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Peroxisome proliferator activated receptor delta, isoform CRA_b (Peroxisome proliferator-activated receptor beta) (Peroxisome proliferator-activated receptor delta)

 Q99ND3_RAT              Unreviewed;       440 AA.
Q99ND3;
01-JUN-2001, integrated into UniProtKB/TrEMBL.
01-JUN-2001, sequence version 1.
22-NOV-2017, entry version 130.
SubName: Full=Peroxisome proliferator activated receptor delta, isoform CRA_b {ECO:0000313|EMBL:EDL96915.1};
SubName: Full=Peroxisome proliferator-activated receptor beta {ECO:0000313|EMBL:CAC29088.1};
SubName: Full=Peroxisome proliferator-activated receptor delta {ECO:0000313|Ensembl:ENSRNOP00000045974};
Name=Ppard {ECO:0000313|EMBL:EDL96915.1,
ECO:0000313|Ensembl:ENSRNOP00000045974, ECO:0000313|RGD:3370};
Synonyms=PPARb {ECO:0000313|EMBL:CAC29088.1};
ORFNames=rCG_60581 {ECO:0000313|EMBL:EDL96915.1};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116 {ECO:0000313|EMBL:CAC29088.1};
[1] {ECO:0000313|EMBL:CAC29088.1}
NUCLEOTIDE SEQUENCE.
STRAIN=Sprague-Dowley {ECO:0000313|EMBL:CAC29088.1};
TISSUE=Liver {ECO:0000313|EMBL:CAC29088.1};
PubMed=11564675; DOI=10.1210/en.142.10.4195;
Escher P., Braissant O., Basu-Modak S., Michalik L., Wahli W.,
Desvergne B.;
"Rat PPARs: quantitative analysis in adult rat tissues and regulation
in fasting and refeeding.";
Endocrinology 142:4195-4202(2001).
[2] {ECO:0000313|Ensembl:ENSRNOP00000045974, ECO:0000313|Proteomes:UP000002494}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000045974,
ECO:0000313|Proteomes:UP000002494};
PubMed=15057822; DOI=10.1038/nature02426;
Rat Genome Sequencing Project Consortium;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3] {ECO:0000313|EMBL:EDL96915.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL96915.1};
PubMed=15632090; DOI=10.1101/gr.2889405;
Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
Istrail S., Li P., Sutton G.;
"Gene and alternative splicing annotation with AIR.";
Genome Res. 15:54-66(2005).
[4] {ECO:0000313|EMBL:EDL96915.1}
NUCLEOTIDE SEQUENCE.
STRAIN=BN {ECO:0000313|EMBL:EDL96915.1};
Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|Ensembl:ENSRNOP00000045974}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000045974};
Ensembl;
Submitted (FEB-2012) to UniProtKB.
[6] {ECO:0000313|Ensembl:ENSRNOP00000069522}
IDENTIFICATION.
STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000069522};
Ensembl;
Submitted (JUN-2015) to UniProtKB.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-
ProRule:PRU00407, ECO:0000256|RuleBase:RU004334,
ECO:0000256|SAAS:SAAS00586772}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family.
{ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00595733}.
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EMBL; AC106225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC132760; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AJ306400; CAC29088.1; -; mRNA.
EMBL; CH473988; EDL96915.1; -; Genomic_DNA.
RefSeq; NP_037273.2; NM_013141.2.
RefSeq; XP_006256228.1; XM_006256166.3.
RefSeq; XP_006256229.1; XM_006256167.3.
RefSeq; XP_006256230.1; XM_006256168.3.
UniGene; Rn.96181; -.
STRING; 10116.ENSRNOP00000045974; -.
Ensembl; ENSRNOT00000042539; ENSRNOP00000045974; ENSRNOG00000000503.
Ensembl; ENSRNOT00000083109; ENSRNOP00000069522; ENSRNOG00000000503.
GeneID; 25682; -.
KEGG; rno:25682; -.
CTD; 5467; -.
RGD; 3370; Ppard.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00870000136388; -.
HOVERGEN; HBG106004; -.
KO; K04504; -.
OMA; SLGMSHN; -.
TreeFam; TF316304; -.
Reactome; R-RNO-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
Reactome; R-RNO-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
Reactome; R-RNO-5362517; Signaling by Retinoic Acid.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000000503; -.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0008144; F:drug binding; ISO:RGD.
