ID A0A2D0SEE8_ICTPU Unreviewed; 757 AA.
AC A0A2D0SEE8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Glucocorticoid receptor {ECO:0000256|ARBA:ARBA00015625};
DE AltName: Full=Nuclear receptor subfamily 3 group C member 1 {ECO:0000256|ARBA:ARBA00031162};
GN Name=nr3c1 {ECO:0000313|RefSeq:XP_017341094.1,
GN ECO:0000313|RefSeq:XP_053541881.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017341094.1};
RN [1] {ECO:0000313|RefSeq:XP_017341094.1, ECO:0000313|RefSeq:XP_053541881.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017341094.1,
RC ECO:0000313|RefSeq:XP_053541881.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}. Nucleus
CC {ECO:0000256|RuleBase:RU004334}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily. {ECO:0000256|ARBA:ARBA00005413}.
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DR RefSeq; XP_017341094.1; XM_017485605.3.
DR RefSeq; XP_053541881.1; XM_053685906.1.
DR STRING; 7998.ENSIPUP00000014813; -.
DR Ensembl; ENSIPUT00000015435; ENSIPUP00000014813; ENSIPUG00000010081.
DR GeneID; 108275050; -.
DR KEGG; ipu:108275050; -.
DR CTD; 2908; -.
DR OMA; FFPMKTE; -.
DR OrthoDB; 5305911at2759; -.
DR Proteomes; UP000221080; Chromosome 14.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0042562; F:hormone binding; IEA:UniProt.
DR GO; GO:0004883; F:nuclear glucocorticoid receptor activity; IEA:Ensembl.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0005496; F:steroid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0055074; P:calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR GO; GO:0071387; P:cellular response to cortisol stimulus; IEA:Ensembl.
DR GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0048512; P:circadian behavior; IEA:Ensembl.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR GO; GO:0036367; P:light adaption; IEA:Ensembl.
DR GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:1902073; P:positive regulation of hypoxia-inducible factor-1alpha signaling pathway; IEA:Ensembl.
DR GO; GO:0120029; P:proton export across plasma membrane; IEA:Ensembl.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; IEA:Ensembl.
DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
DR GO; GO:0055078; P:sodium ion homeostasis; IEA:Ensembl.
DR CDD; cd07172; NR_DBD_GR_PR; 1.
DR CDD; cd06947; NR_LBD_GR_Like; 1.
DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR Gene3D; 1.10.565.10; Retinoid X Receptor; 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 PANTHER; PTHR48092:SF5; GLUCOCORTICOID RECEPTOR; 1.
DR PANTHER; PTHR48092; KNIRPS-RELATED PROTEIN-RELATED; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004334};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|RuleBase:RU004334};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|RuleBase:RU004334};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004334};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU004334}.
FT DOMAIN 398..473
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 504..738
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 82681 MW; 345F5CE0AC9FA84A CRC64;
MEQGGVKNGA KRDEHLMTRS FSESPAEGVL QNGARDTMSF APTTVVPPVS PLLQPVTGDL
PNGVNNTPSP EDITINLPSP LELFVEDPDL KMVGKDLRSQ QSFQQQSSLE LYSLGDNFSR
LEASIADLNS SLTSVDSLIG GGDPTLFPLK NEDFSPMGKG EMDLDQDPFG KDVDGSNPKL
FGENTMDLLE EFDLPESPTD LYLGDDEFPP IADDALLGVM VSDKDSKSVD SLSTSTIANV
NGGASSTPSS VSTSSPVLVI KQEKEPMIQL CTPGVIKQEN ASGRSFCQMT ADLPSPVRNV
SIAICGVSTS SGQSYHFGSP VSSGSQQKDQ KPVFNVYTPQ PTGNEWGQGF GNASAMQQRA
SNSFTATQSF STNYTGSTAR PEANTATSSA TGKASGTHKI CLVCSDDASG CHYGVLTCGS
CKVFFKRAVE GQHNYLCAGR NDCIIDKIRR KNCPACRFRK CLMAGMNLDA RKSKKLKMKG
VQQTNTAEVT PPPAPEARSL VPKAMPQLVP TMLSLLKAIE PETIYAGYDS TVTDTSTRLM
TTLNRLGGRQ FVSAVKWAKA LPGFRNLHLD DQMTLLQSSW LFLMSFGLGW RSYQQCNGSM
LCFAPDLVIN EERMKMPYMG DQCAQMLKIS NEFGRLQVSN EEYLCMKVLL LLSTVPKDGL
KSQAVFDEIR MSYIKELGKA IVRREENSSQ NWQRFYQLTK LLDSMHDMVG GLMNFCFYTF
VNKSLSVEFP EMLAEVISNQ LPKIKAGSVK PLLFHQK
//