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 27-MAR-2024, entry version 115.
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.ENSMAUP00000011079; -.
DR GeneID; 101831958; -.
DR KEGG; maua:101831958; -.
DR eggNOG; KOG0158; Eukaryota.
DR OrthoDB; 1611592at2759; -.
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 CDD; cd20650; CYP3A; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24302:SF8; CYTOCHROME P450 3A-RELATED; 1.
DR PANTHER; PTHR24302; CYTOCHROME P450 FAMILY 3; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00464; EP450II.
DR PRINTS; PR01689; EP450IICYP3A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 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
//
