ID   MD2L2_BOVIN             Reviewed;         211 AA.
AC   Q2KIP7;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 78.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; BC112559; AAI12560.1; -; mRNA.
DR   RefSeq; NP_001039411.1; NM_001045946.2.
DR   AlphaFoldDB; Q2KIP7; -.
DR   SMR; Q2KIP7; -.
DR   STRING; 9913.ENSBTAP00000017655; -.
DR   PaxDb; Q2KIP7; -.
DR   GeneID; 506605; -.
DR   KEGG; bta:506605; -.
DR   CTD; 10459; -.
DR   eggNOG; KOG3186; Eukaryota.
DR   InParanoid; Q2KIP7; -.
DR   OrthoDB; 1630737at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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:0042177; P:negative regulation of protein catabolic process; ISS: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: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   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_0000405243"
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"
SQ   SEQUENCE   211 AA;  24375 MW;  B1083A0207E95246 CRC64;
     MTTLTRQDLN FGQVVADVLC EFLEVAVHLI LYVREVYPVG IFQKRKKYNV PVQMSCHPEL
     NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHRPVEKFVF EITQPPLLPI SSDSLLSHVE
     QLLRAFILKI SVCDAVLDHN PPGCTFTVLV HTREAATRNM EKIQVIKDFP WILADEQDVH
     MHDPRLIPLK TMTSDILKMQ LYVEERAHKS S