MD2L2_XENLA
ID MD2L2_XENLA Reviewed; 211 AA.
AC Q8QFR4;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Mitotic spindle assembly checkpoint protein MAD2B;
DE AltName: Full=Mad2l2-A protein;
DE AltName: Full=Mitotic arrest defective protein 2B;
DE AltName: Full=Mitotic arrest deficient 2-like protein 2;
DE Short=MAD2-like protein 2;
DE Short=xMAD2L2;
GN Name=mad2l2; Synonyms=mad2B, mad2l2-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15218244; DOI=10.1159/000078562;
RA van den Hurk W.H., Martens G.J., Geurts van Kessel A., van Groningen J.J.;
RT "Isolation and characterization of the Xenopus laevis orthologs of the
RT human papillary renal cell carcinoma-associated genes PRCC and MAD2L2
RT (MAD2B).";
RL Cytogenet. Genome Res. 106:68-73(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH FZR1, HOMOOLIGOMERIZATION, SUBCELLULAR LOCATION,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=11459825; DOI=10.1101/gad.897901;
RA Pfleger C.M., Salic A., Lee E., Kirschner M.W.;
RT "Inhibition of Cdh1-APC by the MAD2-related protein MAD2L2: a novel
RT mechanism for regulating Cdh1.";
RL Genes Dev. 15:1759-1764(2001).
CC -!- FUNCTION: Adapter protein able to interact with different proteins and
CC involved in different biological processes. Mediates the interaction
CC between the error-prone DNA polymerase zeta catalytic subunit rev3l and
CC the inserter polymerase rev1, thereby mediating the second polymerase
CC switching in translesion DNA synthesis. Translesion DNA synthesis
CC releases the replication blockade of replicative polymerases, stalled
CC in presence of DNA lesions. May also play a role in signal transduction
CC in response to DNA damage. May regulate the activation of the anaphase
CC promoting complex APC thereby regulating progression through the cell
CC cycle. Through transcriptional regulation may play a role in
CC epithelial-mesenchymal transdifferentiation.
CC {ECO:0000269|PubMed:11459825}.
CC -!- FUNCTION: Inhibits the fzr1-APC complex activity during mitosis. Plays
CC a role in progression of mitosis. {ECO:0000269|PubMed:11459825}.
CC -!- SUBUNIT: Homooligomer. Interacts with rev1 (By similarity). Interacts
CC with rev3l (By similarity). Interacts with fzr1 (in complex with the
CC anaphase promoting complex APC). May interact with cdc20 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11459825}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Maternally and zigotically expressed. Uniformely
CC distributed in embryos. {ECO:0000269|PubMed:11459825}.
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DR EMBL; AJ318530; CAC86900.1; -; mRNA.
DR EMBL; BC084331; AAH84331.1; -; mRNA.
DR RefSeq; NP_001081096.1; NM_001087627.1.
DR AlphaFoldDB; Q8QFR4; -.
DR SMR; Q8QFR4; -.
DR BioGRID; 98982; 1.
DR MaxQB; Q8QFR4; -.
DR DNASU; 394380; -.
DR GeneID; 394380; -.
DR KEGG; xla:394380; -.
DR CTD; 394380; -.
DR Xenbase; XB-GENE-6254429; mad2l2.S.
DR OMA; CEDFPWI; -.
DR OrthoDB; 1630737at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 394380; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0016035; C:zeta DNA polymerase complex; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; NAS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0042772; P:DNA damage response, signal transduction resulting in transcription; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0009794; P:regulation of mitotic cell cycle, embryonic; IMP:UniProtKB.
DR GO; GO:0043393; P:regulation of protein binding; IDA:UniProtKB.
DR Gene3D; 3.30.900.10; -; 1.
DR InterPro; IPR003511; HORMA_dom.
DR InterPro; IPR036570; HORMA_dom_sf.
DR InterPro; IPR045091; Mad2-like.
DR PANTHER; PTHR11842; PTHR11842; 1.
DR Pfam; PF02301; HORMA; 1.
DR SUPFAM; SSF56019; SSF56019; 1.
DR PROSITE; PS50815; HORMA; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; DNA damage; Mitosis;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..211
FT /note="Mitotic spindle assembly checkpoint protein MAD2B"
FT /id="PRO_0000405247"
FT DOMAIN 13..203
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
SQ SEQUENCE 211 AA; 24389 MW; 563718BA8350CB06 CRC64;
MTTLTRQDLN FGQVVADILC EFLEVAVHLI LYVREVYPTG IFQKRKKYNV PVQMSCHPEL
NRYIQDTLHC VKPLIEKNDV EKVVVVILDK EHHPVERFVF EIAQPPLLSI SSDSLLSHVE
QLLRAFILKI SVCDAVLDNN PPGCTFTLLV HTREAATRNM EKIQVIKDFP WILADEQDVH
MQEPRLIPLK TMTSDILKMQ LYVEERAQKS T
