ID   CP3AC_CANLF             Reviewed;         503 AA.
AC   P24463;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Cytochrome P450 3A12;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA12;
DE   AltName: Full=Cytochrome P450-PBD-1;
GN   Name=CYP3A12;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Beagle; TISSUE=Liver;
RX   PubMed=2001406; DOI=10.1016/0167-4781(91)90072-t;
RA   Ciaccio P.J., Graves P.E., Bourque D.P., Glinsmann-Gibson B., Halpert J.R.;
RT   "cDNA and deduced amino acid sequences of a dog liver cytochrome P-450 of
RT   the IIIA gene subfamily.";
RL   Biochim. Biophys. Acta 1088:319-322(1991).
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; X54915; CAA38687.1; -; mRNA.
DR   PIR; S04341; S04341.
DR   PIR; S14275; S14275.
DR   RefSeq; NP_001003340.1; NM_001003340.1.
DR   AlphaFoldDB; P24463; -.
DR   SMR; P24463; -.
DR   STRING; 9615.ENSCAFP00000021934; -.
DR   ChEMBL; CHEMBL1907982; -.
DR   PaxDb; P24463; -.
DR   PRIDE; P24463; -.
DR   Ensembl; ENSCAFT00845042055; ENSCAFP00845032984; ENSCAFG00845023773.
DR   GeneID; 415129; -.
DR   CTD; 415129; -.
DR   VEuPathDB; HostDB:ENSCAFG00845023773; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   GeneTree; ENSGT00950000182958; -.
DR   InParanoid; P24463; -.
DR   OrthoDB; 467733at2759; -.
DR   PRO; PR:P24463; -.
DR   Proteomes; UP000002254; 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:0004497; F:monooxygenase activity; ISS:UniProtKB.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IDA:AgBase.
DR   GO; GO:0050649; F:testosterone 6-beta-hydroxylase activity; IDA:AgBase.
DR   GO; GO:0042445; P:hormone metabolic process; IDA:AgBase.
DR   GO; GO:1901615; P:organic hydroxy compound metabolic process; IDA:AgBase.
DR   GO; GO:0070989; P:oxidative demethylation; IBA:GO_Central.
DR   GO; GO:0042448; P:progesterone metabolic process; IDA:AgBase.
DR   GO; GO:0008202; P:steroid metabolic process; IDA:AgBase.
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 3A12"
FT                   /id="PRO_0000051795"
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;  57721 MW;  52171D03F9BD5D87 CRC64;
     MDLIPSFSTE TWLLLAISLV LLYLYGTYTH GIFRKLGIPG PTPLPFVGTA LGYRNGFYVF
     DMKCFSKYGR MWGFYDGRQP VLAITDPDMI KTVLVKECYS VFTNRRTLGP VGFMKSAISL
     SEDEEWKRMR TLLSPTFTTG KLKEMFPIIG QYGDVLVNNL RKEAEKGKAI NLKDVFGAYS
     MDVITSTSFG VNIDSLNHPQ DPFVENTKKL LKFDFLDPFF FSILLFPFLT PVFEILNIWL
     FPKKVTDFFR KSVERMKESR LKDKQKHRVD FLQLMINSQN SKEMDTHKAL SDLELVAQSI
     IFIFAGYETT STSLSFLMYE LATHPDVQQK LQEEIDATFP NKALPTYDAL VQMEYLDMVL
     NETLRLYPIA GRLERVCKKD VEISGVFIPK GTVVMVPTFT LHRDQSLWPE PEEFRPERFS
     RKNKDSINPY TYLPFGTGPR NCIGMRFAIM NMKLALVRVL QNFSFKPCKE TQIPLKLNAQ
     GIIQPEKPIV LKVEPRDGSV NGA