GCR_XENLA
ID GCR_XENLA Reviewed; 776 AA.
AC P49844;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Embryo;
RX PubMed=8018720; DOI=10.1016/0167-4781(94)90010-8;
RA Gao X., Kalkhoven E., Peterson-Maduro J., van der Burg B., Destree O.H.J.;
RT "Expression of the glucocorticoid receptor gene is regulated during early
RT embryogenesis of Xenopus laevis.";
RL Biochim. Biophys. Acta 1218:194-198(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] 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) (PubMed:8018720). Has a
CC dual mode of action: as a transcription factor that binds to
CC glucocorticoid response elements (GRE), both for nuclear and
CC mitochondrial DNA, and as a modulator of other transcription factors
CC (By similarity). Affects inflammatory responses, cellular proliferation
CC and differentiation in target tissues (By similarity). Involved in
CC chromatin remodeling (By similarity). 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 (By
CC similarity). Could act as a coactivator for STAT5-dependent
CC transcription upon growth hormone (GH) stimulation and could reveal an
CC essential role of hepatic GR in the control of body growth (By
CC similarity). Mediates glucocorticoid-induced apoptosis (By similarity).
CC Promotes accurate chromosome segregation during mitosis (By
CC similarity). May act as a tumor suppressor (By similarity). May play a
CC negative role in adipogenesis through the regulation of lipolytic and
CC antilipogenic gene expression (By similarity).
CC {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537,
CC ECO:0000269|PubMed:8018720}.
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 -!- TISSUE SPECIFICITY: Expressed in liver with relative abundance.
CC {ECO:0000269|PubMed:8018720}.
CC -!- DEVELOPMENTAL STAGE: Rareley expressed between embryonic stages 17 and
CC 24. Expression starts from stage 32. {ECO:0000269|PubMed:8018720}.
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; X72211; CAA51010.1; -; mRNA.
DR EMBL; X77764; CAA54804.1; -; mRNA.
DR PIR; S45348; S44047.
DR AlphaFoldDB; P49844; -.
DR SMR; P49844; -.
DR Proteomes; UP000186698; Genome assembly.
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; PR00528; GLCORTICOIDR.
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; Reference proteome;
KW Steroid-binding; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..776
FT /note="Glucocorticoid receptor"
FT /id="PRO_0000053681"
FT DOMAIN 523..757
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 420..485
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 420..440
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 456..480
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..419
FT /note="Modulating"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..522
FT /note="Hinge"
FT CONFLICT 502
FT /note="S -> P (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="T -> A (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="T -> A (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="P -> N (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="L -> M (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 544
FT /note="Y -> F (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="I -> M (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="S -> R (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="L -> M (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="L -> I (in Ref. 2; CAA54804)"
FT /evidence="ECO:0000305"
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
