BUB3_CAEEL
ID BUB3_CAEEL Reviewed; 343 AA.
AC Q9XWH0;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Mitotic checkpoint protein bub-3 {ECO:0000250|UniProtKB:O43684};
DE AltName: Full=Budding uninhibited by benzimidazole 3 {ECO:0000250|UniProtKB:Q21776};
GN Name=bub-3 {ECO:0000312|WormBase:Y54G9A.6};
GN ORFNames=Y54G9A.6 {ECO:0000312|WormBase:Y54G9A.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18248670; DOI=10.1186/1747-1028-3-6;
RA Hajeri V.A., Stewart A.M., Moore L.L., Padilla P.A.;
RT "Genetic analysis of the spindle checkpoint genes san-1, mdf-2, bub-3 and
RT the CENP-F homologues hcp-1 and hcp-2 in Caenorhabditis elegans.";
RL Cell Div. 3:6-6(2008).
RN [3] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19109417; DOI=10.1091/mbc.e08-10-1047;
RA Essex A., Dammermann A., Lewellyn L., Oegema K., Desai A.;
RT "Systematic analysis in Caenorhabditis elegans reveals that the spindle
RT checkpoint is composed of two largely independent branches.";
RL Mol. Biol. Cell 20:1252-1267(2009).
RN [4] {ECO:0000305}
RP INTERACTION WITH BUB-1.
RX PubMed=24567362; DOI=10.1083/jcb.201311015;
RA Moyle M.W., Kim T., Hattersley N., Espeut J., Cheerambathur D.K.,
RA Oegema K., Desai A.;
RT "A Bub1-Mad1 interaction targets the Mad1-Mad2 complex to unattached
RT kinetochores to initiate the spindle checkpoint.";
RL J. Cell Biol. 204:647-657(2014).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH BUB-1, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25987605; DOI=10.1083/jcb.201412035;
RA Kim T., Moyle M.W., Lara-Gonzalez P., De Groot C., Oegema K., Desai A.;
RT "Kinetochore-localized BUB-1/BUB-3 complex promotes anaphase onset in C.
RT elegans.";
RL J. Cell Biol. 209:507-517(2015).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26483555; DOI=10.1083/jcb.201409035;
RA Bohr T., Nelson C.R., Klee E., Bhalla N.;
RT "Spindle assembly checkpoint proteins regulate and monitor meiotic synapsis
RT in C. elegans.";
RL J. Cell Biol. 211:233-242(2015).
CC -!- FUNCTION: Has a dual function in spindle-assembly checkpoint signaling
CC and in promoting the establishment of correct kinetochore-microtubule
CC (K-MT) attachments (PubMed:18248670, PubMed:19109417, PubMed:25987605).
CC Promotes the formation of stable end-on bipolar attachments of
CC chromosomes (PubMed:25987605). Necessary for expression and kinetochore
CC localization of bub-1 (PubMed:19109417, PubMed:25987605). Plays a role
CC in synapsis checkpoint signaling inducing apoptosis in response to
CC unsynapsed chromosomes and thus controlling chromosomal segregation
CC during oocyte meiosis (PubMed:26483555). {ECO:0000269|PubMed:18248670,
CC ECO:0000269|PubMed:19109417, ECO:0000269|PubMed:25987605,
CC ECO:0000269|PubMed:26483555}.
CC -!- SUBUNIT: May interact with bub-1; for localization at the kinetochore
CC and the onset of anaphase. {ECO:0000269|PubMed:24567362,
CC ECO:0000269|PubMed:25987605}.
CC -!- INTERACTION:
CC Q9XWH0; O02053: san-1; NbExp=5; IntAct=EBI-331258, EBI-316339;
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:19109417, ECO:0000269|PubMed:25987605}. Nucleus
CC {ECO:0000305}. Note=Localizes at kinetochores on condensing chromosomes
CC in late prophase and during metaphase (PubMed:19109417). Localization
CC to the kinetochore is dependent on bub-1 (PubMed:25987605).
CC {ECO:0000269|PubMed:19109417, ECO:0000269|PubMed:25987605}.
