Swiss-Prot entry

ID   GCR_RABIT      STANDARD;      PRT;   772 AA.
AC   P59667;
DT   10-OCT-2003 (Rel. 42, Created)
DT   10-OCT-2003 (Rel. 42, Last sequence update)
DT   01-MAY-2005 (Rel. 47, Last annotation update)
DE   Glucocorticoid receptor (GR).
GN   Name=NR3C1; Synonyms=GRL;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; 
OC   Oryctolagus. 
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lens epithelium;
RA   James E.R., Robertson L.L.;
RT   "Rabbit glucocorticoid receptor from lens epithelial cells.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
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; AY161275; AAN75442.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   HSSP; P06536; 1GDC. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR   SMR; P59667; 412-490, 518-772.
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; P59667.
DR   ProtoNet; P59667.
DR   ProtoMap; P59667.
DR   PRESAGE; P59667.
DR   DIP; P59667.
DR   ModBase; P59667.
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      528    772       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   772 AA;  84863 MW;  C16D6CF799F83148 CRC64;
     MDSKESLSPP GREEVPSSVL RPAERGNVMD LYKTLRGGAP VRVPASSPSL APAAQPDSKQ
     QRLAVDFPKG SASNAQQPDL SRAVSLSMGL YMGETETKVM GSDLAFPQQG QTSLSSGETD
     FRLLEESIAS LNRSASGADN PRSTAPAAGS AAPTEGFPKT HSDLASERQN PKGQTGGSAG
     SAKLHPTDQS TFDILQDLEF SGSPSKDRSE SPWRSDLLMD ENCLLSPLAG EDDPFLLEGN
     SSEDCKPLIL PDTKPKIKDN GDLILSNSNN VPLPQVKTEK EDFIELCTPG VIKQEKLGPV
     YCQASFSGAN IIGNKISAIS VHGVSTSGGQ MYHYDMNAQQ QEQKPLFNVI PPIPVGSENW
     NRCQGSGDDN LTSLGTMNFP GRSVFSNGYS SPGMRPDVSS PPSNSTTAAG PPPKLCLVCS
     DEASGCHYGV LTCGSCKVFF KRAVKGQHNY LCAGRNDCII DKIRRKNCPA CRYRKCLQAG
     MNLEARKTKK KIKGIQQTST GVSQETSENP SNRTVVPAAL PQLTPTLVSL LEVIEPEVLY
     AGYDSSVPDS TWRIMTTLNM LGGRQVIAAV KWAKAIPGFR NLHLDDQMTL LQYSWMFLMA
     FALGWRSYKQ SSGNMLCFAP DLVINEQRMT LPYMYDQCKH MLFVSSELKR LQVSYEEYLC
     MKTLLLLSTV PKEGLKSQEL FDEIRMTYIK ELGKAIVKRE GNSSQNWQRF YQLTKLLDSM
     HEVVENLLHY CFQTFLDKTM SIEFPEMLAE IITNQIPKYS NGNIKKLLFH QK
//