PPARG_BOVIN
ID PPARG_BOVIN Reviewed; 505 AA.
AC O18971; Q1LZB7; Q8HY47;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Peroxisome proliferator-activated receptor gamma;
DE Short=PPAR-gamma;
DE AltName: Full=Nuclear receptor subfamily 1 group C member 3;
GN Name=PPARG; Synonyms=NR1C3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Adipose tissue;
RX PubMed=9367859; DOI=10.1006/bbrc.1997.7564;
RA Sundvold H., Brzozowska A., Lien S.;
RT "Characterisation of bovine peroxisome proliferator-activated receptors
RT gamma 1 and gamma 2: genetic mapping and differential expression of the two
RT isoforms.";
RL Biochem. Biophys. Res. Commun. 239:857-861(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Jeoung Y.-H., Yoon D.-H., Chang E.-R., Kang M.-J.;
RT "Bovine PPAR gamma mRNA.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) 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. 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 pro-inflammatory
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:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
CC -!- ACTIVITY REGULATION: PDPK1 activates its transcriptional activity
CC independently of its kinase activity. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FOXO1 (acetylated form) (By similarity).
CC Heterodimer with other nuclear receptors, such as RXRA. The heterodimer
CC with the retinoic acid receptor RXRA is called adipocyte-specific
CC transcription factor ARF6. Interacts with NCOA6 coactivator, leading to
CC a strong increase in transcription of target genes. Interacts with
CC coactivator PPARBP, leading to a mild increase in transcription of
CC target genes. Interacts with NOCA7 in a ligand-inducible manner.
CC Interacts with NCOA1 and NCOA2 LXXLL motifs. Interacts with ASXL1,
CC ASXL2, DNTTIP2, FAM120B, MAP2K1/MEK1, NR0B2, PDPK1, PRDM16, PRMT2 and
CC TGFB1I1. Interacts (when activated by agonist) with PPP5C. Interacts
CC with HELZ2 and THRAP3; the interaction stimulates the transcriptional
CC activity of PPARG. Interacts with PER2, the interaction is ligand
CC dependent and blocks PPARG recruitment to target promoters. Interacts
CC with NOCT. Interacts with ACTN4. Interacts (when in the liganded
CC conformation) with GPS2 (By similarity). Interacts with CRY1 and CRY2
CC in a ligand-dependent manner (By similarity). In the absence of
CC hormonal ligand, interacts with TACC1 (By similarity).
CC {ECO:0000250|UniProtKB:P37231, ECO:0000250|UniProtKB:P37238}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the
CC cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its
CC nuclear translocation (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=2;
CC IsoId=O18971-1; Sequence=Displayed;
CC Name=1;
CC IsoId=O18971-2; Sequence=VSP_003644;
CC -!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Lower in
CC spleen and lung. Also detected in ovary, mammary gland and small
CC intestine.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P37231}.
CC -!- PTM: Phosphorylated at basal conditions and dephosphorylated when
CC treated with the ligand. May be dephosphorylated by PPP5C. The
CC phosphorylated form may be inactive and dephosphorylation induces
CC adipogenic activity (By similarity). {ECO:0000250|UniProtKB:P37231}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; Y12420; CAA73033.1; -; mRNA.
DR EMBL; Y12419; CAA73032.1; -; mRNA.
DR EMBL; AY179866; AAN75018.1; -; mRNA.
DR EMBL; BC116098; AAI16099.1; -; mRNA.
DR PIR; JC5777; JC5777.
DR RefSeq; NP_851367.1; NM_181024.2. [O18971-1]
DR AlphaFoldDB; O18971; -.
DR BMRB; O18971; -.
DR SMR; O18971; -.
DR STRING; 9913.ENSBTAP00000041555; -.
DR PaxDb; O18971; -.
DR PRIDE; O18971; -.
DR Ensembl; ENSBTAT00000001760; ENSBTAP00000001760; ENSBTAG00000001333. [O18971-2]
DR Ensembl; ENSBTAT00000044038; ENSBTAP00000041555; ENSBTAG00000001333. [O18971-1]
DR Ensembl; ENSBTAT00000044042; ENSBTAP00000041559; ENSBTAG00000001333. [O18971-2]
DR Ensembl; ENSBTAT00000083374; ENSBTAP00000060270; ENSBTAG00000001333. [O18971-2]
DR GeneID; 281993; -.
DR KEGG; bta:281993; -.
DR CTD; 5468; -.
DR VEuPathDB; HostDB:ENSBTAG00000001333; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000158273; -.
DR HOGENOM; CLU_007368_4_2_1; -.
DR InParanoid; O18971; -.
DR OMA; WPINFGI; -.
DR OrthoDB; 1240230at2759; -.
DR TreeFam; TF316304; -.
DR Reactome; R-BTA-383280; Nuclear Receptor transcription pathway.
DR Proteomes; UP000009136; Chromosome 22.
DR Bgee; ENSBTAG00000001333; Expressed in bone marrow and 100 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:AgBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:AgBase.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045165; P:cell fate commitment; ISS:AgBase.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; ISS:AgBase.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; ISS:UniProtKB.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; IBA:GO_Central.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:AgBase.
DR GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:HGNC-UCL.
DR GO; GO:0045923; P:positive regulation of fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:AgBase.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0045598; P:regulation of fat cell differentiation; ISS:AgBase.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:AgBase.
DR GO; GO:0033993; P:response to lipid; IBA:GO_Central.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0050872; P:white fat cell differentiation; ISS:HGNC-UCL.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 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 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; 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 Activator; Alternative splicing; Biological rhythms; Cytoplasm;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Receptor;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..505
FT /note="Peroxisome proliferator-activated receptor gamma"
FT /id="PRO_0000053489"
FT DOMAIN 238..503
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 136..210
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..159
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 176..198
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 205..280
FT /note="Interaction with FAM120B"
FT /evidence="ECO:0000250"
FT MOTIF 495..503
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P37231"
FT MOD_RES 112
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250|UniProtKB:P37238"
FT VAR_SEQ 1..30
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9367859, ECO:0000303|Ref.3"
FT /id="VSP_003644"
FT CONFLICT 81
FT /note="I -> T (in Ref. 2; AAN75018)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="R -> W (in Ref. 2; AAN75018)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="E -> G (in Ref. 2; AAN75018)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="K -> I (in Ref. 2; AAN75018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 57579 MW; 5F20B115087B3C83 CRC64;
MGETLGDALI DPESEPFAVT VSARTSQEIT MVDTEMPFWP TNFGISSVDL SMMDDHSHAF
DIKPFTTVDF SSISTPHYED IPFPRADPMV ADYKYDLKLQ EYQSAIKVEP VSPPYYSEKT
QLYSKPHEEP SNSLMAIECR VCGDKASGFH YGVHACEGCK GFFRRTIRLK LIYDRCDLNC
RIHKKSRNKC QYCRFQKCLA VGMSHNAIRF GRMPQAEKEK LLAEISSDID QLNPESADLR
ALAKHLYDSY IKSFPLTKAK ARAILTGKTT DKSPFVIYDM NSLMMGEDKI KFKHISPLQE
PSKEVAIRIF QGCQFRSVEA VQEITEYAKN IPGFVNLDLN DQVTLLKYGV HEIIYTMLAS
LMNKDGVLIS EGQGFMTREF LKSLRKPFGD FMEPKFEFAV KFNALELDDS DLAIFIAVII
LSGDRPGLLN VKPIEDIQDN LLQALELQLK LNHPESSQLF AKLLQKMTDL RQIVTEHVQL
LQVIKKTETD MSLHPLLQEI YKDLY
