NR0B2_RAT
ID NR0B2_RAT Reviewed; 260 AA.
AC P97947;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Nuclear receptor subfamily 0 group B member 2;
DE AltName: Full=Orphan nuclear receptor SHP;
DE AltName: Full=Small heterodimer partner;
GN Name=Nr0b2; Synonyms=Shp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH HNF4A; RARA;
RP RXRA; PPARA AND THRB, AND TISSUE SPECIFICITY.
RC STRAIN=Fischer 344-Jcl, and Sprague-Dawley; TISSUE=Liver;
RX PubMed=9003453; DOI=10.1016/s0167-4781(96)00196-0;
RA Masuda N., Yasumo H., Tamura T., Hashiguchi N., Furusawa T., Tsukamoto T.,
RA Sadano H., Osumi T.;
RT "An orphan nuclear receptor lacking a zinc-finger DNA-binding domain:
RT interaction with several nuclear receptors.";
RL Biochim. Biophys. Acta 1350:27-32(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 17-28 IN COMPLEX WITH NR5A1.
RX PubMed=15721253; DOI=10.1016/j.molcel.2005.02.002;
RA Li Y., Choi M., Cavey G., Daugherty J., Suino K., Kovach A., Bingham N.C.,
RA Kliewer S.A., Xu H.E.;
RT "Crystallographic identification and functional characterization of
RT phospholipids as ligands for the orphan nuclear receptor steroidogenic
RT factor-1.";
RL Mol. Cell 17:491-502(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 16-26 IN COMPLEX WITH NR5A2 AND OF
RP 115-131 IN COMPLEX WITH PPARG.
RX PubMed=15976031; DOI=10.1073/pnas.0501204102;
RA Li Y., Choi M., Suino K., Kovach A., Daugherty J., Kliewer S.A., Xu H.E.;
RT "Structural and biochemical basis for selective repression of the orphan
RT nuclear receptor liver receptor homolog 1 by small heterodimer partner.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:9505-9510(2005).
CC -!- FUNCTION: Transcriptional regulator that acts as a negative regulator
CC of receptor-dependent signaling pathways (By similarity). Specifically
CC inhibits transactivation of the nuclear receptor with which it
CC interacts (By similarity). Inhibits transcriptional activity of NEUROD1
CC on E-box-containing promoter by interfering with the coactivation
CC function of the p300/CBP-mediated transcription complex for NEUROD1 (By
CC similarity). Essential component of the liver circadian clock which via
CC its interaction with NR1D1 and RORG regulates NPAS2-mediated hepatic
CC lipid metabolism (By similarity). Regulates the circadian expression of
CC cytochrome P450 (CYP) enzymes (By similarity). Represses: NR5A2 and
CC HNF4A to down-regulate CYP2C38, NFLI3 to up-regulate CYP2A5,
CC BHLHE41/HNF1A axis to up-regulate CYP1A2, CYP2E1 and CYP3A11, and NR1D1
CC to up-regulate CYP2B10, CYP4A10 and CYP4A14 (By similarity).
CC {ECO:0000250|UniProtKB:Q15466, ECO:0000250|UniProtKB:Q62227}.
CC -!- SUBUNIT: Heterodimer; efficient DNA binding requires dimerization with
CC another bHLH protein (By similarity). Interacts (via N-terminus) with
CC NEUROD1 (via N-terminus and C-terminus) (By similarity). Interacts with
CC ID2 (By similarity). Interacts with NR1I3 and EID1 (By similarity).
CC Interacts with RARA, RXRA, THRB, NR5A1, NR5A2, PPARA and PPARG
CC (PubMed:9003453, PubMed:15976031, PubMed:15721253). Interacts with
CC RORG, NFIL3, NR1D1 and BHLHE41 (By similarity). Interacts with HNF4A;
CC the resulting heterodimer is transcriptionnally inactive (By
CC similarity). Interacts with DDX3X; this interaction disrupts the
CC interaction between HNF4 and NR0B2/SHP that forms inactive heterodimers
CC and enhances the formation of active HNF4 homodimers (By similarity).