CC -!- DISRUPTION PHENOTYPE: Viable, but with a reduced brood size
CC (PubMed:25987605). Reduced bub-1 expression and localization at the
CC kinetochore which may lead to the delay in the onset of anaphase during
CC embryogenesis (PubMed:25987605). Defective synapsis with increased
CC numbers of nuclei that contain asymmetrically aligned (clustered)
CC chromosomes (PubMed:26483555). RNAi-mediated knockdown results in
CC reduced survival as compared to wild-type animals in anoxic conditions
CC (PubMed:18248670). {ECO:0000269|PubMed:18248670,
CC ECO:0000269|PubMed:25987605, ECO:0000269|PubMed:26483555}.
CC -!- SIMILARITY: Belongs to the WD repeat BUB3 family. {ECO:0000305}.
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DR EMBL; BX284602; CAA21698.1; -; Genomic_DNA.
DR PIR; T27185; T27185.
DR RefSeq; NP_496879.1; NM_064478.4.
DR AlphaFoldDB; Q9XWH0; -.
DR SMR; Q9XWH0; -.
DR ComplexPortal; CPX-400; Bub-1-Bub-3 complex.
DR ComplexPortal; CPX-401; Mitotic checkpoint complex, Mad-1-Mad-2-Bub-1-Bub-3 subcomplex.
DR DIP; DIP-26143N; -.
DR IntAct; Q9XWH0; 7.
DR STRING; 6239.Y54G9A.6; -.
DR EPD; Q9XWH0; -.
DR PaxDb; Q9XWH0; -.
DR PeptideAtlas; Q9XWH0; -.
DR EnsemblMetazoa; Y54G9A.6.1; Y54G9A.6.1; WBGene00013209.
DR GeneID; 175018; -.
DR KEGG; cel:CELE_Y54G9A.6; -.
DR UCSC; Y54G9A.6; c. elegans.
DR CTD; 175018; -.
DR WormBase; Y54G9A.6; CE19233; WBGene00013209; bub-3.
DR eggNOG; KOG1036; Eukaryota.
DR GeneTree; ENSGT00950000183091; -.
DR HOGENOM; CLU_038526_0_0_1; -.
DR InParanoid; Q9XWH0; -.
DR OMA; WDPFNRK; -.
DR OrthoDB; 1048963at2759; -.
DR PhylomeDB; Q9XWH0; -.
DR Reactome; R-CEL-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR PRO; PR:Q9XWH0; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00013209; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:1990298; C:bub1-bub3 complex; IPI:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IBA:GO_Central.
DR GO; GO:0033597; C:mitotic checkpoint complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:1990299; P:Bub1-Bub3 complex localization to kinetochore; IDA:ComplexPortal.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IGI:WormBase.
DR GO; GO:0033316; P:meiotic spindle assembly checkpoint signaling; IGI:WormBase.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Kinetochore; Meiosis;
KW Mitosis; Nucleus; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..343
FT /note="Mitotic checkpoint protein bub-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436607"
FT REPEAT 21..62
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 67..105
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 107..146
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 150..187
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 192..232
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 249..288
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 291..331
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 322..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 38127 MW; 021AD0398C6BD5ED CRC64;
MSTYQAATIV AAPNEFRVPF PPFVQISKVQ FQREAGSRLL AASGWDGTCR VYEVGKLGDI
SEKLVFTHGK PLLTCTFAGY NKVAFGGVDH NVKLADIETG NGTQLGSHAL AVRCMEFNPM
SSLIVSGGWD SSVKLWDARS YGNGAIESVN VSSSVYAMDV LKHTILVGTK DRKIFMYDSR
KLREPLQVRD SPLKYQTRAV QFFPTGEAFV VSSIEGRVAV EYVDQSGEEM MKRKYAFKCH
REKDTDGTEL IHPVHTVAFH PKYGTFATGG ADGIVNIWDP FNRKRIIQLH KFETSISSLS
FNEDGSQLAI ATSYQYEKEI DPSPLPNNSI TIRHITDPES RPK