NR1I3_RAT
ID NR1I3_RAT Reviewed; 358 AA.
AC Q9QUS1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Nuclear receptor subfamily 1 group I member 3;
DE AltName: Full=Constitutive androstane receptor;
DE Short=CAR;
GN Name=Nr1i3; Synonyms=Car;
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 [MRNA].
RC STRAIN=Fischer, and Wistar Kyoto; TISSUE=Liver;
RX PubMed=11160864; DOI=10.1124/mol.59.2.278;
RA Yoshinari K., Sueyoshi T., Moore R., Negishi M.;
RT "Nuclear receptor CAR as a regulatory factor for the sexually dimorphic
RT induction of CYB2B1 gene by phenobarbital in rat livers.";
RL Mol. Pharmacol. 59:278-284(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Wistar; TISSUE=Liver;
RA Kanno Y., Aoki S., Nakahama T., Inouye Y.;
RT "Role of the defective splicing of mRNA in the lack of pulmonary expression
RT of constitutively active receptor in rat.";
RL J. Health Sci. 49:541-546(2003).
CC -!- FUNCTION: Binds and transactivates the retinoic acid response elements
CC that control expression of the retinoic acid receptor beta 2 and
CC alcohol dehydrogenase 3 genes. Transactivates both the phenobarbital
CC responsive element module of the human CYP2B6 gene and the CYP3A4
CC xenobiotic response element (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of NR1I3 and RXR. Interacts with PSMC4. Interacts
CC with ECT2. Directly interacts with DNAJC7; this complex may also
CC include HSP90 (By similarity). Interacts with CRY1 (By similarity).
CC Interacts with CRY2 in a ligand-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:O35627}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Recruited to the cytoplasm by DNAJC7. {ECO:0000250}.
CC -!- DOMAIN: Composed by a short N-terminal domain followed by the DNA
CC binding, hinge, and ligand binding/dimerization domains.
CC -!- PTM: Phosphorylated at Thr-48 by PKC, dephosphorylation of Thr-48 is
CC required for nuclear translocation and activation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; AF133095; AAF22567.1; -; mRNA.
DR EMBL; AF133094; AAF22566.1; -; mRNA.
DR EMBL; AB104736; BAC82431.1; -; mRNA.
DR EMBL; AB105071; BAC84955.1; -; Genomic_DNA.
DR RefSeq; NP_075230.1; NM_022941.4.
DR AlphaFoldDB; Q9QUS1; -.
DR SMR; Q9QUS1; -.
DR STRING; 10116.ENSRNOP00000048836; -.
DR ChEMBL; CHEMBL3509594; -.
DR PhosphoSitePlus; Q9QUS1; -.
DR PaxDb; Q9QUS1; -.
DR Ensembl; ENSRNOT00000049873; ENSRNOP00000048836; ENSRNOG00000003260.
DR GeneID; 65035; -.
DR KEGG; rno:65035; -.
DR UCSC; RGD:621400; rat.
DR CTD; 9970; -.
DR RGD; 621400; Nr1i3.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000160641; -.
DR HOGENOM; CLU_007368_12_0_1; -.
DR InParanoid; Q9QUS1; -.
DR OrthoDB; 297114at2759; -.
DR PhylomeDB; Q9QUS1; -.
DR TreeFam; TF316304; -.
DR Reactome; R-RNO-383280; Nuclear Receptor transcription pathway.
DR PRO; PR:Q9QUS1; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Genevisible; Q9QUS1; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0001649; P:osteoblast differentiation; IEP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001728; ThyrH_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 PRINTS; PR00546; THYROIDHORMR.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; Cytoskeleton; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..358
FT /note="Nuclear receptor subfamily 1 group I member 3"
FT /id="PRO_0000053556"
FT DOMAIN 119..358
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 18..93
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 21..41
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 57..81
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT MOD_RES 48
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q14994"
SQ SEQUENCE 358 AA; 40923 MW; 13691F49CAD8F1ED CRC64;
MTATLTLETM TSEEEYGPRN CVVCGDRATG YHFHALTCEG CKGFFRRTVS KTIGPICPFA
GRCEVSKAQR RHCPACRLQK CLNVGMRKDM ILSAEALALR RARQARRRAQ KASLQLSQQQ
KELIQTLLGA HTRHVGPMFD QFVQFRPPAY LFSHHRPFQP LAPVLPLLTH FADINTFMVQ
QIIKFTKDLP LFRSLTMEDQ ISLLKGAAVE ILHISLNTTF CLQTQNFFCG PLCYKMEDAV
HVGFQYEFLE LIIHFHKTLK RLQLQEPEYA LMAAMALFSP DRPGVTQREE IDQLQEEVAL
ILNNHIMEQQ SRLQSRFLYA KLMGLLAELR SINSAYSYEI HRIQGLSAMM PLLGEICS
