MAD2_CANAL
ID MAD2_CANAL Reviewed; 214 AA.
AC Q59VQ3; A0A1D8PD73; Q59VU9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Spindle assembly checkpoint component MAD2 {ECO:0000303|PubMed:12100546};
GN Name=MAD2 {ECO:0000303|PubMed:12100546};
GN OrderedLocusNames=CAALFM_C104080WA; ORFNames=CaO19.1040, CaO19.8642;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=12100546; DOI=10.1046/j.1365-2958.2002.02995.x;
RA Bai C., Ramanan N., Wang Y.M., Wang Y.;
RT "Spindle assembly checkpoint component CaMad2p is indispensable for Candida
RT albicans survival and virulence in mice.";
RL Mol. Microbiol. 45:31-44(2002).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=21571923; DOI=10.1128/ec.05093-11;
RA Thakur J., Sanyal K.;
RT "The essentiality of the fungus-specific Dam1 complex is correlated with a
RT one-kinetochore-one-microtubule interaction present throughout the cell
RT cycle, independent of the nature of a centromere.";
RL Eukaryot. Cell 10:1295-1305(2011).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=22542681; DOI=10.1016/j.fgb.2012.04.004;
RA Hu K., Li W., Wang H., Chen K., Wang Y., Sang J.;
RT "Shp1, a regulator of protein phosphatase 1 Glc7, has important roles in
RT cell morphogenesis, cell cycle progression and DNA damage response in
RT Candida albicans.";
RL Fungal Genet. Biol. 49:433-442(2012).
CC -!- FUNCTION: Central component of the spindle assembly checkpoint which is
CC a feedback control that prevents cells with incompletely assembled
CC spindles from leaving mitosis. Plays a key role in virulence, probably
CC through cell cycle checkpoint functions, especially those monitoring
CC the integrity of DNA and chromosome segregation, which might be
CC required for the pathogen to repair damage caused by host defense.
CC {ECO:0000269|PubMed:12100546}.
CC -!- SUBUNIT: Component of the mitotic checkpoint complex (MCC).
CC {ECO:0000250|UniProtKB:P40958}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P40958}.
CC -!- DISRUPTION PHENOTYPE: Quickly loses viability when treated with
CC nocodazole, which causes disassembly of mitotic spindles. Exhibits
CC increased frequency of chromosome loss and greatly reduced virulence in
CC mice. {ECO:0000269|PubMed:12100546, ECO:0000269|PubMed:21571923,
CC ECO:0000269|PubMed:22542681}.
CC -!- SIMILARITY: Belongs to the MAD2 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26083.1; -; Genomic_DNA.
DR RefSeq; XP_713645.1; XM_708552.1.
DR AlphaFoldDB; Q59VQ3; -.
DR SMR; Q59VQ3; -.
DR STRING; 237561.Q59VQ3; -.
DR GeneID; 3644696; -.
DR KEGG; cal:CAALFM_C104080WA; -.
DR CGD; CAL0000196404; MAD2.
DR VEuPathDB; FungiDB:C1_04080W_A; -.
DR eggNOG; KOG3285; Eukaryota.
DR HOGENOM; CLU_072097_0_0_1; -.
DR InParanoid; Q59VQ3; -.
DR OMA; MLDGNCT; -.
DR OrthoDB; 1197019at2759; -.
DR PHI-base; PHI:262; -.
DR PRO; PR:Q59VQ3; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:CGD.
DR GO; GO:1990333; C:mitotic checkpoint complex, CDC20-MAD2 subcomplex; IEA:EnsemblFungi.
DR GO; GO:0034399; C:nuclear periphery; IDA:CGD.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:EnsemblFungi.
DR GO; GO:0051701; P:biological process involved in interaction with host; IMP:CGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:CGD.
DR GO; GO:0044774; P:mitotic DNA integrity checkpoint signaling; IEA:EnsemblFungi.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:CGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:CGD.
DR GO; GO:1902499; P:positive regulation of protein autoubiquitination; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Cell cycle; Cell division; Mitosis; Nucleus; Reference proteome; Virulence.
FT CHAIN 1..214
FT /note="Spindle assembly checkpoint component MAD2"
FT /id="PRO_0000430604"
FT DOMAIN 14..209
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
SQ SEQUENCE 214 AA; 24540 MW; FC32BA4385BEDDB1 CRC64;
MPSSLEPSSK LALKGSSKIV CDYFEFALNS ILYQRGIYPQ EDFVTVKKYD LPMVINDDYD
VQKYINNIMK QIKKWIYGSL MSKFIIVIVS KTNLENIERW EFNIETKDQE ETTENGDGDG
DGVGKSRQEI QKEIRTIIRQ ITSSVSYLPV LKDDDEYTFN VLVYTDPNTS VPIEWCDTQG
DGKVLDGDNV DNVKFTSFST DIHQVGTSVS YKYE
