PPARA_CANLF
ID PPARA_CANLF Reviewed; 468 AA.
AC Q95N78;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Peroxisome proliferator-activated receptor alpha;
DE Short=PPAR-alpha;
DE AltName: Full=Nuclear receptor subfamily 1 group C member 1;
GN Name=PPARA; Synonyms=NR1C1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Nagasawa M., Ide T., Murakami K.;
RT "Dog PPAR alpha cDNA sequence.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
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 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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer; with RXRA. This heterodimerization is required
CC for DNA binding and transactivation activity. Interacts with NCOA3
CC coactivator. Interacts with CITED2; the interaction stimulates its
CC transcriptional activity. Also interacts with PPARBP in vitro.
CC Interacts with AKAP13, LPIN1, PRDM16 and coactivator NCOA6. Interacts
CC with ASXL1 and ASXL2. Interacts with PER2. Interacts with SIRT1; the
CC interaction seems to be modulated by NAD(+) levels (By similarity).
CC Interacts with CRY1 and CRY2 (By similarity).
CC {ECO:0000250|UniProtKB:P23204, ECO:0000250|UniProtKB:P37230,
CC ECO:0000250|UniProtKB:Q07869}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF350327; AAK38655.1; -; mRNA.
DR RefSeq; NP_001003093.1; NM_001003093.1.
DR RefSeq; XP_005625734.1; XM_005625677.1.
DR RefSeq; XP_013972720.1; XM_014117245.1.
DR AlphaFoldDB; Q95N78; -.
DR SMR; Q95N78; -.
DR STRING; 9615.ENSCAFP00000054067; -.
DR BindingDB; Q95N78; -.
DR ChEMBL; CHEMBL2847; -.
DR PaxDb; Q95N78; -.
DR GeneID; 403654; -.
DR KEGG; cfa:403654; -.
DR CTD; 5465; -.
DR eggNOG; KOG3575; Eukaryota.
DR HOGENOM; CLU_007368_4_1_1; -.
DR InParanoid; Q95N78; -.
DR OMA; EMGSIQE; -.
DR OrthoDB; 1240230at2759; -.
DR TreeFam; TF316304; -.
DR Reactome; R-CFA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-CFA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-CFA-9707564; Cytoprotection by HMOX1.
DR PRO; PR:Q95N78; -.
DR Proteomes; UP000002254; Chromosome 10.
DR Bgee; ENSCAFG00000000788; Expressed in tongue and 45 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0008289; F:lipid binding; ISS:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:AgBase.
DR GO; GO:0038023; F:signaling receptor activity; ISS:AgBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0008544; P:epidermis development; ISS:AgBase.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:AgBase.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0032099; P:negative regulation of appetite; 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: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:AgBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0019217; P:regulation of fatty acid metabolic process; ISS:AgBase.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IBA:GO_Central.
DR GO; GO:0033993; P:response to lipid; IBA:GO_Central.
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; IPR003076; PPAR-alpha.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
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; 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; Biological rhythms; DNA-binding; Lipid-binding; Metal-binding;
KW Nucleus; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..468
FT /note="Peroxisome proliferator-activated receptor alpha"
FT /id="PRO_0000053479"
FT DOMAIN 239..466
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 99..173
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 102..122
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 139..161
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..433
FT /note="Required for heterodimerization with RXRA"
FT /evidence="ECO:0000250"
FT COMPBIAS 65..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 433
FT /note="Essential for heterodimerization with RXRA"
FT /evidence="ECO:0000250"
SQ 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
