Cyp1a1

CYP1A1 (Cytochrome P450 Family 1 Subfamily A Member 1) is a Protein Coding gene. Diseases associated with CYP1A1 include Aryl Hydrocarbon Hydroxylase Inducibility and Ehrlich Tumor Carcinoma. Among its related pathways are Estrogen Receptor Pathway and Aryl Hydrocarbon Receptor. Gene Ontology (GO) annotations related to this gene include enzyme binding and iron ion binding. An important paralog of this gene is CYP1A2.

Cytochrome P450 Family 1 Subfamily A Member 1

A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997, PubMed:10681376).

Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase) (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301, PubMed:15041462, PubMed:18577768, PubMed:19965576, PubMed:20972997, PubMed:10681376).

Catalyzes the hydroxylation of carbon-hydrogen bonds. Exhibits high catalytic activity for the formation of hydroxyestrogens from estrone (E1) and 17beta-estradiol (E2), namely 2-hydroxy E1 and E2, as well as D-ring hydroxylated E1 and E2 at the C15-alpha and C16-alpha positions (PubMed:11555828, PubMed:14559847, PubMed:12865317, PubMed:15805301).

Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation (PubMed:15041462, PubMed:18577768).

Catalyzes the epoxidation of double bonds of certain PUFA (PubMed:15041462, PubMed:19965576, PubMed:20972997).

Converts arachidonic acid toward epoxyeicosatrienoic acid (EET) regioisomers, 8,9-, 11,12-, and 14,15-EET, that function as lipid mediators in the vascular system (PubMed:20972997).

Displays an absolute stereoselectivity in the epoxidation of eicosapentaenoic acid (EPA) producing the 17(R),18(S) enantiomer (PubMed:15041462).

May play an important role in all-trans retinoic acid biosynthesis in extrahepatic tissues. Catalyzes two successive oxidative transformation of all-trans retinol to all-trans retinal and then to the active form all-trans retinoic acid (PubMed:10681376).

May also participate in eicosanoids metabolism by converting hydroperoxide species into oxo metabolites (lipoxygenase-like reaction, NADPH-independent) (PubMed:21068195).

9-cis-retinoic acid biosynthetic process Source: Ensembl
Aging Source: Ensembl
Amine metabolic process Source: Ensembl
Camera-type eye development Source: Ensembl
Cell population proliferation Source: Ensembl
Cellular response to copper ion Source: Ensembl
Cellular response to organic cyclic compound Source: MGI
Coumarin metabolic process Source: Ensembl
Dibenzo-p-dioxin catabolic process Source: Ensembl
Digestive tract development Source: Ensembl
DNA methylation Source: Ensembl
Drug metabolic process Source: BHF-UCL
Epoxygenase P450 pathway Source: Reactome
Estrogen metabolic process Source: UniProtKB
Ethylene metabolic process Source: Reactome
Fatty acid metabolic process Source: UniProtKB
Flavonoid metabolic process Source: Ensembl
Hepatocyte differentiation Source: Ensembl
Hydrogen peroxide biosynthetic process Source: Ensembl
Insecticide metabolic process Source: Ensembl
Lipid hydroxylation Source: BHF-UCL
Long-chain fatty acid biosynthetic process Source: Reactome
Maternal process involved in parturition Source: Ensembl
Omega-hydroxylase P450 pathway Source: Reactome
Porphyrin-containing compound metabolic process Source: Ensembl
Positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
Regulation of metabolic process Source: Reactome
Response to antibiotic Source: Ensembl
Response to arsenic-containing substance Source: Ensembl
Response to drug Source: Ensembl
Response to food Source: Ensembl
Response to herbicide Source: Ensembl
Response to hyperoxia Source: Ensembl
Response to hypoxia Source: Ensembl
Response to immobilization stress Source: Ensembl
Response to iron(III) ion Source: Ensembl
Response to lipopolysaccharide Source: Ensembl
Response to nematode Source: Ensembl
Response to virus Source: Ensembl
Response to vitamin A Source: Ensembl
Response to wounding Source: Ensembl
Retinol metabolic process Source: UniProtKB
Steroid biosynthetic process Source: UniProtKB-KW
Steroid metabolic process Source: BHF-UCL
Vitamin D metabolic process Source: BHF-UCL

Cytoplasm; Endoplasmic reticulum membrane; Microsome membrane; Mitochondrion inner membrane