MAF_MOUSE
ID MAF_MOUSE Reviewed; 370 AA.
AC P54843; Q3V1Z2; Q4QY62;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 174.
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; Synonyms=Maf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Cerebellum;
RX PubMed=7799931; DOI=10.1128/mcb.15.1.246;
RA Kurschner C., Morgan J.I.;
RT "The maf proto-oncogene stimulates transcription from multiple sites in a
RT promoter that directs Purkinje neuron-specific gene expression.";
RL Mol. Cell. Biol. 15:246-254(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=14707122; DOI=10.1074/jbc.m312414200;
RA Cui W., Tomarev S.I., Piatigorsky J., Chepelinsky A.B., Duncan M.K.;
RT "Mafs, Prox1, and Pax6 can regulate chicken betaB1-crystallin gene
RT expression.";
RL J. Biol. Chem. 279:11088-11095(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP FUNCTION, HETEROTETRAMER, INTERACTION WITH USF2, AND MUTAGENESIS OF
RP LEU-334.
RX PubMed=9070273; DOI=10.1006/bbrc.1997.6097;
RA Kurschner C., Morgan J.I.;
RT "USF2/FIP associates with the b-Zip transcription factor, c-Maf, via its
RT bHLH domain and inhibits c-Maf DNA binding activity.";
RL Biochem. Biophys. Res. Commun. 231:333-339(1997).
RN [6]
RP FUNCTION, AND INTERACTION WITH ETS1 AND MYB.
RX PubMed=9566892; DOI=10.1128/mcb.18.5.2729;
RA Hedge S.P., Kumar A., Kurschner C., Shapiro L.H.;
RT "c-Maf interacts with c-Myb to regulate transcription of an early myeloid
RT gene during differentiation.";
RL Mol. Cell. Biol. 18:2729-2737(1998).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10403649; DOI=10.1016/s1074-7613(00)80073-4;
RA Kim J.I., Ho I.-C., Grusby M.J., Glimcher L.H.;
RT "The transcription factor c-Maf controls the production of interleukin-4
RT but not other Th2 cytokines.";
RL Immunity 10:745-751(1999).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=10383433; DOI=10.1074/jbc.274.27.19254;
RA Kawauchi S., Takahashi S., Nakajima O., Ogino H., Morita M., Nishizawa M.,
RA Yasuda K., Yamamoto M.;
RT "Regulation of lens fiber cell differentiation by transcription factor c-
RT Maf.";
RL J. Biol. Chem. 274:19254-19260(1999).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10097114; DOI=10.1073/pnas.96.7.3781;
RA Kim J.I., Li T., Ho I.C., Grusby M.J., Glimcher L.H.;
RT "Requirement for the c-Maf transcription factor in crystallin gene
RT regulation and lens development.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3781-3785(1999).
RN [10]
RP FUNCTION, DNA-BINDING, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=10603348; DOI=10.1242/dev.127.2.307;
RA Ring B.Z., Cordes S.P., Overbeek P.A., Barsh G.S.;
RT "Regulation of mouse lens fiber cell development and differentiation by the
RT Maf gene.";
RL Development 127:307-317(2000).
RN [11]
RP FUNCTION, AND INTERACTION WITH CREBBP AND EP300.
RX PubMed=11943779; DOI=10.1074/jbc.m201821200;
RA Chen Q., Dowhan D.H., Liang D., Moore D.D., Overbeek P.A.;
RT "CREB-binding protein/p300 co-activation of crystallin gene expression.";
RL J. Biol. Chem. 277:24081-24089(2002).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=14512017; DOI=10.1016/s0012-1606(03)00324-5;
RA MacLean H.E., Kim J.I., Glimcher M.J., Wang J., Kronenberg H.M.,
RA Glimcher L.H.;
RT "Absence of transcription factor c-maf causes abnormal terminal
RT differentiation of hypertrophic chondrocytes during endochondral bone
RT development.";
RL Dev. Biol. 262:51-63(2003).
RN [13]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=15249232; DOI=10.1016/j.bbrc.2004.05.222;
RA Imaki J., Tsuchiya K., Mishima T., Onodera H., Kim J.I., Yoshida K.,
RA Ikeda H., Sakai M.;
RT "Developmental contribution of c-maf in the kidney: distribution and
RT developmental study of c-maf mRNA in normal mice kidney and histological
RT study of c-maf knockout mice kidney and liver.";
RL Biochem. Biophys. Res. Commun. 320:1323-1327(2004).
RN [14]
RP FUNCTION, AND INTERACTION WITH MYB.
RX PubMed=17823980; DOI=10.1002/eji.200636979;
RA Peng S., Lalani S., Leavenworth J.W., Ho I.-C., Pauza M.E.;
RT "c-Maf interacts with c-Myb to down-regulate Bcl-2 expression and increase
RT apoptosis in peripheral CD4 cells.";
RL Eur. J. Immunol. 37:2868-2880(2007).
RN [15]
RP FUNCTION, MUTAGENESIS OF SER-15 AND SER-70, DNA-BINDING, AND TISSUE
RP SPECIFICITY.
