MAFA_CHICK
ID MAFA_CHICK Reviewed; 286 AA.
AC O42290; Q8AWH8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Transcription factor MafA;
DE AltName: Full=Lens-specific Maf {ECO:0000303|PubMed:9525857};
DE Short=L-Maf;
GN Name=MAFA;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Lens;
RX PubMed=9525857; DOI=10.1126/science.280.5360.115;
RA Ogino H., Yasuda K.;
RT "Induction of lens differentiation by activation of a bZIP transcription
RT factor, L-Maf.";
RL Science 280:115-118(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF SER-14 AND
RP SER-65.
RX PubMed=12970735; DOI=10.1038/sj.onc.1206526;
RA Nishizawa M., Kataoka K., Vogt P.K.;
RT "MafA has strong cell transforming ability but is a weak transactivator.";
RL Oncogene 22:7882-7890(2003).
CC -!- FUNCTION: Transcription factor involved in transcription regulation
CC during lens development, including that of crystallin and
CC filensin/BFSP1 genes (PubMed:9525857). Binds to CRE-type MARE 5'-
CC TGCTGACGTCAGCA-3' and TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequences
CC (PubMed:12970735). {ECO:0000269|PubMed:12970735,
CC ECO:0000269|PubMed:9525857}.
CC -!- SUBUNIT: Forms homodimers or heterodimers. May interact (via leucine-
CC zipper domain) with MAFB. May interact with FOS and JUN. Interacts with
CC PCAF; this interaction impairs MAFA ubiquitination.
CC {ECO:0000250|UniProtKB:O57342}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- DEVELOPMENTAL STAGE: First detected in the lens placode at stage 11,
CC when the head ectoderm makes contact with the optic vesicle. The
CC expression remains restricted to the invaginating lens placode, and
CC subsequently to the developing lens vesicle. In 8-day old embryo,
CC almost exclusively expressed in lens with very weak expression in
CC brain. {ECO:0000269|PubMed:9525857}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; AF034570; AAC15781.1; -; mRNA.
DR EMBL; AY152408; AAN75524.1; -; Genomic_DNA.
DR RefSeq; NP_990356.1; NM_205025.1.
DR AlphaFoldDB; O42290; -.
DR SMR; O42290; -.
DR STRING; 9031.ENSGALP00000042973; -.
DR iPTMnet; O42290; -.
DR GeneID; 395881; -.
DR KEGG; gga:395881; -.
DR CTD; 389692; -.
DR VEuPathDB; HostDB:geneid_395881; -.
DR eggNOG; KOG4196; Eukaryota.
DR InParanoid; O42290; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; O42290; -.
DR PRO; PR:O42290; -.
DR Proteomes; UP000000539; Unplaced.
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:0030073; P:insulin secretion; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; 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 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..286
FT /note="Transcription factor MafA"
FT /id="PRO_0000320276"
FT DOMAIN 199..262
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 51..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..224
FT /note="Basic motif"
FT REGION 227..248
FT /note="Leucine-zipper"
FT REGION 265..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MUTAGEN 14
FT /note="S->A: Abolishes transactivation activity. when
FT associated with A-65."
FT /evidence="ECO:0000269|PubMed:12970735"
FT MUTAGEN 65
FT /note="S->A: Abolishes transactivation activity; when
FT associated with A-14."
FT /evidence="ECO:0000269|PubMed:12970735"
FT CONFLICT 28..29
FT /note="KF -> NL (in Ref. 2; AAN75524)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="N -> K (in Ref. 2; AAN75524)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 32445 MW; 15DBD7B9B8DFA522 CRC64;
MASELAMTAE LPTSPLAIEY VNDFDLMKFE VKKEPAEAER LCHRLPAGSL SSTPLSTPCS
SVPSSPSFCA PSPGGQPSAG PTAAPLGSKP QLEELYWMSG YQHHLNPEAL NLTPEDAVEA
LIGAPHHHHH HHQSYESFRP QPFGGEELPP AAHHHNAHHH HHHHHLRLEE RFSDDQLVSM
SVRELNRQLR GFSKEEVIRL KQNRRTLKNR GYAQSCRYKR VQQRHILENE KCQLQSQVEQ
LKQEVSRLAK ERDLYKEKYE KLAARGFPRE PSPPAAPKTT AADFFM
