Swiss-Prot entry
ID GCR_ONCMY STANDARD; PRT; 758 AA.
AC P49843;
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 Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Euteleostei;
OC Protacanthopterygii; Salmoniformes; Salmonidae; Oncorhynchus.
OX NCBI_TaxID=8022;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=95377204; PubMed=7649084 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1210/en.136.9.3774;
RA Ducouret B., Tujague M., Ashraf J., Mouchel N., Servel N.,
RA Valotaire Y., Thompson E.B.;
RT "Cloning of a teleost fish glucocorticoid receptor shows that it
RT contains a deoxyribonucleic acid-binding domain different from that of
RT mammals.";
RL Endocrinology 136:3774-3783(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RX PubMed=8766708 [NCBI, ExPASy, EBI, Israel, Japan];
RA Takeo J., Hata J., Segawa C., Toyohara H., Yamashita S.;
RT "Fish glucocorticoid receptor with splicing variants in the DNA
RT binding domain.";
RL FEBS Lett. 389:244-248(1996).
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. Interacts with TRIM28 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic in the absence of ligand;
CC nuclear after ligand-binding (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49843-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49843-2; Sequence=VSP_012542;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed in most tissues.
CC Isoform 2 is found only in testis.
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; Z54210; CAA90937.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; S60586; S60586.
DR HSSP; P06536; 1RGD. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P49843; 381-466, 499-750.
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; 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; P49843.
DR ProtoNet; P49843.
DR ProtoMap; P49843.
DR PRESAGE; P49843.
DR DIP; P49843.
DR ModBase; P49843.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Alternative splicing; DNA-binding; Nuclear protein; Receptor;
KW Steroid-binding; Trans-acting factor; Transcription;
KW Transcription regulation; Zinc-finger.
FT DOMAIN 1 386 Modulating.
FT DNA_BIND 387 461 Nuclear receptor-type.
FT ZN_FING 387 407 C4-type.
FT ZN_FING 432 456 C4-type.
FT DOMAIN 462 502 Hinge.
FT DOMAIN 503 758 Steroid-binding.
FT VARSPLIC 417 425 Missing (in isoform 2).
FT /FTId=VSP_012542.
SQ SEQUENCE 758 AA; 83345 MW; 429CDCCBEB35DB5D CRC64;
MDPGGLKHSK DKGLAFGKLS ESSVEGSFSG DTGGSKSTTS TSLMHLPGSR PQPPARDSAN
GLNVTTTQME LSTGGLTIEE AEVKVMEKAI RMQQPQKPQQ NQQLFENFAL LEASIADLNR
SNTPGSSVLG RPHDLFSLKT ENFSPMDKDR LDMGSVSFGQ SQKDLDVNER LLGDNTMDIL
QDLDLPGSLS DLNEFYVSDE AAFLSSLSVE DVLLEDGNME TKPIDCSNGG NCTNVDSADQ
QKQLLEAGVS MPVIKTEEDA DTSFIQLCTP GVIKQENDRR SFCQISSLDL PSTHNSAGSI
SGPSYPYGAN TSTAVSLQQD QKPVFGLYPP LPSVSDSWNR GNGYATGSGM SSSSFPVGFS
SPKARPEASG SASSAPAKPS GPTHKICLVC SDEASGCHYG VLTCGSCKVF FKRAVEGWRA
RQNTDGQHNY LCAGRNDCII DKIRRKNCPA CRFRKCLQAG MNLEARKNKK LIRLKGQQTT
MEPNPPPPDE RACALIPKSM PQLVPTMLSL LKAIEPEAIY SGYDSTIPDT STRLMTTLNR
LGGQQVVSAV KWAKSLPGFR NLHLDDQMTL LQCSWLFLMS FGLGWRSYQQ CNGGMLCFAP
DLVINDERMK LPYMTDQCEQ MLKISTEFVR LQVSYDEYLC MKVLLLLSTV PKDGLKSQAV
FDEIRMTYIK ELGKAIVKRE ENSSQNWQRF YQLTKLLDSM QEMVGGLLQI CFYTFVNKSL
SVEFPEMLAE IISNQLPKFK DGSVKPLLFH ALNHDTMP
//