ID   CP3A8_MACFA             Reviewed;         503 AA.
AC   P33268; P25231;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   28-JAN-2026, entry version 134.
DE   RecName: Full=Cytochrome P450 3A8;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA8;
DE   AltName: Full=Cytochrome P-450-MK2;
DE   AltName: Full=Cytochrome P450-MKNF2;
GN   Name=CYP3A8;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=1282830; DOI=10.1016/0167-4781(92)90113-e;
RA   Komori M., Kikuchi O., Sakuma T., Funaki J., Kitada M., Kamataki T.;
RT   "Molecular cloning of monkey liver cytochrome P-450 cDNAs: similarity of
RT   the primary sequences to human cytochromes P-450.";
RL   Biochim. Biophys. Acta 1171:141-146(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-22.
RC   TISSUE=Liver;
RX   PubMed=2500151; DOI=10.1016/0167-4838(89)90107-6;
RA   Ohta K., Kitada M., Hashizume T., Komori M., Ohi H., Kamataki T.;
RT   "Purification of cytochrome P-450 from polychlorinated biphenyl-treated
RT   crab-eating monkeys: high homology to a form of human cytochrome P-450.";
RL   Biochim. Biophys. Acta 996:142-145(1989).
RN   [3]
RP   CHARACTERIZATION.
RX   PubMed=8373178; DOI=10.1006/abbi.1993.1439;
RA   Ohmori S., Horie T., Guengerich F.P., Kiuchi M., Kitada M.;
RT   "Purification and characterization of two forms of hepatic microsomal
RT   cytochrome P450 from untreated cynomolgus monkeys.";
RL   Arch. Biochem. Biophys. 305:405-413(1993).
CC   -!- FUNCTION: Catalyzes nifedipine and nilvadipine oxidations.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + reduced [NADPH--hemoprotein reductase] +
CC         O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O +
CC         H(+); Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:142491; EC=1.14.14.1;
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   -!- INDUCTION: By polychlorinated biphenyl (PCB).
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; S53047; AAB24952.1; -; mRNA.
DR   PIR; S28168; S28168.
DR   AlphaFoldDB; P33268; -.
DR   SMR; P33268; -.
DR   STRING; 9541.ENSMFAP00000039737; -.
DR   VEuPathDB; HostDB:ENSMFAG00000046026; -.
DR   VGNC; VGNC:83080; CYP3A4.
DR   eggNOG; KOG0158; Eukaryota.
DR   OMA; QPFHTGP; -.
DR   Proteomes; UP000233100; Chromosome 3.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; IEA:TreeGrafter.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0050649; F:testosterone 6-beta-hydroxylase activity; IEA:TreeGrafter.
DR   GO; GO:0070989; P:oxidative demethylation; IEA:TreeGrafter.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:TreeGrafter.
DR   CDD; cd20650; CYP3A; 1.
DR   FunFam; 1.10.630.10:FF:000096; Cytochrome P450 3A4; 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   InterPro; IPR050705; Cytochrome_P450_3A.
DR   PANTHER; PTHR24302:SF38; CYTOCHROME P450 3A5; 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   Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW   Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..503
FT                   /note="Cytochrome P450 3A8"
FT                   /id="PRO_0000051791"
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;  57511 MW;  D701B6FE83AC8BFB CRC64;
     MDLIPDLAVE TWLLLAVTLV LLYLYGTHSH GLFKKLGIPG PTPLPLLGNI LSYRKGFWTF
     DMECYKKYGK VWGFYDGRQP VLAITDPNMI KTVLVKECYS VFTNRRPFGP VGFMKNAISI
     AEDEEWKRIR SLLSPTFTSG KLKEMVPIIA KYGDVLVRNL RREAETGKPV TLKDVFGAYS
     MDVITSTSFG VNIDSLNNPQ DPFVENTKKL LRFDFLDPFF LSITIFPFII PILEVLNISI
     FPREVTSFLR KSVKRIKESR LKDTQKHRVD FLQLMIDSQN SKETESHKAL SDLELVAQSI
     IFIFAGYETT SSVLSFIIYE LATHPDVQQK LQEEIDTVLP NKAPPTYDTV LQMEYLDMVV
     NETLRIFPIA MRLERVCKKD VEINGIFIPK GVVVMIPSYA LHHDPKYWPE PEKFLPERFS
     KKNNDNIDPY IYTPFGSGPR NCIGMRFALM NMKLAIIRVL QNFSFKPCKE TQIPLKLRLG
     GLLQTEKPIV LKIESRDGTV SGA
//