MAF_RAT
ID MAF_RAT Reviewed; 369 AA.
AC P54844;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 142.
DE RecName: Full=Transcription factor Maf;
DE AltName: Full=Proto-oncogene c-Maf;
DE AltName: Full=Transcription factor Maf-2;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog;
GN Name=Maf; Synonyms=Maf2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=9038383; DOI=10.1038/sj.onc.1200869;
RA Sakai M., Imaki J., Yoshida K., Ogata A., Matsushima-Hibaya Y., Kuboki Y.,
RA Nishizawa M., Nishi S.;
RT "Rat maf related genes: specific expression in chondrocytes, lens and
RT spinal cord.";
RL Oncogene 14:745-750(1997).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=9375588;
RA Yoshida K., Imaki J., Koyama Y., Harada T., Shinmei Y., Oishi C.,
RA Matsushima-Hibiya Y., Matsuda A., Nishi S., Matsuda H., Sakai M.;
RT "Differential expression of maf-1 and maf-2 genes in the developing rat
RT lens.";
RL Invest. Ophthalmol. Vis. Sci. 38:2679-2683(1997).
CC -!- FUNCTION: Acts as a transcriptional activator or repressor. When
CC overexpressed, represses anti-oxidant response element (ARE)-mediated
CC transcription. Involved either as an oncogene or as a tumor suppressor,
CC depending on the cell context. Binds to the ARE sites of detoxifying
CC enzyme gene promoters. Involved in embryonic lens fiber cell
CC development. Recruits the transcriptional coactivators CREBBP and/or
CC EP300 to crystallin promoters leading to up-regulation of crystallin
CC gene during lens fiber cell differentiation. Activates the expression
CC of IL4 in T-helper 2 (Th2) cells. Increases T-cell susceptibility to
CC apoptosis by interacting with MYB and decreasing BCL2 expression.
CC Together with PAX6, transactivates strongly the glucagon gene promoter
CC through the G1 element. Activates transcription of the CD13 proximal
CC promoter in endothelial cells. Represses transcription of the CD13
CC promoter in early stages of myelopoiesis by affecting the ETS1 and MYB
CC cooperative interaction. Involved in the initial chondrocyte terminal
CC differentiation and the disappearance of hypertrophic chondrocytes
CC during endochondral bone development. Binds to the sequence 5'-
CC [GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the T-MARE (Maf
CC response element) sites of lens-specific alpha- and beta-crystallin
CC gene promoters. Binds element G1 on the glucagon promoter. Binds an AT-
CC rich region adjacent to the TGC motif (atypical Maf response element)
CC in the CD13 proximal promoter in endothelial cells. It may interact
CC with additional basic-zipper proteins that determine a subtype of Maf-
CC responsive element binding (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:9038383}.
CC -!- SUBUNIT: Homodimer or heterodimer with other bHLH-Zip transcription
CC factors. Binds DNA as a homodimer or as a heterodimer. Heterotetramer
CC of two MAF and two USF2. Interacts with PAX6; the interaction is
CC direct. Interacts with MYB; interaction takes place weakly in normal T-
CC cells and increases in T-cells following stimulation through the TCR
CC engagement. Interacts with MYB; the ternary complex formed with MYB and
CC the CD13 promoter is regulated in response to differentiating signals.
CC Interacts with USF2; the interaction inhibits its DNA-binding activity
CC on the L7 promoter. Interacts with CREBBP, EP300 and ETS1 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978,
CC ECO:0000269|PubMed:9038383}.
CC -!- TISSUE SPECIFICITY: Expressed in the muscle, uterus, intestine, kidney,
CC liver and skin. Expressed in the lens epithelial and fiber cells.
CC {ECO:0000269|PubMed:9038383, ECO:0000269|PubMed:9375588}.
CC -!- DEVELOPMENTAL STAGE: Expressed in lens cells at 12 dpc. Expressed in
CC the cartilage of ribs and limbs, in the eyes and spinal cord at 15 dpc.
CC Expressed in the outer equatorial epithelium and lens fibers at 16 dpc
CC (at protein level). Expressed throughout the lens fiber cells at 13 and
CC 16 dpc; not detected in the epithelium of the lens. In the eyes,
CC confined to the lens; not detected in the retina at 15 dpc. In spinal
CC cord, expressed in the dorsal and ventral part of the dorsal horn at 15
CC dpc. Predominantly expressed in post-mitotic cells.
CC {ECO:0000269|PubMed:9038383}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC Ubiquitination is triggered by glucocorticoids (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by GSK3 and MAPK13 on serine and threonine
CC residues. The phosphorylation status can serve to either stimulate or
CC inhibit transcription (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; U56242; AAB50063.1; -; mRNA.
DR RefSeq; NP_062191.1; NM_019318.1.
DR AlphaFoldDB; P54844; -.
DR SMR; P54844; -.
DR STRING; 10116.ENSRNOP00000016577; -.
DR PaxDb; P54844; -.
DR GeneID; 54267; -.
DR KEGG; rno:54267; -.
DR UCSC; RGD:3034; rat.
DR CTD; 4094; -.
DR RGD; 3034; Maf.
DR eggNOG; KOG4196; Eukaryota.
DR InParanoid; P54844; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; P54844; -.
DR PRO; PR:P54844; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
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; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0048468; P:cell development; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0002088; P:lens development in camera-type eye; ISO:RGD.
DR GO; GO:0070306; P:lens fiber cell differentiation; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
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; DNA-binding; Isopeptide bond; Nucleus; Proto-oncogene;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation.
FT CHAIN 1..369
FT /note="Transcription factor Maf"
FT /id="PRO_0000076493"
FT DOMAIN 284..347
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 57..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..369
FT /note="Represses ARE-mediated transcription"
FT /evidence="ECO:0000250"
FT REGION 175..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..309
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 312..333
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 179..193
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75444"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75444"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75444"
SQ SEQUENCE 369 AA; 38457 MW; 288E464708DA6C7D CRC64;
MASELAMNNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM
STPCSSVPPS PSFSAPSPAS GSEQKAHLED YYWMTGYPQQ LNPEALGFSP EDAVEALISN
SHQLQGGFDG YARGAQQLAA AAGAGAGASL GGSGEEMGPA AAVVSAVIAA AAAQSGGAPH
YHHHHHHATG HHHHPTAGAP GAAGSASASA SGAGGAGGGG PASAGGGGGG GGGGTAGAGG
ALHPHHAAGG LHFDDRFSDE QLVTMSVREL NRQLRGVSKE EVIRLKQKRR TLKNRGYAQS
CRFKRVQQRH VLESEKNQLL QQVDHLKQEI SRLVRERDAY KEKYEKLVSS GFRENCSSSD
NPSSPEFFM
