ID   Q9WVT5_RAT              Unreviewed;       499 AA.
AC   Q9WVT5;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   SubName: Full=Sterol 12alpha-hydroxylase P450 {ECO:0000313|EMBL:BAA82169.1};
GN   Name=Cyp8b1 {ECO:0000313|RGD:71016};
GN   Synonyms=CYP8B {ECO:0000313|EMBL:BAA82169.1};
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 {ECO:0000313|EMBL:BAA82169.1};
RN   [1] {ECO:0000313|EMBL:BAA82169.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver {ECO:0000313|EMBL:BAA82169.1};
RX   PubMed=10393316;
RA   Ishida H., Kuruta Y., Gotoh O., Yamashita C., Yoshida Y., Noshiro M.;
RT   "Structure, evolution, and liver-specific expression of sterol 12alpha-
RT   hydroxylase P450 (CYP8B).";
RL   J. Biochem. 126:19-25(1999).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR000047, ECO:0000256|PIRSR:PIRSR000047-1};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|PIRNR:PIRNR000047}.
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DR   EMBL; AB009686; BAA82169.1; -; mRNA.
DR   RefSeq; NP_112520.1; NM_031241.1.
DR   AlphaFoldDB; Q9WVT5; -.
DR   PhosphoSitePlus; Q9WVT5; -.
DR   GeneID; 81924; -.
DR   KEGG; rno:81924; -.
DR   UCSC; RGD:71016; rat.
DR   AGR; RGD:71016; -.
DR   CTD; 1582; -.
DR   RGD; 71016; Cyp8b1.
DR   OrthoDB; 1537669at2759; -.
DR   PhylomeDB; Q9WVT5; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008397; F:sterol 12-alpha-hydroxylase activity; IDA:RGD.
DR   GO; GO:0006699; P:bile acid biosynthetic process; ISO:RGD.
DR   GO; GO:0038183; P:bile acid signaling pathway; IEP:RGD.
DR   GO; GO:0045797; P:positive regulation of intestinal cholesterol absorption; ISO:RGD.
DR   GO; GO:0070723; P:response to cholesterol; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR024204; Cyt_P450_CYP7A1-type.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   InterPro; IPR030686; Cytochrome_CYP8B1.
DR   PANTHER; PTHR24306; -; 1.
DR   PANTHER; PTHR24306:SF0; 7-ALPHA-HYDROXYCHOLEST-4-EN-3-ONE 12-ALPHA-HYDROXYLASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PIRSF; PIRSF500627; Cytochrome_CYP8B1; 1.
DR   PIRSF; PIRSF000047; Cytochrome_CYPVIIA1; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   Genevisible; Q9WVT5; RN.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|PIRNR:PIRNR000047};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000047};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000047};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022516};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000047};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000047}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..499
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004336928"
FT   BINDING         107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT   BINDING         284
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000047-2"
FT   BINDING         438
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000047-1"
SQ   SEQUENCE   499 AA;  57585 MW;  1923F68539C02122 CRC64;
     MLWGSVLGAL LMAVGCLCLS LLPRHRRPWE PPLDKGFVPW LGHTMAFRKN MFEFLKGMRA
     KHGDVFTLQL GGQYFTFVMD PLSFGPIIKS TQKVLDFVTY ARELVFKVFG YQSMDEDHQM
     LHVASTKHLM GQGLEDLNRA MLDSLSLVML GPKGRSLGAR SWCEDGLFHF CYSILFKAGF
     LSLFGCTKDK EQDLDEADEL FRKFRRFDLL FPRFVYSLLG PLEWVEVSQL QRLFHQRLSV
     EQNLEKDGIS NWLGFMLRFL RERGMASSMQ DKFNFMMLWA SQGNTGPTCF WALLFLLKHQ
     DAMKAVREEA TRVLGEARLE AETSFAFTLS ALKCTPVLDS VMEETLRLCA TPTLLGVVQE
     DYVLKMASGQ EYQIRRGDKV ALFPYLSVHM DPDIHPEPTT FKYNRFLNPD GTRKVDFYKS
     GKKIHHYNMP WGSGVSICPG RFFAPSEMKT FVLLMVMYFD FELVDPDMPV PPIDPRRWGF
     GTSQPSHEVR FRYRLKPMQ
//