PPARA_CAVPO
ID PPARA_CAVPO Reviewed; 467 AA.
AC O35507;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Dunkin-Hartley; TISSUE=Liver;
RX PubMed=9520140; DOI=10.1007/s002040050483;
RA Tugwood J.D., Holden P.R., James N.H., Prince R.A., Roberts R.A.;
RT "A peroxisome proliferator-activated receptor-alpha (PPARalpha) cDNA cloned
RT from guinea-pig liver encodes a protein with similar properties to the
RT mouse PPARalpha: implications for species differences in responses to
RT peroxisome proliferators.";
RL Arch. Toxicol. 72:169-177(1998).
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; AJ000222; CAA03951.1; -; mRNA.
DR RefSeq; NP_001166475.1; NM_001173004.1.
DR AlphaFoldDB; O35507; -.
DR SMR; O35507; -.
DR STRING; 10141.ENSCPOP00000001339; -.
DR Ensembl; ENSCPOT00000001502; ENSCPOP00000001339; ENSCPOG00000001483.
DR GeneID; 100135604; -.
DR KEGG; cpoc:100135604; -.
DR CTD; 5465; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000157097; -.
DR HOGENOM; CLU_007368_4_1_1; -.
DR InParanoid; O35507; -.
DR OMA; EMGSIQE; -.
DR OrthoDB; 1240230at2759; -.
DR TreeFam; TF316304; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000001483; Expressed in heart left ventricle and 12 other tissues.
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; ISS:UniProtKB.
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:0009267; P:cellular response to starvation; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; IEA:Ensembl.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR GO; GO:0032099; P:negative regulation of appetite; ISS:UniProtKB.
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 protein kinase B signaling; 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:2000272; P:negative regulation of signaling receptor activity; 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:0046321; P:positive regulation of fatty acid oxidation; IEA:Ensembl.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
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..467
FT /note="Peroxisome proliferator-activated receptor alpha"
FT /id="PRO_0000053480"
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 304..433
FT /note="Required for heterodimerization with RXRA"
FT /evidence="ECO:0000250"
FT SITE 433
FT /note="Essential for heterodimerization with RXRA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 52313 MW; D55DD2A6ED0205DE CRC64;
MVDMESPLCP LSPLEAEDLE SPLSEYFLQE MGTIQDISRS LGEDSSGSFG FPEYQYLGSG
PGSDGSVITD TLSPASSPSS VSYPEVPCGV DEPPSSALNI ECRICGDKAS GYHYGVHACE
GCKGFFRRTI RLKLVYDKCD RSCKIQKKNR NKCQYCRFHK CLSVGMSHNA IRFGRMPRSE
KAKLKAEVLT CDRDSEGAET ADLKSLAKRI YEAYLKNFHM NKVKARIILA GKTSSHPLFV
IHDMETLCTA EKTLMAKVVS DGIRDKEAEV RIFHCCQCVS VETVTNLTEF AKAIPGFASL
DLNDQVTLLK YGVYEAIFTM LSSTMNKDGM LVAYGHGFIT REFLKNLRKP FCDMMEPKFN
FAMKFNALEL DDSDISLFVA AIICCGDRPG LLNIDHIEKM QEAIVHVLKL HLQSNHPDDT
FLFPKLLQKL ADLRQLVTEH AQLVQVIKTE SDAALHPLLQ EIYRDMY
