ID   NR1I3_PUSSI             Reviewed;         348 AA.
AC   P62045;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 91.
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   Pusa sibirica (Baikal seal) (Phoca sibirica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Pusa.
OX   NCBI_TaxID=9719;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15178021; DOI=10.1016/j.marenvres.2004.03.003;
RA   Sakai H., Iwata H., Kim E.Y., Tanabe S., Baba N.;
RT   "Identification of constitutive androstane receptor cDNA in northern fur
RT   seal (Callorhinus ursinus).";
RL   Mar. Environ. Res. 58:107-111(2004).
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; AB109553; BAD00038.1; -; mRNA.
DR   AlphaFoldDB; P62045; -.
DR   SMR; P62045; -.
DR   PRIDE; P62045; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004879; F:nuclear receptor activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..348
FT                   /note="Nuclear receptor subfamily 1 group I member 3"
FT                   /id="PRO_0000053555"
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;  39553 MW;  70D2FC0863D2FF1E CRC64;
     MASGEDGPRS CMVCGDRATG YHFHALTCEG CKGFFRRTVS KNTGLTCPFA GSCKVNKAQR
     RHCPACRLQK CLDAGMKKEM ILSAEALAQR RAKQAQRRAQ WAAVQLSKGQ QELVQTLLGA
     HARHVGTMFD QFVQFRPPAH LFIHHQRLPI PLPPLPLLEH FAEVNTFMVQ QVIKFTKDLP
     LFRSLPMEDQ ISLLKGAAVE ICHIALNTTF CLQTRNFLCG PLRYTLEDGV HVGFQEEFLE
     LLFRFHATLR RFQLQEPEYV LMAAMALFSP DRPGVTQKEE IDRLQEMMAL TLQSYIKGQP
     PRHRDRFLYA KLLGLLAELR SINNAYGYQI QHIQGLSAMM PLLQEICS