ID   MD2L2_DANRE             Reviewed;         211 AA.
AC   Q568H3;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-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; ORFNames=si:dkey-23c22.2, zgc:110299;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (APR-2005) 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. 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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homooligomer. Interacts with rev1. Interacts with rev3l.
CC       Interacts with fzr1 (in complex with the anaphase promoting complex
CC       APC). May interact with cdc20 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton,
CC       spindle {ECO:0000250}. Cytoplasm {ECO:0000250}.
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DR   EMBL; CT737125; CAQ13963.1; -; Genomic_DNA.
DR   EMBL; BC092858; AAH92858.1; -; mRNA.
DR   RefSeq; NP_001017595.1; NM_001017595.1.
DR   RefSeq; XP_005167091.1; XM_005167034.3.
DR   AlphaFoldDB; Q568H3; -.
DR   SMR; Q568H3; -.
DR   STRING; 7955.ENSDARP00000013423; -.
DR   PaxDb; Q568H3; -.
DR   Ensembl; ENSDART00000062254; ENSDARP00000062253; ENSDARG00000042456.
DR   GeneID; 550258; -.
DR   KEGG; dre:550258; -.
DR   CTD; 10459; -.
DR   ZFIN; ZDB-GENE-050417-61; mad2l2.
DR   eggNOG; KOG3186; Eukaryota.
DR   GeneTree; ENSGT00940000153395; -.
DR   HOGENOM; CLU_050394_2_0_1; -.
DR   InParanoid; Q568H3; -.
DR   OMA; CEDFPWI; -.
DR   OrthoDB; 1630737at2759; -.
DR   PhylomeDB; Q568H3; -.
DR   TreeFam; TF101085; -.
DR   Reactome; R-DRE-110312; Translesion synthesis by REV1.
DR   Reactome; R-DRE-5655862; Translesion synthesis by POLK.
DR   Reactome; R-DRE-5656121; Translesion synthesis by POLI.
DR   PRO; PR:Q568H3; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 8.
DR   Bgee; ENSDARG00000042456; Expressed in testis and 26 other tissues.
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: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; 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   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_0000405246"
FT   DOMAIN          13..203
FT                   /note="HORMA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00109"
SQ   SEQUENCE   211 AA;  24224 MW;  9B8835EF1A7C9F97 CRC64;
     MATLTRQDLN FGQVVADILC EFLEVAIHLI LYVRDIYPSG IFQKRQKYNV PVQMSCHPQL
     NQYIQDTLHC VKPLIEKNEA EKVVVVIMNK EHHPVERFVF EISQPPLLAI SSETLLSHVE
     QLLRAMILKI SVCDAVLDSN PPGCTFTVLV HTREAATRNM EKVQVIKDFP WIVADEQEVH
     MEEAKLIPLK TMTSDILKMQ LYVEEKTQKS S