ID   CP1A2_CANLF             Reviewed;         512 AA.
AC   P56592;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Cytochrome P450 1A2;
DE            EC=1.14.14.1 {ECO:0000250|UniProtKB:P05177};
DE   AltName: Full=CYPIA2;
DE   AltName: Full=Cholesterol 25-hydroxylase {ECO:0000250|UniProtKB:P05177};
DE   AltName: Full=Cytochrome P450-D2;
DE   AltName: Full=DAH2;
DE   AltName: Full=Hydroperoxy icosatetraenoate dehydratase;
DE            EC=4.2.1.152 {ECO:0000250|UniProtKB:P05177};
GN   Name=CYP1A2;
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   PROTEIN SEQUENCE OF 2-17.
RC   STRAIN=Beagle; TISSUE=Liver;
RX   PubMed=2910310; DOI=10.1016/0006-2952(89)90154-8;
RA   Ohta K., Motoya M., Komori M., Miura T., Kitada M., Kamataki T.;
RT   "A novel form of cytochrome P-450 in beagle dogs. P-450-D3 is a low spin
RT   form of cytochrome P-450 but with catalytic and structural properties
RT   similar to P-450d.";
RL   Biochem. Pharmacol. 38:91-96(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-512.
RC   STRAIN=Beagle; TISSUE=Liver;
RX   PubMed=2122230;
RA   Uchida T., Komori M., Kitada M., Kamataki T.;
RT   "Isolation of cDNAs coding for three different forms of liver microsomal
RT   cytochrome P-450 from polychlorinated biphenyl-treated beagle dogs.";
RL   Mol. Pharmacol. 38:644-651(1990).
CC   -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC       various endogenous substrates, including fatty acids, steroid hormones
CC       and vitamins. Mechanistically, uses molecular oxygen inserting one
CC       oxygen atom into a substrate, and reducing the second into a water
CC       molecule, with two electrons provided by NADPH via cytochrome P450
CC       reductase (NADPH--hemoprotein reductase). Catalyzes the hydroxylation
CC       of carbon-hydrogen bonds. Exhibits high catalytic activity for the
CC       formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol
CC       (E2), namely 2-hydroxy E1 and E2. Metabolizes cholesterol toward 25-
CC       hydroxycholesterol, a physiological regulator of cellular cholesterol
CC       homeostasis. May act as a major enzyme for all-trans retinoic acid
CC       biosynthesis in the liver. Catalyzes two successive oxidative
CC       transformation of all-trans retinol to all-trans retinal and then to
CC       the active form all-trans retinoic acid. Primarily catalyzes
CC       stereoselective epoxidation of the last double bond of polyunsaturated
CC       fatty acids (PUFA), displaying a strong preference for the (R,S)
CC       stereoisomer. Catalyzes bisallylic hydroxylation and omega-1
CC       hydroxylation of PUFA. May also participate in eicosanoids metabolism
CC       by converting hydroperoxide species into oxo metabolites (lipoxygenase-
CC       like reaction, NADPH-independent). Plays a role in the oxidative
CC       metabolism of xenobiotics. Catalyzes the N-hydroxylation of
CC       heterocyclic amines and the O-deethylation of phenacetin. Metabolizes
CC       caffeine via N3-demethylation. {ECO:0000250|UniProtKB:P05177}.
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         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 2-hydroxy-17beta-estradiol + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47212, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:28744, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47213;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=17beta-estradiol + O2 + reduced [NADPH--hemoprotein reductase]
CC         = 4-hydroxy-17beta-estradiol + H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:47280, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16469,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:62845;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47281;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 2-
CC         hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:47208, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:1156, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:17263, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47209;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone + O2 + reduced [NADPH--hemoprotein reductase] = 4-
CC         hydroxyestrone + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:47292, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17263, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:87602; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47293;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] =
CC         25-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:50256, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16113, ChEBI:CHEBI:42977, ChEBI:CHEBI:57618,
CC         ChEBI:CHEBI:58210; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50257;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = all-trans-retinal + H(+) + 2 H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42092, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17336,
CC         ChEBI:CHEBI:17898, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42093;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-retinal + O2 + reduced [NADPH--hemoprotein
CC         reductase] = all-trans-retinoate + 2 H(+) + H2O + oxidized
CC         [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:42088, Rhea:RHEA-
CC         COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17898,
CC         ChEBI:CHEBI:35291, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42089;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (14R,15S)-epoxy-(5Z,8Z,11Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49860, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131965; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49861;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (14S,15R)-epoxy-(5Z,8Z,11Z)-
CC         eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:49856, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:131964; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49857;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39779, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:58562,
CC         ChEBI:CHEBI:76634; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = (19R,20S)-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC         docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52120, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016,
CC         ChEBI:CHEBI:136410; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52121;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5S)-hydroperoxy-(6E,8Z,11Z,14Z)-eicosatetraenoate = 5-oxo-
CC         (6E,8Z,11Z,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48632,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57450, ChEBI:CHEBI:65342;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48633;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate = 12-oxo-
CC         (5Z,8Z,10E,14Z)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:37947,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57444, ChEBI:CHEBI:75231;
CC         EC=4.2.1.152; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37948;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate = 15-oxo-
CC         (5Z,8Z,11Z,13E)-eicosatetraenoate + H2O; Xref=Rhea:RHEA:48636,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57410, ChEBI:CHEBI:57446;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48637;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(13S)-hydroperoxy-(9Z,11E)-octadecadienoate = 13-oxo-(9Z,11E)-
CC         octadecadienoate + H2O; Xref=Rhea:RHEA:48716, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57466, ChEBI:CHEBI:90781;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48717;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 13-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:52292, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:136524; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52293;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC         [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:76627; Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein
CC         reductase] = 11-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O +
CC         oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:52284,
CC         Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245,
CC         ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:136522;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52285;
CC         Evidence={ECO:0000250|UniProtKB:P05177};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC       {ECO:0000250|UniProtKB:P05177}.
