MAF_CHICK
ID MAF_CHICK Reviewed; 359 AA.
AC Q789F3; Q789F2; Q90786; Q92171;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Transcription factor Maf;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog;
GN Name=MAF;
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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND TISSUE
RP SPECIFICITY.
RX PubMed=7935473; DOI=10.1128/mcb.14.11.7581-7591.1994;
RA Kataoka K., Fujiwara K.T., Noda M., Nishizawa M.;
RT "MafB,a new Maf family transcription activator that can associate with Maf
RT and Fos but not with Jun.";
RL Mol. Cell. Biol. 14:7581-7591(1994).
RN [2]
RP SUBUNIT, INTERACTION WITH HOXD12; PAX6 AND PRRX1, AND MUTAGENESIS OF
RP LEU-309 AND LEU-316.
RX PubMed=11036080; DOI=10.1074/jbc.m007643200;
RA Kataoka K., Yoshitomo-Nakagawa K., Shioda S., Nishizawa M.;
RT "A set of Hox proteins interact with the Maf oncoprotein to inhibit its DNA
RT binding, transactivation, and transforming activities.";
RL J. Biol. Chem. 276:819-826(2001).
RN [3]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=12081646; DOI=10.1046/j.1365-2443.2002.00548.x;
RA Yoshida T., Yasuda K.;
RT "Characterization of the chicken L-Maf, MafB and c-Maf in crystallin gene
RT regulation and lens differentiation.";
RL Genes Cells 7:693-706(2002).
CC -!- FUNCTION: Acts as a transcriptional activator or repressor. Positively
CC regulates the expression of alpha A crystallin genes during lens fiber
CC cell differentiation. Binds to Maf recognition elements (MARE).
CC {ECO:0000269|PubMed:12081646}.
CC -!- SUBUNIT: Homodimer or heterodimer. Binds DNA as a homodimer or a
CC heterodimer. Interacts with HOXD12, PAX6 and PRRX1; interaction is
CC direct and inhibits its DNA-binding and transactivating activity.
CC {ECO:0000269|PubMed:11036080}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Short;
CC IsoId=Q789F3-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=Q789F3-2; Sequence=VSP_036410;
CC -!- TISSUE SPECIFICITY: Expressed in kidney, brain, lung, gut, mesenterium,
CC testis and ovary. {ECO:0000269|PubMed:7935473}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the lens placode at stage 14.
CC Expressed at stage 18 when the invaginating lens placode closes to form
CC the lens vesicle.
CC -!- DOMAIN: The basic region and the leucine zipper structure are necessary
CC for association with HOXD12 and PRRX1.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; D28596; BAA05935.1; -; Genomic_DNA.
DR EMBL; D28596; BAA05936.1; -; Genomic_DNA.
DR EMBL; D28598; BAA05937.1; -; mRNA.
DR RefSeq; NP_001038136.1; NM_001044671.1. [Q789F3-2]
DR RefSeq; XP_015148000.1; XM_015292514.1. [Q789F3-2]
DR AlphaFoldDB; Q789F3; -.
DR SMR; Q789F3; -.
DR MINT; Q789F3; -.
DR STRING; 9031.ENSGALP00000041121; -.
DR Ensembl; ENSGALT00000043755; ENSGALP00000041121; ENSGALG00000026258. [Q789F3-2]
DR Ensembl; ENSGALT00000093301; ENSGALP00000071848; ENSGALG00000026258. [Q789F3-2]
DR GeneID; 693248; -.
DR KEGG; gga:693248; -.
DR CTD; 4094; -.
DR VEuPathDB; HostDB:geneid_693248; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000161531; -.
DR InParanoid; Q789F3; -.
DR OMA; SMPGEEM; -.
DR PhylomeDB; Q789F3; -.
DR PRO; PR:Q789F3; -.
DR Proteomes; UP000000539; Chromosome 11.
DR Bgee; ENSGALG00000026258; Expressed in kidney and 12 other tissues.
DR ExpressionAtlas; Q789F3; baseline and differential.
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: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; IPR028573; Maf/V-MAF.
DR InterPro; IPR013592; Maf_TF_N.
DR InterPro; IPR008917; TF_DNA-bd_sf.
DR InterPro; IPR024874; Transcription_factor_Maf_fam.
DR PANTHER; PTHR10129; PTHR10129; 1.
DR PANTHER; PTHR10129:SF9; PTHR10129:SF9; 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; Alternative splicing; DNA-binding; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..359
FT /note="Transcription factor Maf"
FT /id="PRO_0000364082"
FT DOMAIN 274..337
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 57..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..299
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 302..323
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 340..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..359
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 359
FT /note="M -> MYPRESSTTVM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7935473"
FT /id="VSP_036410"
FT MUTAGEN 309
FT /note="L->P: Reduces interaction with HOXD12; in
FT association with P-316."
FT /evidence="ECO:0000269|PubMed:11036080"
FT MUTAGEN 316
FT /note="L->P: Reduces interaction with HOXD12; in
FT association with P-309."
FT /evidence="ECO:0000269|PubMed:11036080"
SQ SEQUENCE 359 AA; 37708 MW; FEC6C89295E0A913 CRC64;
MASELAMSGS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM
STPCSSVPPS PSFSAPSPGS GTDQKTHLED YYWMTGYPQQ LNPEALGFSP EDAVEALINS
SHHPLPGAFD GYARGQQLAA AAGGSVPAEE MGSAAAVVSA VIAAAAAQGG APHYHHHHHH
PHHGGGGGGG GHPHGAAPGS APPSSASSSA AGSGGGGGGG GGGAGGLHHP HHGGGGGGGG
LHFDDRFSDE QLVTMSVREL NRQLRGVSKE EVIRLKQKRR TLKNRGYAQS CRFKRVQQRH
VLESEKNQLL QQVEHLKQEI SRLVRERDAY KEKYEKLVSN GFRENGSSSD NPSSPEFFM
