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Database: UniProt
Entry: P20393
LinkDB: P20393
Original site: P20393 
ID   NR1D1_HUMAN             Reviewed;         614 AA.
AC   P20393; Q0P5Z4; Q15304;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   26-NOV-2014, entry version 169.
DE   RecName: Full=Nuclear receptor subfamily 1 group D member 1;
DE   AltName: Full=Rev-erbA-alpha;
DE   AltName: Full=V-erbA-related protein 1;
DE            Short=EAR-1;
GN   Name=NR1D1; Synonyms=EAR1, HREV, THRAL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=2539258; DOI=10.1016/0092-8674(89)90169-4;
RA   Miyajima N., Horiuchi R., Shibuya Y., Fukushige S., Matsubara K.,
RA   Toyoshima K., Yamamoto T.;
RT   "Two erbA homologs encoding proteins with different T3 binding
RT   capacities are transcribed from opposite DNA strands of the same
RT   genetic locus.";
RL   Cell 57:31-39(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Fetal skeletal muscle;
RX   PubMed=1971514; DOI=10.1089/dna.1990.9.77;
RA   Lazar M.A., Jones K.E., Chin W.W.;
RT   "Isolation of a cDNA encoding human Rev-ErbA alpha: transcription from
RT   the noncoding DNA strand of a thyroid hormone receptor gene results in
RT   a related protein that does not bind thyroid hormone.";
RL   DNA Cell Biol. 9:77-83(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PNS;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 549-614.
RX   PubMed=1850510; DOI=10.1093/nar/19.5.1105;
RA   Laudet V., Begue A., Henry C., Joubel A., Martin P., Stehelin D.,
RA   Saule S.;
RT   "Genomic organization of the human thyroid hormone receptor alpha (c-
RT   erbA-1) gene.";
RL   Nucleic Acids Res. 19:1105-1112(1991).
RN   [5]
RP   FUNCTION.
RX   PubMed=12021280; DOI=10.1074/jbc.M203421200;
RA   Coste H., Rodriguez J.C.;
RT   "Orphan nuclear hormone receptor Rev-erbalpha regulates the human
RT   apolipoprotein CIII promoter.";
RL   J. Biol. Chem. 277:27120-27129(2002).
RN   [6]
RP   FUNCTION.
RX   PubMed=15761026; DOI=10.1210/me.2005-0057;
RA   Yin L., Lazar M.A.;
RT   "The orphan nuclear receptor Rev-erbalpha recruits the N-CoR/histone
RT   deacetylase 3 corepressor to regulate the circadian Bmal1 gene.";
RL   Mol. Endocrinol. 19:1452-1459(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=16968709; DOI=10.1074/jbc.M607873200;
RA   Wang J., Yin L., Lazar M.A.;
RT   "The orphan nuclear receptor Rev-erb alpha regulates circadian
RT   expression of plasminogen activator inhibitor type 1.";
RL   J. Biol. Chem. 281:33842-33848(2006).
RN   [8]
RP   PHOSPHORYLATION AT SER-55 AND SER-59, AND UBIQUITINATION.
RX   PubMed=16484495; DOI=10.1126/science.1121613;
RA   Yin L., Wang J., Klein P.S., Lazar M.A.;
RT   "Nuclear receptor Rev-erbalpha is a critical lithium-sensitive
RT   component of the circadian clock.";
RL   Science 311:1002-1005(2006).
RN   [9]
RP   INTERACTION WITH ZNHIT1.
RX   PubMed=17892483; DOI=10.1111/j.1742-4658.2007.06062.x;
RA   Wang J., Li Y., Zhang M., Liu Z., Wu C., Yuan H., Li Y.Y., Zhao X.,
RA   Lu H.;
RT   "A zinc finger HIT domain-containing protein, ZNHIT-1, interacts with
RT   orphan nuclear hormone receptor Rev-erbbeta and removes Rev-erbbeta-
RT   induced inhibition of apoCIII transcription.";
RL   FEBS J. 274:5370-5381(2007).
RN   [10]
RP   FUNCTION, AND HEME-BINDING.
