MAF_BOVIN
ID MAF_BOVIN Reviewed; 377 AA.
AC A7Z017;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Transcription factor Maf;
DE AltName: Full=Proto-oncogene c-Maf;
DE AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog;
GN Name=MAF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- 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 residues
CC (Probable). The phosphorylation status can serve to either stimulate or
CC inhibit transcription (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; BC153214; AAI53215.1; -; mRNA.
DR RefSeq; NP_001099107.1; NM_001105637.2.
DR AlphaFoldDB; A7Z017; -.
DR SMR; A7Z017; -.
DR STRING; 9913.ENSBTAP00000053555; -.
DR PaxDb; A7Z017; -.
DR PRIDE; A7Z017; -.
DR GeneID; 782481; -.
DR KEGG; bta:782481; -.
DR CTD; 4094; -.
DR InParanoid; A7Z017; -.
DR OrthoDB; 1395389at2759; -.
DR Proteomes; UP000009136; 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; 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 2: Evidence at transcript 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..377
FT /note="Transcription factor Maf"
FT /id="PRO_0000364081"
FT DOMAIN 292..355
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 57..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 126..377
FT /note="Represses ARE-mediated transcription"
FT /evidence="ECO:0000250"
FT REGION 175..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..317
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 320..341
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 358..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..195
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..377
FT /note="Polar 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 335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75444"
SQ SEQUENCE 377 AA; 38987 MW; 43DE41822B802BCD CRC64;
MASELAMSNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM
STPCSSVPPS PSFSAPSPGS GSEQKAHLED YYWMTGYPQQ LNPEALGFSP EDAVEALISN
SHQLQGGFDG YARGAQQLAS AAGAGAGASL GGSGEEMGPA AAVVSAVIAA AAAQSGAAPH
YHHHHHHHHA AGHHHHPTAG APGAAGSASA SAGGAGGSGG GSGGPASAGG GGGGGGGGGG
GAAGAGGALH PHHAAAGGLH FDDRFSDEQL VTMSVRELNR QLRGVSKEEV IRLKQKRRTL
KNRGYAQSCR FKRVQQRHVL ESEKNQLLQQ VDHLKQEISR LVRERDAYKE KYEKLVSSGF
RENGSSSDNP SSPEFFM
