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 01-MAY-2013, entry version 152.
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 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: Functions as a constitutive transcriptional repressor.
CC In collaboration with SP1, activates GJA1 transcription (By
CC similarity). Possible receptor for triiodothyronine.
CC -!- SUBUNIT: Interacts with C1D and NR2E3 (By similarity). Interacts
CC with SP1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- TISSUE SPECIFICITY: Expressed in all tissues and cell lines
CC examined. Expressed at high levels in some squamous carcinoma cell
CC lines.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC a DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily.
CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
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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 IPI; IPI00023603; -.
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 DIP; DIP-48396N; -.
DR IntAct; P20393; 1.
DR STRING; 9606.ENSP00000246672; -.
DR PhosphoSite; P20393; -.
DR DMDM; 119100; -.
DR PaxDb; P20393; -.
DR PRIDE; P20393; -.
DR DNASU; 9572; -.
DR Ensembl; ENST00000246672; ENSP00000246672; ENSG00000126368.
DR GeneID; 9572; -.
DR KEGG; hsa:9572; -.
DR UCSC; uc002htz.2; 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 HOGENOM; HOG000261691; -.
DR HOVERGEN; HBG106790; -.
DR InParanoid; P20393; -.
DR KO; K03728; -.
DR OMA; SCHQPNS; -.
DR OrthoDB; EOG4DV5KZ; -.
DR Pathway_Interaction_DB; circadianpathway; Circadian rhythm pathway.
DR Reactome; REACT_24941; Circadian Clock.
DR Reactome; REACT_71; Gene Expression.
DR BindingDB; P20393; -.
DR ChEMBL; CHEMBL1961783; -.
DR ChiTaRS; NR1D1; human.
DR EvolutionaryTrace; P20393; -.
DR GenomeRNAi; 9572; -.
DR NextBio; 35899; -.
DR ArrayExpress; P20393; -.
DR Bgee; P20393; -.
DR CleanEx; HS_NR1D1; -.
DR Genevestigator; P20393; -.
DR GermOnline; ENSG00000126368; Homo sapiens.
DR GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0004879; F:ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity; TAS:ProtInc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003707; F:steroid hormone receptor activity; TAS:ProtInc.
DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
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:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
DR GO; GO:0007623; P:circadian rhythm; IEA:Compara.
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; IMP:BHF-UCL.
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; Str_ncl_receptor; 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; Activator; Complete proteome; DNA-binding;
KW Metal-binding; Nucleus; Receptor; Reference proteome; Repressor;
KW Transcription; Transcription regulation; 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.
FT ZN_FING 132 152 NR C4-type.
FT ZN_FING 169 193 NR C4-type.
FT COMPBIAS 82 93 Poly-Ser.
FT CONFLICT 147 147 H -> L (in Ref. 2; CAB53540).
FT CONFLICT 564 564 E -> Q (in Ref. 2).
FT TURN 133 135
FT STRAND 136 138
FT STRAND 141 143
FT STRAND 146 148
FT HELIX 150 160
FT STRAND 170 173
FT TURN 179 183
FT HELIX 186 193
FT TURN 194 197
FT HELIX 200 202
FT HELIX 285 299
FT HELIX 434 456
FT HELIX 460 462
FT HELIX 465 486
FT HELIX 509 511
FT HELIX 514 529
FT HELIX 534 546
FT HELIX 556 577
FT HELIX 584 589
FT HELIX 591 602
FT STRAND 606 610
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
//
