Swiss-Prot entry
ID GCR_SAIBB STANDARD; PRT; 777 AA.
AC O13186;
DT 15-JUL-1998 (Rel. 36, Created)
DT 15-JUL-1998 (Rel. 36, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Glucocorticoid receptor (GR).
GN Name=NR3C1; Synonyms=GRL;
OS Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Platyrrhini; Cebidae;
OC Cebinae; Saimiri.
OX NCBI_TaxID=39432;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver;
RX MEDLINE=97176699; PubMed=9024238 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1210/jc.82.2.465;
RA Reynolds P.D., Pittler S.J., Scammell J.G.;
RT "Cloning and expression of the glucocorticoid receptor from the
RT squirrel monkey (Saimiri boliviensis boliviensis), a glucocorticoid-
RT resistant primate.";
RL J. Clin. Endocrinol. Metab. 82:465-472(1997).
CC -!- FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of
CC action: as a transcription factor that binds to glucocorticoid
CC response elements (GRE) and as a modulator of other transcription
CC factors. Affects inflammatory responses, cellular proliferation
CC and differentiation in target tissues (By similarity).
CC -!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90, HSP70,
CC and an immunophilin. Upon ligand binding the complex undergoes a
CC conformation change and moves to the nucleus, where it
CC dissociates. Binds to DNA as a homodimer, and as heterodimer with
CC NR3C2 or the retinoid X receptor. Interacts with the coactivator
CC NCOA6, leading to a strong increase in transcription of target
CC genes. Interaction with numerous other transcription factors
CC modulates transcription activation. Interacts with TRIM28 (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic in the absence of ligand;
CC nuclear after ligand-binding (By similarity).
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC a DNA-binding domain and a C-terminal steroid-binding domain.
CC -!- PTM: Increased proteasome-mediated degradation in response to
CC glucocorticoids (By similarity).
CC -!- PTM: Phosphorylated in the absence of hormone; becomes
CC hyperphosphorylated in the presence of glucocorticoids (By
CC similarity).
CC -!- PTM: Sumoylated; this reduces transcription transactivation (By
CC similarity).
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily.
CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; U87951; AAC51131.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P06536; 1GDC. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; O13186; 417-491, 523-777.
DR InterPro; IPR001409; Glcrtcd_receptor.
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR001723; Stdhrmn_receptor.
DR InterPro; IPR008946; Str_ncl_receptor.
DR InterPro; IPR001628; Znf_C4steroid.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF02155; GCR; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00528; GLCORTICOIDR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR ProDom; PD000035; Znf_C4steroid; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; O13186.
DR ProtoNet; O13186.
DR ProtoMap; O13186.
DR PRESAGE; O13186.
DR DIP; O13186.
DR ModBase; O13186.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Phosphorylation; Receptor;
KW Steroid-binding; Trans-acting factor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc-finger.
FT DOMAIN 1 420 Modulating.
FT DOMAIN 399 419 Glu/Ser/Pro/Thr-rich (PEST region)
FT (Potential).
FT DNA_BIND 421 486 Nuclear receptor-type.
FT ZN_FING 421 441 C4-type.
FT ZN_FING 457 481 C4-type.
FT DOMAIN 487 527 Hinge.
FT DOMAIN 528 777 Steroid-binding.
FT MOD_RES 113 113 Phosphoserine (By similarity).
FT MOD_RES 141 141 Phosphoserine (By similarity).
FT MOD_RES 203 203 Phosphoserine (By similarity).
FT MOD_RES 211 211 Phosphoserine (By similarity).
FT MOD_RES 226 226 Phosphoserine (By similarity).
SQ SEQUENCE 777 AA; 85611 MW; CE3CD9E8D6A4F3AB CRC64;
MDSKESLTPG KEENPSSVLT QERGNVMDFC KILRGGATLK VSVSSTSLAA ASQSDSKQQR
LLVDFPKGSV SNAQQPDLSK AVSLSMGLYM GETETKVMGN DLGFPQQGQI SLSSGETDLQ
LLEESIANLN RSTSVPENPK SSASSSVSAA PKEKEFPKTH SDVSSEQQNL KGQTGSNGGN
VKLYTADQST FDILQDLEFS SGSPGKETNQ SPWKSDLLID ENCLLSPLAG EEDSFLLEGN
SNEDCKPLIL PDTKPKIKDN GDLVLSSSSN VTLPQVKTEK EDFIELCTPG VIKQEKLSTV
YCQASFPGAN IIGNKMSAIS IHGVSTSGGQ MYHYDMNTAS LSQQQDQKPI FNVIPPIPVG
SENWNRCQGS GDDNLTSLGT LNFPGRTVFS NGYSSPSMRP DVSSPPSSSS TATTGPPPKL
CLVCSDEASG CHYGVLTCGS CKVFFKRAVE GQHNYLCAGR NDCIIDKIRR KNCPACRYRK
CLQAGMNLEA RKTKKKIKGI QQATTGVSQE TSENPANKTI VPATLPQLTP TLVSLLEVIE
PEVLYAGYDS TVPDSTWRIM TTLNMLGGRQ VIAAVKWAKA IPGFRNLHLD DQMTLLQYSW
MFLMAFALGW RSYRQASSNL LCFAPDLIIN EQRMTLPCMY DQCKHMLYVS SELHRLQVSY
EEYLCMKTLL LLSSVPKDGL KSQELFDEIR MTYIKELGKA IVKREGNSSQ NWQRFYQLTK
LLDSMHEVVE NLLNYCFQTF LDKTMSIEFP EMLAEIITNQ LPKYSNGNIK KLLFHQK
//