PPARG_XENLA
ID PPARG_XENLA Reviewed; 477 AA.
AC P37234;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1312391; DOI=10.1016/0092-8674(92)90031-7;
RA Dreyer C., Krey G., Keller H., Givel F., Helftenbein G., Wahli W.;
RT "Control of the peroxisomal beta-oxidation pathway by a novel family of
RT nuclear hormone receptors.";
RL Cell 68:879-887(1992).
RN [2]
RP CHARACTERIZATION.
RX PubMed=8274443; DOI=10.1016/0960-0760(93)90058-5;
RA Krey G., Keller H., Mahfoudi A., Medin J., Ozato K., Dreyer C., Wahli W.;
RT "Xenopus peroxisome proliferator activated receptors: genomic organization,
RT response element recognition, heterodimer formation with retinoid X
RT receptor and activation by fatty acids.";
RL J. Steroid Biochem. Mol. Biol. 47:65-73(1993).
CC -!- FUNCTION: Receptor that binds peroxisome proliferators such as
CC hypolipidemic drugs and fatty acids. Once activated by a ligand, the
CC receptor binds to a promoter element in the gene for acyl-CoA oxidase
CC and activates its transcription. It therefore controls the peroxisomal
CC beta-oxidation pathway of fatty acids. Key regulator of adipocyte
CC differentiation and glucose homeostasis. May play a role in the
CC regulation of circadian rhythm (By similarity).
CC {ECO:0000250|UniProtKB:P37238}.
CC -!- SUBUNIT: Heterodimer with the retinoid X receptor.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed mainly in adipose tissue and kidney.
CC -!- DEVELOPMENTAL STAGE: Adult.
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 -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; M84163; AAA49937.1; -; mRNA.
DR PIR; C42214; C42214.
DR RefSeq; NP_001081312.1; NM_001087843.1.
DR AlphaFoldDB; P37234; -.
DR SMR; P37234; -.
DR BioGRID; 99108; 1.
DR DNASU; 397769; -.
DR GeneID; 397769; -.
DR KEGG; xla:397769; -.
DR CTD; 397769; -.
DR Xenbase; XB-GENE-483140; pparg.L.
DR OrthoDB; 1240230at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 397769; Expressed in internal ear and 2 other tissues.
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:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Activator; Biological rhythms; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..477
FT /note="Peroxisome proliferator-activated receptor gamma"
FT /id="PRO_0000053498"
FT DOMAIN 252..475
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 110..184
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 113..133
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 150..172
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 231..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 467..475
FT /note="9aaTAD"
FT /evidence="ECO:0000250|UniProtKB:P37231"
FT MOD_RES 87
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 54056 MW; 160F87A401CB7246 CRC64;
MVDTEMPFWS NLNFGMNSMD MSALEDHCQP YDIKPFTTVD FSSINSHYDD ILDEKTFLCR
NDQSPIDYKY DLKLQECQSS IKLEPPSPPY FSDKPQCSKA FEDTPNSFIA IECRVCGDKA
SGFHYGVHAC EGCKGFFRRT IRLKLIYERC DLNCRIHKKS RNKCQFCRFQ KCLAVGMSHN
AIRFGRMPQA EKEKLLAEIS SDIDQLNPES ADQRVLAKHL YDSYVKSFPL TKAKAPGHPD
GQSHRQNSRG YTRHELADDG GGSDQGAVRE PRAEQGGGDS NLPALSVALR GGVREITEFA
KNIPGFVSLD LNDQVTLLKY GVHEIIFTML ASLMNKDGVL VAEGQGFMTR EFLKSLRKPF
SDFMEPKFEF AIRFNSLELD DSDLAIFVAV IILSGDRPGL LNVKPIEDIQ DSLLQALELQ
LKLNHPDSAQ LFAKLLQKMT DLRQVVTEHV QLLQLIKKTE ADMCLHPLLQ EIYKDLY
