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Database: UniProt
Entry: A0A1S3G8A6_DIPOR
LinkDB: A0A1S3G8A6_DIPOR
Original site: A0A1S3G8A6_DIPOR 
ID   A0A1S3G8A6_DIPOR        Unreviewed;       433 AA.
AC   A0A1S3G8A6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Peroxisome proliferator-activated receptor delta isoform X1 {ECO:0000313|RefSeq:XP_012885051.1};
GN   Name=Ppard {ECO:0000313|RefSeq:XP_012885051.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012885051.1};
RN   [1] {ECO:0000313|RefSeq:XP_012885051.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012885051.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {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   RefSeq; XP_012885051.1; XM_013029597.1.
DR   AlphaFoldDB; A0A1S3G8A6; -.
DR   STRING; 10020.ENSDORP00000008598; -.
DR   GeneID; 105995757; -.
DR   KEGG; dord:105995757; -.
DR   CTD; 5467; -.
DR   InParanoid; A0A1S3G8A6; -.
DR   OMA; RPGLMDV; -.
DR   OrthoDB; 3475284at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0070539; F:linoleic acid binding; IEA:Ensembl.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:Ensembl.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IEA:Ensembl.
DR   GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0008366; P:axon ensheathment; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:Ensembl.
DR   GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0070341; P:fat cell proliferation; IEA:Ensembl.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:Ensembl.
DR   GO; GO:0015908; P:fatty acid transport; IEA:Ensembl.
DR   GO; GO:0051546; P:keratinocyte migration; IEA:Ensembl.
DR   GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:1902894; P:negative regulation of miRNA transcription; IEA:Ensembl.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR   GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0001890; P:placenta development; IEA:Ensembl.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR   GO; GO:0070346; P:positive regulation of fat cell proliferation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:2000288; P:positive regulation of myoblast proliferation; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IEA:Ensembl.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IEA:Ensembl.
DR   GO; GO:0042060; P:wound healing; 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; IPR003075; 1Cnucl_rcpt_B.
DR   InterPro; IPR035500; NHR-like_dom_sf.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR   InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   PANTHER; PTHR24082; NUCLEAR HORMONE RECEPTOR; 1.
DR   PANTHER; PTHR24082:SF15; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR DELTA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR01288; PROXISOMEPAR.
DR   PRINTS; PR01290; PROXISOMPABR.
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:UP000081671};
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          63..137
FT                   /note="Nuclear receptor"
FT                   /evidence="ECO:0000259|PROSITE:PS51030"
FT   DOMAIN          203..431
FT                   /note="NR LBD"
FT                   /evidence="ECO:0000259|PROSITE:PS51843"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   433 AA;  48915 MW;  8D40AF6BE1AFC56A CRC64;
     MEQPQEAAPE VREEEEKEEE AAAEGAPLPS SSSCTDLSQS ASPPSLLDQL QMGCDGASGG
     GLNMECRVCG DKASGFHYGV HACEGCKGFF RRTIRMKLEY EKCDRSCKIQ KKNRNKCQYC
     RFQKCLALGM SHNAIRFGRM PEAEKRKLVA GLTASEGHQH NPQLADLKAF SKHIYNAYLK
     NFNMTKKKAR SILTGKSSHT APFVIHDIET LWQAEKGLVW KQLVNSLPPY KEISVHVFYR
     CQCTTVETVR ELTEFAKSIP NFSSLFLNDQ VTLLKYGVHE AIFAMLASIV NKDGLLVANG
     SGFVTHEFLR SLRKPFSDII EPKFEFAVKF NALELDDSDL ALFIAAIILC GDRPGLMNVP
     QVEAIQDTIL RALEFHLQAN HPDSQYLFPK LLQKMADLRQ LVTEHAQMMQ WLKKTETETL
     LHPLLQEIYK DMY
//
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