MAD3_SCHPO
ID MAD3_SCHPO Reviewed; 310 AA.
AC O59767;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Mitotic spindle checkpoint component mad3;
GN Name=mad3; ORFNames=SPCC1795.01c, SPCC895.02;
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 [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 [2]
RP FUNCTION, INTERACTION WITH BUB3; MAD2 AND SLP1, AND SUBCELLULAR LOCATION.
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 [3]
RP INTERACTION WITH ARK1 AND CUT17.
RX PubMed=12676091; DOI=10.1016/s0960-9822(03)00205-7;
RA Petersen J., Hagan I.M.;
RT "S. pombe aurora kinase/survivin is required for chromosome condensation
RT and the spindle checkpoint attachment response.";
RL Curr. Biol. 13:590-597(2003).
CC -!- FUNCTION: Has a role in transducing the anaphase inhibitory signal to
CC the anaphase promoting complex (APC). Forms part of the mad2 feedback
CC control. {ECO:0000269|PubMed:11909965}.
CC -!- SUBUNIT: Interacts with ark1, cut17, mad2 and slp1 to form part of the
CC mad2 complex involved in checkpoint activation. Interacts also with
CC bub3. {ECO:0000269|PubMed:11909965, ECO:0000269|PubMed:12676091}.
CC -!- INTERACTION:
CC O59767; O14417: mad2; NbExp=5; IntAct=EBI-1269284, EBI-1269310;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11909965}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:11909965}.
CC Note=Associated with the kinetochore.
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DR EMBL; CU329672; CAA18636.1; -; Genomic_DNA.
DR PIR; T41640; T41640.
DR RefSeq; NP_588043.2; NM_001023035.2.
DR PDB; 4AEZ; X-ray; 2.30 A; C/F/I=1-223.
DR PDBsum; 4AEZ; -.
DR AlphaFoldDB; O59767; -.
DR SMR; O59767; -.
DR BioGRID; 275789; 53.
DR ComplexPortal; CPX-3924; Mitotic Checkpoint Complex.
DR DIP; DIP-39397N; -.
DR IntAct; O59767; 5.
DR STRING; 4896.SPCC1795.01c.1; -.
DR iPTMnet; O59767; -.
DR MaxQB; O59767; -.
DR PaxDb; O59767; -.
DR PRIDE; O59767; -.
DR EnsemblFungi; SPCC1795.01c.1; SPCC1795.01c.1:pep; SPCC1795.01c.
DR GeneID; 2539219; -.
DR KEGG; spo:SPCC1795.01c; -.
DR PomBase; SPCC1795.01c; mad3.
DR VEuPathDB; FungiDB:SPCC1795.01c; -.
DR eggNOG; KOG1166; Eukaryota.
DR HOGENOM; CLU_043742_0_0_1; -.
DR InParanoid; O59767; -.
DR OMA; LRIWMQY; -.
DR PhylomeDB; O59767; -.
DR PRO; PR:O59767; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0033597; C:mitotic checkpoint complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IPI:PomBase.
DR GO; GO:1990948; F:ubiquitin ligase inhibitor activity; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 InterPro; IPR015661; Bub1/Mad3.
DR InterPro; IPR013212; Mad3/Bub1_I.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR14030; PTHR14030; 1.
DR Pfam; PF08311; Mad3_BUB1_I; 1.
DR SMART; SM00777; Mad3_BUB1_I; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS51489; BUB1_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Kinetochore; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..310
FT /note="Mitotic spindle checkpoint component mad3"
FT /id="PRO_0000084548"
FT DOMAIN 56..218
FT /note="BUB1 N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00822"
FT REGION 20..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 13..18
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 32..39
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 45..64
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 72..85
FT /evidence="ECO:0007829|PDB:4AEZ"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:4AEZ"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 150..162
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 166..179
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 184..201
FT /evidence="ECO:0007829|PDB:4AEZ"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:4AEZ"
SQ SEQUENCE 310 AA; 36086 MW; EEC3EA6D3790C4BF CRC64;
MEPLDAGKNW VHMDVIEQSK ENIEPRKAGH SASALAKSSS RNHTEKEVAG LQKERMGHER
KIETSESLDD PLQVWIDYIK WTLDNFPQGE TKTSGLVTLL ERCTREFVRN PLYKDDVRYL
RIWMQYVNYI DEPVELFSFL AHHHIGQESS IFYEEYANYF ESRGLFQKAD EVYQKGKRMK
AKPFLRFQQK YQQFTHRWLE FAPQSFSSNT NSVNPLQTTF ESTNIQEISQ SRTKISKPKF
KFSVYSDADG SGKDGQPGTW QTLGTVDQRR KENNISATSW VGEKLPLKSP RKLDPLGKFQ
VHCDEEVSKE
