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   27-MAR-2024, entry version 186.
DE   RecName: Full=Anaphase-promoting complex subunit 2;
GN   Name=APC2; Synonyms=RSI1; OrderedLocusNames=YLR127C;
GN   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   PDB; 8A3T; EM; 3.50 A; T=1-853.
DR   PDB; 8A5Y; EM; 4.90 A; T=1-853.
DR   PDB; 8A61; EM; 5.40 A; T=1-853.
DR   PDBsum; 1LDD; -.
DR   PDBsum; 8A3T; -.
DR   PDBsum; 8A5Y; -.
DR   PDBsum; 8A61; -.
DR   AlphaFoldDB; Q12440; -.
DR   EMDB; EMD-15199; -.
DR   SMR; Q12440; -.
DR   BioGRID; 31396; 146.
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; 4932-YLR127C; -.
DR   PeptideAtlas; Q12440; -.
DR   EnsemblFungi; YLR127C_mRNA; YLR127C; YLR127C.
DR   GeneID; 850818; -.
DR   KEGG; sce:YLR127C; -.
DR   AGR; SGD:S000004117; -.
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   OrthoDB; 2786196at2759; -.
DR   BioCyc; YEAST:G3O-32269-MONOMER; -.
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; NAS:ComplexPortal.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; NAS:ComplexPortal.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR   PANTHER; PTHR45957:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT 2; 1.
DR   Pfam; PF08672; ANAPC2; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   SMART; SM01013; APC2; 1.
DR   SUPFAM; SSF75632; Cullin homology domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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           11..26
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           31..41
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            46..48
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           57..66
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           93..120
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           122..124
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           128..144
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           154..169
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           171..186
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           190..203
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           209..228
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           238..258
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           265..292
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            295..298
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           299..308
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           312..329
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           337..354
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           359..374
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           378..387
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           391..397
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           404..415
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           455..468
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           491..496
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           503..519
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           527..543
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           568..575
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           577..598
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          607..610
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           611..613
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           632..648
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          652..668
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          674..680
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           681..688
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           702..709
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           713..725
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          728..732
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          735..738
FT                   /evidence="ECO:0007829|PDB:8A3T"
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
//