RX PubMed=17897790; DOI=10.1016/j.gene.2007.08.010;
RA Mahoney K.M., Petrovic N., Schacke W., Shapiro L.H.;
RT "CD13/APN transcription is regulated by the proto-oncogene c-Maf via an
RT atypical response element.";
RL Gene 403:178-187(2007).
RN [16]
RP FUNCTION, SUBUNIT, INTERACTION WITH PAX6, DNA-BINDING, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=17901057; DOI=10.1074/jbc.m702795200;
RA Gosmain Y., Avril I., Mamin A., Philippe J.;
RT "Pax-6 and c-Maf functionally interact with the alpha-cell-specific DNA
RT element G1 in vivo to promote glucagon gene expression.";
RL J. Biol. Chem. 282:35024-35034(2007).
RN [17]
RP REVIEW, AND FUNCTION.
RX PubMed=19143053; DOI=10.1038/nrc2460;
RA Eychene A., Rocques N., Pouponnot C.;
RT "A new MAFia in cancer.";
RL Nat. Rev. Cancer 8:683-693(2008).
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 (By similarity). Involved in embryonic lens fiber
CC cell development. Recruits the transcriptional coactivators CREBBP
CC and/or EP300 to crystallin promoters leading to up-regulation of
CC crystallin gene during lens fiber cell differentiation. Activates the
CC expression of IL4 in T helper 2 (Th2) cells. Increases T-cell
CC susceptibility to apoptosis by interacting with MYB and decreasing BCL2
CC expression. Together with PAX6, transactivates strongly the glucagon
CC gene promoter through the G1 element. Activates transcription of the
CC CD13 proximal promoter in endothelial cells. Represses transcription of
CC the CD13 promoter in early stages of myelopoiesis by affecting the ETS1
CC and MYB cooperative interaction. Involved in the initial chondrocyte
CC terminal differentiation and the disappearance of hypertrophic
CC chondrocytes during endochondral bone development. Binds to the
CC sequence 5'-[GT]G[GC]N[GT]NCTCAGNN-3' in the L7 promoter. Binds to the
CC T-MARE (Maf response element) sites of lens-specific alpha- and beta-
CC crystallin gene promoters. Binds element G1 on the glucagon promoter.
CC Binds an AT-rich region adjacent to the TGC motif (atypical Maf
CC response element) in the CD13 proximal promoter in endothelial cells.
CC It may interact with additional basic-zipper proteins that determine a
CC subtype of Maf-responsive element binding. {ECO:0000250,
CC ECO:0000269|PubMed:10097114, ECO:0000269|PubMed:10383433,
CC ECO:0000269|PubMed:10403649, ECO:0000269|PubMed:10603348,
CC ECO:0000269|PubMed:11943779, ECO:0000269|PubMed:14512017,
CC ECO:0000269|PubMed:17823980, ECO:0000269|PubMed:17897790,
CC ECO:0000269|PubMed:17901057, ECO:0000269|PubMed:19143053,
CC ECO:0000269|PubMed:9070273, ECO:0000269|PubMed:9566892}.
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 -!- INTERACTION:
CC P54843; Q91ZW3: Smarca5; NbExp=2; IntAct=EBI-3842521, EBI-927547;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P54843-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=P54843-2; Sequence=VSP_036408;
CC Name=3;
CC IsoId=P54843-3; Sequence=VSP_036409;
CC -!- TISSUE SPECIFICITY: Expressed in tubules of the renal cortex and
CC hepatocytes. Expressed in the lens (at protein level). Expressed in
CC pancreatic islets and endothelial cells. {ECO:0000269|PubMed:15249232,
CC ECO:0000269|PubMed:17897790, ECO:0000269|PubMed:17901057}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the floor of the diencephalon at 10
CC dpc (at protein level). Expressed in the midline of the forebrain and
CC in the eye region at 9 dpc. Expressed in the head ectoderm destined to
CC become the lens vesicle at 9 and 10 dpc. Expressed in the lens placode
CC at 10.5 dpc. Expressed in the lens vesicle in both epithelial and fiber
CC cells at 11 dpc. Expressed in secondary fiber cells at the equatorial
CC region that divides the lens into anterior and posterior hemispheres
CC between 11 and 14 dpc. Expressed in the neural tube and in primary
CC fiber cells of the lens at 11.5 dpc. Expressed in proximal tubules of
CC the cortex in the kidney at 16 and 17 dpc. Expressed in hypertrophic
CC chondrocytes at 14.5 to 18.5 dpc. Expressed in the pancreas at 12.5 dpc
CC until the adult stage. {ECO:0000269|PubMed:10383433,
CC ECO:0000269|PubMed:10603348, ECO:0000269|PubMed:14512017,
CC ECO:0000269|PubMed:15249232, ECO:0000269|PubMed:17901057}.
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 (By similarity). The phosphorylation status can serve to either
CC stimulate or inhibit transcription. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice lacking this gene exhibit small
CC eyes or microphthalmia with an absence of normal lens structures, an
CC abnormal chondrocyte development, with terminal differentiation of
CC hypertrophic chondrocytes initially delayed, followed by a subsequent
CC expansion of the hypertrophic chondrocyte domain in the growth plates
CC of embryonic and postnatal long bones. They also show a lack of IL4
CC production. {ECO:0000269|PubMed:10097114, ECO:0000269|PubMed:10383433,
CC ECO:0000269|PubMed:10403649, ECO:0000269|PubMed:10603348,
CC ECO:0000269|PubMed:14512017}.
