MD2L2_RAT
ID MD2L2_RAT Reviewed; 211 AA.
AC D3Z8D9; Q5PPH8;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Mitotic spindle assembly checkpoint protein MAD2B;
DE AltName: Full=Mitotic arrest deficient 2-like protein 2;
DE Short=MAD2-like protein 2;
GN Name=Mad2l2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. Component of the shieldin complex, which
CC plays an important role in repair of DNA double-stranded breaks (DSBs).
CC During G1 and S phase of the cell cycle, the complex functions
CC downstream of TP53BP1 to promote non-homologous end joining (NHEJ) and
CC suppress DNA end resection. Mediates various NHEJ-dependent processes
CC including immunoglobulin class-switch recombination, and fusion of
CC unprotected telomeres. May also regulate another aspect of cellular
CC response to DNA damage through regulation of the JNK-mediated
CC phosphorylation and activation of the transcriptional activator ELK1.
CC Inhibits the FZR1- and probably CDC20-mediated activation of the
CC anaphase promoting complex APC thereby regulating progression through
CC the cell cycle. Regulates TCF7L2-mediated gene transcription and may
CC play a role in epithelial-mesenchymal transdifferentiation.
CC {ECO:0000250|UniProtKB:Q9UI95}.
CC -!- SUBUNIT: Homooligomer. Heterodimer with REV3L. This dimer forms the
CC minimal DNA polymerase zeta complex (Pol-zeta2), with REV3L bearing DNA
CC polymerase catalytic activity, although its activity is very low in
CC this context. Component of the tetrameric Pol-zeta complex (Pol-zeta4),
CC which consists of REV3L, MAD2L2, POLD2 and POLD3; Pol-zeta4 is the
CC fully active form of DNA polymerase zeta. Component of the shieldin
CC complex, consisting of SHLD1, SHLD2, SHLD3 and MAD2L2/REV7. Within the
CC complex, SHLD2 forms a scaffold which interacts with a SHLD3-MAD2L2
CC subcomplex via its N-terminus, and with SHLD1 via its C-terminus.
CC Interacts with REV1. Interacts with ADAM9. Interacts with CHAMP1.
CC Interacts with FZR1 (in complex with the anaphase promoting complex
CC APC). May interact with CDC20. Interacts with RAN. Interacts with ELK1;
CC the interaction is direct and recruits MAD2L2 to ELK1-specific
CC promoters. May interact with the JNK kinases MAPK8 and/or MAPK9 to
CC stimulate ELK1 phosphorylation and transcriptional activity upon DNA
CC damage. Interacts with TCF7L2; prevents its binding to promoters and
CC negatively modulates its transcriptional activity. Interacts with
CC YY1AP1. Interacts with PRCC; the interaction is direct. Interacts with
CC POGZ. {ECO:0000250|UniProtKB:Q9UI95}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=D3Z8D9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=D3Z8D9-2; Sequence=VSP_040650;
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DR EMBL; CH473968; EDL81101.1; -; Genomic_DNA.
DR EMBL; BC087687; AAH87687.1; -; mRNA.
DR RefSeq; NP_001012106.1; NM_001012106.1. [D3Z8D9-2]
DR RefSeq; XP_006239452.1; XM_006239390.3. [D3Z8D9-2]
DR RefSeq; XP_006239453.1; XM_006239391.3. [D3Z8D9-1]
DR RefSeq; XP_008762478.1; XM_008764256.2. [D3Z8D9-2]
DR AlphaFoldDB; D3Z8D9; -.
DR SMR; D3Z8D9; -.
DR STRING; 10116.ENSRNOP00000052521; -.
DR PaxDb; D3Z8D9; -.
DR Ensembl; ENSRNOT00000055658; ENSRNOP00000052521; ENSRNOG00000009134. [D3Z8D9-2]
DR Ensembl; ENSRNOT00000083678; ENSRNOP00000070808; ENSRNOG00000009134. [D3Z8D9-1]
DR GeneID; 313702; -.
DR KEGG; rno:313702; -.
DR CTD; 10459; -.
DR RGD; 1307499; Mad2l2.
DR eggNOG; KOG3186; Eukaryota.
DR GeneTree; ENSGT00940000153395; -.
DR HOGENOM; CLU_1184726_0_0_1; -.
DR InParanoid; D3Z8D9; -.
DR OMA; CEDFPWI; -.
DR OrthoDB; 1630737at2759; -.
DR PhylomeDB; D3Z8D9; -.
DR TreeFam; TF101085; -.
DR Reactome; R-RNO-110312; Translesion synthesis by REV1.
DR Reactome; R-RNO-5655862; Translesion synthesis by POLK.
DR Reactome; R-RNO-5656121; Translesion synthesis by POLI.
DR PRO; PR:D3Z8D9; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000009134; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; D3Z8D9; baseline and differential.
DR Genevisible; D3Z8D9; RN.
DR GO; GO:0005680; C:anaphase-promoting complex; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0016035; C:zeta DNA polymerase complex; ISS:UniProtKB.
DR GO; GO:0008432; F:JUN kinase binding; ISS:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
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:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0042276; P:error-prone translesion synthesis; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; ISO:RGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; ISO:RGD.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISO:RGD.
DR GO; GO:1904667; P:negative regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; ISO:RGD.
DR GO; GO:0045830; P:positive regulation of isotype switching; ISO:RGD.
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:0001558; P:regulation of cell growth; ISS: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 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW DNA damage; Mitosis; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..211
FT /note="Mitotic spindle assembly checkpoint protein MAD2B"
FT /id="PRO_0000405244"
FT DOMAIN 13..203
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT REGION 21..155
FT /note="Mediates interaction with REV1 and REV3L and
FT homodimerization"
FT /evidence="ECO:0000250"
FT VAR_SEQ 111..211
FT /note="NSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEK
FT IQVIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKNS -> KLGGLK
FT QTVSLTVLGSWRYADLSGTLGVLSTAEYLSDLKGPLYPTSIQSVQTPSCLMWSSCFEPS
FT FLRLVCVTLSSTIILQAARLQFSCTQEKLPLGTWRRYRSSRTSPGSWQMSKMSTCMIPG
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040650"
SQ SEQUENCE 211 AA; 24402 MW; 0E47D0D8AC28AB5C CRC64;
MTTLTRQDLN FGQVVADVLS EFLEVAVHLI LYVREVYPVG IFQKRKKYNV PVQMSCHPEL
NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHRPVEKFVF EITQPPLLSI NSDSLLSHVE
QLLRAFILKI SVCDAVLDHN PPGCTFTVLV HTREAATRNM EKIQVIKDFP WILADEQDVH
MHDPRLIPLK TMTSDILKMQ LYVEERAHKN S
