MAFA_COTJA
ID MAFA_COTJA Reviewed; 286 AA.
AC O57342;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Transcription factor MafA;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog A;
GN Name=MAFA;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DEVELOPMENTAL STAGE,
RP DIMERIZATION, INTERACTION WITH MAFB; JUN AND FOS, AND MUTAGENESIS OF
RP LEU-234 AND LEU-241.
RX PubMed=9674710; DOI=10.1038/sj.onc.1201898;
RA Benkhelifa S., Provot S., Lecoq O., Pouponnot C., Calothy G.,
RA Felder-Schmittbuhl M.-P.;
RT "mafA, a novel member of the maf proto-oncogene family, displays
RT developmental regulation and mitogenic capacity in avian neuroretina
RT cells.";
RL Oncogene 17:247-254(1998).
RN [2]
RP FUNCTION, PHOSPHORYLATION AT SER-14; THR-57; THR-113 AND SER-272, AND
RP MUTAGENESIS OF THR-57; THR-113 AND SER-272.
RX PubMed=15963504; DOI=10.1016/j.febslet.2005.04.086;
RA Sii-Felice K., Pouponnot C., Gillet S., Lecoin L., Girault J.-A.,
RA Eychene A., Felder-Schmittbuhl M.-P.;
RT "MafA transcription factor is phosphorylated by p38 MAP kinase.";
RL FEBS Lett. 579:3547-3554(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-14 AND SER-65, AND
RP MUTAGENESIS OF SER-14 AND SER-65.
RX PubMed=11416124; DOI=10.1128/mcb.21.14.4441-4452.2001;
RA Benkhelifa S., Provot S., Nabais E., Eychene A., Calothy G.,
RA Felder-Schmittbuhl M.-P.;
RT "Phosphorylation of MafA is essential for its transcriptional and
RT biological properties.";
RL Mol. Cell. Biol. 21:4441-4452(2001).
RN [4]
RP FUNCTION, INTERACTION WITH PCAF, PHOSPHORYLATION AT SER-49; THR-53; THR-57;
RP SER-61 AND SER-65, MUTAGENESIS OF SER-49; THR-53; THR-57; SER-61 AND
RP SER-65, AND UBIQUITINATION.
RX PubMed=18042454; DOI=10.1016/j.molcel.2007.11.009;
RA Rocques N., Abou Zeid N., Sii-Felice K., Lecoin L.,
RA Felder-Schmittbuhl M.-P., Eychene A., Pouponnot C.;
RT "GSK-3-mediated phosphorylation enhances Maf-transforming activity.";
RL Mol. Cell 28:584-597(2007).
CC -!- FUNCTION: Transcription factor involved in transcription regulation
CC during lens development, including that of crystallin genes
CC (PubMed:9674710, PubMed:15963504, PubMed:18042454). Binds to CRE-type
CC MARE 5'-TGCTGACGTCAGCA-3' and TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA
CC sequences (PubMed:9674710). {ECO:0000269|PubMed:15963504,
CC ECO:0000269|PubMed:18042454, ECO:0000269|PubMed:9674710}.
CC -!- SUBUNIT: Forms homodimers or heterodimers (PubMed:9674710). May
CC interact (via leucine-zipper domain) with MAFB (PubMed:9674710). May
CC interact with FOS and JUN (PubMed:9674710). Interacts with PCAF; this
CC interaction impairs MAFA ubiquitination (PubMed:18042454).
CC {ECO:0000269|PubMed:18042454, ECO:0000269|PubMed:9674710}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:11416124}.
CC -!- DEVELOPMENTAL STAGE: In neuroretina, expression starts around embryonic
CC day 7 (ED7) and increases until ED15. Still present after hatching. At
CC ED7, also expressed in brain, but not detected on other tissues.
CC {ECO:0000269|PubMed:9674710}.
CC -!- PTM: Phosphorylation at Ser-14 and Ser-65 is required for transcription
CC regulation activity and lens differentiation in neuroretina cells
CC (PubMed:11416124). Phosphorylation at Ser-65 may be required for
CC efficient phosphorylation at Thr-53, Thr57 and Ser-61 by GSK3
CC (PubMed:18042454). {ECO:0000269|PubMed:11416124,
CC ECO:0000269|PubMed:18042454}.
CC -!- PTM: Ubiquitinated and degraded by the proteasome, following
CC phosphorylation by GSK3. {ECO:0000269|PubMed:18042454}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; AF034693; AAC60377.1; -; Genomic_DNA.
DR AlphaFoldDB; O57342; -.
DR SMR; O57342; -.
DR iPTMnet; O57342; -.
