MD2L2_CHICK
ID MD2L2_CHICK Reviewed; 211 AA.
AC Q4KWZ6;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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; Synonyms=REV7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=15988022; DOI=10.1128/mcb.25.14.6103-6111.2005;
RA Okada T., Sonoda E., Yoshimura M., Kawano Y., Saya H., Kohzaki M.,
RA Takeda S.;
RT "Multiple roles of vertebrate REV genes in DNA repair and recombination.";
RL Mol. Cell. Biol. 25:6103-6111(2005).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF TYR-63 AND TRP-171.
RX PubMed=20164194; DOI=10.1074/jbc.m109.092403;
RA Hara K., Hashimoto H., Murakumo Y., Kobayashi S., Kogame T., Unzai S.,
RA Akashi S., Takeda S., Shimizu T., Sato M.;
RT "Crystal structure of human REV7 in complex with a human REV3 fragment and
RT structural implication of the interaction between DNA polymerase zeta and
RT REV1.";
RL J. Biol. Chem. 285:12299-12307(2010).
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. Component of the shieldin complex, which plays an important role
CC in repair of DNA double-stranded breaks (DSBs). During G1 and S phase
CC of the cell cycle, the complex functions downstream of TP53BP1 to
CC promote non-homologous end joining (NHEJ) and suppress DNA end
CC resection (By similarity). Through transcriptional regulation may play
CC a role in epithelial-mesenchymal transdifferentiation.
CC {ECO:0000250|UniProtKB:Q9UI95, ECO:0000269|PubMed:15988022,
CC ECO:0000269|PubMed:20164194}.
CC -!- SUBUNIT: Homooligomer. Interacts with REV1. Interacts with FZR1 (in
CC complex with the anaphase promoting complex APC). May interact with
CC CDC20 (By similarity). 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 {ECO:0000250|UniProtKB:Q9UI95}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UI95}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9UI95}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q9UI95}. Chromosome
CC {ECO:0000250|UniProtKB:Q9UI95}.
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DR EMBL; AY675170; AAV97594.1; -; mRNA.
DR RefSeq; NP_001020749.1; NM_001025578.1.
DR RefSeq; XP_015152403.1; XM_015296917.1.
DR RefSeq; XP_015152404.1; XM_015296918.1.
DR RefSeq; XP_015152405.1; XM_015296919.1.
DR AlphaFoldDB; Q4KWZ6; -.
DR SMR; Q4KWZ6; -.
DR STRING; 9031.ENSGALP00000007380; -.
DR PaxDb; Q4KWZ6; -.
DR Ensembl; ENSGALT00000007392; ENSGALP00000007380; ENSGALG00000004640.
DR Ensembl; ENSGALT00000067924; ENSGALP00000044503; ENSGALG00000004640.
DR Ensembl; ENSGALT00000086802; ENSGALP00000059484; ENSGALG00000004640.
DR Ensembl; ENSGALT00000087131; ENSGALP00000063368; ENSGALG00000004640.
DR GeneID; 419493; -.
DR KEGG; gga:419493; -.
DR CTD; 10459; -.
DR VEuPathDB; HostDB:geneid_419493; -.
DR eggNOG; KOG3186; Eukaryota.
DR GeneTree; ENSGT00940000153395; -.
DR HOGENOM; CLU_050394_2_0_1; -.
DR InParanoid; Q4KWZ6; -.
DR OMA; CEDFPWI; -.
DR OrthoDB; 1630737at2759; -.
DR PhylomeDB; Q4KWZ6; -.
DR TreeFam; TF101085; -.
DR Reactome; R-GGA-110312; Translesion synthesis by REV1.
DR Reactome; R-GGA-353299; RAD18 and ubiquitinated PCNA-mediated recruitment of translesion polymerases.
DR Reactome; R-GGA-353473; Translesion synthesis by Pol zeta.
DR Reactome; R-GGA-5655862; Translesion synthesis by POLK.
DR Reactome; R-GGA-5656121; Translesion synthesis by POLI.
DR PRO; PR:Q4KWZ6; -.
DR Proteomes; UP000000539; Chromosome 21.
DR Bgee; ENSGALG00000004640; Expressed in skeletal muscle tissue and 12 other tissues.
DR ExpressionAtlas; Q4KWZ6; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0017125; F:deoxycytidyl transferase activity; ISS:AgBase.
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:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0042276; P:error-prone translesion synthesis; ISS:AgBase.
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; IMP:UniProtKB.
DR GO; GO:0009411; P:response to UV; ISS:AgBase.
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; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA repair; Mitosis; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..211
FT /note="Mitotic spindle assembly checkpoint protein MAD2B"
FT /id="PRO_0000405245"
FT DOMAIN 13..203
FT /note="HORMA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
FT MUTAGEN 63
FT /note="Y->A: Loss of function in DNA repair; when
FT associated with W-171."
FT /evidence="ECO:0000269|PubMed:20164194"
FT MUTAGEN 171
FT /note="W->A: Loss of function in DNA repair; when
FT associated with Y-63."
FT /evidence="ECO:0000269|PubMed:20164194"
SQ SEQUENCE 211 AA; 24346 MW; E4D42349C60CEA05 CRC64;
MTTLTRQDLN FGQVVADVLS EFLEVAVHLI LYVREVYPIG IFQKRKKYNV PVQMSCHPEL
NQYIQDTLHC VKPLLEKNDV EKVVVVILDK EHHPVERFVF EITQPPLLSI SSESLLSHVE
QLLRAFILKI SVCDAVLDNN PPGCTFTVLV HTREAATRNM EKIQVIKDFP WILADEQDVH
MHDPRLIPLK TMTSDILKMQ LYVEERAHKG T
