MAFA_RAT
ID MAFA_RAT Reviewed; 361 AA.
AC D3ZNT6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Transcription factor MafA;
DE AltName: Full=Pancreatic beta-cell-specific transcriptional activator;
GN Name=Mafa;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY GLUCOSE.
RX PubMed=15665000; DOI=10.1074/jbc.m409475200;
RA Zhao L., Guo M., Matsuoka T.A., Hagman D.K., Parazzoli S.D., Poitout V.,
RA Stein R.;
RT "The islet beta cell-enriched MafA activator is a key regulator of insulin
RT gene transcription.";
RL J. Biol. Chem. 280:11887-11894(2005).
RN [3]
RP PHOSPHORYLATION BY GSK3.
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 that activates insulin gene expression
CC (PubMed:15665000). Acts synergistically with NEUROD1/BETA2 and PDX1 (By
CC similarity). Binds the insulin enhancer C1/RIPE3b element
CC (PubMed:15665000). Binds to consensus TRE-type MARE 5'-TGCTGACTCAGCA-3'
CC DNA sequence (By similarity). {ECO:0000250|UniProtKB:Q8CF90,
CC ECO:0000250|UniProtKB:Q8NHW3, ECO:0000269|PubMed:15665000}.
CC -!- SUBUNIT: Forms homodimers. Monomers and dimers are able to bind DNA,
CC but the off-rate is faster for monomers (By similarity). Interacts with
CC NEUROD1 and PDX1 (By similarity). May interact with MAFB, FOS, JUN and
CC PCAF (By similarity). {ECO:0000250|UniProtKB:O57342,
CC ECO:0000250|UniProtKB:Q8CF90, ECO:0000250|UniProtKB:Q8NHW3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15665000}.
CC -!- INDUCTION: Up-regulated by glucose in Langerhans islets (at protein
CC level). {ECO:0000269|PubMed:15665000}.
CC -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC {ECO:0000250|UniProtKB:O57342}.
CC -!- PTM: Phosphorylated at tyrosines. {ECO:0000250|UniProtKB:Q8CF90}.
CC -!- SIMILARITY: Belongs to the bZIP family. {ECO:0000255}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC133673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006241965.1; XM_006241903.2.
DR AlphaFoldDB; D3ZNT6; -.
DR SMR; D3ZNT6; -.
DR STRING; 10116.ENSRNOP00000010084; -.
DR PaxDb; D3ZNT6; -.
DR PRIDE; D3ZNT6; -.
DR Ensembl; ENSRNOT00000010084; ENSRNOP00000010084; ENSRNOG00000007668.
DR GeneID; 366949; -.
DR KEGG; rno:366949; -.
DR UCSC; RGD:1562627; rat.
DR CTD; 389692; -.
DR RGD; 1562627; Mafa.
DR eggNOG; KOG4196; Eukaryota.
DR GeneTree; ENSGT00940000162747; -.
DR HOGENOM; CLU_063062_0_0_1; -.
DR InParanoid; D3ZNT6; -.
DR OMA; GAHHTAH; -.
DR OrthoDB; 1395389at2759; -.
DR PhylomeDB; D3ZNT6; -.
DR TreeFam; TF325689; -.
DR PRO; PR:D3ZNT6; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007668; Expressed in quadriceps femoris and 8 other tissues.
DR GO; GO:0005634; C:nucleus; IDA: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: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; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; ISO:RGD.
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; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..361
FT /note="Transcription factor MafA"
FT /id="PRO_0000445278"
FT DOMAIN 262..325
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 40..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..287
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 290..311
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 324..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..213
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 57
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O57342"
FT CROSSLNK 32
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NHW3"
SQ SEQUENCE 361 AA; 37780 MW; 0055A8D0DBE65620 CRC64;
MAAELAMGAE LPSSPLAIEY VNDFDLMKFE VKKEPPEAER FCHRLPPGSL SSTPLSTPCS
SVPSSPSFCA PSPGTGSSAG GGGSAAQAGG APGPPSGGPG TVGGASGKAV LEDLYWMSGY
QHHLNPEALN LTPEDAVEAL IGSGHHSAHH GAHHPAAAAA YEAFRGQSFA GGGGGGADDM
GAGHHHGAHH TAHHHHSAHH HHHHHHHHGG SGHHGGGAGH GGGGAGHHVR LEERFSDDQL
VSMSVRELNR QLRGFSKEEV IRLKQKRRTL KNRGYAQSCR FKRVQQRHIL ESEKCQLQSQ
VEQLKLEVGR LAKERDLYKE KYEKLAGRGG PGGAGGAGFP REPSPAQAGP GAAKGAPDFF
L
