Swiss-Prot entry
ID GCR_XENLA STANDARD; PRT; 776 AA.
AC P49844;
DT 01-OCT-1996 (Rel. 34, Created)
DT 01-OCT-1996 (Rel. 34, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Glucocorticoid receptor (GR).
GN Name=NR3C1; Synonyms=GRL;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Embryo;
RX MEDLINE=94289478; PubMed=8018720 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1016/0167-4781(94)90010-8;
RA Gao X., Kalkhoven E., Peterson-Maduro J., van der Burg B.,
RA Destree O.H.J.;
RT "Expression of the glucocorticoid receptor gene is regulated during
RT early embryogenesis of Xenopus laevis.";
RL Biochim. Biophys. Acta 1218:194-198(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 452-776.
RC TISSUE=Liver;
RA Picard D.;
RL Submitted (FEB-1994) 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. Upon
CC ligand binding the complex undergoes a conformation change and
CC moves to the nucleus, where it dissociates. Binds to DNA as a
CC homodimer, and as heterodimer with NR3C2. Interaction with
CC numerous other transcription factors modulates transcription
CC activation (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 -!- 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; X72211; CAA51010.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; X77764; CAA54804.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; S45348; S44047.
DR HSSP; P06536; 1GDC. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P49844; 416-494, 522-776.
DR TRANSFAC; T04685; -.
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; P49844.
DR ProtoNet; P49844.
DR ProtoMap; P49844.
DR PRESAGE; P49844.
DR DIP; P49844.
DR ModBase; P49844.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Steroid-binding;
KW Trans-acting factor; Transcription; Transcription regulation;
KW Zinc-finger.
FT DOMAIN 1 419 Modulating.
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 CONFLICT 502 502 S -> P (in Ref. 2).
FT CONFLICT 504 504 T -> A (in Ref. 2).
FT CONFLICT 506 506 T -> A (in Ref. 2).
FT CONFLICT 511 511 P -> N (in Ref. 2).
FT CONFLICT 519 519 L -> M (in Ref. 2).
FT CONFLICT 544 544 Y -> F (in Ref. 2).
FT CONFLICT 551 551 I -> M (in Ref. 2).
FT CONFLICT 654 654 S -> R (in Ref. 2).
FT CONFLICT 740 740 L -> M (in Ref. 2).
FT CONFLICT 768 768 L -> I (in Ref. 2).
SQ SEQUENCE 776 AA; 84977 MW; DCB7D051B361872B CRC64;
MDPKDLLKPS SGSPAVRGSP HYNDKPGNVI EFFGNYRGGV SVSVSASCPT STASQSNTRQ
QQHFQKQLTA TGDSTNGLNN NVPQPDLSKA VSLSMGLYMG ESDTKVMSSD IAFPSQEQIG
ISTGETDFSL LEESIANLQA KSLAPDKLIE ISEDPGGFKC DISAQPRPSM GQGGSNGSSS
TNLFPKDQCT FDLLRDLGIS PDSPLDGKSN PWLDPLFDEQ EAFNLLSPLG TGDPFFMKSE
VLSEGSKTLS LEDGTQRLGD HAKDMLLPSA DRPISQVKTE KEDYIELCTP GVVNEEKFGP
VYCVGNFSGS GLFGNKSSAI SVHGVSTSGG QMYHYDLNTA TISQQDVKPV FNLGSPGTSI
AEGWNRCHGS GNDTAASPGN VNFPNRSVFS NGYSSPGIRS DASPSPSTSS TSTGPPPKLC
LVCSDEASGC HYGVLTCGSC KVFFKRAVEG QHNYLCAGRN DCIIDKIRRK NCPACRYRKC
LQAGMNLEAR KTKKKIKGIQ QSTTATARES PETSMTRTLV PASVAQLTPT LISLLEVIEP
EVLYSGYDSS IPDTTRRLMS SLNMLGGRQV VSAVRWAKAI PGFRNLHLDD QMTLLQYSWM
FLMVFALGWR SYKQTNGSIL YFAPDLVITE DRMHLPFMQE RCQEMLKIAG EMSSLQISYD
EYLCMKVLLL MCTIPKEGLK SHALFEEIRM TYIKELGKAI VKREGNSSQN WQRFYQLTKL
LDSMHEVAEN LLAFCFLSFL DKSMSIEFPD MLSEIISNQI PKYSSGNLKK LLFHQK
//