GENTAUR Molecular Products.

 PPARA_CANLF             Reviewed;         468 AA.
 Q95N78;
 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
 01-DEC-2001, sequence version 1.
 28-MAR-2018, entry version 134.
 RecName: Full=Peroxisome proliferator-activated receptor alpha;
          Short=PPAR-alpha;
 AltName: Full=Nuclear receptor subfamily 1 group C member 1;
 Name=PPARA; Synonyms=NR1C1;
 Canis lupus familiaris (Dog) (Canis familiaris).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
 Canis.
 NCBI_TaxID=9615;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 Nagasawa M., Ide T., Murakami K.;
 "Dog PPAR alpha cDNA sequence.";
 Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
 -!- FUNCTION: Ligand-activated transcription factor. Key regulator of
     lipid metabolism. Activated by the endogenous ligand 1-palmitoyl-
     2-oleoyl-sn-glycerol-3-phosphocholine (16:0/18:1-GPC). Activated
     by oleylethanolamide, a naturally occurring lipid that regulates
     satiety. Receptor for peroxisome proliferators such as
     hypolipidemic drugs and fatty acids. Regulates the peroxisomal
     beta-oxidation pathway of fatty acids. Functions as transcription
     activator for the ACOX1 and P450 genes. Transactivation activity
     requires heterodimerization with RXRA and is antagonized by NR2C2.
     May be required for the propagation of clock information to
     metabolic pathways regulated by PER2 (By similarity).
     {ECO:0000250}.
 -!- SUBUNIT: Heterodimer; with RXRA. This heterodimerization is
     required for DNA binding and transactivation activity. Interacts
     with NCOA3 coactivator. Interacts with CITED2; the interaction
     stimulates its transcriptional activity. Also interacts with
     PPARBP in vitro. Interacts with AKAP13, LPIN1, PRDM16 and
     coactivator NCOA6. Interacts with ASXL1 and ASXL2. Interacts with
     PER2. Interacts with SIRT1; the interaction seems to be modulated
     by NAD(+) levels (By similarity). {ECO:0000250|UniProtKB:P23204,
     ECO:0000250|UniProtKB:P37230, ECO:0000250|UniProtKB:Q07869}.
 -!- SUBCELLULAR LOCATION: Nucleus.
 -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
     subfamily. {ECO:0000305}.
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 EMBL; AF350327; AAK38655.1; -; mRNA.
 RefSeq; NP_001003093.1; NM_001003093.1.
 RefSeq; XP_005625734.1; XM_005625677.1.
 RefSeq; XP_013972720.1; XM_014117245.1.
 UniGene; Cfa.3519; -.
 ProteinModelPortal; Q95N78; -.
 SMR; Q95N78; -.
 STRING; 9615.ENSCAFP00000001118; -.
 BindingDB; Q95N78; -.
 ChEMBL; CHEMBL2847; -.
 PaxDb; Q95N78; -.
 Ensembl; ENSCAFT00000001222; ENSCAFP00000001118; ENSCAFG00000000788.
 GeneID; 403654; -.
 KEGG; cfa:403654; -.
 CTD; 5465; -.
 VGNC; VGNC:44834; PPARA.
 eggNOG; KOG3575; Eukaryota.
 eggNOG; ENOG410XRZC; LUCA.
 GeneTree; ENSGT00870000136388; -.
 HOGENOM; HOG000261626; -.
 HOVERGEN; HBG106004; -.
 InParanoid; Q95N78; -.
 KO; K07294; -.
 OMA; FSFTEYQ; -.
 OrthoDB; EOG091G05U8; -.
 TreeFam; TF316304; -.
 Reactome; R-CFA-383280; Nuclear Receptor transcription pathway.
 Reactome; R-CFA-400206; Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
 PRO; PR:Q95N78; -.
 Proteomes; UP000002254; Chromosome 10.
 Bgee; ENSCAFG00000000788; -.
 GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
 GO; GO:0003677; F:DNA binding; ISS:AgBase.
 GO; GO:0003700; F:DNA binding transcription factor activity; ISS:AgBase.
 GO; GO:0008144; F:drug binding; ISS:UniProtKB.
 GO; GO:0008289; F:lipid binding; ISS:UniProtKB.
 GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
 GO; GO:0004872; F:receptor activity; ISS:AgBase.
 GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
 GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IEA:Ensembl.
 GO; GO:0043565; F:sequence-specific DNA binding; ISS:AgBase.
 GO; GO:0003707; F:steroid hormone receptor activity; IEA:Ensembl.
 GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
 GO; GO:0001190; F:transcriptional activator activity, RNA polymerase II transcription factor binding; IEA:Ensembl.
 GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IEA:Ensembl.
 GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
 GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
 GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
 GO; GO:0008544; P:epidermis development; ISS:AgBase.
 GO; GO:0006631; P:fatty acid metabolic process; ISS:AgBase.
 GO; GO:0032099; P:negative regulation of appetite; ISS:UniProtKB.
 GO; GO:0010887; P:negative regulation of cholesterol storage; IEA:Ensembl.
 GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
 GO; GO:1903038; P:negative regulation of leukocyte cell-cell adhesion; IEA:Ensembl.
 GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
 GO; GO:1902894; P:negative regulation of pri-miRNA transcription by RNA polymerase II; IEA:Ensembl.
 GO; GO:0010871; P:negative regulation of receptor biosynthetic process; IEA:Ensembl.
 GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IEA:Ensembl.
 GO; GO:0046321; P:positive regulation of fatty acid oxidation; IEA:Ensembl.
 GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
 GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:AgBase.
 GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
 GO; GO:0072366; P:regulation of cellular ketone metabolic process by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
 GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
 GO; GO:0019217; P:regulation of fatty acid metabolic process; ISS:AgBase.
 GO; GO:0072363; P:regulation of glycolytic process by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
 GO; GO:0072369; P:regulation of lipid transport by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
 GO; GO:0042060; P:wound healing; IEA:Ensembl.
 Gene3D; 3.30.50.10; -; 1.
 InterPro; IPR003074; 1Cnucl_rcpt.
 InterPro; IPR035500; NHR_like_dom_sf.
 InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
 InterPro; IPR001723; Nuclear_hrmn_rcpt.
 InterPro; IPR003076; PPAR-alpha.
 InterPro; IPR001628; Znf_hrmn_rcpt.
 InterPro; IPR013088; Znf_NHR/GATA.
 Pfam; PF00104; Hormone_recep; 1.
 Pfam; PF00105; zf-C4; 1.
 PRINTS; PR01288; PROXISOMEPAR.
 PRINTS; PR01289; PROXISOMPAAR.
 PRINTS; PR00398; STRDHORMONER.
 PRINTS; PR00047; STROIDFINGER.
 SMART; SM00430; HOLI; 1.
 SMART; SM00399; ZnF_C4; 1.
 SUPFAM; SSF48508; SSF48508; 1.
 PROSITE; PS51843; NR_LBD; 1.
 PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
 PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
 2: Evidence at transcript level;
 Activator; Biological rhythms; Complete proteome; DNA-binding;
 Lipid-binding; Metal-binding; Nucleus; Receptor; Reference proteome;
 Transcription; Transcription regulation; Zinc; Zinc-finger.
 CHAIN         1    468       Peroxisome proliferator-activated
                              receptor alpha.
                              /FTId=PRO_0000053479.
 DOMAIN      239    466       NR LBD. {ECO:0000255|PROSITE-
                              ProRule:PRU01189}.
 DNA_BIND     99    173       Nuclear receptor. {ECO:0000255|PROSITE-
                              ProRule:PRU00407}.
 ZN_FING     102    122       NR C4-type. {ECO:0000255|PROSITE-
                              ProRule:PRU00407}.
 ZN_FING     139    161       NR C4-type. {ECO:0000255|PROSITE-
                              ProRule:PRU00407}.
 REGION      304    433       Required for heterodimerization with
                              RXRA. {ECO:0000250}.
 SITE        433    433       Essential for heterodimerization with
                              RXRA. {ECO:0000250}.
 SEQUENCE   468 AA;  52123 MW;  11F2C2F9AAB176D5 CRC64;
 MVDTESPICP LSPLEADDLE SPLSEEFLQE MGNIQEISQS IGEDSSGSFS FTEYQYLGSG
 PGSDGSVITD TLSPAPSPSS VTHPAAPGGA EEPSSVALNI ECRICGDRAS GYHYGVHACE
 GCKGFFRRTI RLKLAYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE
 KAKLKAEILT CEQDPEDAET ADLKSLAKRI YEAYLKNFNM NKVKARVILA GKASNNPPFV
 IHDMETLCMA EKTLVAKLVA NGIQNKEAEV RIFHCCQCTS VETVTELTEF AKSIPGFANL
 DLNDQVTLLK YGVYEAIFAM LSSVMNKDGM LVAYGNGFIT REFLKSLRKP FCDIMEPKFD
 FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNVGHIEKM QEGIVHVLKL HLQTNHPDNI
 FLFPKLLQKM ADLRQLVTEH AQLVQVIKKT ESDAALHPLL QEIYRDMY

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