MAFA_DANRE
ID MAFA_DANRE Reviewed; 315 AA.
AC A3KMR8; Q98UK3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Transcription factor MafAa;
DE AltName: Full=Somite Maf1 {ECO:0000303|PubMed:11134968};
DE Short=SMaf1;
GN Name=mafaa; Synonyms=mafa, mafl;
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 [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11134968; DOI=10.1093/oxfordjournals.jbchem.a002825;
RA Kajihara M., Kawauchi S., Kobayashi M., Ogino H., Takahashi S., Yasuda K.;
RT "Isolation, characterization, and expression analysis of zebrafish large
RT Mafs.";
RL J. Biochem. 129:139-146(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcription factor, possibly involved in transcription
CC regulation during lens development, including that of crystallin genes
CC (PubMed:11134968). Specifically binds to the alphaCE2 enhancer element
CC of crystallin gene (PubMed:11134968). {ECO:0000269|PubMed:11134968}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- DEVELOPMENTAL STAGE: Detected first in each somite at the 7-somite
CC stage (12 hpf). By 24 hpf, expressed in each newly formed somite.
CC Expression persists at low levels in each maturing somite until after
CC 35 hpf. At 20 hpf, detected in the hindbrain and in olfactory cells.
CC {ECO:0000269|PubMed:11134968}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; AB006324; BAB21104.2; -; mRNA.
DR EMBL; BC133072; AAI33073.1; -; mRNA.
DR PIR; JC7572; JC7572.
DR RefSeq; NP_001076409.1; NM_001082940.2.
DR AlphaFoldDB; A3KMR8; -.
DR SMR; A3KMR8; -.
DR STRING; 7955.ENSDARP00000064832; -.
DR PaxDb; A3KMR8; -.
DR Ensembl; ENSDART00000064833; ENSDARP00000064832; ENSDARG00000044155.
DR GeneID; 100000492; -.
DR KEGG; dre:100000492; -.
DR CTD; 100000492; -.
DR ZFIN; ZDB-GENE-010605-3; mafaa.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000162747; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; A3KMR8; -.
DR OMA; GAHHTAH; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; A3KMR8; -.
DR TreeFam; TF325689; -.
DR PRO; PR:A3KMR8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 6.
DR Bgee; ENSDARG00000044155; Expressed in muscle tissue and 17 other tissues.
DR ExpressionAtlas; A3KMR8; baseline.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:ZFIN.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR004826; bZIP_Maf.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR013592; Maf_TF_N.
DR InterPro; IPR028562; MafA.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF30; PTHR10129:SF30; 1.
DR Pfam; PF03131; bZIP_Maf; 1.
DR Pfam; PF08383; Maf_N; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF47454; SSF47454; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..315
FT /note="Transcription factor MafAa"
FT /id="PRO_0000320278"
FT DOMAIN 223..286
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 52..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..248
FT /note="Basic motif"
FT REGION 229..243
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 251..272
FT /note="Leucine-zipper"
FT REGION 290..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..189
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 154
FT /note="E -> K (in Ref. 1; BAB21104)"
FT /evidence="ECO:0000305"
FT CONFLICT 164..165
FT /note="ED -> KN (in Ref. 1; BAB21104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 35708 MW; 3F8D0349E4E211CD CRC64;
MATDLAMSAE LPNSPLAIEY VNDFDLMKFE IKKEPPEADR YCHRLPPGSL SSTPISTPCS
SVPSSPSFCA PSPGSQPGQN LVNGVNNNNN NSGNGNNNTQ GSSGKPQMED LYWIPNYQHH
ISPEALNLTP EDAVEALIGN AHHHHHHHHH QPYEGFRGQQ YVGEDLSAAT NGHHHPVHHH
HHHHGHHAHA RLEDRFSDEQ LVSMTVRELN RQLRGFSKEE VIRLKQKRRT LKNRGYAQSC
RYKRVQQRHM LESEKCTLQS QVEQLKQDVA RLIKERDLYK EKYEKLASRA FNGGGNTRDP
SSGNHVKTTS TDFFM