RX   PubMed=18006707; DOI=10.1126/science.1150179;
RA   Yin L., Wu N., Curtin J.C., Qatanani M., Szwergold N.R., Reid R.A.,
RA   Waitt G.M., Parks D.J., Pearce K.H., Wisely G.B., Lazar M.A.;
RT   "Rev-erbalpha, a heme sensor that coordinates metabolic and circadian
RT   pathways.";
RL   Science 318:1786-1789(2007).
RN   [11]
RP   FUNCTION.
RX   PubMed=19710360; DOI=10.1101/gad.1825809;
RA   Wu N., Yin L., Hanniman E.A., Joshi S., Lazar M.A.;
RT   "Negative feedback maintenance of heme homeostasis by its receptor,
RT   Rev-erbalpha.";
RL   Genes Dev. 23:2201-2209(2009).
RN   [12]
RP   REVIEW.
RX   PubMed=20414452; DOI=10.1621/nrs.08001;
RA   Yin L., Wu N., Lazar M.A.;
RT   "Nuclear receptor Rev-erbalpha: a heme receptor that coordinates
RT   circadian rhythm and metabolism.";
RL   Nucl. Recept. Signal. 8:E001-E001(2010).
RN   [13]
RP   INTERACTION WITH OPHN1.
RX   PubMed=21874017; DOI=10.1038/nn.2911;
RA   Valnegri P., Khelfaoui M., Dorseuil O., Bassani S., Lagneaux C.,
RA   Gianfelice A., Benfante R., Chelly J., Billuart P., Sala C.,
RA   Passafaro M.;
RT   "A circadian clock in hippocampus is regulated by interaction between
RT   oligophrenin-1 and Rev-erbalpha.";
RL   Nat. Neurosci. 14:1293-1301(2011).
RN   [14]
RP   INTERACTION WITH CRY1 AND PER2.
RX   PubMed=22170608; DOI=10.1038/nature10700;
RA   Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H.,
RA   Jonker J.W., Downes M., Evans R.M.;
RT   "Cryptochromes mediate rhythmic repression of the glucocorticoid
RT   receptor.";
RL   Nature 480:552-556(2011).
RN   [15]
RP   FUNCTION.
RX   PubMed=21479263; DOI=10.1371/journal.pone.0017290;
RA   Crumbley C., Burris T.P.;
RT   "Direct regulation of CLOCK expression by REV-ERB.";
RL   PLoS ONE 6:E17290-E17290(2011).
RN   [16]
RP   REVIEW.
RX   PubMed=22682217; DOI=10.1016/j.cmet.2012.05.006;
RA   Stratmann M., Schibler U.;
RT   "REV-ERBs: more than the sum of the individual parts.";
RL   Cell Metab. 15:791-793(2012).
RN   [17]
RP   REVIEW.
RX   PubMed=22613952; DOI=10.1038/cr.2012.81;
RA   Ripperger J.A., Albrecht U.;
RT   "REV-ERB-erating nuclear receptor functions in circadian metabolism
RT   and physiology.";
RL   Cell Res. 22:1319-1321(2012).
RN   [18]
RP   FUNCTION.
RX   PubMed=22184247; DOI=10.1073/pnas.1106750109;
RA   Gibbs J.E., Blaikley J., Beesley S., Matthews L., Simpson K.D.,
RA   Boyce S.H., Farrow S.N., Else K.J., Singh D., Ray D.W., Loudon A.S.;
RT   "The nuclear receptor REV-ERBalpha mediates circadian regulation of
RT   innate immunity through selective regulation of inflammatory
RT   cytokines.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:582-587(2012).
RN   [19]
RP   FUNCTION, INTERACTION WITH CCAR2, PHOSPHORYLATION AT SER-55 AND
RP   SER-59, AND UBIQUITINATION.
RX   PubMed=23398316; DOI=10.1042/BJ20121085;
RA   Chini C.C., Escande C., Nin V., Chini E.N.;
RT   "DBC1 (Deleted in Breast Cancer 1) modulates the stability and
RT   function of the nuclear receptor Rev-erbalpha.";
RL   Biochem. J. 451:453-461(2013).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 123-215.
