ID A0A452QYA4_URSAM Unreviewed; 503 AA.
AC A0A452QYA4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Peroxisome proliferator-activated receptor alpha {ECO:0000256|ARBA:ARBA00019236};
DE AltName: Full=Nuclear receptor subfamily 1 group C member 1 {ECO:0000256|ARBA:ARBA00032723};
GN Name=PPARA {ECO:0000313|Ensembl:ENSUAMP00000010848.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000010848.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000010848.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Ligand-activated transcription factor. Key regulator of lipid
CC metabolism. Activated by the endogenous ligand 1-palmitoyl-2-oleoyl-sn-
CC glycerol-3-phosphocholine (16:0/18:1-GPC). Activated by
CC oleylethanolamide, a naturally occurring lipid that regulates satiety.
CC Receptor for peroxisome proliferators such as hypolipidemic drugs and
CC fatty acids. Regulates the peroxisomal beta-oxidation pathway of fatty
CC acids. Functions as a transcription activator for the ACOX1 and P450
CC genes. Transactivation activity requires heterodimerization with RXRA
CC and is antagonized by NR2C2. May be required for the propagation of
CC clock information to metabolic pathways regulated by PER2.
CC {ECO:0000256|ARBA:ARBA00043860}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU004334}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000256|ARBA:ARBA00008092}.
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DR AlphaFoldDB; A0A452QYA4; -.
DR STRING; 9643.ENSUAMP00000010848; -.
DR Ensembl; ENSUAMT00000012196.1; ENSUAMP00000010848.1; ENSUAMG00000008877.1.
DR GeneTree; ENSGT00940000157097; -.
DR OMA; ANNNPPF; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0008289; F:lipid binding; IEA:Ensembl.
DR GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
DR GO; GO:0003707; F:nuclear steroid receptor activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0010887; P:negative regulation of cholesterol storage; IEA:Ensembl.
DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; IEA:Ensembl.
DR GO; GO:0045820; P:negative regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:1903944; P:negative regulation of hepatocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IEA:Ensembl.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:1904189; P:positive regulation of transformation of host cell by virus; IEA:Ensembl.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; IEA:Ensembl.
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; IPR003076; PPAR-alpha.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR PANTHER; PTHR24082:SF197; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR ALPHA; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01288; PROXISOMEPAR.
DR PRINTS; PR01289; PROXISOMPAAR.
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};
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 Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU004334};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
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 134..208
FT /note="Nuclear receptor"
FT /evidence="ECO:0000259|PROSITE:PS51030"
FT DOMAIN 274..501
FT /note="NR LBD"
FT /evidence="ECO:0000259|PROSITE:PS51843"
SQ SEQUENCE 503 AA; 56149 MW; 4AD58670B06FF2C4 CRC64;
MFSLKEKCSS MSVSLVTSLS SQVGARLHFQ NHLVKMVDTE SPICPLSPLE ANDLESPLSE
EFLQEMGSIQ EISQSIGEDS SGSFSFTEYQ YLGSGPGSDG SVITDTLSPA SSPSSITYPV
APSSADEPAS VALNIECRIC GDRASGYHYG VHACEGCKGF FRRTVRLKLA YDRCDRHCKI
QKKNRNKCQY CRFHKCLSVG MSHNAIRFGR MPRSEKAKLK AEILTCEHEP EDAETADLKS
LAKRIYEAYL KNFNMNKVKA RVILAGKASN NLPFVIHDME TLCMAEKTLV AKLVANGIQN
KEAEVRIFHC CQCTSVETVT ELTEFAKSIP GFANLDLNDQ VTLLKYGVYE AIFAMLSSVM
NKDGMLVAYG NGFITREFLK SLRKPFCDIM EPKFDFAMKF NALELDDSDL SLFVAAIICC
GDRPGLLNVG HIEKMQEGIV HVLKLHLQTN HPDNIFLFPK LLQKMADLRQ LVTEHAQLVQ
VIKKTESDAA LHPLLQEIYR DMY
//
