ID   GMEB1_RAT               Reviewed;         562 AA.
AC   Q9QUZ8; B0BN09;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 3.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Glucocorticoid modulatory element-binding protein 1;
DE            Short=GMEB-1;
GN   Name=Gmeb1;
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;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 123-129; 183-195 AND 317-334.
RX   PubMed=7665613; DOI=10.1074/jbc.270.37.21893;
RA   Oshima H., Szapary D., Simons S.S. Jr.;
RT   "The factor binding to the glucocorticoid modulatory element of the
RT   tyrosine aminotransferase gene is a novel and ubiquitous heteromeric
RT   complex.";
RL   J. Biol. Chem. 270:21893-21901(1995).
CC   -!- FUNCTION: Trans-acting factor that binds to glucocorticoid modulatory
CC       elements (GME) present in the TAT (tyrosine aminotransferase) promoter
CC       and increases sensitivity to low concentrations of glucocorticoids.
CC       Binds also to the transferrin receptor promoter (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer, and heterodimer of GMEB1 and GMEB2. Interacts with
CC       the glucocorticoid receptor (NR3C1) and NCOA2/TIF2. May interact with
CC       HSP27 and CREB-binding protein (CBP). Interacts with TRIM63 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=May be also cytoplasmic.
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; CH473968; EDL80619.1; -; Genomic_DNA.
DR   EMBL; BC158640; AAI58641.1; -; mRNA.
DR   RefSeq; NP_001102738.1; NM_001109268.2.
DR   RefSeq; XP_008762387.1; XM_008764165.1.
DR   RefSeq; XP_008762389.1; XM_008764167.2.
DR   RefSeq; XP_008762390.1; XM_008764168.1.
DR   AlphaFoldDB; Q9QUZ8; -.
DR   SMR; Q9QUZ8; -.
DR   STRING; 10116.ENSRNOP00000014506; -.
DR   PhosphoSitePlus; Q9QUZ8; -.
DR   PaxDb; Q9QUZ8; -.
DR   PRIDE; Q9QUZ8; -.
DR   Ensembl; ENSRNOT00000014506; ENSRNOP00000014506; ENSRNOG00000010910.
DR   GeneID; 500558; -.
DR   KEGG; rno:500558; -.
DR   UCSC; RGD:1563208; rat.
DR   CTD; 10691; -.
DR   RGD; 1563208; Gmeb1.
DR   eggNOG; KOG4333; Eukaryota.
DR   GeneTree; ENSGT00410000025596; -.
DR   HOGENOM; CLU_030344_1_0_1; -.
DR   InParanoid; Q9QUZ8; -.
DR   OMA; MVNPVEL; -.
DR   OrthoDB; 692814at2759; -.
DR   PhylomeDB; Q9QUZ8; -.
DR   TreeFam; TF317090; -.
DR   PRO; PR:Q9QUZ8; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Proteomes; UP000234681; Chromosome 5.
DR   Bgee; ENSRNOG00000010910; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q9QUZ8; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; 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:0051008; F:Hsp27 protein binding; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.10.390.10; -; 1.
DR   InterPro; IPR024830; GMEB1/2.
DR   InterPro; IPR010919; SAND-like_dom_sf.
DR   InterPro; IPR000770; SAND_dom.
DR   PANTHER; PTHR10417; PTHR10417; 1.
DR   Pfam; PF01342; SAND; 1.
DR   SMART; SM00258; SAND; 1.
DR   SUPFAM; SSF63763; SSF63763; 1.
DR   PROSITE; PS50864; SAND; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   DNA-binding; Metal-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y692"
FT   CHAIN           2..562
FT                   /note="Glucocorticoid modulatory element-binding protein 1"
FT                   /id="PRO_0000074091"
FT   DOMAIN          72..156
FT                   /note="SAND"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT   REGION          360..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          311..357
FT                   /evidence="ECO:0000255"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y692"
SQ   SEQUENCE   562 AA;  61194 MW;  B1A23491A5A76A38 CRC64;
     MANAEVSVPV GDVVVVPTEG NEGENPEDTK TQVILQLQPV QQGIYEAGSE NSAAVVAVET
     HTIHKIEEGI DASSIEANED MEIAYPITCG ESKAVLLWKK FVCPGINVKC VKFNDQLISP
     KHFVHLAGKS TLKDWKRAIR LGGIMLRKMM DSGQIDFYQH DKVCSNTCRS TKFDLLISSA
     RAPVPGQQTS VVQTPTSADG NITQIAISEE SMEEAGLEWN SALTAAVTMA TEEGIKKESE
     EISEDTLMFW KGIADVGLME EVVCNIQKEI EELLRGVQQR LIHAPFQVTD AAVLNNVANT
     FGLMDTVKRV LDNRRKQVEH GEEQFLYTLA DLERQLEEQK KQAQDPRLKS QTVQNVVLMP
     VSTPKPPKRP RLQRPASTTV LSPSPVQQPQ FTVISPITIT PVGQSFSMGN IPVATLSQGT
     SPVTVHTLPS GPQLFRYATV VSSAKSNSPD TVTIHPSSSL ALLSSTSMQD GSTLGNMATM
     VSPVELVAME SGLTSAIQAV ESTSEDGQTI IEIDPAPDPE ADDPEGKAVI LETELRTEEK
     VVANMEERQH QVHNVEIVVL ED