CC   -!- PATHWAY: Steroid metabolism; cholesterol metabolism.
CC       {ECO:0000250|UniProtKB:P05177}.
CC   -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC       {ECO:0000250|UniProtKB:P05177}.
CC   -!- SUBUNIT: Interacts with PGRMC1; the interaction requires PGRMC1
CC       homodimerization. {ECO:0000250|UniProtKB:P05177}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P05177}. Microsome membrane
CC       {ECO:0000250|UniProtKB:P05177}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P05177}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in liver.
CC   -!- INDUCTION: By polychlorinated biphenyl (PCB) in liver and kidney.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   PIR; B37222; B37222.
DR   AlphaFoldDB; P56592; -.
DR   SMR; P56592; -.
DR   STRING; 9615.ENSCAFP00000059348; -.
DR   GlyCosmos; P56592; 1 site, No reported glycans.
DR   PaxDb; 9612-ENSCAFP00000035314; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; P56592; -.
DR   UniPathway; UPA00296; -.
DR   UniPathway; UPA00383; -.
DR   UniPathway; UPA00912; -.
DR   Proteomes; UP000002254; Unplaced.
DR   Proteomes; UP000694429; Unplaced.
DR   Proteomes; UP000694542; Unplaced.
DR   Proteomes; UP000805418; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0101020; F:estrogen 16-alpha-hydroxylase activity; ISS:UniProtKB.
DR   GO; GO:0101021; F:estrogen 2-hydroxylase activity; ISS:UniProtKB.
DR   GO; GO:0020037; F:heme binding; ISS:UniProtKB.
DR   GO; GO:0106256; F:hydroperoxy icosatetraenoate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008210; P:estrogen metabolic process; ISS:UniProtKB.
DR   GO; GO:0042572; P:retinol metabolic process; ISS:UniProtKB.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR008066; Cyt_P450_E_grp-I_CYP1.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24289:SF18; CYTOCHROME P450 1A2; 1.
DR   PANTHER; PTHR24289; STEROID 17-ALPHA-HYDROXYLASE/17,20 LYASE; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01683; EP450ICYP1A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Fatty acid metabolism;
KW   Glycoprotein; Heme; Iron; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW   Microsome; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Steroid metabolism; Sterol metabolism.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2910310"
FT   CHAIN           2..512
FT                   /note="Cytochrome P450 1A2"
FT                   /id="PRO_0000051649"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         454
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   CARBOHYD        65
FT                   /note="O-linked (GlcNAc) serine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   512 AA;  57637 MW;  E49DF4C54F4B3CFB CRC64;
     MALSQMATGL LLASTIFCLI LWVVKAWQPR LPKGLKSPPG PWGWPLLGNV LTLGKSPHLA
     LSRLSQRYGD VLQIRIGSTP VLVLSGLDTI RQALVRQGDD FKGRPDLYSL SLITDSQSMS
     FSPDSGPVWA AGRRLAQNAL NTFSIASDPA SSCSCYLEEH VSKEAEALLS RLQEQMAEVG
     RFDPYNQVLL SVANVIGAMC FGHHFSQRSE EMLPLLMSSS DFVETVSSGN PLDFFPILQY
     MPNSALQRFK NFNQTFVQSL QKIVQEHYQD FDERSVQDIT GALLKHNEKS SRASDGHIPQ
     EKIVNLINDI FGAGFDTVTT AISWSLMYLV ANPEIQRQIQ KELDTVIGRA RQPRLSDRPQ
     LPLMEAFILE IFRHTSFVPF TIPHSTTKDT TLKGFYIPKE CCVFINQWQV NHDQQVWGDP
     FAFRPERFLT ADGTTINKTL SEKVMLFGMG KRRCIGEVLA KWEIFLFLAI LLQRLEFSVP
     AGVKVDLTPI YGLTMKHTRC EHVQARPRFS IK
//