ID A0A0N4SV67_MOUSE Unreviewed; 222 AA. AC A0A0N4SV67; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 11-DEC-2019, entry version 30. DE RecName: Full=Peroxisome proliferator-activated receptor gamma {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|RuleBase:RU364110}; DE Flags: Fragment; GN Name=Pparg {ECO:0000313|Ensembl:ENSMUSP00000144975, GN ECO:0000313|MGI:MGI:97747}; GN Synonyms=PPARG {ECO:0000256|RuleBase:RU364110}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000144975, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000144975, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000144975, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000144975} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000144975}; RG Ensembl; RL Submitted (MAR-2016) 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. ARF6 acts as a key regulator of the tissue-specific CC adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut CC homeostasis by suppressing NF-kappa-B-mediated proinflammatory CC responses. Plays a role in the regulation of cardiovascular circadian CC rhythms by regulating the transcription of ARNTL/BMAL1 in the blood CC vessels. {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, ECO:0000256|SAAS:SAAS00586772}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1 CC subfamily. {ECO:0000256|RuleBase:RU364110}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC153828; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC171970; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A0N4SV67; -. DR Ensembl; ENSMUST00000205213; ENSMUSP00000144975; ENSMUSG00000000440. DR MGI; MGI:97747; Pparg. DR GeneTree; ENSGT00940000158273; -. DR OMA; QRCQFRS; -. DR ChiTaRS; Pparg; mouse. DR Proteomes; UP000000589; Chromosome 6. DR Bgee; ENSMUSG00000000440; Expressed in 164 organ(s), highest expression level in placenta. DR ExpressionAtlas; A0A0N4SV67; baseline and differential. 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 Gene3D; 3.30.50.10; -; 1. DR InterPro; IPR003074; 1Cnucl_rcpt. DR InterPro; IPR003077; PPAR-gamma. DR InterPro; IPR022590; PPARgamma_N. DR InterPro; IPR001628; Znf_hrmn_rcpt. DR InterPro; IPR013088; Znf_NHR/GATA. DR Pfam; PF12577; PPARgamma_N; 1. DR Pfam; PF00105; zf-C4; 1. DR PRINTS; PR01288; PROXISOMEPAR. DR PRINTS; PR01291; PROXISOMPAGR. DR PRINTS; PR00047; STROIDFINGER. DR SMART; SM00399; ZnF_C4; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. PE 1: Evidence at protein level; KW Activator {ECO:0000256|RuleBase:RU364110}; KW Biological rhythms {ECO:0000256|RuleBase:RU364110}; KW Cytoplasm {ECO:0000256|RuleBase:RU364110}; KW DNA-binding {ECO:0000256|RuleBase:RU364110, ECO:0000256|SAAS:SAAS00476383}; KW Metal-binding {ECO:0000256|RuleBase:RU364110, KW ECO:0000256|SAAS:SAAS00116612}; KW Nucleus {ECO:0000256|RuleBase:RU364110, ECO:0000256|SAAS:SAAS00476518}; KW Proteomics identification {ECO:0000213|EPD:A0A0N4SV67, KW ECO:0000213|PeptideAtlas:A0A0N4SV67}; KW Receptor {ECO:0000256|RuleBase:RU364110}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transcription {ECO:0000256|RuleBase:RU364110, KW ECO:0000256|SAAS:SAAS00476418}; KW Transcription regulation {ECO:0000256|RuleBase:RU364110, KW ECO:0000256|SAAS:SAAS00116499}; KW Zinc {ECO:0000256|RuleBase:RU364110, ECO:0000256|SAAS:SAAS00476357}; KW Zinc-finger {ECO:0000256|RuleBase:RU364110, ECO:0000256|SAAS:SAAS00476458}. FT DOMAIN 106..180 FT /note="Nuclear receptor" FT /evidence="ECO:0000259|PROSITE:PS51030" FT NON_TER 222 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000144975" SQ SEQUENCE 222 AA; 25583 MW; 4132BC143EA88EFE CRC64; MVDTEMPFWP TNFGISSVDL SVMEDHSHSF DIKPFTTVDF SSISAPHYED IPFTRADPMV ADYKYDLKLQ EYQSAIKVEP ASPPYYSEKT QLYNRPHEEP SNSLMAIECR VCGDKASGFH YGVHACEGCK GFFRRTIRLK LIYDRCDLNC RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR ALAKHLYDSY IK //