Swiss-Prot entry
ID GCR_TUPGB STANDARD; PRT; 776 AA.
AC Q95267;
DT 01-NOV-1997 (Rel. 35, Created)
DT 01-NOV-1997 (Rel. 35, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Glucocorticoid receptor (GR).
GN Name=NR3C1; Synonyms=GRL;
OS Tupaia glis belangeri (Common tree shrew).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Scandentia; Tupaiidae; Tupaia.
OX NCBI_TaxID=37347;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain;
RX MEDLINE=98250805; PubMed=9582428 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/S0169-328X(98)00004-7;
RA Meyer U., Kruhoeffer M., Flugge G., Fuchs E.;
RT "Cloning of glucocorticoid receptor and mineralocorticoid receptor
RT cDNA and gene expression in the central nervous system of the tree
RT shrew (Tupaia belangeri).";
RL Brain Res. Mol. Brain Res. 55:243-253(1998).
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; Z75079; CAA99379.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P06536; 1RGD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q95267; 416-490, 522-776.
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; Q95267.
DR ProtoNet; Q95267.
DR ProtoMap; Q95267.
DR PRESAGE; Q95267.
DR DIP; Q95267.
DR ModBase; Q95267.
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 1 419 Modulating.
FT DOMAIN 399 418 Glu/Ser/Pro/Thr-rich (PEST region)
FT (Potential).
FT DNA_BIND 417 492 Nuclear receptor-type.
FT DNA_BIND 420 485 Nuclear receptor-type.
FT ZN_FING 420 440 C4-type.
FT ZN_FING 456 480 C4-type.
FT DOMAIN 486 526 Hinge.
FT DOMAIN 527 776 Steroid-binding.
FT MOD_RES 113 113 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 776 AA; 85838 MW; 972C1CA2334C6058 CRC64;
MDSKESLTSP SEEIPSSVHG QERGNVMDFY KTRRGGATVK VFMPSPSLGG SSQSDSKQQR
LLVDFPKGSV SNVQQPDLSK AVSLSMGLYM GETETKVMGN DLGFPQQGQI TLSSGETNLQ
LLEESIANLN RSTSVPEHPK ISASVAVSAA LLKKELPETP SDVSSEQQNL KGQTGTNGGN
VKLCTADQST FDILQDLEFS SASPGRETNE SPWRSDLLLD ENCLLSPLAV EDDPFLSEGN
LKEDCKPLIL PDTKPKIKDN GDLILSSPKN VPLPQVKTEK EDFIELCTPG VIKQEKLGPV
YCQANFSGAN IIGNKMSAIS VHGVSTSGGQ MYHYDMNTAT LSQQQDQKPI FNVIPPIPVS
SENWNRCQGS GDENLTSLGT LNFSGRSVFS NGYSSPGMRP DVSSPPSNSL SAVGPPPKFC
LVCSDEASGC HYGVLTCGSC KVFFKRAVEG QHNYLCAGRN DCIIDKIRRK NCPACRYRKC
LQAGMNLEAR KTKKKIKGIQ QTTTGISQET PENSANKTIV PATLPQLTPT PVSLLEVIEP
EVLYAGYDSS LPDTTWRIMS ALNMLGGRQV IAAVKWAKAI PGFRNLHLDD QMTLLQYSWM
FLMAFALGWR SYKQASANLL CFAPDLIINE QRMSLPFMYD QCKHMLFVSS ELQRLQVSYE
EYLCMKTLLL LSSVPKEGLK SQELFDEIRM TYIKELGKAI VKREGNSSQN WQRFYQLTKL
LDSMHDVVEN LLNYCFQTFL DKTMRIEFPE MLAEIITNQI PKYSSGNIKK LLFHQK
//