RX   PubMed=9660968; DOI=10.1016/S1097-2765(00)80084-2;
RA   Zhao Q., Khorasanizadeh S., Miyoshi Y., Lazar M.A., Rastinejad F.;
RT   "Structural elements of an orphan nuclear receptor-DNA complex.";
RL   Mol. Cell 1:849-861(1998).
CC   -!- FUNCTION: Transcriptional repressor which coordinates circadian
CC       rhythm and metabolic pathways in a heme-dependent manner. Integral
CC       component of the complex transcription machinery that governs
CC       circadian rhythmicity and forms a critical negative limb of the
CC       circadian clock by directly repressing the expression of core
CC       clock components ARTNL/BMAL1, CLOCK and CRY1. Also regulates genes
CC       involved in metabolic functions, including lipid and bile acid
CC       metabolism, adipogenesis, gluconeogenesis and the macrophage
CC       inflammatory response. Acts as a receptor for heme which
CC       stimulates its interaction with the NCOR1/HDAC3 corepressor
CC       complex, enhancing transcriptional repression. Recognizes two
CC       classes of DNA response elements within the promoter of its target
CC       genes and can bind to DNA as either monomers or homodimers,
CC       depending on the nature of the response element. Binds as a
CC       monomer to a response element composed of the consensus half-site
CC       motif 5'-[A/G]GGTCA-3' preceded by an A/T-rich 5' sequence
CC       (RevRE), or as a homodimer to a direct repeat of the core motif
CC       spaced by two nucleotides (RevDR-2). Acts as a potent competitive
CC       repressor of ROR alpha (RORA) function and regulates the levels of
CC       its ligand heme by repressing the expression of PPARGC1A, a potent
CC       inducer of heme synthesis. Regulates lipid metabolism by
CC       repressing the expression of APOC3 and by influencing the activity
CC       of sterol response element binding proteins (SREBPs); represses
CC       INSIG2 which interferes with the proteolytic activation of SREBPs
CC       which in turn govern the rhythmic expression of enzymes with key
CC       functions in sterol and fatty acid synthesis. Regulates
CC       gluconeogenesis via repression of G6PC and PEPCK and adipocyte
CC       differentiation via repression of PPARG. Regulates glucagon
CC       release in pancreatic alpha-cells via the AMPK-NAMPT-SIRT1 pathway
CC       and the proliferation, glucose-induced insulin secretion and
CC       expression of key lipogenic genes in pancreatic-beta cells.
CC       Positively regulates bile acid synthesis by increasing hepatic
CC       expression of CYP7A1 via repression of NR0B2 and NFIL3 which are
CC       negative regulators of CYP7A1. Modulates skeletal muscle oxidative
CC       capacity by regulating mitochondrial biogenesis and autophagy;
CC       controls mitochondrial biogenesis and respiration by interfering
CC       with the STK11-PRKAA1/2-SIRT1-PPARGC1A signaling pathway.
CC       Represses the expression of SERPINE1/PAI1, an important modulator
CC       of cardiovascular disease and the expression of inflammatory
CC       cytokines and chemokines in macrophages. Represses gene expression
CC       at a distance in macrophages by inhibiting the transcription of
CC       enhancer-derived RNAs (eRNAs). Plays a role in the circadian
CC       regulation of body temperature and negatively regulates
CC       thermogenic transcriptional programs in brown adipose tissue
CC       (BAT); imposes a circadian oscillation in BAT activity, increasing
CC       body temperature when awake and depressing thermogenesis during
CC       sleep. In concert with NR2E3, regulates transcriptional networks
CC       critical for photoreceptor development and function. In addition
CC       to its activity as a repressor, can also act as a transcriptional
CC       activator. In the ovarian granulosa cells acts as a
CC       transcriptional activator of STAR which plays a role in steroid
CC       biosynthesis. In collaboration with SP1, activates GJA1
CC       transcription in a heme-independent manner.
CC       {ECO:0000269|PubMed:12021280, ECO:0000269|PubMed:15761026,
CC       ECO:0000269|PubMed:16968709, ECO:0000269|PubMed:18006707,
CC       ECO:0000269|PubMed:19710360, ECO:0000269|PubMed:1971514,
CC       ECO:0000269|PubMed:21479263, ECO:0000269|PubMed:22184247,
CC       ECO:0000269|PubMed:23398316, ECO:0000269|PubMed:2539258}.
