APC2_YEAST
ID APC2_YEAST Reviewed; 853 AA.
AC Q12440; D6VYC2; Q2VQX4; Q7LGV7;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Anaphase-promoting complex subunit 2;
GN Name=APC2; Synonyms=RSI1; OrderedLocusNames=YLR127C; ORFNames=L3105, L3108;
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 90840 / EAY235 / FY23;
RX PubMed=9090053;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<241::aid-yea61>3.0.co;2-#;
RA Verhasselt P., Volckaert G.;
RT "Sequence analysis of a 37.6 kbp cosmid clone from the right arm of
RT Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-
RT Arg3 and 23 new open reading frames, among which several homologies to
RT proteins involved in cell division control and to mammalian growth factors
RT and other animal proteins are found.";
RL Yeast 13:241-250(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-78.
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=15905473; DOI=10.1093/nar/gki583;
RA Zhang Z., Dietrich F.S.;
RT "Mapping of transcription start sites in Saccharomyces cerevisiae using 5'
RT SAGE.";
RL Nucleic Acids Res. 33:2838-2851(2005).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, 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 [6]
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 [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 773-846.
RX PubMed=11961546; DOI=10.1038/416703a;
RA Zheng N., Schulman B.A., Song L., Miller J.J., Jeffrey P.D., Wang P.,
RA Chu C., Koepp D.M., Elledge S.J., Pagano M., Conaway R.C., Conaway J.W.,
RA Harper J.W., Pavletich N.P.;
RT "Structure of the Cul1-Rbx1-Skp1-F box Skp2 SCF ubiquitin ligase complex.";
RL Nature 416:703-709(2002).
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:9469814}.
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. APC2
CC interacts directly with APC11 thereby anchoring APC11 to the core
CC complex. {ECO:0000269|PubMed:9469814}.
CC -!- INTERACTION:
CC Q12440; P40577: MND2; NbExp=3; IntAct=EBI-33503, EBI-25433;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 432 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
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DR EMBL; X89514; CAA61705.1; -; Genomic_DNA.
DR EMBL; Z73299; CAA97696.1; -; Genomic_DNA.
DR EMBL; U53877; AAB82373.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62638.1; -; Genomic_DNA.
DR EMBL; Z73300; CAA97698.1; -; Genomic_DNA.
DR EMBL; AY899244; AAX83929.1; -; mRNA.
DR EMBL; BK006945; DAA09438.1; -; Genomic_DNA.
DR PIR; S59315; S59315.
DR RefSeq; NP_013228.1; NM_001182014.1.
DR PDB; 1LDD; X-ray; 2.00 A; A/B/C/D=773-846.
DR PDBsum; 1LDD; -.
DR AlphaFoldDB; Q12440; -.
DR SMR; Q12440; -.
DR BioGRID; 31396; 140.
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-939N; -.
DR IntAct; Q12440; 16.
DR MINT; Q12440; -.
DR STRING; 4932.YLR127C; -.
DR iPTMnet; Q12440; -.
DR MaxQB; Q12440; -.
DR PaxDb; Q12440; -.
DR PRIDE; Q12440; -.
DR EnsemblFungi; YLR127C_mRNA; YLR127C; YLR127C.
DR GeneID; 850818; -.
DR KEGG; sce:YLR127C; -.
DR SGD; S000004117; APC2.
DR VEuPathDB; FungiDB:YLR127C; -.
DR eggNOG; KOG2165; Eukaryota.
DR GeneTree; ENSGT00390000016127; -.
DR HOGENOM; CLU_357897_0_0_1; -.
DR InParanoid; Q12440; -.
DR OMA; QFIKIRI; -.
DR BioCyc; YEAST:G3O-32269-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q12440; -.
DR PRO; PR:Q12440; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12440; protein.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; IGI:SGD.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:0120151; P:positive regulation of mitotic actomyosin contractile ring disassembly; IMP:SGD.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; 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 Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR044554; APC2-like.
DR InterPro; IPR014786; APC2_C.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR45957; PTHR45957; 1.
DR Pfam; PF08672; ANAPC2; 1.
DR Pfam; PF00888; Cullin; 1.
DR SMART; SM01013; APC2; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..853
FT /note="Anaphase-promoting complex subunit 2"
FT /id="PRO_0000119814"
FT HELIX 775..792
FT /evidence="ECO:0007829|PDB:1LDD"
FT STRAND 794..796
FT /evidence="ECO:0007829|PDB:1LDD"
FT HELIX 797..807
FT /evidence="ECO:0007829|PDB:1LDD"
FT HELIX 810..812
FT /evidence="ECO:0007829|PDB:1LDD"
FT HELIX 819..831
FT /evidence="ECO:0007829|PDB:1LDD"
FT STRAND 834..836
FT /evidence="ECO:0007829|PDB:1LDD"
FT TURN 839..841
FT /evidence="ECO:0007829|PDB:1LDD"
FT STRAND 842..845
FT /evidence="ECO:0007829|PDB:1LDD"
SQ SEQUENCE 853 AA; 99978 MW; E559A0E28C784DE2 CRC64;
MSFQITPTRD LKVITDELQT LSSYIFHTNI VDDLNSLLTW MSPNDAKSNH QLRPPSLRIK
NIIKVLFPNN ATTSPYSMIN TSQANNSIVN EGNTNKELQL QLFSTLKEFY IFQVRYHFFL
HFNNINYLKD IQRWENYYEF PLRYVPIFDV NVNDWALELN SLRHYLLNRN IKFKNNLRTR
LDKLIMDDDF DLADNLIQWL KSANGSLSST ELIVNALYSK INKFCEDNMS RVWNKRFMIM
ETFNKFINQY WSQFSKLVGC PEDDHELTTT VFNCFESNFL RIRTNEIFDI CVLAYPDSKV
TLLELRKIMK DFKDYTNIVT TFLSDFKKYI LNPSVTTVDA LLRYVKTIKA FLVLDPTGRC
LHSITTFVKP YFQERKHLVN VLLYAMLDLP EEELKEKINF NVDMKALLSL VDTLHDSDIN
QDTNITKRDK NKKSPFLWNL KVKGKRELNK DLPIRHAMLY EHILNYYIAW VPEPNDMIPG
NIKSSYIKTN LFEVLLDLFE SREFFISEFR NLLTDRLFTL KFYTLDEKWT RCLKLIREKI
VKFTETSHSN YITNGILGLL ETTAPAADAD QSNLNSIDVM LWDIKCSEEL CRKMHEVAGL
DPIIFPKFIS LLYWKYNCDT QGSNDLAFHL PIDLERELQK YSDIYSQLKP GRKLQLCKDK
GKVEIQLAFK DGRKLVLDVS LEQCSVINQF DSPNDEPICL SLEQLSESLN IAPPRLTHLL
DFWIQKGVLL KENGTYSVIE HSEMDFDQAQ KTAPMEIENS NYELHNDSEI ERKYELTLQR
SLPFIEGMLT NLGAMKLHKI HSFLKITVPK DWGYNRITLQ QLEGYLNTLA DEGRLKYIAN
GSYEIVKNGH KNS
