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Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1)

 GCR_SAISC               Reviewed;         778 AA.
O46567;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
18-JUL-2018, entry version 124.
RecName: Full=Glucocorticoid receptor;
Short=GR;
AltName: Full=Nuclear receptor subfamily 3 group C member 1;
Name=NR3C1; Synonyms=GRL;
Saimiri sciureus (Common squirrel monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Platyrrhini; Cebidae; Saimiriinae; Saimiri.
NCBI_TaxID=9521;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CORTISOL
AND DEXAMETHASONE.
TISSUE=Brain;
PubMed=10775802; DOI=10.1016/S0960-0760(00)00023-6;
Patel P.D., Lyons D.M., Zhang Z., Ngo H., Schatzberg A.F.;
"Impaired transactivation of the glucocorticoid receptor cloned from
the Guyanese squirrel monkey.";
J. Steroid Biochem. Mol. Biol. 72:115-123(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INDUCTION.
PubMed=11703081; DOI=10.1006/gcen.2001.7696;
Scammell J.G., Denny W.B., Valentine D.L., Smith D.F.;
"Overexpression of the FK506-binding immunophilin FKBP51 is the common
cause of glucocorticoid resistance in three New World primates.";
Gen. Comp. Endocrinol. 124:152-165(2001).
[3]
TISSUE SPECIFICITY.
PubMed=11165305; DOI=10.1016/S0022-3956(00)00035-2;
Patel P.D., Lopez J.F., Lyons D.M., Burke S., Wallace M.,
Schatzberg A.F.;
"Glucocorticoid and mineralocorticoid receptor mRNA expression in
squirrel monkey brain.";
J. Psychiatr. Res. 34:383-392(2000).
[4]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLN-120; GLN-210;
ALA-517; THR-552; ALA-617; SER-619 AND LEU-762.
PubMed=15857751; DOI=10.1016/j.jsbmb.2004.11.010;
Her S., Patel P.D., Schatzberg A.F., Lyons D.M.;
"Mutations in squirrel monkey glucocorticoid receptor impair nuclear
translocation.";
J. Steroid Biochem. Mol. Biol. 94:319-326(2005).
-!- FUNCTION: Receptor for glucocorticoids (GC) (PubMed:10775802,
PubMed:11703081). Has a dual mode of action: as a transcription
factor that binds to glucocorticoid response elements (GRE), both
for nuclear and mitochondrial DNA, and as a modulator of other
transcription factors (PubMed:10775802, PubMed:11703081,
PubMed:15857751). Affects inflammatory responses, cellular
proliferation and differentiation in target tissues. Involved in
chromatin remodeling (By similarity). Plays a role in rapid mRNA
degradation by binding to the 5' UTR of target mRNAs and
interacting with PNRC2 in a ligand-dependent manner which recruits
the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading
to RNA decay (By similarity). Could act as a coactivator for
STAT5-dependent transcription upon growth hormone (GH) stimulation
and could reveal an essential role of hepatic GR in the control of
body growth (By similarity). Mediates glucocorticoid-induced
apoptosis (By similarity). Promotes accurate chromosome
segregation during mitosis (By similarity). May act as a tumor
suppressor (By similarity). May play a negative role in
adipogenesis through the regulation of lipolytic and antilipogenic
gene expression (By similarity). {ECO:0000250|UniProtKB:P04150,
ECO:0000250|UniProtKB:P06537, ECO:0000269|PubMed:10775802,
ECO:0000269|PubMed:11703081, ECO:0000269|PubMed:15857751}.
-!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90AA1,
HSPA1A/HSPA1B, and FKBP5 or another immunophilin such as PPID,
STIP1, or the immunophilin homolog PPP5C. Upon ligand binding
FKBP5 dissociates from the complex and FKBP4 takes its place,
thereby linking the complex to dynein and mediating transport to
the nucleus, where the complex dissociates. Probably forms a
complex composed of chaperones HSP90 and HSP70, co-chaperones
CDC37, PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and
NR3C1; this complex does not contain co-chaperones STIP1/HOP and
PTGES3/p23. Directly interacts with UNC45A. Binds to DNA as a
homodimer, and as heterodimer with NR3C2 or the retinoid X
receptor. Binds STAT5A and STAT5B homodimers and heterodimers.