CC   -!- SUBUNIT: Binds DNA as a monomer or a homodimer. Interacts with
CC       C1D, NR2E3 and SP1. Interacts with OPHN1 (via C-terminus).
CC       Interacts with ZNHIT1. Interacts with PER2; the interaction
CC       associates PER2 to ARNTL promoter region. Interacts with CRY1.
CC       Interacts with CCAR2. {ECO:0000269|PubMed:17892483,
CC       ECO:0000269|PubMed:21874017, ECO:0000269|PubMed:22170608,
CC       ECO:0000269|PubMed:23398316}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Cell
CC       projection, dendrite {ECO:0000250}. Cell projection, dendritic
CC       spine {ECO:0000250}. Note=Localizes to the cytoplasm, dendrites
CC       and dendritic spine in the presence of OPHN1. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
CC       the liver, adipose tissue, skeletal muscle and brain. Also
CC       expressed in endothelial cells (ECs), vascular smooth muscle cells
CC       (VSMCs) and macrophages. Expression oscillates diurnally in the
CC       suprachiasmatic nucleus (SCN) of the hypothalamus as well as in
CC       peripheral tissues. Expression increases during the
CC       differentiation of pre-adipocytes into mature adipocytes.
CC       Expressed at high levels in some squamous carcinoma cell lines.
CC       {ECO:0000269|PubMed:2539258}.
CC   -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC       a DNA-binding domain and a C-terminal ligand-binding domain.
CC   -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC       {ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:23398316}.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC       subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00407}.
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DR   EMBL; M24898; AAA52335.1; -; mRNA.
DR   EMBL; M24900; AAA52332.1; -; mRNA.
DR   EMBL; X55066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X55067; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X72631; CAB53540.1; -; mRNA.
DR   EMBL; BC047875; AAH47875.1; -; mRNA.
DR   EMBL; BC056148; AAH56148.1; -; mRNA.
DR   EMBL; M34339; AAA36561.1; -; mRNA.
DR   EMBL; M34340; AAA36562.2; -; mRNA.
DR   CCDS; CCDS11361.1; -.
DR   PIR; A32286; A32608.
DR   RefSeq; NP_068370.1; NM_021724.4.
DR   UniGene; Hs.592130; -.
DR   UniGene; Hs.724; -.
DR   PDB; 1A6Y; X-ray; 2.30 A; A/B=123-216.
DR   PDB; 1EF6; Model; -; A=281-301, B=430-614.
DR   PDB; 1GA5; X-ray; 2.40 A; A/B/E/F=123-216.
DR   PDB; 1HLZ; X-ray; 2.80 A; A/B=123-216.
DR   PDB; 3N00; X-ray; 2.60 A; A=281-614.
DR   PDBsum; 1A6Y; -.
DR   PDBsum; 1EF6; -.
DR   PDBsum; 1GA5; -.
DR   PDBsum; 1HLZ; -.
DR   PDBsum; 3N00; -.
DR   ProteinModelPortal; P20393; -.
DR   SMR; P20393; 127-245, 416-611.
DR   BioGrid; 114941; 10.
DR   DIP; DIP-48396N; -.
DR   IntAct; P20393; 2.
DR   STRING; 9606.ENSP00000246672; -.
DR   BindingDB; P20393; -.
DR   ChEMBL; CHEMBL1961783; -.
DR   GuidetoPHARMACOLOGY; 596; -.
DR   PhosphoSite; P20393; -.
DR   DMDM; 119100; -.
DR   MaxQB; P20393; -.
DR   PaxDb; P20393; -.
DR   PRIDE; P20393; -.
DR   DNASU; 9572; -.
DR   Ensembl; ENST00000246672; ENSP00000246672; ENSG00000126368.
DR   GeneID; 9572; -.
DR   KEGG; hsa:9572; -.
DR   UCSC; uc002htz.3; human.
DR   CTD; 9572; -.
