ID A0A091JR95_EGRGA Unreviewed; 480 AA.
AC A0A091JR95;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma {ECO:0000256|ARBA:ARBA00018974, ECO:0000256|RuleBase:RU364110};
DE Short=PPAR-gamma {ECO:0000256|RuleBase:RU364110};
DE AltName: Full=Nuclear receptor subfamily 1 group C member 3 {ECO:0000256|ARBA:ARBA00032721, ECO:0000256|RuleBase:RU364110};
DE Flags: Fragment;
GN Name=PPARG {ECO:0000256|RuleBase:RU364110};
GN ORFNames=Z169_12609 {ECO:0000313|EMBL:KFP14166.1};
OS Egretta garzetta (Little egret).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Ardeidae; Egretta.
OX NCBI_TaxID=188379 {ECO:0000313|EMBL:KFP14166.1, ECO:0000313|Proteomes:UP000053119};
RN [1] {ECO:0000313|EMBL:KFP14166.1, ECO:0000313|Proteomes:UP000053119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Z169 {ECO:0000313|EMBL:KFP14166.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Nuclear receptor that binds peroxisome proliferators such as
CC hypolipidemic drugs and fatty acids. Once activated by a ligand, the
CC nuclear receptor binds to DNA specific PPAR response elements (PPRE)
CC and modulates the transcription of its target genes, such as acyl-CoA
CC oxidase. It therefore controls the peroxisomal beta-oxidation pathway
CC of fatty acids. Key regulator of adipocyte differentiation and glucose
CC homeostasis. May play a role in the regulation of circadian rhythm.
CC {ECO:0000256|RuleBase:RU364110}.
CC -!- SUBUNIT: Heterodimer with other nuclear receptors.
CC {ECO:0000256|RuleBase:RU364110}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU364110}.
CC Nucleus {ECO:0000256|RuleBase:RU364110}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000256|ARBA:ARBA00008092,
CC ECO:0000256|RuleBase:RU364110}.
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DR EMBL; KK501311; KFP14166.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091JR95; -.
DR STRING; 188379.A0A091JR95; -.
DR Proteomes; UP000053119; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR CDD; cd06965; NR_DBD_Ppar; 1.
DR CDD; cd06932; NR_LBD_PPAR; 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; IPR003074; 1Cnucl_rcpt.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003077; PPAR-gamma.
DR InterPro; IPR022590; PPARgamma_N.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24082:SF488; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF12577; PPARgamma_N; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01288; PROXISOMEPAR.
DR PRINTS; PR01291; PROXISOMPAGR.
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 Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|RuleBase:RU364110};
KW Biological rhythms {ECO:0000256|ARBA:ARBA00023108,
KW ECO:0000256|RuleBase:RU364110};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU364110};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004334};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004334};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004334};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW Reference proteome {ECO:0000313|Proteomes:UP000053119};
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 111..185
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 213..478
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP14166.1"
FT NON_TER 480
FT /evidence="ECO:0000313|EMBL:KFP14166.1"
SQ SEQUENCE 480 AA; 54983 MW; C67DFB85B1311CA9 CRC64;
FSGITMVDTE MPFWPINFGI SPVDLSAMDD HTHSFDIKPF TTVDFSSISS PHYEDIPLAR
TDQTSIDYKY DIKLQDCQSA IKMEPPSPPY FSEKVQLYNK PHEESSNSLM AIECRVCGDK
ASGFHYGVHA CEGCKGFFRR TIRLKLIYDR CDLNCRIHKK SRNKCQYCRF QKCLAVGMSH
NAIRFGRMPQ AEKEKLLAEI SSDIDQLNPE SADLRALAKH LYDSYIKSFP LTKAKARAIL
TGKTTDKSPF VIYDMNSLMM GEDQIKCKHV SPLQEENKEV AIRIFQRCQF RSVEAVQEIT
EFAKNIPGFV NLDLNDQVTL LKYGVHEIIY TLLASLMNKD GVLISDGQGF MTREFLKSLR
KPFCDFMEPK FEFAVKFNAL ELDDSDLAIF IAVIILSGDR PGLLNVKPIE DIQDNLLQAL
ELQLKLNHPE SSQLFAKLLQ KMTDLRQIVT EHVQLLQIIK KTETDMSLHP LLQEIYKDLY
//
