APC11_YEAST
ID APC11_YEAST Reviewed; 165 AA.
AC Q12157; D6VRX9;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Anaphase-promoting complex subunit 11;
DE EC=6.3.2.-;
GN Name=APC11; OrderedLocusNames=YDL008W; ORFNames=D2900;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=9469814; DOI=10.1126/science.279.5354.1216;
RA Zachariae W., Shevchenko A., Andrews P.D., Ciosk R., Galova M., Stark M.J.,
RA Mann M., Nasmyth K.;
RT "Mass spectrometric analysis of the anaphase-promoting complex from yeast:
RT identification of a subunit related to cullins.";
RL Science 279:1216-1219(1998).
RN [4]
RP FUNCTION, AND MUTAGENESIS OF SER-10; CYS-41; CYS-44; TRP-81 AND CYS-91.
RX PubMed=10888670; DOI=10.1091/mbc.11.7.2315;
RA Leverson J.D., Joazeiro C.A., Page A.M., Huang H., Hieter P., Hunter T.;
RT "The APC11 RING-H2 finger mediates E2-dependent ubiquitination.";
RL Mol. Biol. Cell 11:2315-2325(2000).
RN [5]
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: Probably catalytic subunit of the anaphase promoting
CC complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein
CC ligase complex that controls progression through mitosis and the G1
CC phase of the cell cycle. The APC/C is thought to confer substrate
CC specificity and, in the presence of ubiquitin-conjugating E2 enzymes,
CC it catalyzes the formation of protein-ubiquitin conjugates that are
CC subsequently degraded by the 26S proteasome. In early mitosis, the
CC APC/C is activated by CDC20 and targets securin PDS1, the B-type cyclin
CC CLB5, 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 APC11 is required to recruit the ubiquitin-conjugating enzyme E2 to the
CC APC/C. {ECO:0000269|PubMed:10888670}.
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:9469814}.
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z74056; CAA98564.1; -; Genomic_DNA.
DR EMBL; Z48432; CAA88351.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11839.1; -; Genomic_DNA.
DR PIR; S52511; S52511.
DR RefSeq; NP_010276.3; NM_001180067.3.
DR AlphaFoldDB; Q12157; -.
DR BioGRID; 32044; 686.
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-1130N; -.
DR IntAct; Q12157; 15.
DR MINT; Q12157; -.
DR STRING; 4932.YDL008W; -.
DR PaxDb; Q12157; -.
DR PRIDE; Q12157; -.
DR EnsemblFungi; YDL008W_mRNA; YDL008W; YDL008W.
DR GeneID; 851554; -.
DR KEGG; sce:YDL008W; -.
DR SGD; S000002166; APC11.
DR VEuPathDB; FungiDB:YDL008W; -.
DR eggNOG; KOG1493; Eukaryota.
DR GeneTree; ENSGT00550000075186; -.
DR HOGENOM; CLU_115512_0_0_1; -.
DR InParanoid; Q12157; -.
DR OMA; FHVHCIY; -.
DR BioCyc; YEAST:G3O-29439-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q12157; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12157; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd16456; RING-H2_APC11; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR024991; RING-H2_APC11.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF12861; zf-ANAPC11; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Ligase; Metal-binding; Mitosis;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..165
FT /note="Anaphase-promoting complex subunit 11"
FT /id="PRO_0000055751"
FT ZN_FING 52..95
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MUTAGEN 10
FT /note="S->R: In APC11-13; G2/M cell cycle arrest at 37
FT degrees Celsius."
FT /evidence="ECO:0000269|PubMed:10888670"
FT MUTAGEN 41
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10888670"
FT MUTAGEN 44
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10888670"
FT MUTAGEN 81
FT /note="W->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10888670"
FT MUTAGEN 91
FT /note="C->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10888670"
SQ SEQUENCE 165 AA; 18865 MW; 99F8E8C6BC841934 CRC64;
MKVKINEVHS VFAWSWHIPS TSDEDAANND PIGNDEDEDV CGICRASYNG TCPSCKFPGD
QCPLVIGLCH HNFHDHCIYR WLDTPTSKGL CPMCRQTFQL QKGLAINDAH VQKFVEIVSR
RREEMIEEGV AEEFVDFDEP IRQNTDNPIG RQQVDTILDE DFLLR