CC -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR EMBL; S74567; AAB32820.1; -; mRNA.
DR EMBL; AY560005; AAY81957.1; -; mRNA.
DR EMBL; AK132165; BAE21007.1; -; mRNA.
DR EMBL; AC113301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS40486.1; -. [P54843-1]
DR RefSeq; NP_001020748.2; NM_001025577.2. [P54843-1]
DR AlphaFoldDB; P54843; -.
DR SMR; P54843; -.
DR BioGRID; 201281; 2.
DR IntAct; P54843; 2.
DR MINT; P54843; -.
DR STRING; 10090.ENSMUSP00000104732; -.
DR iPTMnet; P54843; -.
DR PhosphoSitePlus; P54843; -.
DR MaxQB; P54843; -.
DR PaxDb; P54843; -.
DR PRIDE; P54843; -.
DR ProteomicsDB; 287293; -. [P54843-1]
DR ProteomicsDB; 287294; -. [P54843-2]
DR ProteomicsDB; 287295; -. [P54843-3]
DR Antibodypedia; 4143; 502 antibodies from 39 providers.
DR DNASU; 17132; -.
DR Ensembl; ENSMUST00000069009; ENSMUSP00000067704; ENSMUSG00000055435. [P54843-3]
DR Ensembl; ENSMUST00000109104; ENSMUSP00000104732; ENSMUSG00000055435. [P54843-1]
DR GeneID; 17132; -.
DR KEGG; mmu:17132; -.
DR UCSC; uc009noe.2; mouse. [P54843-3]
DR UCSC; uc009nof.1; mouse. [P54843-1]
DR CTD; 4094; -.
DR MGI; MGI:96909; Maf.
DR VEuPathDB; HostDB:ENSMUSG00000055435; -.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000161531; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; P54843; -.
DR OMA; LMSEITW; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; P54843; -.
DR TreeFam; TF325689; -.
DR BioGRID-ORCS; 17132; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Maf; mouse.
DR PRO; PR:P54843; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P54843; protein.
DR Bgee; ENSMUSG00000055435; Expressed in stroma of bone marrow and 251 other tissues.
DR Genevisible; P54843; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR GO; GO:0070306; P:lens fiber cell differentiation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IMP:MGI.
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; IMP:MGI.
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; Isopeptide bond; Nucleus;
KW Proto-oncogene; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..370
FT /note="Transcription factor Maf"
FT /id="PRO_0000076492"
FT DOMAIN 285..348
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..370
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 285..310
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 313..334
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 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O75444"
FT VAR_SEQ 370
FT /note="M -> MCVCVCALFIL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14707122"
FT /id="VSP_036408"
FT VAR_SEQ 370
FT /note="M -> MYPRDSSTSVM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_036409"
FT MUTAGEN 15
FT /note="S->A: Inhibition on transcriptional activation on
FT CD13 proximal promoter in endothelial cells."
FT /evidence="ECO:0000269|PubMed:17897790"
FT MUTAGEN 70
FT /note="S->A: No effect on transcriptional activation on
FT CD13 proximal promoter. Increases liver specific
FT transactivation on the IL-4 promoter."
FT /evidence="ECO:0000269|PubMed:17897790"
FT MUTAGEN 334
FT /note="L->P: Abolishes interaction with USF2."
FT /evidence="ECO:0000269|PubMed:9070273"
FT CONFLICT 202
FT /note="A -> T (in Ref. 1; AAB32820)"
FT /evidence="ECO:0000305"
FT CONFLICT 208..211
FT /note="ASAS -> SSSN (in Ref. 1; AAB32820)"
FT /evidence="ECO:0000305"
FT CONFLICT 223..224
FT /note="SA -> NT (in Ref. 1; AAB32820)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="G -> D (in Ref. 1; AAB32820)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="A -> S (in Ref. 1; AAB32820)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 38435 MW; 1E8722C8287AAAC9 CRC64;
MASELAMNNS DLPTSPLAME YVNDFDLMKF EVKKEPVETD RIISQCGRLI AGGSLSSTPM
STPCSSVPPS PSFSAPSPGS GSEQKAHLED YYWMTGYPQQ LNPEALGFSP EDAVEALISN
SHQLQGGFDG YARGAQQLAA AAGAGAGASL GGSGEEMGPA AAVVSAVIAA AAAQSGAAPH
YHHHHHHAAG HHHHPTAGAP GAAGGASASA SGAGGAGGGG PASAGGGGGG GGGGGTAGAG
GALHPHHAAG GLHFDDRFSD EQLVTMSVRE LNRQLRGVSK EEVIRLKQKR RTLKNRGYAQ
SCRFKRVQQR HVLESEKNQL LQQVDHLKQE ISRLVRERDA YKEKYEKLVS NGFRENGSSS
DNPSSPEFFM
