NR0B1_MOUSE
ID NR0B1_MOUSE Reviewed; 472 AA.
AC Q61066; O09068; O09147;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Nuclear receptor subfamily 0 group B member 1;
DE AltName: Full=Nuclear receptor DAX-1;
GN Name=Nr0b1; Synonyms=Ahch, Dax1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=8921887; DOI=10.1016/0378-1119(96)00320-4;
RA Guo W., Lovell R.S., Zhang Y.H., Huang B.L., Burris T.P., Craigen W.J.,
RA McCabe E.R.B.;
RT "Ahch, the mouse homologue of DAX1: cloning, characterization and synteny
RT with GyK, the glycerol kinase locus.";
RL Gene 178:31-34(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8756567; DOI=10.1210/endo.137.9.8756567;
RA Bae D.S., Schaefer M.L., Partan B.W., Muglia L.;
RT "Characterization of the mouse DAX-1 gene reveals evolutionary conservation
RT of a unique amino-terminal motif and widespread expression in mouse
RT tissue.";
RL Endocrinology 137:3921-3927(1996).
RN [3]
RP DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=16466956; DOI=10.1016/j.ymgme.2005.12.010;
RA Niakan K.K., Davis E.C., Clipsham R.C., Jiang M., Dehart D.B., Sulik K.K.,
RA McCabe E.R.B.;
RT "Novel role for the orphan nuclear receptor Dax1 in embryogenesis,
RT different from steroidogenesis.";
RL Mol. Genet. Metab. 88:261-271(2006).
RN [4]
RP INTERACTION WITH ESRRB.
RX PubMed=27601327; DOI=10.1016/j.bbrc.2016.09.011;
RA Uranishi K., Akagi T., Koide H., Yokota T.;
RT "Esrrb directly binds to Gata6 promoter and regulates its expression with
RT Dax1 and Ncoa3.";
RL Biochem. Biophys. Res. Commun. 478:1720-1725(2016).
CC -!- FUNCTION: Orphan nuclear receptor. Component of a cascade required for
CC the development of the hypothalamic-pituitary-adrenal-gonadal axis.
CC Acts as a coregulatory protein that inhibits the transcriptional
CC activity of other nuclear receptors through heterodimeric interactions.
CC May also have a role in the development of the embryo and in the
CC maintenance of embryonic stem cell pluripotency (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:16466956}.
CC -!- SUBUNIT: Homodimer. Interacts with NR5A1, NR5A2, NR0B2 and with COPS2
CC (By similarity). Interacts with ESRRB; represses ESRRB activity at the
CC GATA6 promoter (PubMed:27601327). {ECO:0000250,
CC ECO:0000269|PubMed:27601327}.
CC -!- INTERACTION:
CC Q61066; Q61539: Esrrb; NbExp=2; IntAct=EBI-2312665, EBI-2312731;
CC Q61066; Q80Z64: Nanog; NbExp=7; IntAct=EBI-2312665, EBI-2312517;
CC Q61066; P20263: Pou5f1; NbExp=5; IntAct=EBI-2312665, EBI-1606219;
CC Q61066; Q6PR54: Rif1; NbExp=2; IntAct=EBI-2312665, EBI-2312621;
CC Q61066; P70414: Slc8a1; NbExp=2; IntAct=EBI-2312665, EBI-2312694;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Shuttles between the cytoplasm and nucleus. Homodimers exits in
CC the cytoplasm and in the nucleus (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in adult cerebral cortex, spinal cord,
CC thymus, heart, lung, ovary, testis, adrenal gland, hypothalamus, spleen
CC and kidney. {ECO:0000269|PubMed:8756567}.
CC -!- DEVELOPMENTAL STAGE: Expressed at 5.5 dpc throughout the embryo except
CC in the proximal visceral endoderm. {ECO:0000269|PubMed:16466956}.
CC -!- DOMAIN: Homodimerization involved an interaction between amino and
CC carboxy termini involving LXXLL motifs and steroid binding domain (AF-2
CC motif). Heterodimerizes with NR5A1 and NROB2 through its N-terminal
CC LXXLL motifs (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR0
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S83180; AAB46875.1; -; Genomic_DNA.
DR EMBL; S83178; AAB46875.1; JOINED; Genomic_DNA.
DR EMBL; U41568; AAC52920.1; -; mRNA.
DR CCDS; CCDS30260.1; -.
DR PIR; JC5199; JC5199.
DR RefSeq; NP_031456.1; NM_007430.5.
DR PDB; 3F5C; X-ray; 3.00 A; B/C=205-472.
DR PDBsum; 3F5C; -.
DR AlphaFoldDB; Q61066; -.
DR SMR; Q61066; -.
DR BioGRID; 198035; 17.
DR DIP; DIP-29929N; -.
DR IntAct; Q61066; 13.
DR MINT; Q61066; -.
DR STRING; 10090.ENSMUSP00000026036; -.