Interacts with NRIP1, POU2F1, POU2F2 and TRIM28. Interacts with
several coactivator complexes, including the SMARCA4 complex,
CREBBP/EP300, TADA2L (Ada complex) and p160 coactivators such as
NCOA2 and NCOA6. Interaction with BAG1 inhibits transactivation.
Interacts with HEXIM1, PELP1 and TGFB1I1. Interacts with NCOA1.
Interacts with NCOA3, SMARCA4, SMARCC1, SMARCD1, and SMARCE1.
Interacts with CLOCK, CRY1 and CRY2 in a ligand-dependent fashion.
Interacts with CIART. Interacts with RWDD3. Interacts with
UBE2I/UBC9 and this interaction is enhanced in the presence of
RWDD3. Interacts with GRIP1. Interacts with NR4A3 (via nuclear
receptor DNA-binding domain), represses transcription activity of
NR4A3 on the POMC promoter Nur response element (NurRE). Directly
interacts with PNRC2 to attract and form a complex with UPF1 and
DCP1A; the interaction leads to rapid mRNA degradation. Interacts
with GSK3B. Interacts with FNIP1 and FNIP2. Interacts (via C-
terminus) with HNRNPU (via C-terminus).
{ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06536,
ECO:0000250|UniProtKB:P06537}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15857751}.
Nucleus {ECO:0000269|PubMed:15857751}. Mitochondrion
{ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:P04150}. Note=After ligand activation,
translocates from the cytoplasm to the nucleus.
{ECO:0000269|PubMed:15857751}.
-!- TISSUE SPECIFICITY: Expressed in brain. Regions of high expression
include CA1 and CA2 of hippocampus, dentate gyrus, paraventricular
hypothalamus, lateral geniculate, lateral-medial amygdala, and
cerebellum. In the cerebral cortex, laminar patterns of expression
were apparent in all cortical layers, particularly the pyramidal
cell-rich layers II/III and V. {ECO:0000269|PubMed:11165305}.
-!- INDUCTION: Binding activity reduced by FKBP5.
{ECO:0000269|PubMed:11703081}.
-!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
a DNA-binding domain and a C-terminal ligand-binding domain. The
ligand-binding domain is required for correct chromosome
segregation during mitosis although ligand binding is not
required. {ECO:0000250|UniProtKB:P04150}.
-!- PTM: Acetylation by CLOCK reduces its binding to glucocorticoid
response elements and its transcriptional activity. {ECO:0000250}.
-!- PTM: Increased proteasome-mediated degradation in response to
glucocorticoids. {ECO:0000250|UniProtKB:P04150}.
-!- PTM: Phosphorylated in the absence of hormone; becomes
hyperphosphorylated in the presence of glucocorticoid. The Ser-
203, Ser-226 and Ser-404-phosphorylated forms are mainly
cytoplasmic, and the Ser-211-phosphorylated form is nuclear.
Phosphorylation at Ser-211 increases transcriptional activity.
Phosphorylation at Ser-203, Ser-226 and Ser-404 decreases
signaling capacity. Phosphorylation at Ser-404 may protect from
glucocorticoid-induced apoptosis. Phosphorylation at Ser-203 and
Ser-211 is not required in regulation of chromosome segregation.
May be dephosphorylated by PPP5C, attenuates NR3C1 action.
{ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
-!- PTM: Ubiquitinated; restricts glucocorticoid-mediated
transcriptional signaling. {ECO:0000250|UniProtKB:P06537}.
-!- PTM: Sumoylation at Lys-277 and Lys-293 negatively regulates its
transcriptional activity. Sumoylation at Lys-704 positively
regulates its transcriptional activity in the presence of RWDD3.
Sumoylation at Lys-277 and Lys-293 is dispensable whereas
sumoylation at Lys-704 is critical for the stimulatory effect of
RWDD3 on its transcriptional activity. Heat shock increases
sumoylation in a RWDD3-dependent manner.
{ECO:0000250|UniProtKB:P06536}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF041834; AAB97369.1; -; mRNA.
EMBL; AF337042; AAK01303.1; -; mRNA.
ProteinModelPortal; O46567; -.
SMR; O46567; -.
HOVERGEN; HBG007583; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0003700; F:DNA binding transcription factor activity; ISS:UniProtKB.
GO; GO:0038050; F:RNA polymerase II transcription factor activity, glucocorticoid-activated sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISS:UniProtKB.
GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR001409; Glcrtcd_rcpt.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF02155; GCR; 1.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00528; GLCORTICOIDR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
Acetylation; Chromatin regulator; Cytoplasm; Cytoskeleton;
DNA-binding; Isopeptide bond; Lipid-binding; Metal-binding;
Methylation; Mitochondrion; Nucleus; Phosphoprotein; Receptor;
Steroid-binding; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 778 Glucocorticoid receptor.
/FTId=PRO_0000053676.
DOMAIN 525 759 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 421 486 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 421 441 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 457 481 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
REGION 1 420 Modulating.
REGION 485 778 Interaction with CLOCK. {ECO:0000250}.
REGION 487 524 Hinge.
REGION 533 698 Interaction with CRY1. {ECO:0000250}.
COMPBIAS 399 419 Glu/Pro/Ser/Thr-rich (PEST region).
MOD_RES 8 8 Phosphothreonine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 23 23 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 45 45 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 113 113 Phosphoserine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 134 134 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000250|UniProtKB:P06537}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 267 267 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 404 404 Phosphoserine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 480 480 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 492 492 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 494 494 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04150}.
MOD_RES 495 495 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 258 258 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P04150}.
CROSSLNK 419 419 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:P06537}.
CROSSLNK 704 704 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:P04150}.
MUTAGEN 120 120 Q->L: No effect on nuclear translocation
or transactivation.
{ECO:0000269|PubMed:15857751}.
MUTAGEN 210 210 Q->E: No effect on nuclear translocation
or transactivation.
{ECO:0000269|PubMed:15857751}.
MUTAGEN 517 517 A->G: No effect on nuclear translocation.
{ECO:0000269|PubMed:15857751}.
MUTAGEN 552 552 T->S: Increased nuclear translocation;
when associated with S-617 and A-619.
{ECO:0000269|PubMed:15857751}.
MUTAGEN 617 617 A->S: Increased nuclear translocation.
when associated with S-552 and A-619.
{ECO:0000269|PubMed:15857751}.
MUTAGEN 619 619 S->A: Increased nuclear translocation.
when associated with S-552 and S-617.
{ECO:0000269|PubMed:15857751}.
MUTAGEN 762 762 L->I: No effect on nuclear translocation.
{ECO:0000269|PubMed:15857751}.
CONFLICT 498 498 Missing (in Ref. 2; AAK01303).
{ECO:0000305}.
SEQUENCE 778 AA; 85738 MW; 721B8203939D1389 CRC64;
MDSKESLTPG KEENPSSVLT QERGNVMDFC KILRGGATLK VSVSSTSLAA ASQSDSKQQR
LLVDFPKGSV SNAQQPDLSK AVSLSMGLYM GETETKVMGN DLGFPQQGQI SLSSGETDLQ
LLEESIANLN RSTSVPENPK SSASSSVSAA PKEKEFPKTH SDVSSEQQNL KGQTGTNGGN
VKLYTADQST FDILQDLEFS SGSPGKETNQ SPWKSDLLID ENCLLSPLAG EEDSFLLEGN
SNEDCKPLIL PDTKPKIKDN GDLVLSSSSN VTLPQVKTEK EDFIELCTPG VIKQEKLSTV
YCQASFPGAN IIGNKMSAIS IHGVSTSGGQ MYHYDMNTAS LSQQQDQKPI FNVIPPIPVG
SENWNRCQGS GDDNLTSLGT LNFPGRTVFS NGYSSPSMRP DVSSPPSSSS TATTGPPPKL
CLVCSDEASG CHYGVLTCGS CKVFFKRAVE GQHNYLCAGR NDCIIDKIRR KNCPACRYRK
CLQAGMNLEA RKTKKKIIKG IQQATTGVSQ ETSENPANKT IVPATLPQLT PTLVSLLEVI
EPEVLYAGYD STVPDSTWRI MTTLNMLGGR QVIAAVKWAK AIPGFRNLHL DDQMTLLQYS
WMFLMAFALG WRSYRQASSN LLCFAPDLII NEQRMTLPCM YDQCKHMLYV SSELHRLQVS
YEEYLCMKTL LLLSSVPKDG LKSQELFDEI RMTYIKELGK AIVKREGNSS QNWQRFYQLT
KLLDSMHEVV ENLLNYCFQT FLDKTMSIEF PEMLAEIITN QLPKYSNGNI KKLLFHQK


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