DR   GeneCards; GC17M038249; -.
DR   HGNC; HGNC:7962; NR1D1.
DR   HPA; HPA007935; -.
DR   MIM; 602408; gene.
DR   neXtProt; NX_P20393; -.
DR   PharmGKB; PA31748; -.
DR   eggNOG; NOG324222; -.
DR   GeneTree; ENSGT00760000119049; -.
DR   HOGENOM; HOG000261691; -.
DR   HOVERGEN; HBG106790; -.
DR   InParanoid; P20393; -.
DR   KO; K03728; -.
DR   OMA; GTSPGNF; -.
DR   OrthoDB; EOG776SQ0; -.
DR   PhylomeDB; P20393; -.
DR   TreeFam; TF328382; -.
DR   Reactome; REACT_111118; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR   Reactome; REACT_116145; PPARA activates gene expression.
DR   Reactome; REACT_118659; RORA activates circadian gene expression.
DR   Reactome; REACT_118789; REV-ERBA represses gene expression.
DR   Reactome; REACT_15525; Nuclear Receptor transcription pathway.
DR   Reactome; REACT_200608; Transcriptional activation of mitochondrial biogenesis.
DR   Reactome; REACT_24941; Circadian Clock.
DR   SignaLink; P20393; -.
DR   ChiTaRS; NR1D1; human.
DR   EvolutionaryTrace; P20393; -.
DR   GeneWiki; Rev-ErbA_alpha; -.
DR   GenomeRNAi; 9572; -.
DR   NextBio; 35899; -.
DR   PRO; PR:P20393; -.
DR   Bgee; P20393; -.
DR   CleanEx; HS_NR1D1; -.
DR   ExpressionAtlas; P20393; baseline and differential.
DR   Genevestigator; P20393; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR   GO; GO:0004879; F:ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity; TAS:ProtInc.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IMP:NTNU_SB.
DR   GO; GO:0001078; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription; IDA:NTNU_SB.
DR   GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
DR   GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
DR   GO; GO:0001222; F:transcription corepressor binding; IDA:UniProtKB.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0060086; P:circadian temperature homeostasis; ISS:UniProtKB.
DR   GO; GO:0010467; P:gene expression; TAS:Reactome.
DR   GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0030522; P:intracellular receptor signaling pathway; TAS:GOC.
DR   GO; GO:0010871; P:negative regulation of receptor biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0070859; P:positive regulation of bile acid biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0010498; P:proteasomal protein catabolic process; ISS:UniProtKB.
DR   GO; GO:2000188; P:regulation of cholesterol homeostasis; ISS:UniProtKB.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; ISS:UniProtKB.
DR   GO; GO:0035947; P:regulation of gluconeogenesis by regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR   GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
DR   GO; GO:0061469; P:regulation of type B pancreatic cell proliferation; ISS:UniProtKB.
DR   GO; GO:0044321; P:response to leptin; ISS:UniProtKB.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
DR   Gene3D; 1.10.565.10; -; 2.
DR   Gene3D; 3.30.50.10; -; 1.
DR   InterPro; IPR008946; Nucl_hormone_rcpt_ligand-bd.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
DR   InterPro; IPR001723; Str_hrmn_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; SSF48508; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Biological rhythms;
KW   Cell projection; Complete proteome; Cytoplasm; Differentiation;
KW   DNA-binding; Heme; Iron; Metal-binding; Nucleus; Phosphoprotein;
KW   Receptor; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    614       Nuclear receptor subfamily 1 group D
FT                                member 1.
FT                                /FTId=PRO_0000053499.
FT   DNA_BIND    129    205       Nuclear receptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     132    152       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   ZN_FING     169    193       NR C4-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00407}.
FT   REGION        1    128       Modulating.
FT   REGION       49    284       Crucial for activation of GJA1.
FT                                {ECO:0000250}.
FT   REGION      206    284       Hinge.
FT   REGION      285    614       Ligand-binding.
FT   COMPBIAS     82     93       Poly-Ser.
FT   BINDING     418    418       Heme. {ECO:0000250}.
FT   BINDING     602    602       Heme.