DR iPTMnet; Q61066; -.
DR PhosphoSitePlus; Q61066; -.
DR PaxDb; Q61066; -.
DR PRIDE; Q61066; -.
DR ProteomicsDB; 293716; -.
DR Antibodypedia; 10329; 651 antibodies from 45 providers.
DR DNASU; 11614; -.
DR Ensembl; ENSMUST00000026036; ENSMUSP00000026036; ENSMUSG00000025056.
DR GeneID; 11614; -.
DR KEGG; mmu:11614; -.
DR UCSC; uc009tsd.1; mouse.
DR CTD; 190; -.
DR MGI; MGI:1352460; Nr0b1.
DR VEuPathDB; HostDB:ENSMUSG00000025056; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00390000015719; -.
DR HOGENOM; CLU_674314_0_0_1; -.
DR InParanoid; Q61066; -.
DR OMA; WGCSCGA; -.
DR OrthoDB; 955476at2759; -.
DR PhylomeDB; Q61066; -.
DR TreeFam; TF332386; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR BioGRID-ORCS; 11614; 3 hits in 74 CRISPR screens.
DR EvolutionaryTrace; Q61066; -.
DR PRO; PR:Q61066; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q61066; protein.
DR Bgee; ENSMUSG00000025056; Expressed in indifferent gonad and 36 other tissues.
DR ExpressionAtlas; Q61066; baseline and differential.
DR Genevisible; Q61066; MM.
DR GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0042788; C:polysomal ribosome; IDA:HGNC-UCL.
DR GO; GO:0050682; F:AF-2 domain binding; ISO:MGI.
DR GO; GO:0032448; F:DNA hairpin binding; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:HGNC-UCL.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IGI:MGI.
DR GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR GO; GO:0030325; P:adrenal gland development; IGI:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; IMP:MGI.
DR GO; GO:0008406; P:gonad development; ISO:MGI.
DR GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0030238; P:male sex determination; IMP:MGI.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0033144; P:negative regulation of intracellular steroid hormone receptor signaling pathway; ISO:MGI.
DR GO; GO:0010894; P:negative regulation of steroid biosynthetic process; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR GO; GO:0035902; P:response to immobilization stress; IMP:MGI.
DR GO; GO:0060008; P:Sertoli cell differentiation; IMP:MGI.
DR GO; GO:0007530; P:sex determination; IGI:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR IDEAL; IID50228; -.
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 InterPro; IPR025900; Nuclear_receptor_repeat.
DR PANTHER; PTHR24081; PTHR24081; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF14046; NR_Repeat; 4.
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; Cytoplasm; Nucleus; Receptor; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..472
FT /note="Nuclear receptor subfamily 0 group B member 1"
FT /id="PRO_0000053749"
FT REPEAT 1..67
FT /note="1"
FT REPEAT 68..135
FT /note="2"
FT REPEAT 136..202
FT /note="3"
FT DOMAIN 190..471
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT REPEAT 203..255
FT /note="4; truncated"
FT REGION 1..255
FT /note="4 X 67 AA tandem repeats"
FT REGION 214..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 324..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..17
FT /note="LXXLL motif 1"
FT MOTIF 80..84
FT /note="LXXLL motif 2"
FT MOTIF 148..152
FT /note="LXXLL motif 3"
FT MOTIF 463..468
FT /note="AF-2 motif"
FT COMPBIAS 214..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 253..272
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 275..278
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 282..303
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 359..372
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 399..420
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 426..438
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 445..450
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 452..455
FT /evidence="ECO:0007829|PDB:3F5C"
FT HELIX 460..467
FT /evidence="ECO:0007829|PDB:3F5C"
SQ SEQUENCE 472 AA; 52576 MW; DE1FB01C30F883CF CRC64;
MAGEDHPWQG SILYNLLMSA KQKHASQEER EVRLGAQCWG CACGAQPVLG GERLSGGQAR
SLLYRCCFCG ENHPRQGGIL YSMLTNARQP SVATQAPRAR FGAPCWGCAC GSAEPLVGRE
GLPAGQAPSL LYRCCFCGEE HPRQGSILYS LLTSAQQTHV SREAPEAHRR GEWWQLSYCT
QSVGGPEGLQ STQAMAFLYR SYVCGEEQPQ QISVASGTPV SADQTPATPQ EQPRAPWWDA
SPGVQRLITL KDPQVVCEAA SAGLLKTLRF VKYLPCFQIL PLDQQLVLVR SCWAPLLMLE
LAQDHLHFEM MEIPETNTTQ EMLTTRRQET EGPEPAEPQA TEQPQMVSAE AGHLLPAAAV
QAIKSFFFKC WSLNIDTKEY AYLKGTVLFN PDLPGLQCVK YIEGLQWRTQ QILTEHIRMM
QREYQIRSAE LNSALFLLRF INSDVVTELF FRPIIGAVSM DDMMLEMLCA KL