DR Proteomes; UP000694412; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
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 Activator; DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..286
FT /note="Transcription factor MafA"
FT /id="PRO_0000320277"
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:0000269|PubMed:11416124,
FT ECO:0000269|PubMed:15963504"
FT MOD_RES 49
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000269|PubMed:18042454"
FT MOD_RES 53
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000269|PubMed:18042454"
FT MOD_RES 57
FT /note="Phosphothreonine; by GSK3"
FT /evidence="ECO:0000269|PubMed:15963504,
FT ECO:0000269|PubMed:18042454"
FT MOD_RES 61
FT /note="Phosphoserine; by GSK3"
FT /evidence="ECO:0000269|PubMed:18042454"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11416124,
FT ECO:0000269|PubMed:15963504, ECO:0000269|PubMed:18042454"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15963504"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15963504"
FT MUTAGEN 14
FT /note="S->A: Partially reduced phosphorylation and
FT decreased transcription activation activity. Strong
FT decrease in phosphorylation and in transcription activation
FT activity; when associated with A-65. Does not affect DNA-
FT binding in vitro."
FT /evidence="ECO:0000269|PubMed:11416124,
FT ECO:0000269|PubMed:15963504"
FT MUTAGEN 49
FT /note="S->A: Reduced phosphorylation. Loss of
FT phosphorylation, loss of ubiquitination, decreased
FT transcription activation activity, decreased PCAF-binding
FT and decreased induction of lens differentiation; when
FT associated with A-53; A-57 and A-61."
FT /evidence="ECO:0000269|PubMed:18042454"
FT MUTAGEN 53
FT /note="T->A: Reduced phosphorylation. Loss of
FT phosphorylation, loss of ubiquitination, decreased
FT transcription activation activity, decreased PCAF-binding
FT and decreased induction of lens differentiation; when
FT associated with A-49; A-57 and A-61.//Diminishes
FT transcriptional activity and transforming activity and
FT abolishes ubiquitination; when associated with A-49; A-53
FT and A-61."
FT /evidence="ECO:0000269|PubMed:18042454"
FT MUTAGEN 57
FT /note="T->A: Reduced phosphorylation and decreased
FT induction of lens differentiation; when associated with A-
FT 113 and A-272."
FT /evidence="ECO:0000269|PubMed:15963504"
FT MUTAGEN 57
FT /note="T->A: Reduced phosphorylation. Loss of
FT phosphorylation, loss of ubiquitination, decreased
FT transcription activation activity, decreased PCAF-binding
FT and decreased induction of lens differentiation; when
FT associated with A-49; A-53 and A-61."
FT /evidence="ECO:0000269|PubMed:18042454"
FT MUTAGEN 61
FT /note="S->A: Reduced phosphorylation. Loss of
FT phosphorylation, loss of ubiquitination, decreased
FT transcription activation activity, decreased PCAF-binding
FT and decreased induction of lens differentiation; when
FT associated with A-49; A-53 and A-57."
FT /evidence="ECO:0000269|PubMed:18042454"
FT MUTAGEN 65
FT /note="S->A: Partially reduced phosphorylation,
FT transcription activation activity and decreased induction
FT of lens differentiation. Strongly decreased phosphorylation
FT and transcription activation activity; when associated with
FT A-14. Does not affect DNA-binding in vitro."
FT /evidence="ECO:0000269|PubMed:11416124,
FT ECO:0000269|PubMed:18042454"
FT MUTAGEN 113
FT /note="T->A: Reduced phosphorylation and decreased
FT induction of lens differentiation; when associated with A-
FT 57 and A-272."
FT /evidence="ECO:0000269|PubMed:15963504"
FT MUTAGEN 234
FT /note="L->P: Abolishes DNA-binding; when associated with P-
FT 241."
FT /evidence="ECO:0000269|PubMed:9674710"
FT MUTAGEN 241
FT /note="L->P: Abolishes DNA-binding; when associated with P-
FT 234."
FT /evidence="ECO:0000269|PubMed:9674710"
FT MUTAGEN 272
FT /note="S->A: Reduced phosphorylation and decreased
FT induction of lens differentiation; when associated with A-
FT 57 and A-113."
FT /evidence="ECO:0000269|PubMed:15963504"
SQ SEQUENCE 286 AA; 32464 MW; 0D4ED7BF08D91397 CRC64;
MASELAMTAE LPTSPLAIEY VNDFDLMKFE VKKEPAEAER LCHRLPAGSL SSTPLSTPCS
SVPSSPSFCA PSPGGQPSAG PTAAPLGSKP QLEELYWMSG YQHHLNPEAL NLTPEDAVEA
LIGAPHHHHH HHQSYESFRP QPFGGEELPP AAHHHNAHHH HHHHHLRLEE RFSDDQLVSM
SVRELNRQLR GFSKEEVIRL KQKRRTLKNR GYAQSCRYKR VQQRHILENE KCQLQSQVEQ
LKQEVSRLAK ERDLYKEKYE KLAARGFPRE TSPPAAPKTT AADFFM
