ID   CP3AE_CAVPO             Reviewed;         503 AA.
AC   Q64417; Q64407;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Cytochrome P450 3A14;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA14;
GN   Name=CYP3A14;
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;
RA   Mori T., Itoh S., Kamataki T.;
RT   "cDNA and deduced amino acid sequence of a novel cytochrome P450 from male
RT   guinea pig liver mRNA with high homology to CYP3A family.";
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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; D16363; BAA03865.1; -; mRNA.
DR   EMBL; D49731; BAA08568.1; -; mRNA.
DR   RefSeq; NP_001166587.1; NM_001173116.1.
DR   AlphaFoldDB; Q64417; -.
DR   SMR; Q64417; -.
DR   STRING; 10141.ENSCPOP00000001435; -.
DR   GeneID; 100379244; -.
DR   KEGG; cpoc:100379244; -.
DR   CTD; 100379244; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   InParanoid; Q64417; -.
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 3A14"
FT                   /id="PRO_0000051797"
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"
FT   CONFLICT        121
FT                   /note="S -> P (in Ref. 1; BAA03865)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        452
FT                   /note="L -> I (in Ref. 1; BAA03865)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   503 AA;  58118 MW;  2348B0B3013FD2DD CRC64;
     MDLVPSFSLE TWVLLALSLV LLYRYATYSH GFFKKLGIPG PKPLPLFGNV LSYRKGMWSF
     DIECRKKYGN MWGLYDGPQP VLAITEPDMI KAVLVKECYS VFTNRRSLVP VGFMKKAVSL
     SEDEEWKRIR TQLSPNFTSG KLKEMFPIIK QYGDVLVKNL RQEAEKGKPV QLKEIFGAYS
     MDIIVATAFG VNVDSLNNPH DPFVSKARKL FRFDFLSPFL LSIVMFPFLT QLYEMLSISI
     FPRDSLKFFT KFVKKTKENH LESNKKQRVD FLQMMLNSQN FKDTESHKAL SDVEILAQSI
     IFIFAGYETT SSTLSFIMYS LATHPDVQKK LQQEIDKTLP NKAFPTYDVM MEMEYLDMVV
     NETLRLYPVT NRIERMSKKD FEINGMSFPK GTGVMIPSFA LHRDSKYWPE PDEFRPERFS
     KKNKENIDPY IYMPFGNGPR NCIGMRMALM NLKLALIRLL QNFSFYPCKE TQIPLRLGSE
     ALLQPAKPII LKVVSRDETI RGA