ID   CP3AI_RAT               Reviewed;         497 AA.
AC   Q64581;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Cytochrome P450 3A18;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA18;
DE   AltName: Full=Cytochrome P450(6)beta-2;
GN   Name=Cyp3a18;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=7873612; DOI=10.1016/0167-4781(94)00244-w;
RA   Strotkamp D., Roos P.H., Hanstein W.G.;
RT   "A novel CYP3 gene from female rats.";
RL   Biochim. Biophys. Acta 1260:341-344(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=8845857; DOI=10.1097/00008571-199602000-00009;
RA   Nagata K., Murayama N., Miyata M., Shimada M., Urahashi A., Yamazoe Y.,
RA   Kato R.;
RT   "Isolation and characterization of a new rat P450 (CYP3A18) cDNA encoding
RT   P450(6)beta-2 catalyzing testosterone 6 beta- and 16 alpha-
RT   hydroxylations.";
RL   Pharmacogenetics 6:103-111(1996).
CC   -!- FUNCTION: Catalyzes 16-beta- and 6-alpha-hydroxylations of
CC       testosterone.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC         reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; 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 pregnenolone-alpha-carbonitrile, dexamethasone,
CC       phenobarbital, and triacetyloleandomycin.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; X79991; CAA56312.1; -; mRNA.
DR   EMBL; D38381; BAA22526.1; -; mRNA.
DR   PIR; PX0033; PX0033.
DR   PIR; S52097; S52097.
DR   RefSeq; NP_665725.1; NM_145782.1.
DR   AlphaFoldDB; Q64581; -.
DR   SMR; Q64581; -.
DR   STRING; 10116.ENSRNOP00000001285; -.
DR   PaxDb; Q64581; -.
DR   PRIDE; Q64581; -.
DR   GeneID; 252931; -.
DR   KEGG; rno:252931; -.
DR   CTD; 252931; -.
DR   RGD; 628709; Cyp3a18.
DR   eggNOG; KOG0158; Eukaryota.
DR   InParanoid; Q64581; -.
DR   OrthoDB; 467733at2759; -.
DR   PhylomeDB; Q64581; -.
DR   Reactome; R-RNO-211958; Miscellaneous substrates.
DR   Reactome; R-RNO-211981; Xenobiotics.
DR   PRO; PR:Q64581; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008390; F:testosterone 16-alpha-hydroxylase activity; IDA:RGD.
DR   GO; GO:0050649; F:testosterone 6-beta-hydroxylase activity; IDA:RGD.
DR   GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Cytochrome P450 3A18"
FT                   /id="PRO_0000051801"
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   497 AA;  57307 MW;  9FA3F5B221293489 CRC64;
     MEIIPNLSIE TWVLLATSLM LFYIYGTYSH GLFKKLGIPG PKPVPLFGTI FNYGDGMWKF
     DDDCYKKYGK IWGFYEGPQP FLAIMDPEII KMVLVKECYS VFTNRRCFGP MGFMKKAITM
     SEDEEWKRLR TILSPTFTSG KLKEMFPLMR QYGDTLLKNL RREEAKGEPI NMKDIFGAYS
     MDVITGTSFG VNVDSLNNPQ DPFVQKAKKI LKFQIFDPFL LSVVLFPFLT PIYEMLNFSI
     FPRQSMNFFK KFVKTMKKNR LDSNQKNRVD FLQLMMNTQN SKGQESQKAL SDLEMAAQAI
     IFIFGGYDAT STSISFIMYE LATRPNVQKK LQNEIDRALP NKAPVTYDAL MEMEYLDMVV
     NESLRLYPIA TRLDRVSKKD VEINGVFIPK GTVVTIPIYP LHRNPEYWLE PEEFNPERFS
     KENKGSIDPY VYLPFGNGPR NCIGMRFALI SMKLAVIGVL QNFNIQPCEK TQIPLKISRQ
     PIFQPEGPII LKLVSRD