NR1I3_PANTR
ID NR1I3_PANTR Reviewed; 348 AA.
AC A2T7D9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nickel G.C., Tefft D.L., Trevarthen K., Funt J., Adams M.D.;
RT "Positive selection in transcription factor genes on the human lineage.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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-38 by PKC, dephosphorylation of Thr-38 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; DQ977427; ABM92094.1; -; Genomic_DNA.
DR RefSeq; NP_001129087.1; NM_001135615.1.
DR AlphaFoldDB; A2T7D9; -.
DR SMR; A2T7D9; -.
DR STRING; 9598.ENSPTRP00000002647; -.
DR PaxDb; A2T7D9; -.
DR GeneID; 458014; -.
DR KEGG; ptr:458014; -.
DR CTD; 9970; -.
DR eggNOG; KOG3575; Eukaryota.
DR InParanoid; A2T7D9; -.
DR OrthoDB; 297114at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 3: Inferred from homology;
KW Activator; Cytoplasm; Cytoskeleton; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Receptor; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..348
FT /note="Nuclear receptor subfamily 1 group I member 3"
FT /id="PRO_0000285531"
FT DOMAIN 109..348
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 8..83
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 11..31
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 47..71
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT MOD_RES 38
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q14994"
SQ SEQUENCE 348 AA; 39558 MW; 92EAAD07D7DCB9DA CRC64;
MASREDELRN CVVCGDQATG YHFNALTCEG CKGFFRRTVS KSIGPTCPFA GSCEVSKTQR
RHCPACRLQK CLDAGMRKDM ILSAEALALR RAKQAQRRAQ QTPVQLSKEQ EELIRTLLGA
HTRHMGTMFE QFVQFRPPAH LFIHHQPLPT LAPVLPLVTH FADINTFMVL QVIKFTKDLP
VFRSLPIEDQ ISLLKGAAVE ICHIVLNTTF CLQTQNFLCG PLRYTIEDGA RVGFQVEFLE
LLFHFHGTLR KLQLQEPEYV LLAAMALFSP DRPGVTQRDE IDQLQEEMAL TLQSYIKGQQ
RRPRDRFLYA KLLGLLAELR SINEAYGYQI QHIQGLSAMM PLLQEICS