FT   MOD_RES      55     55       Phosphoserine; by GSK3-beta.
FT                                {ECO:0000269|PubMed:16484495,
FT                                ECO:0000269|PubMed:23398316}.
FT   MOD_RES      59     59       Phosphoserine; by GSK3-beta.
FT                                {ECO:0000269|PubMed:16484495,
FT                                ECO:0000269|PubMed:23398316}.
FT   MOD_RES     191    191       N6-acetyllysine; by KAT5. {ECO:0000250}.
FT   MOD_RES     192    192       N6-acetyllysine; by KAT5. {ECO:0000250}.
FT   CONFLICT    147    147       H -> L (in Ref. 2; CAB53540).
FT                                {ECO:0000305}.
FT   CONFLICT    564    564       E -> Q (in Ref. 2). {ECO:0000305}.
FT   TURN        133    135       {ECO:0000244|PDB:1A6Y}.
FT   STRAND      136    138       {ECO:0000244|PDB:1A6Y}.
FT   STRAND      141    143       {ECO:0000244|PDB:1A6Y}.
FT   STRAND      146    148       {ECO:0000244|PDB:1A6Y}.
FT   HELIX       150    160       {ECO:0000244|PDB:1A6Y}.
FT   STRAND      170    173       {ECO:0000244|PDB:1GA5}.
FT   TURN        179    183       {ECO:0000244|PDB:1A6Y}.
FT   HELIX       186    193       {ECO:0000244|PDB:1A6Y}.
FT   TURN        194    197       {ECO:0000244|PDB:1A6Y}.
FT   HELIX       200    202       {ECO:0000244|PDB:1GA5}.
FT   HELIX       285    299       {ECO:0000244|PDB:3N00}.
FT   HELIX       434    456       {ECO:0000244|PDB:3N00}.
FT   HELIX       460    462       {ECO:0000244|PDB:3N00}.
FT   HELIX       465    486       {ECO:0000244|PDB:3N00}.
FT   HELIX       509    511       {ECO:0000244|PDB:3N00}.
FT   HELIX       514    529       {ECO:0000244|PDB:3N00}.
FT   HELIX       534    546       {ECO:0000244|PDB:3N00}.
FT   HELIX       556    577       {ECO:0000244|PDB:3N00}.
FT   HELIX       584    589       {ECO:0000244|PDB:3N00}.
FT   HELIX       591    602       {ECO:0000244|PDB:3N00}.
FT   STRAND      606    610       {ECO:0000244|PDB:3N00}.
SQ   SEQUENCE   614 AA;  66805 MW;  67C71758E166508A CRC64;
     MTTLDSNNNT GGVITYIGSS GSSPSRTSPE SLYSDNSNGS FQSLTQGCPT YFPPSPTGSL
     TQDPARSFGS IPPSLSDDGS PSSSSSSSSS SSSFYNGSPP GSLQVAMEDS SRVSPSKSTS
     NITKLNGMVL LCKVCGDVAS GFHYGVHACE GCKGFFRRSI QQNIQYKRCL KNENCSIVRI
     NRNRCQQCRF KKCLSVGMSR DAVRFGRIPK REKQRMLAEM QSAMNLANNQ LSSQCPLETS
     PTQHPTPGPM GPSPPPAPVP SPLVGFSQFP QQLTPPRSPS PEPTVEDVIS QVARAHREIF
     TYAHDKLGSS PGNFNANHAS GSPPATTPHR WENQGCPPAP NDNNTLAAQR HNEALNGLRQ
     APSSYPPTWP PGPAHHSCHQ SNSNGHRLCP THVYAAPEGK APANSPRQGN SKNVLLACPM
     NMYPHGRSGR TVQEIWEDFS MSFTPAVREV VEFAKHIPGF RDLSQHDQVT LLKAGTFEVL
     MVRFASLFNV KDQTVMFLSR TTYSLQELGA MGMGDLLSAM FDFSEKLNSL ALTEEELGLF
     TAVVLVSADR SGMENSASVE QLQETLLRAL RALVLKNRPL ETSRFTKLLL KLPDLRTLNN
     MHSEKLLSFR VDAQ
//
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