GO; GO:0005504; F:fatty acid binding; IDA:RGD.
GO; GO:0070539; F:linoleic acid binding; ISO:RGD.
GO; GO:0008289; F:lipid binding; ISO:RGD.
GO; GO:0051059; F:NF-kappaB binding; IPI:RGD.
GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; IDA:RGD.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:RGD.
GO; GO:0008134; F:transcription factor binding; ISO:RGD.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; ISO:RGD.
GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
GO; GO:0008366; P:axon ensheathment; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:RGD.
GO; GO:0046697; P:decidualization; IEP:RGD.
GO; GO:0007566; P:embryo implantation; IEP:RGD.
GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
GO; GO:0019395; P:fatty acid oxidation; IDA:RGD.
GO; GO:0015908; P:fatty acid transport; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEP:RGD.
GO; GO:0051546; P:keratinocyte migration; IEA:Ensembl.
GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; IDA:RGD.
GO; GO:0009299; P:mRNA transcription; IDA:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:0030308; P:negative regulation of cell growth; IDA:RGD.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; IMP:RGD.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IDA:RGD.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:1902894; P:negative regulation of pri-miRNA transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IDA:RGD.
GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:RGD.
GO; GO:0008654; P:phospholipid biosynthetic process; IDA:RGD.
GO; GO:0097755; P:positive regulation of blood vessel diameter; IDA:RGD.
GO; GO:0045684; P:positive regulation of epidermis development; IDA:RGD.
GO; GO:0032024; P:positive regulation of insulin secretion; IDA:RGD.
GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
GO; GO:0006029; P:proteoglycan metabolic process; IDA:RGD.
GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0009749; P:response to glucose; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
GO; GO:0006776; P:vitamin A metabolic process; IMP:RGD.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 1.10.565.10; -; 2.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR003074; 1Cnucl_rcpt.
InterPro; IPR003075; 1Cnucl_rcpt_B.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR01288; PROXISOMEPAR.
PRINTS; PR01290; PROXISOMPABR.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
2: Evidence at transcript level;
Complete proteome {ECO:0000313|Proteomes:UP000002494};
DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00407,
ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00517091};
Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00407,
ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00517125};
Nucleus {ECO:0000256|PROSITE-ProRule:PRU00407,
ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00517080};
Receptor {ECO:0000256|RuleBase:RU004334, ECO:0000313|EMBL:CAC29088.1};
Reference proteome {ECO:0000313|Proteomes:UP000002494};
Transcription {ECO:0000256|PROSITE-ProRule:PRU00407,
ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00517167};
Transcription regulation {ECO:0000256|PROSITE-ProRule:PRU00407,
ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00517167};
Zinc {ECO:0000256|PROSITE-ProRule:PRU00407,
ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00517125};
Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00407,
ECO:0000256|RuleBase:RU004334, ECO:0000256|SAAS:SAAS00517125}.
DOMAIN 70 144 Nuclear receptor.
{ECO:0000259|PROSITE:PS51030}.
DNA_BIND 70 144 Nuclear receptor. {ECO:0000256|PROSITE-
ProRule:PRU00407}.
SEQUENCE 440 AA; 49675 MW; 362F943C37D4CFF3 CRC64;
MEQPQEETPE AREEEKEEVA TGDGAPELNG GPEHTLPSSS CTDLSQNSSP SSLLDQLQMG
CDGASGGSLN MECRVCGDKA SGFHYGVHAC EGCKGFFRRT IRMKLKYEKC DRICKIQKKN
RNKCQYCRFQ KCLALGMSHN AIRFGRMPEA EKRKLVAGLT ASEGCQQNPQ LADLKAFSKH
IYNAYLKNFN MTKKKARSIL TGKSSHNAPF IIHDIETLWQ AEKGLVWKQL VNGPPPYNEI
SVHVFYRCQS TTVETVRELT EFAKNIPNFS SLFLNDQVTL LKYGVHEAIF AMLASIVNKD
GLLVANGSGF VTHEFLRSIR KPFSDIIEPK FEFAVKFNAL ELDDSDLALF IAAIILCGDR
PGLMNVPQVE AIQDTILQAL EFHLQVNHPD SQYLFPKLLQ KMADLRQLVT EHAQMMQWLK
KTESETLLHP LLQEIYKDMY


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