MAD2_SCHPO
ID MAD2_SCHPO Reviewed; 203 AA.
AC O14417;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Mitotic spindle checkpoint component mad2;
GN Name=mad2 {ECO:0000303|PubMed:9223296};
GN ORFNames=SPBC20F10.06 {ECO:0000312|PomBase:SPBC20F10.06};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=9223296; DOI=10.1073/pnas.94.15.7965;
RA He X., Patterson T.E., Sazer S.;
RT "The Schizosaccharomyces pombe spindle checkpoint protein mad2p blocks
RT anaphase and genetically interacts with the anaphase-promoting complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7965-7970(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND INTERACTION WITH SLP1.
RX PubMed=9461438; DOI=10.1126/science.279.5353.1045;
RA Kim S.H., Lin D.P., Matsumoto S., Kitazono A., Matsumoto T.;
RT "Fission yeast Slp1: an effector of the Mad2-dependent spindle
RT checkpoint.";
RL Science 279:1045-1047(1998).
RN [4]
RP INTERACTION WITH MAD3.
RX PubMed=11909965; DOI=10.1128/mcb.22.8.2728-2742.2002;
RA Millband D.N., Hardwick K.G.;
RT "Fission yeast Mad3p is required for Mad2p to inhibit the anaphase-
RT promoting complex and localizes to kinetochores in a Bub1p-, Bub3p-, and
RT Mph1p-dependent manner.";
RL Mol. Cell. Biol. 22:2728-2742(2002).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=28974540; DOI=10.1083/jcb.201612194;
RA Salas-Pino S., Gallardo P., Barrales R.R., Braun S., Daga R.R.;
RT "The fission yeast nucleoporin Alm1 is required for proteasomal degradation
RT of kinetochore components.";
RL J. Cell Biol. 216:3591-3608(2017).
CC -!- FUNCTION: Feedback control that prevents cells with incompletely
CC assembled spindles from leaving mitosis. It interacts with the anaphase
CC promoting complex/cyclosome (APC/C) thereby inhibiting APC/C-dependent
CC proteolysis, a step required for exit from mitosis.
CC {ECO:0000269|PubMed:9461438}.
CC -!- SUBUNIT: Interacts with mad3 and slp1. {ECO:0000269|PubMed:11909965,
CC ECO:0000269|PubMed:9461438}.
CC -!- INTERACTION:
CC O14417; P87169: mad1; NbExp=4; IntAct=EBI-1269310, EBI-16079828;
CC O14417; O59767: mad3; NbExp=5; IntAct=EBI-1269310, EBI-1269284;
CC O14417; P78972: slp1; NbExp=8; IntAct=EBI-1269310, EBI-1252744;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous disruption of nucleoporin alm1
CC results in a growth defect. {ECO:0000269|PubMed:28974540}.
CC -!- SIMILARITY: Belongs to the MAD2 family. {ECO:0000305}.
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DR EMBL; U72150; AAB68597.1; -; Genomic_RNA.
DR EMBL; CU329671; CAA16846.1; -; Genomic_DNA.
DR PIR; T39877; T39877.
DR RefSeq; NP_596370.1; NM_001022291.2.
DR PDB; 4AEZ; X-ray; 2.30 A; B/E/H=1-203.
DR PDBsum; 4AEZ; -.
DR AlphaFoldDB; O14417; -.
DR SMR; O14417; -.
DR BioGRID; 277115; 117.
DR ComplexPortal; CPX-3924; Mitotic Checkpoint Complex.
DR DIP; DIP-38037N; -.
DR IntAct; O14417; 3.
DR STRING; 4896.SPBC20F10.06.1; -.
DR MaxQB; O14417; -.
DR PaxDb; O14417; -.
DR EnsemblFungi; SPBC20F10.06.1; SPBC20F10.06.1:pep; SPBC20F10.06.
DR GeneID; 2540589; -.
DR KEGG; spo:SPBC20F10.06; -.
DR PomBase; SPBC20F10.06; mad2.
DR VEuPathDB; FungiDB:SPBC20F10.06; -.
DR eggNOG; KOG3285; Eukaryota.
DR HOGENOM; CLU_072097_0_0_1; -.
DR InParanoid; O14417; -.
DR OMA; MLDGNCT; -.
DR PhylomeDB; O14417; -.
DR Reactome; R-SPO-141405; Inhibition of the proteolytic activity of APC/C required for the onset of anaphase by mitotic spindle checkpoint components.
DR Reactome; R-SPO-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR PRO; PR:O14417; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0033597; C:mitotic checkpoint complex; IDA:PomBase.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IPI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1905318; P:meiosis I spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:PomBase.
DR GO; GO:0045841; P:negative regulation of mitotic metaphase/anaphase transition; IPI:PomBase.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IC:ComplexPortal.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR003511; HORMA_dom.
DR InterPro; IPR036570; HORMA_dom_sf.
DR InterPro; IPR027097; Mad2.
DR InterPro; IPR045091; Mad2-like.
DR PANTHER; PTHR11842; PTHR11842; 1.
DR PANTHER; PTHR11842:SF11; PTHR11842:SF11; 1.
DR Pfam; PF02301; HORMA; 1.
DR SUPFAM; SSF56019; SSF56019; 1.
DR PROSITE; PS50815; HORMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..203
FT /note="Mitotic spindle checkpoint component mad2"
FT /id="PRO_0000126114"
FT DOMAIN 13..197
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT HELIX 14..33
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 58..76
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 80..89
FT /evidence="ECO:0007829|PDB:4AEZ"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 95..105
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 118..137
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:4AEZ"
FT STRAND 189..199
FT /evidence="ECO:0007829|PDB:4AEZ"
SQ SEQUENCE 203 AA; 23583 MW; DC9D1D213450C925 CRC64;
MSSVPIRTNF SLKGSSKLVS EFFEYAVNSI LFQRGIYPAE DFKVVRKYGL NMLVSVDEEV
KTYIRKIVSQ LHKWMFAKKI QKLILVITSK CSGEDLERWQ FNVEMVDTAD QFQNIGNKED
ELRVQKEIQA LIRQITATVT FLPQLEEQCT FNVLVYADKD SEVPTDWVDS DPRILRDAEQ
VQLRSFSTSM HKIDCQVAYR VNP
