ID   GMEB1_BOVIN             Reviewed;         563 AA.
AC   Q2HJ87;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Glucocorticoid modulatory element-binding protein 1;
DE            Short=GMEB-1;
GN   Name=GMEB1;
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=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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       TRIM63 (By similarity). Interacts with the glucocorticoid receptor
CC       (NR3C1) and NCOA2/TIF2. May interact with HSP27 and CREB-binding
CC       protein (CBP) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185}.
CC       Cytoplasm {ECO:0000250}. Note=May be also cytoplasmic. {ECO:0000250}.
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; BC113252; AAI13253.1; -; mRNA.
DR   RefSeq; NP_001039940.1; NM_001046475.1.
DR   AlphaFoldDB; Q2HJ87; -.
DR   SMR; Q2HJ87; -.
DR   STRING; 9913.ENSBTAP00000001544; -.
DR   PaxDb; Q2HJ87; -.
DR   PRIDE; Q2HJ87; -.
DR   GeneID; 540374; -.
DR   KEGG; bta:540374; -.
DR   CTD; 10691; -.
DR   eggNOG; KOG4333; Eukaryota.
DR   InParanoid; Q2HJ87; -.
DR   OrthoDB; 692814at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
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; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y692"
FT   CHAIN           2..563
FT                   /note="Glucocorticoid modulatory element-binding protein 1"
FT                   /id="PRO_0000244594"
FT   DOMAIN          72..156
FT                   /note="SAND"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT   REGION          360..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          304..355
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   563 AA;  61321 MW;  42DBCBB519973DF4 CRC64;
     MANAEVSVPV GDVVVVPTEG NEGENPEDTK TQVILQLQPV QQGIYEAGSE NNTAVVAVET
     HTIHKIEEGI DASTIEANED MEIAYPITCG ESKAILLWKK FVCPGINVKC VKFNDQLISP
     KHFVHLAGKS TLKDWKRAIR LGGIMLRKMM DSGQIDFYQH DKVCSNTCRS TKFDLLISSA
     RAPVPGQQTS VVQTPTSADG SITQIAISEE SMEEAGLEWN SALTAAVTMA TEEGVKKDSE
     EISQDTLMFW KGIADVGLME EVVCNIQKEI EELLRGVQQR LIQAPFQVTD AAVLNNVAHT
     FGLMDTVKKV LDNRKNQVEQ GEEQFLYTLT DLERQLEEQK KQAQDHRLKS QTVQNVVLMP
     VSTPKPPKRP RLQRPASTTV LSPSPPVHQP QFTVISPITI TPVGQSFSMG NIPVATLSQG
     SSPVTVHTLP SGPQLFRYAT VVSSAKSSSP DTVTIHPSSS LALLSSTAMQ DGSTLGNMTT
     MVSPVELVAM ESGLTSAIQA VESTSEDGQT IIEIDPAPDP EAEDTEGKAV ILETELRTEE
     KVVAEMEEHQ HQVHNVEIVV LED