ID   CP3AA_MESAU             Reviewed;         503 AA.
AC   Q64148;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Lithocholate 6-beta-hydroxylase;
DE            Short=6 beta-hydroxylase;
DE            EC=1.14.14.138 {ECO:0000269|PubMed:8484723};
DE   AltName: Full=CYPIIIA10;
DE   AltName: Full=Cytochrome P450 3A10;
GN   Name=CYP3A10;
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1840595; DOI=10.1016/s0021-9258(18)54816-x;
RA   Teixeira J., Gil G.;
RT   "Cloning, expression and regulation of lithocholic acid 6beta-
RT   hydroxylase.";
RL   J. Biol. Chem. 266:21030-21036(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RX   PubMed=7651384; DOI=10.1128/mcb.15.9.4672;
RA   Subramanian A., Teixeira J., Wang J., Gil G.;
RT   "A STAT factor mediates the sexually dimorphic regulation of hepatic
RT   cytochrome P450 3A10/lithocholic acid 6 beta-hydroxylase gene expression by
RT   growth hormone.";
RL   Mol. Cell. Biol. 15:4672-4682(1995).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION.
RX   PubMed=8484723; DOI=10.1042/bj2910429;
RA   Chang T.K.H., Teixeira J., Gil G., Waxman D.J.;
RT   "The lithocholic acid 6 beta-hydroxylase cytochrome P-450, CYP 3A10, is an
RT   active catalyst of steroid-hormone 6 beta-hydroxylation.";
RL   Biochem. J. 291:429-433(1993).
CC   -!- FUNCTION: Catalyzes the 6 beta-hydroxylation of lithocholic acid and
CC       steroid hormones. {ECO:0000269|PubMed:8484723}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=lithocholate + O2 + reduced [NADPH--hemoprotein reductase] =
CC         6beta-hydroxylithocholate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:18857, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:29744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:58876; EC=1.14.14.138;
CC         Evidence={ECO:0000269|PubMed:8484723};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
CC   -!- DEVELOPMENTAL STAGE: Expressed only in male hamsters.
CC   -!- INDUCTION: P450 can be induced to high levels in liver and other
CC       tissues by various foreign compounds, including drugs, pesticides, and
CC       carcinogens.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M73992; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; S79317; AAB35091.1; -; Genomic_DNA.
DR   PIR; A40843; A40843.
DR   RefSeq; XP_005079966.1; XM_005079909.2.
DR   AlphaFoldDB; Q64148; -.
DR   SMR; Q64148; -.
DR   STRING; 10036.XP_005079966.1; -.
DR   PRIDE; Q64148; -.
DR   GeneID; 101831958; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   OrthoDB; 467733at2759; -.
DR   Proteomes; UP000189706; Unplaced.
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:0033777; F:lithocholate 6beta-hydroxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR008072; Cyt_P450_E_CYP3A.
DR   InterPro; IPR002402; Cyt_P450_E_grp-II.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..503
FT                   /note="Lithocholate 6-beta-hydroxylase"
FT                   /id="PRO_0000051793"
FT   BINDING         442
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:0000250"
SQ   SEQUENCE   503 AA;  57693 MW;  D4D24FEE87FD7F51 CRC64;
     MELIPNLSIE TWVLLAISLV LIYIYGTYSH GTFKKLGIPG PKPLPFFGTI LGYHDGTWKF
     DETCYKKYGK IWGFYDGRVP VLAIADPEII KTVLVKECYS NFTNRRSFGP VGFMKKSITI
     SKDEEWKRLR TLLSPAFTSG KLKEMFPIIG QYGDTLVKNL RREEEKGKPV NMKEILGAYS
     MDVITGTSFG VNVDSLNNPE DPFVQKARKI LKFNFFDPFI LSIILFPFLT TIYDLLRFSI
     FPRQSTNFFK KFITTMKKNR LHSNQKTRMD FFQLMMNTQN SKGKESQKAL SDLEMAAQAI
     IFIFAGYEST STSICLVLYE LATHPDVQKK LHDEIDSALP NKAPVTYDVL MGMEYLDMVI
     NEGLRLYPIA NRLERISKKA VEINGLFIPK GITVMVPTYP LHRDPEYWPE PEEFRPERFS
     KENKGSIDPY VYMPFGNGPR NCIGMRFALL SMKLAVVSVL QNFTLQTCEQ TENHLKFARQ
     IILQPENPII LKIISRDKPI TGA