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MAFG_CHICK
ID   MAFG_CHICK              Reviewed;         162 AA.
AC   Q90889;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Transcription factor MafG;
DE   AltName: Full=V-maf musculoaponeurotic fibrosarcoma oncogene homolog G;
GN   Name=MAFG;
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].
RX   PubMed=7891713; DOI=10.1128/mcb.15.4.2180;
RA   Kataoka K., Igarashi K., Itoh K., Fujiwara K.T., Noda M., Yamamoto M.,
RA   Nishizawa M.;
RT   "Small Maf proteins heterodimerize with Fos and may act as competitive
RT   repressors of the NF-E2 transcription factor.";
RL   Mol. Cell. Biol. 15:2180-2190(1995).
CC   -!- FUNCTION: Since they lack a putative transactivation domain, the small
CC       Mafs behave as transcriptional repressors when they dimerize among
CC       themselves. However, they seem to serve as transcriptional activators
CC       by dimerizing with other (usually larger) basic-zipper proteins and
CC       recruiting them to specific DNA-binding sites. Small Maf proteins
CC       heterodimerize with Fos and may act as competitive repressors of the
CC       NF-E2 transcription factor. Transcription factor, component of
CC       erythroid-specific transcription factor NF-E2. May be involved in
CC       signal transduction of extracellular H(+) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer or heterodimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Sumoylation at Lys-14 is required for active transcriptional
CC       repression. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the bZIP family. Maf subfamily. {ECO:0000305}.
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DR   EMBL; D28602; BAA05939.1; -; Genomic_DNA.
DR   PIR; I50378; A56254.
DR   RefSeq; NP_001072957.1; NM_001079489.1.
DR   RefSeq; XP_015150912.1; XM_015295426.1.
DR   RefSeq; XP_015150913.1; XM_015295427.1.
DR   RefSeq; XP_015150914.1; XM_015295428.1.
DR   RefSeq; XP_015150915.1; XM_015295429.1.
DR   RefSeq; XP_015150916.1; XM_015295430.1.
DR   RefSeq; XP_015150917.1; XM_015295431.1.
DR   AlphaFoldDB; Q90889; -.
DR   SMR; Q90889; -.
DR   MINT; Q90889; -.
DR   STRING; 9031.ENSGALP00000011799; -.
DR   PaxDb; Q90889; -.
DR   Ensembl; ENSGALT00000058728; ENSGALP00000052002; ENSGALG00000031475.
DR   GeneID; 769355; -.
DR   KEGG; gga:769355; -.
DR   CTD; 4097; -.
DR   VEuPathDB; HostDB:geneid_769355; -.
DR   eggNOG; KOG4196; Eukaryota.
DR   GeneTree; ENSGT00940000160070; -.
DR   HOGENOM; CLU_112948_0_0_1; -.
DR   InParanoid; Q90889; -.
DR   OMA; IREQEHP; -.
DR   OrthoDB; 1395389at2759; -.
DR   PhylomeDB; Q90889; -.
DR   TreeFam; TF325689; -.
DR   PRO; PR:Q90889; -.
DR   Proteomes; UP000000539; Chromosome 18.
DR   Bgee; ENSGALG00000031475; Expressed in lung and 14 other tissues.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0045604; P:regulation of epidermal cell differentiation; 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; IPR028551; MafG.
DR   InterPro; IPR008917; TF_DNA-bd_sf.
DR   InterPro; IPR024874; Transcription_factor_Maf_fam.
DR   PANTHER; PTHR10129; PTHR10129; 1.
DR   PANTHER; PTHR10129:SF15; PTHR10129:SF15; 1.
DR   Pfam; PF03131; bZIP_Maf; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; SSF47454; 1.
DR   SUPFAM; SSF57959; SSF57959; 1.
DR   PROSITE; PS50217; BZIP; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Isopeptide bond; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN           1..162
FT                   /note="Transcription factor MafG"
FT                   /id="PRO_0000076502"
FT   DOMAIN          51..114
FT                   /note="bZIP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..76
FT                   /note="Basic motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   REGION          79..93
FT                   /note="Leucine-zipper"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT   CROSSLNK        14
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   162 AA;  18077 MW;  C7E0FCD18800696C CRC64;
     MTTPNKGNKA LKVKREPGEN GTSLTDEELV TMSVRELNQH LRGLSKEEII QLKQRRRTLK
     NRGYAASCRV KRVTQKEELE KQKAELQQEV EKLASENASM KMELDALRSK YEALQNFART
     VARSPVTPVR GPLTSSMGPL VPGKVATTSV ITIVKSKTDA RS
 
 
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