ID   MND2_YEAST              Reviewed;         368 AA.
AC   P40577; D6VVV6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 165.
DE   RecName: Full=Anaphase-promoting complex subunit MND2;
DE   AltName: Full=Meiotic nuclear division protein 2;
GN   Name=MND2; OrderedLocusNames=YIR025W;
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=9169870; DOI=10.1038/387s084;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(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   SUBUNIT.
RX   PubMed=12477395; DOI=10.1016/s0960-9822(02)01331-3;
RA   Yoon H.-J., Feoktistova A., Wolfe B.A., Jennings J.L., Link A.J.,
RA   Gould K.L.;
RT   "Proteomics analysis identifies new components of the fission and budding
RT   yeast anaphase-promoting complexes.";
RL   Curr. Biol. 12:2048-2054(2002).
RN   [4]
RP   SUBUNIT, AND INTERACTION WITH APC1; APC5 AND CDC23.
RX   PubMed=12609981; DOI=10.1074/jbc.m213109200;
RA   Hall M.C., Torres M.P., Schroeder G.K., Borchers C.H.;
RT   "Mnd2 and Swm1 are core subunits of the Saccharomyces cerevisiae anaphase-
RT   promoting complex.";
RL   J. Biol. Chem. 278:16698-16705(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND IDENTIFICATION BY
RP   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   -!- 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. MND2
CC       interacts directly with APC1, APC5 and CDC23.
CC       {ECO:0000269|PubMed:12477395, ECO:0000269|PubMed:12609981}.
CC   -!- INTERACTION:
CC       P40577; P53886: APC1; NbExp=4; IntAct=EBI-25433, EBI-29017;
CC       P40577; Q12440: APC2; NbExp=4; IntAct=EBI-25433, EBI-33503;
CC       P40577; Q04601: APC4; NbExp=6; IntAct=EBI-25433, EBI-32842;
CC       P40577; Q08683: APC5; NbExp=5; IntAct=EBI-25433, EBI-35371;
CC       P40577; P16522: CDC23; NbExp=4; IntAct=EBI-25433, EBI-4216;
CC       P40577; Q12379: SWM1; NbExp=5; IntAct=EBI-25433, EBI-33330;
CC   -!- SIMILARITY: Belongs to the APC15 family. {ECO:0000305}.
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DR   EMBL; Z38061; CAA86185.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08572.1; -; Genomic_DNA.
DR   PIR; S48487; S48487.
DR   RefSeq; NP_012291.1; NM_001179547.1.
DR   PDB; 8A3T; EM; 3.50 A; N=1-368.
DR   PDB; 8A5Y; EM; 4.90 A; N=1-368.
DR   PDB; 8A61; EM; 5.40 A; N=1-368.
DR   AlphaFoldDB; P40577; -.
DR   EMDB; EMD-15123; -.
DR   EMDB; EMD-15199; -.
DR   EMDB; EMD-15201; -.
DR   SMR; P40577; -.
DR   BioGRID; 35016; 68.
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-1536N; -.
DR   FunCoup; P40577; 170.
DR   IntAct; P40577; 15.
DR   MINT; P40577; -.
DR   STRING; 4932.YIR025W; -.
DR   iPTMnet; P40577; -.
DR   PaxDb; 4932-YIR025W; -.
DR   PeptideAtlas; P40577; -.
DR   EnsemblFungi; YIR025W_mRNA; YIR025W; YIR025W.
DR   GeneID; 854843; -.
DR   KEGG; sce:YIR025W; -.
DR   AGR; SGD:S000001464; -.
DR   SGD; S000001464; MND2.
DR   VEuPathDB; FungiDB:YIR025W; -.
DR   HOGENOM; CLU_759012_0_0_1; -.
DR   InParanoid; P40577; -.
DR   OMA; HERYNMR; -.
DR   OrthoDB; 4047136at2759; -.
DR   BioCyc; YEAST:G3O-31444-MONOMER; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 854843; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40577; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P40577; protein.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:SGD.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:ComplexPortal.
DR   GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:SGD.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR   GO; GO:1905785; P:negative regulation of anaphase-promoting complex-dependent catabolic process; IGI:SGD.
DR   GO; GO:1902499; P:positive regulation of protein autoubiquitination; IDA:SGD.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:ComplexPortal.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:SGD.
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   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:SGD.
DR   InterPro; IPR008402; APC_su15/mnd2_N.
DR   InterPro; IPR016807; Mnd2.
DR   Pfam; PF05841; Apc15p; 1.
DR   PIRSF; PIRSF022699; MND2; 1.
DR   PDBsum; 8A3T; -.
DR   PDBsum; 8A5Y; -.
DR   PDBsum; 8A61; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Mitosis; Phosphoprotein;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..368
FT                   /note="Anaphase-promoting complex subunit MND2"
FT                   /id="PRO_0000096523"
FT   REGION          140..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         293
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   TURN            4..6
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           9..19
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   TURN            70..72
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           86..88
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           96..112
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           113..115
FT                   /evidence="ECO:0007829|PDB:8A3T"
FT   HELIX           129..139
FT                   /evidence="ECO:0007829|PDB:8A3T"
SQ   SEQUENCE   368 AA;  42826 MW;  D41276561E6ED509 CRC64;
     MARALRDISL FNDIRKDQNS AGAKHERYNM RDLRSKKNQH VNGIDDYEDD SLDRFIRRKK
     SRVVKYIPSL SAYNVFNEFP YYPTSASQLL DGKLDEFLML SEQYKSRLPK IRKLGWNRFK
     PIGINKTMYE LEMLRSRARA QNAEGNNEED FRQHDSREED PRNNGSIGRV ILPHILQENE
     EYDTGEGVTG LHSMPNDSMA ILANNSANNS QNEEVSEEDE ISYDYDAEFD HVVDEDDNEE
     GEVPGEGVEG IEVQRERIVP DDLLMRPTSL SRSLQQFVEE AHHLDRNPYD IDSDNDGEDS
     KVELDMNPDF EDDVGREHDY NSEYSQEPTS YGGITPDLAS NWRNWTRERI TSLDELMERR
     ARQQRGQD
//