CP3AF_CAVPO
ID CP3AF_CAVPO Reviewed; 503 AA.
AC Q64406;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cytochrome P450 3A15;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA15;
GN Name=CYP3A15;
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; D26487; BAA05498.1; -; mRNA.
DR RefSeq; NP_001166588.1; NM_001173117.1.
DR AlphaFoldDB; Q64406; -.
DR SMR; Q64406; -.
DR GeneID; 100379245; -.
DR KEGG; cpoc:100379245; -.
DR CTD; 100379245; -.
DR InParanoid; Q64406; -.
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 3A15"
FT /id="PRO_0000051798"
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; 58139 MW; 071E187ADACDC4F9 CRC64;
MDLIPSFSLE TWVLLALSLV LLYQYATYSH GFFKKLGIPG PKPLPLFGNV LSYRKGMWSF
DIECRKKYGN MWGLYDGPQP VLAITEPDMI KAVLVKECYS VFTNRRSLVP VGFMKKSVSL
SEDEEWKRIR TQLSPNFTSG KLKEMFPIIK QYGDVLVKNL RQEAEKGKPV QLKEIFGAYG
MDIIIATAFG VNVDSLNNPH DPFVSKANKL FRFDFLSPFL LSTVMFPFLT QLYEMLSISI
FPRDSLKFFT KFVKKTKENH LESNKKQRVN FLQMMLNSQN FKDTESHKAL SDVEILAQSI
IFIFAGYETS SSTLSCIMYS LATHPDVQKK LHQEIDKTLP NKAFPTYDVM MEMEYLDMVV
NETLRLYPVA NRIERMSKKD FEINGMSFPK GTLVMIPSFA LHRDSKYWPE PDEFRPERFS
KKNKENIDPY IYMPFGNGPR NCIGRRMALM NLKLALIRLL QNFSFYPCKE TQIPLRLSSE
ALLQPEKPLI LKVVSRDETI RGA