34109; 177.
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-25N; -.
DR IntAct; P09798; 30.
DR MINT; P09798; -.
DR STRING; 4932.YKL022C; -.
DR iPTMnet; P09798; -.
DR MaxQB; P09798; -.
DR PaxDb; P09798; -.
DR PRIDE; P09798; -.
DR TopDownProteomics; P09798; -.
DR EnsemblFungi; YKL022C_mRNA; YKL022C; YKL022C.
DR GeneID; 853846; -.
DR KEGG; sce:YKL022C; -.
DR SGD; S000001505; CDC16.
DR VEuPathDB; FungiDB:YKL022C; -.
DR eggNOG; KOG1173; Eukaryota.
DR GeneTree; ENSGT00950000182950; -.
DR HOGENOM; CLU_011751_4_0_1; -.
DR InParanoid; P09798; -.
DR OMA; DPFHNNA; -.
DR BioCyc; YEAST:G3O-31830-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P09798; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P09798; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; 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:0032297; P:negative regulation of DNA-templated DNA replication initiation; IMP:SGD.
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; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 8.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 7.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat; Ubl conjugation pathway.
FT CHAIN 1..840
FT /note="Anaphase-promoting complex subunit CDC16"
FT /id="PRO_0000106269"
FT REPEAT 229..260
FT /note="TPR 1"
FT REPEAT 263..288
FT /note="TPR 2"
FT REPEAT 296..319
FT /note="TPR 3"
FT REPEAT 357..388
FT /note="TPR 4"
FT REPEAT 393..416
FT /note="TPR 5"
FT REPEAT 426..454
FT /note="TPR 6"
FT REPEAT 464..492
FT /note="TPR 7"
FT REPEAT 499..526
FT /note="TPR 8"
FT REPEAT 531..560
FT /note="TPR 9"
FT REPEAT 565..593
FT /note="TPR 10"
FT REPEAT 600..628
FT /note="TPR 11"
FT REPEAT 633..665
FT /note="TPR 12"
FT REPEAT 671..703
FT /note="TPR 13"
FT REPEAT 708..737
FT /note="TPR 14"
FT REGION 67..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..830
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 44
FT /note="S->A: Abolishes phosphorylation; when associated
FT with A-59; A-95; A-103; A-115 and A-406."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 59
FT /note="S->A: Abolishes phosphorylation; when associated
FT with A-44; A-95; A-103; A-115 and A-406."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 95
FT /note="S->A: Abolishes phosphorylation; when associated
FT with A-44; A-59; A-103; A-115 and A-406."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 103
FT /note="S->A: Abolishes phosphorylation; when associated
FT with A-44; A-59; A-95; A-115 and A-406."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 115
FT /note="T->A: Abolishes phosphorylation; when associated
FT with A-44; A-59; A-95; A-103 and A-406."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 406
FT /note="T->A: Abolishes phosphorylation; when associated
FT with A-44; A-59; A-95; A-103 and A-115."
FT /evidence="ECO:0000269|PubMed:10871279"
FT MUTAGEN 482
FT /note="C->Y: In CDC16-264; G2/M cell cycle arrest at 36
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9660930"
FT MUTAGEN 530
FT /note="S->P: In CDC16-183; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:12928868"
FT MUTAGEN 557
FT /note="S->F: In CDC16-1; G2/M cell cycle arrest at 36
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:9660930"
SQ SEQUENCE 840 AA; 94992 MW; A096B34441083488 CRC64;
MKFCLYCCHC YIVICGKATH YYKSSKATSN LKSSNRVLMR NPMSPSEQHS QHNSTLAASP
FVSNVSAART QQSLPTDAQN DRLQQPWNRT NTATSPYQSL ANSPLIQKLQ ANIMTPHQPS
ANSNSNSNSI TGNVVNDNNL LASMSKNSMF GSTIPSTLRK VSLQREYKDS VDGVVRDEDN
DEDVHNNGDA AANANNDRES KLGHNGPLTT TTLTTTTTAT QLDVSELSAI ERLRLWRFDA
LMQHMYRTAE YIADKVYNIS NDPDDAFWLG QVYYNNNQYV RAVELITRNN LDGVNILCRY
LLGLSFVKLQ RFDDALDVIG EYNPFSEDPS TTAANTMSNN GNNSNTSQPV TDGGIKMESS
LCFLRGKIYF AQNNFNKARD AFREAILVDI KNFEAFEMLL SKNLLTPQEE WDLFDSLDFK
EFGEDKEIMK NLYKINLSKY INTEDITKSN EILAKDYKLA DNVDVVRSKV DICYTQCKFN
ECLELCETVL ENDEFNTNIL PAYIGCLYEL SNKNKLFLLS HRLAETFPKS AITWFSVATY
YMSLDRISEA QKYYSKSSIL DPSFAAAWLG FAHTYALEGE QDQALTAYST ASRFFPGMHL
PKLFLGMQFM AMNSLNLAES YFVLAYDICP NDPLVLNEMG VMYFKKNEFV KAKKYLKKAL
EVVKDLDPSS RTTISIQLNL GHTYRKLNEN EIAIKCFRCV LEKNDKNSEI HCSLGYLYLK
TKKLQKAIDH LHKSLYLKPN NSSATALLKN ALELNVTLSL DASHPLIDKS NLMSQASKDK
ASLNKKRSSL TYDPVNMAKR LRTQKEIFDQ NNKALRKGGH DSKTGSNNAD DDFDADMELE
