MAD3_XENLA
ID MAD3_XENLA Reviewed; 200 AA.
AC Q0VH33; A0JPG7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Max dimerization protein 3;
DE Short=Max dimerizer 3;
DE AltName: Full=Max-associated protein 3;
DE AltName: Full=Max-interacting transcriptional repressor MAD3;
GN Name=mxd3; Synonyms=mad3;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15973701; DOI=10.1002/dvdy.20470;
RA Juergens K., Rust B., Pieler T., Henningfeld K.A.;
RT "Isolation and comparative expression analysis of the Myc-regulatory
RT proteins Mad1, Mad3, and Mnt during Xenopus development.";
RL Dev. Dyn. 233:1554-1559(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional repressor. Binds with MAX to form a sequence-
CC specific DNA-binding protein complex which recognizes the core sequence
CC 5'-CAC[GA]TG-3' (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC -!- TISSUE SPECIFICITY: Expressed broadly throughout the CNS and the eye,
CC starting at neurula stages. {ECO:0000269|PubMed:15973701}.
CC -!- DEVELOPMENTAL STAGE: In embryos at stage 20, expressed in the eye
CC vesicle, and later in the neural tube, olfactory placode, midbrain and
CC hindbrain. In addition to expression in the CNS at stage 29, expression
CC is also visible in the pronephros, otic placodes and tailtip.
CC Expression in the eye is localized to the retina. Broadly present
CC throughout the midbrain and hindbrain and expression is not limited to
CC the proliferating cells of the ventricular layer, but detected
CC throughout all layers of the hindbrain. {ECO:0000269|PubMed:15973701}.
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DR EMBL; AY964105; AAY32592.1; -; mRNA.
DR EMBL; BC127416; AAI27417.1; -; mRNA.
DR RefSeq; NP_001090188.1; NM_001096719.1.
DR AlphaFoldDB; Q0VH33; -.
DR SMR; Q0VH33; -.
DR DNASU; 779069; -.
DR GeneID; 779069; -.
DR KEGG; xla:779069; -.
DR CTD; 779069; -.
DR Xenbase; XB-GENE-867580; mxd3.L.
DR OMA; IVFDCVD; -.
DR OrthoDB; 1545091at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 779069; Expressed in testis and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..200
FT /note="Max dimerization protein 3"
FT /id="PRO_0000253711"
FT DOMAIN 54..106
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 31..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 200 AA; 23129 MW; CA8690B93A05F974 CRC64;
MEQLPSNLQV LLQAAEYVER REREAEHGYA SILPCDPATP GRRKRQRTNS NPDNVRSVHN
ELEKHRRAQL RRCLEQLKQQ VPLSMENSRH TTLSLLHRAK QHIKKLEDQE LRAKSLKEKL
RADQQKLRQR LKRLLPPNTE RIRTDSLDSS NLSSERSDSD QEDLEVDVEG IILSGNEGEL
FVSFSAGLEH SYSTPAHAWL