ID A0A2K5WFM9_MACFA Unreviewed; 483 AA.
AC A0A2K5WFM9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 24-JAN-2024, entry version 29.
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};
GN Name=PPARG {ECO:0000256|RuleBase:RU364110};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000035861.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000035861.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000035861.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 RefSeq; XP_015300831.1; XM_015445345.1.
DR RefSeq; XP_015300832.1; XM_015445346.1.
DR RefSeq; XP_015300833.1; XM_015445347.1.
DR AlphaFoldDB; A0A2K5WFM9; -.
DR Ensembl; ENSMFAT00000010102.2; ENSMFAP00000035861.2; ENSMFAG00000034317.2.
DR GeneID; 102120453; -.
DR CTD; 5468; -.
DR VEuPathDB; HostDB:ENSMFAG00000034317; -.
DR GeneTree; ENSGT00940000158273; -.
DR OrthoDB; 3475284at2759; -.
DR Proteomes; UP000233100; Chromosome 2.
DR Bgee; ENSMFAG00000034317; Expressed in bone marrow and 10 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
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:UP000233100};
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 114..188
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 216..481
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
SQ SEQUENCE 483 AA; 55331 MW; BBDB4AD100BAB1F7 CRC64;
MKGFSEITMV DTEMPFWPTN FGISSVDLSV MDDHSHSFDI KPFTTVDFSS ISAPHYEDIP
FTRTDPMVAD YKYDLKLQEY QSAIKVEPAS PPYYSEKTQL YNKPHEEPSN SLMAIECRVC
GDKASGFHYG VHACEGCKGF FRRTIRLKLI YDRCDLNCRI HKKSRNKCQY CRFQKCLAVG
MSHNAIRFGR MPQAEKEKLL AEISSDIDQL NPESADLRAL AKHLYDSYIK SFPLTKAKAR
AILTGKTTDK SPFVIYDMNS LMMGEDKIKF KHITPLQEQS KEVAIRIFQG CQFRSVEAVQ
EITEYAKSIP GFVNLDLNDQ VTLLKYGVHE IIYTMLASLM NKDGVLISEG QGFMTREFLK
SLRKPFGDFM EPKFEFAVKF NALELDDSDL AIFIAVIILS GDRPGLLNVK PIEDIQDNLL
QALELQLKLN HPESSQLFAK LLQKMTDLRQ IVTEHVQLLQ VIKKTETDMS LHPLLQEIYK
DLY
//
