MND2_YEAST
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 03-AUG-2022, entry version 152.
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;
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=3; IntAct=EBI-25433, EBI-29017;
CC P40577; Q12440: APC2; NbExp=3; IntAct=EBI-25433, EBI-33503;
CC P40577; Q04601: APC4; NbExp=5; IntAct=EBI-25433, EBI-32842;
CC P40577; Q08683: APC5; NbExp=4; IntAct=EBI-25433, EBI-35371;
CC P40577; P16522: CDC23; NbExp=3; IntAct=EBI-25433, EBI-4216;
CC -!- SIMILARITY: Belongs to the APC15 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; 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 IntAct; P40577; 15.
DR MINT; P40577; -.
DR STRING; 4932.YIR025W; -.
DR iPTMnet; P40577; -.
DR MaxQB; P40577; -.
DR PaxDb; P40577; -.
DR PRIDE; P40577; -.
DR EnsemblFungi; YIR025W_mRNA; YIR025W; YIR025W.
DR GeneID; 854843; -.
DR KEGG; sce:YIR025W; -.
DR SGD; S000001464; MND2.
DR VEuPathDB; FungiDB:YIR025W; -.
DR HOGENOM; CLU_759012_0_0_1; -.
DR InParanoid; P40577; -.
DR OMA; HERYNMR; -.
DR BioCyc; YEAST:G3O-31444-MON; -.
DR UniPathway; UPA00143; -.
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:0051301; P:cell division; IEA:UniProtKB-KW.
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:1904667; P:negative regulation of ubiquitin protein ligase activity; IDA: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; IC:ComplexPortal.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IMP:SGD.
DR InterPro; IPR008402; APC_su15/mnd2.
DR InterPro; IPR016807; Mnd2.
DR Pfam; PF05841; Apc15p; 1.
DR PIRSF; PIRSF022699; MND2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Mitosis; Phosphoprotein; Reference proteome;
KW 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 142..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..323
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"
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
