ID   CP3AH_CAVPO             Reviewed;         503 AA.
AC   Q64409;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Cytochrome P450 3A17;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA17;
GN   Name=CYP3A17;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Hartley; TISSUE=Liver;
RX   PubMed=9434738; DOI=10.1006/abbi.1997.0409;
RA   Mori T., Itoh S., Ohgiya S., Ishizaki K., Kamataki T.;
RT   "Regulation of CYP1A and CYP3A mRNAs by ascorbic acid in guinea pigs.";
RL   Arch. Biochem. Biophys. 348:268-277(1997).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       In liver microsomes, this enzyme is involved in an NADPH-dependent
CC       electron transport pathway. It oxidizes a variety of structurally
CC       unrelated compounds, including steroids, fatty acids, and xenobiotics.
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: 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; D28515; BAA05873.1; -; mRNA.
DR   RefSeq; NP_001166540.1; NM_001173069.1.
DR   AlphaFoldDB; Q64409; -.
DR   SMR; Q64409; -.
DR   GeneID; 100301487; -.
DR   KEGG; cpoc:100301487; -.
DR   CTD; 100301487; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   InParanoid; Q64409; -.
DR   OrthoDB; 467733at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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   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..503
FT                   /note="Cytochrome P450 3A17"
FT                   /id="PRO_0000051800"
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;  58203 MW;  48A676A491F89047 CRC64;
     MDLIPSFSLE TWVLLALSLV LLYQYATYSH GFFKKLGIPG PKPLPLFGNV LSYRKGIWNF
     DIECHKKYGN MWGLYDGPRP VLSITEPDMI KAVLVKECYS VFTNRRSIFP AGFMKKALSI
     SKDEEWKRIR TQLSQNFTSG KLKEMFPIIK QYGDVLVKNL RQEAEKGKPV QLKEIFGAYS
     MDIIIATAFG VNVDSLNNPH DPFVSKASKL FRFDFLSPFL LSVVIFPFLT QLYEMLNISI
     FPRDSLNFFT KFVKRTKENH LESNEKQRVN FLQMMLKSQN FKDTESHKAL SDVEILAQSI
     FFIVAGYETT SSTLCFIMYS LATHPDVQKK LQQEIDKTLP NKAFPTYDVM MEMEYLDMVV
     NETLRLYPVT NRIERMSKKD FEINGMSFPK GTGVMIPSFA LHRDSKYWPE PDEFRPERFS
     KKNKENIDPY IYMPFGNGPR NCIGMRMALM NLKLALIRLL QNFSFYTCKE TQIPLRLGSQ
     VILQPAKPII LKVVSRDETI RGA