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   04-NOV-2026, entry version 160.
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 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 IN COMPLEX WITH NR5A2 AND OF 115-131 IN COMPLEX WITH
RP   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:15721253, PubMed:15976031, PubMed:9003453). Interacts with
CC       RORG, NFIL3, NR1D1 and BHLHE41 (By similarity). Interacts with HNF4A;
CC       the resulting heterodimer is transcriptionally 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   AlphaFoldDB; P97947; -.
DR   SMR; P97947; -.
DR   BioGRID; 250721; 4.
DR   CORUM; P97947; -.
DR   DIP; DIP-46314N; -.
DR   FunCoup; P97947; 83.
DR   IntAct; P97947; 3.
DR   STRING; 10116.ENSRNOP00000009683; -.
DR   PhosphoSitePlus; P97947; -.
DR   PaxDb; 10116-ENSRNOP00000009683; -.
DR   Ensembl; ENSRNOT00000009683.4; ENSRNOP00000009683.1; ENSRNOG00000007229.4.
DR   Ensembl; ENSRNOT00055044436; ENSRNOP00055036343; ENSRNOG00055025765.
DR   Ensembl; ENSRNOT00060052804; ENSRNOP00060043891; ENSRNOG00060030410.
DR   Ensembl; ENSRNOT00065040071; ENSRNOP00065032576; ENSRNOG00065023452.
DR   GeneID; 117274; -.
DR   KEGG; rno:117274; -.
DR   UCSC; RGD:621032; rat.
DR   AGR; RGD:621032; -.
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; AACPCQG; -.
DR   OrthoDB; 9926883at2759; -.
DR   PhylomeDB; P97947; -.
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 cell types or tissues.
DR   ExpressionAtlas; P97947; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0017053; C:transcription repressor complex; ISO:RGD.
DR   GO; GO:0016922; F:nuclear receptor binding; IBA:GO_Central.
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:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:RGD.
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:0007219; P:Notch signaling pathway; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; 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:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0009749; P:response to glucose; IMP:RGD.
DR   FunFam; 1.10.565.10:FF:000028; Nuclear receptor subfamily 0 group B member 2; 1.
DR   Gene3D; 1.10.565.10; Retinoid X Receptor; 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; NUCLEAR RECEPTOR SUBFAMILY 0 GROUP B; 1.
DR   PANTHER; PTHR24081:SF0; NUCLEAR RECEPTOR SUBFAMILY 0 GROUP B MEMBER 2; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   SMART; SM00430; HOLI; 1.
DR   SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 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
//