GCR_PAROL
ID GCR_PAROL Reviewed; 807 AA.
AC O73673;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glucocorticoid receptor;
DE Short=GR;
DE AltName: Full=Nuclear receptor subfamily 3 group C member 1;
GN Name=nr3c1; Synonyms=grl;
OS Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Paralichthyidae;
OC Paralichthys.
OX NCBI_TaxID=8255;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Tokuda Y.;
RT "Japanese flounder mRNA for glucocorticoid receptor, complete cds.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for glucocorticoids (GC). Has a dual mode of action:
CC as a transcription factor that binds to glucocorticoid response
CC elements (GRE), both for nuclear and mitochondrial DNA, and as a
CC modulator of other transcription factors. Affects inflammatory
CC responses, cellular proliferation and differentiation in target
CC tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA
CC degradation by binding to the 5' UTR of target mRNAs and interacting
CC with PNRC2 in a ligand-dependent manner which recruits the RNA helicase
CC UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay. Could
CC act as a coactivator for STAT5-dependent transcription upon growth
CC hormone (GH) stimulation and could reveal an essential role of hepatic
CC GR in the control of body growth. Mediates glucocorticoid-induced
CC apoptosis. Promotes accurate chromosome segregation during mitosis. May
CC act as a tumor suppressor. May play a negative role in adipogenesis
CC through the regulation of lipolytic and antilipogenic gene expression.
CC {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
CC -!- SUBUNIT: Heteromultimeric cytoplasmic complex with HSP90. Upon ligand
CC binding the complex undergoes a conformation change and moves to the
CC nucleus, where it dissociates. Binds to DNA as a homodimer, and as
CC heterodimer with NR3C2. Interaction with numerous other transcription
CC factors modulates transcription activation (By similarity).
CC {ECO:0000250|UniProtKB:P04150}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus
CC {ECO:0000250|UniProtKB:P04150}. Mitochondrion
CC {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P04150}.
CC Note=After ligand activation, translocates from the cytoplasm to the
CC nucleus. {ECO:0000250|UniProtKB:P04150}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain. The ligand-
CC binding domain is required for correct chromosome segregation during
CC mitosis although ligand binding is not required.
CC {ECO:0000250|UniProtKB:P04150}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000305}.
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DR EMBL; AB013444; BAA25997.1; -; mRNA.
DR RefSeq; XP_019952853.1; XM_020097294.1.
DR AlphaFoldDB; O73673; -.
DR SMR; O73673; -.
DR GeneID; 109635852; -.
DR KEGG; pov:109635852; -.
DR OrthoDB; 333292at2759; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0004883; F:nuclear glucocorticoid receptor activity; IEA:InterPro.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; ISS:UniProtKB.
DR GO; GO:1990239; F:steroid hormone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:UniProtKB.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR001409; Glcrtcd_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF02155; GCR; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; Cytoplasm; Cytoskeleton; DNA-binding; Lipid-binding;
KW Metal-binding; Mitochondrion; Nucleus; Receptor; Steroid-binding;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..807
FT /note="Glucocorticoid receptor"
FT /id="PRO_0000053680"
FT DOMAIN 554..788
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 445..519
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 445..465
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 490..514
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..444
FT /note="Modulating"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..553
FT /note="Hinge"
FT COMPBIAS 246..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..276
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 807 AA; 88986 MW; F075E7784A394728 CRC64;
MDQGGLKRNC NRDDSLTFGE TAVGVGSDTG DTAGSLLQPA AMHLPSPSSL PQLTVAPNGG
AGTKDQGEFG GLFESPRGQC EGSEMKEGKI IRLQKRKHHL DIGMFNMEDN LSLLNQNISD
LNRTSTSVIS TSDTSVLGKL PLPNLFPQHI KQEGGFSLEK ELGTYGGHTG GGPCDLDGNS
GHLIEDTEIW QDLDLPNSLP EISDFELDSE VAHLDNILHD SSGGCGPDGS LLKETKVLVG
NGGNCTDVNG TDQQHPLQHH QHQQQQHRHL LQHQQHQLHH QHQQPPSLLS SVMIKEEKDH
DNSFIHIRTP GVVKQEKQEN GSFCQSQCLQ SSMSSLHGGG PMSSTMGAGA VPGYHYKASP
SSTVGLQDQK PFGIFSNLPA VAESWTRGGR FGEPSGIQRG NDGLPSAAMS PFSVSFSSSS
PRTGENSSSA VPGLSKPSGP THKICLVCSD EASGCHYGVV TCGSCKVFFK RAVEGWRARQ
NTDGQHNYLC AGRNDCIIDK IRRKNCPACR FRKCLQAGMN LEARKNKKLI KMKVHRPTGS
AEPISNMPVP VIPRMPQLVP TMLSVLKAIE PEIIYSGYDS TLPDTSTRLM TTLNRLGGQQ
VISAVKWAKS LPGFRNLHLD DQMTLLQCSW LFLMSFSLGW RSYEQCNGNM LCFAPDLVIN
KERMKLPFMT DQCEQMLKIC NEFVRLQVSY DEYLCMKVLL LLSTVPKDGL KSQAVFDEIR
MTYIKELGKA IVKREENASQ NWQRFYQLTK LLDSMQEMVE GLLQICFYTF VNKTLSVEFP
EMLAEIITNQ IPKFKDGSVK PLLFHQK