CC {ECO:0000250|UniProtKB:Q15466, ECO:0000250|UniProtKB:Q62227,
CC ECO:0000269|PubMed:15721253, ECO:0000269|PubMed:15976031,
CC ECO:0000269|PubMed:9003453}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q15466}. Nucleus
CC {ECO:0000305}. Note=Colocalizes with NEUROD1 in the nucleus.
CC {ECO:0000250|UniProtKB:Q15466}.
CC -!- TISSUE SPECIFICITY: Detected in kidney, testis, heart and liver.
CC {ECO:0000269|PubMed:9003453}.
CC -!- PTM: Arginine methylation by PRMT5 enhances repression activity of
CC metabolic genes in liver in response to bile acid signaling, by
CC increasing interaction with cofactors. {ECO:0000250|UniProtKB:Q62227}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR0
CC subfamily. {ECO:0000305}.
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DR EMBL; D86839; BAA13171.1; -; Genomic_DNA.
DR EMBL; D86580; BAA13127.1; -; mRNA.
DR EMBL; BC088117; AAH88117.1; -; mRNA.
DR RefSeq; NP_476474.1; NM_057133.1.
DR PDB; 1YP0; X-ray; 1.50 A; B=17-28.
DR PDB; 1ZGY; X-ray; 1.80 A; B=115-131.
DR PDB; 1ZH7; X-ray; 2.50 A; C/D=16-26.
DR PDBsum; 1YP0; -.
DR PDBsum; 1ZGY; -.
DR PDBsum; 1ZH7; -.
DR AlphaFoldDB; P97947; -.
DR SMR; P97947; -.
DR BioGRID; 250721; 4.
DR DIP; DIP-46314N; -.
DR IntAct; P97947; 3.
DR STRING; 10116.ENSRNOP00000009683; -.
DR PhosphoSitePlus; P97947; -.
DR PaxDb; P97947; -.
DR Ensembl; ENSRNOT00000009683; ENSRNOP00000009683; ENSRNOG00000007229.
DR GeneID; 117274; -.
DR KEGG; rno:117274; -.
DR UCSC; RGD:621032; rat.
DR CTD; 8431; -.
DR RGD; 621032; Nr0b2.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00390000015719; -.
DR HOGENOM; CLU_093194_0_0_1; -.
DR InParanoid; P97947; -.
DR OMA; FFRPIVG; -.
DR OrthoDB; 955476at2759; -.
DR PhylomeDB; P97947; -.
DR TreeFam; TF332386; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR EvolutionaryTrace; P97947; -.
DR PRO; PR:P97947; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007229; Expressed in stomach and 16 other tissues.
DR Genevisible; P97947; RN.
DR GO; GO:0000785; C:chromatin; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; IPI:RGD.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IPI:RGD.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:RGD.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; ISO:RGD.
DR GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
DR GO; GO:0015721; P:bile acid and bile salt transport; IEP:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009749; P:response to glucose; IMP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR IDEAL; IID50220; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR033544; NR0B1/2.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR PANTHER; PTHR24081; PTHR24081; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR SMART; SM00430; HOLI; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Cytoplasm; Methylation; Nucleus;
KW Receptor; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..260
FT /note="Nuclear receptor subfamily 0 group B member 2"
FT /id="PRO_0000232757"
FT DOMAIN 16..260
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT MOD_RES 57
FT /note="Symmetric dimethylarginine; by PRMT5"
FT /evidence="ECO:0000250|UniProtKB:Q62227"
FT HELIX 20..25
FT /evidence="ECO:0007829|PDB:1YP0"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1ZGY"
SQ SEQUENCE 260 AA; 28750 MW; 71C1E09C8B912A79 CRC64;
MSSSQSGVCP CQGSASHPTI LYTLLSPGPR TRPMAPASRS HCLCQQHRPV RLCAPHRTCR
EALDVLGKTV AFLRNLPSFC LLPHEDQRRL LEGCWGPLFL LGLAQDTVTF EVAEAPVPSI
LKKILLEEPN SGAQGAQPPD PPQPSLAAVQ WLQHCLESFW SLELGPKEYA YLKGTILFNP
DVPGLHASCH IAHLQQEAHW ALCEVLEPWY PASQGRLARI LLMASTLKNI SCTLLVDLFF
RPVIGDVDIT ELLEDMLLLR
