Swiss-Prot entry
ID GCR_CAVPO STANDARD; PRT; 771 AA.
AC P49115;
DT 01-FEB-1996 (Rel. 33, Created)
DT 01-FEB-1996 (Rel. 33, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Glucocorticoid receptor (GR).
GN Name=NR3C1; Synonyms=GRL;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC Hystricognathi; Caviidae; Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Liver;
RX MEDLINE=94329100; PubMed=8052264 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1210/me.8.4.431;
RA Keightley M.C., Fuller P.J.;
RT "Unique sequences in the guinea pig glucocorticoid receptor induce
RT constitutive transactivation and decrease steroid sensitivity.";
RL Mol. Endocrinol. 8:431-439(1994).
RN [2]
RP ERRATUM.
RA Keightley M.C., Fuller P.J.;
RL Mol. Endocrinol. 8:731-731(1994).
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 a heterodimer
CC with NR3C2 or the retinoid X receptor. Interacts with the
CC coactivator NCOA6, leading to a strong increase in transcription
CC of target genes. Interaction with numerous other transcription
CC factors modulates transcription activation. Interacts with TRIM28
CC (By 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; L13196; AAA61612.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P06536; 1GDC. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P49115; 412-486, 517-771.
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; P49115.
DR ProtoNet; P49115.
DR ProtoMap; P49115.
DR PRESAGE; P49115.
DR DIP; P49115.
DR ModBase; P49115.
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 1 415 Modulating.
FT DOMAIN 395 414 Glu/Ser/Pro/Thr-rich (PEST region)
FT (Potential).
FT DNA_BIND 416 481 Nuclear receptor-type.
FT ZN_FING 416 436 C4-type.
FT ZN_FING 452 476 C4-type.
FT DOMAIN 482 522 Hinge.
FT DOMAIN 523 771 Steroid-binding.
FT DOMAIN 48 51 Poly-Ala.
FT DOMAIN 403 406 Poly-Ser.
FT DOMAIN 663 666 Poly-Leu.
FT MOD_RES 148 148 Phosphothreonine (By similarity).
FT MOD_RES 199 199 Phosphoserine (By similarity).
FT MOD_RES 207 207 Phosphoserine (By similarity).
FT MOD_RES 222 222 Phosphoserine (By similarity).
FT MOD_RES 303 303 Phosphoserine (By similarity).
SQ SEQUENCE 771 AA; 84862 MW; 4C0710E9C980F09E CRC64;
MDLKESVTSS KEVPSSVLGS ERRNVIDFYK TVRGGATVKV SASSPSLAAA AQSDSKQRRL
LVDFPKGSGS NAQQPDLSKA VSLSMGLYMG ETETKVMGND LGFPQQGQIS LPSGETDFRL
LEESIANLSR STSVPENPKN SASAVSGTPT EEFPKTQSDL SSEQENLKSQ AGTNGGNVKF
PPDQSTFDIL KDLEFSSGSP GKERSESPWR PDLLMDESCL LSPLAGEDDP FLLEGNSNED
CKPLILPDTK PKIKDNGDGI LSSSNSVPQP QVKIGKEDFI ELCTPGVIKQ EKLGPVYCQA
SFSGANIIGN KMSAISVHGV STSGGQMYHY DMNTASLSQQ QDQKPIFNVI PPIPVGSENW
NRCQGSGEDN LTSLGTVNFP GRSVFSNGYS SPGLRPDVSS PPSSSSTTTG PPPKLCLVCS
DELSGCHYGV LTCGSCKVFF KRAVEGQHNY LCAGRNDCII DKIRRENCPA CRYRKCLQAG
MNLQARKTKK KIKGIQQATT GVSQNTSENP NKTIVPATLP QLTPTLVSLL EVIEPEVIHS
GYDSTSPDST WRIMTTLNML GGRQVIAAVK WAKAIPGFKN LHLDDQMTLL QYSWMFLMAF
ALGWRSYKQS NGSLLCFAPD LIINEQRMSL PWMYDQCRYM LYVSSELKRL QVSYEEYLCM
KTLLLLSSVP KEGLKSQELF DEIRMTYIKE LGKAIVKREG NSSQNWQRFY QLTKLLDSLH
EIVGNLLNIC FKTFLDKTMN IEFPEMLAEI ITNQLPKYSN GDIKKLLFHQ K
//