Mouse Cyp1a1 encodes cytochrome P450 1A1, a CYP1-family heme-thiolate monooxygenase best supported as an inducible microsomal/endoplasmic-reticulum enzyme in the AHR xenobiotic-response program. Its core activity is paired-donor monooxygenation/hydroxylation of xenobiotic aromatic substrates, especially PAHs and heterocyclic amines, with context-dependent detoxication or metabolic activation. It also metabolizes endogenous estrogens, retinoids, polyunsaturated fatty acids and eicosanoid hydroperoxides, forming 2- and 16-alpha-hydroxyestrogens among other products; that activity is inferred from the characterized human orthologue rather than demonstrated in mouse, where the direct experimental work is chiefly xenobiotic- and toxin-oriented, so for the mouse enzyme these are secondary substrate classes rather than its primary activity. Mitochondrial localization and HSP70/HSP90 interactions are also inferred from homology rather than shown directly in mouse.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0008395 steroid hydroxylase activity | IBA GO_REF:0000033 | MODIFY | Summary: CYP1A1 has supported estrogen hydroxylase activities, but the broader steroid hydroxylase/steroid catabolism framing is not the best representation of the evidence and is not the core xenobiotic function. Reason: Prefer specific estrogen hydroxylase/metabolic terms where retained; do not treat broad steroid catabolism as core. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN008400367 SUPPORTS TRANSFER The steroid-hydroxylase IBD sits at this node. Scoping the two seed sets separately, because they differ: this row's GOA WITH/FROM lists three human accessions, three ZFIN ids and one rat id, RGD:2458, which is the only rat entry there and is not enumerated below because nothing local resolves it to a gene symbol. PTHR24289-paint.tsv carries a wider set for the same node - a second rat seed RGD:2460, and a mouse seed MGI:MGI:88590 which is NOT the target (Cyp1a1-uniprot.txt:480 gives this gene as MGI:88588), so the block claims no self-seed. Neither of those two resolves to a symbol locally either. Steroid oxidation is genuinely shared across the vertebrate CYP1 enzymes that seed this node, so the biology transfers to mouse Cyp1a1; the fault is that a term covering members with differing regiochemistry can only be the generic steroid-hydroxylase parent. UniProtKB:P04798 · human CYP1A1 (cytochrome P450 1A1) SUPPORTS TRANSFER The human orthologue and the closest comparator for the mouse enzyme; its characterized estrogen hydroxylation is the activity the proposed replacement terms name. UniProtKB:P05177 · human CYP1A2 (cytochrome P450 1A2) SUPPORTS TRANSFER A CYP1A seed whose steroid-oxidizing evidence supports the transfer of the biology to the mouse enzyme. UniProtKB:Q16678 · human CYP1B1 (cytochrome P450 1B1) SUPPORTS TRANSFER A further CYP1 seed. Its steroid-hydroxylase evidence supports the generic transfer, but the characterized CYP1A1 activity - specifically 2- and 16-alpha-hydroxyestrogen formation, documented for the human orthologue and carried to the mouse entry by similarity (ECO:0000250|UniProtKB:P04798) - is narrower than the generic parent term expresses. ZFIN:ZDB-GENE-041114-179 SUPPORTS TRANSFER Zebrafish seed, cited by identifier because the local index does not resolve it; it extends the node beyond mammals and supports the antiquity of CYP1 steroid oxidation. Proposed replacements: estrogen 2-hydroxylase activity estrogen 16-alpha-hydroxylase activity Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | IBA GO_REF:0000033 | ACCEPT | Summary: Cyp1a1 encodes a CYP1-family heme monooxygenase. UniProt and the Falcon synthesis describe the canonical P450 paired-donor monooxygenase reaction, and mouse enzyme studies support CYP1A1-dependent oxidation of aromatic xenobiotic substrates. Reason: Core catalytic activity of CYP1A1. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md CYP1A1 is a membrane-associated heme-thiolate monooxygenase (cytochrome P450) classically found in microsomal/endoplasmic reticulum (ER) membranes as part of the mixed-function oxidase system. PMID:8274012 Kinetics of benzo[alpha]pyrene hydroxylase (AHH), 7-methoxyresorufin o-demethylase (MROD), and 7-ethoxyresorufin o-deethylase (EROD) were estimated in microsomes of Hep G2 cells infected with a recombinant vaccinia virus bearing mouse CYP1A1 or CYP1A2 cDNAs. |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The annotation has homology or database support but is not the primary catalytic site emphasized for mouse CYP1A1; the core location remains ER/microsomal membrane. Reason: Supported as a secondary or inferred localization, not the core catalytic compartment. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Mitochondrion inner membrane. Microsome membrane. Cytoplasm. |
| GO:0006706 steroid catabolic process | IBA GO_REF:0000033 | MODIFY | Summary: CYP1A1 has supported estrogen hydroxylase activities, but the broader steroid hydroxylase/steroid catabolism framing is not the best representation of the evidence and is not the core xenobiotic function. Reason: Prefer specific estrogen hydroxylase/metabolic terms where retained; do not treat broad steroid catabolism as core. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN001210461 SUPPORTS TRANSFER The steroid-catabolism IBD sits at this node and is carried by a CYP1A seed. The short seed list is not weak support - the PAINT curator placed the assertion after weighing the family's experimental annotations, and CYP1A oxidation of steroids is not in doubt - so the transfer of the biology to mouse Cyp1a1 stands. The issue is the term, which names steroid catabolism in general where the characterized substrates of the CYP1A1 orthologue are estrogens. UniProtKB:P05177 · human CYP1A2 (cytochrome P450 1A2) SUPPORTS TRANSFER The CYP1A seed for this term. Its steroid-oxidation biology transfers to mouse Cyp1a1. Formation of hydroxyestrogens from estrone and 17beta-estradiol is documented for the human orthologue and carried to the mouse entry by similarity (ECO:0000250|UniProtKB:P04798); the replacement term names that substrate class rather than steroid catabolism at large. Proposed replacements: estrogen metabolic process Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0008210 estrogen metabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0009404 toxin metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: This process captures the main biological role of CYP1A1: phase I metabolism of xenobiotics, especially PAHs and related aromatic toxicants. Mouse knockout and enzyme studies support detoxication and metabolic activation roles depending on substrate and tissue. Reason: Core biological process for CYP1A1 xenobiotic and toxin metabolism. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md Recent mouse work highlights polycyclic aromatic hydrocarbons (PAHs) as major CYP1A1 substrates/inducers; benzo[a]pyrene (B[a]P/BaP) is a prototypic example. PMID:17166882 the major CYP1 enzymes that metabolize DBC are CYP1A1 in beta-naphthoflavone (BNF)-induced liver, CYP1A2 in non-induced liver, CYP1B1 and CYP1A1 in induced lung and none in non-induced lung. |
| GO:0042178 xenobiotic catabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: This process captures the main biological role of CYP1A1: phase I metabolism of xenobiotics, especially PAHs and related aromatic toxicants. Mouse knockout and enzyme studies support detoxication and metabolic activation roles depending on substrate and tissue. Reason: Core biological process for CYP1A1 xenobiotic and toxin metabolism. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md Recent mouse work highlights polycyclic aromatic hydrocarbons (PAHs) as major CYP1A1 substrates/inducers; benzo[a]pyrene (B[a]P/BaP) is a prototypic example. PMID:16377763 inducible CYP1A1, probably in both intestine and liver, is most important in detoxication |
| GO:0004497 monooxygenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Cyp1a1 encodes a CYP1-family heme monooxygenase. UniProt and the Falcon synthesis describe the canonical P450 paired-donor monooxygenase reaction, and mouse enzyme studies support CYP1A1-dependent oxidation of aromatic xenobiotic substrates. Reason: Core catalytic activity of CYP1A1. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md CYP1A1 is a membrane-associated heme-thiolate monooxygenase (cytochrome P450) classically found in microsomal/endoplasmic reticulum (ER) membranes as part of the mixed-function oxidase system. PMID:8274012 Kinetics of benzo[alpha]pyrene hydroxylase (AHH), 7-methoxyresorufin o-demethylase (MROD), and 7-ethoxyresorufin o-deethylase (EROD) were estimated in microsomes of Hep G2 cells infected with a recombinant vaccinia virus bearing mouse CYP1A1 or CYP1A2 cDNAs. |
| GO:0005506 iron ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: This describes the heme/iron cofactor chemistry of a cytochrome P450 enzyme. It is valid supporting biology but is not a standalone core molecular function. Reason: Necessary cofactor binding but not informative as a core gene function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt COFACTOR: Name=heme |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The annotation has homology or database support but is not the primary catalytic site emphasized for mouse CYP1A1; the core location remains ER/microsomal membrane. Reason: Supported as a secondary or inferred localization, not the core catalytic compartment. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Mitochondrion inner membrane. Microsome membrane. Cytoplasm. |
| GO:0005743 mitochondrial inner membrane | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The annotation has homology or database support but is not the primary catalytic site emphasized for mouse CYP1A1; the core location remains ER/microsomal membrane. Reason: Supported as a secondary or inferred localization, not the core catalytic compartment. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Mitochondrion inner membrane. Microsome membrane. Cytoplasm. |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: CYP1A1 is principally a microsomal/endoplasmic-reticulum membrane cytochrome P450. UniProt lists ER and microsome membrane localization, and Falcon highlights ER/microsomal localization as the main catalytic context. Reason: Primary subcellular site for microsomal CYP1A1 catalysis. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Mitochondrion inner membrane. Microsome membrane. Cytoplasm. file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md CYP1A1 is a membrane-associated heme-thiolate monooxygenase (cytochrome P450) classically found in microsomal/endoplasmic reticulum (ER) membranes as part of the mixed-function oxidase system. |
| GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | IEA GO_REF:0000002 | MODIFY | Summary: The annotation captures CYP1A1 oxidoreductase chemistry but is less precise than the P450 paired-donor monooxygenase term supported by UniProt, Falcon, and mouse enzyme evidence. Reason: Replace with the more specific CYP monooxygenase/paired-donor oxidoreductase term. |
| GO:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | IEA GO_REF:0000120 | ACCEPT | Summary: Cyp1a1 encodes a CYP1-family heme monooxygenase. UniProt and the Falcon synthesis describe the canonical P450 paired-donor monooxygenase reaction, and mouse enzyme studies support CYP1A1-dependent oxidation of aromatic xenobiotic substrates. Reason: Core catalytic activity of CYP1A1. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md CYP1A1 is a membrane-associated heme-thiolate monooxygenase (cytochrome P450) classically found in microsomal/endoplasmic reticulum (ER) membranes as part of the mixed-function oxidase system. PMID:8274012 Kinetics of benzo[alpha]pyrene hydroxylase (AHH), 7-methoxyresorufin o-demethylase (MROD), and 7-ethoxyresorufin o-deethylase (EROD) were estimated in microsomes of Hep G2 cells infected with a recombinant vaccinia virus bearing mouse CYP1A1 or CYP1A2 cDNAs. |
| GO:0020037 heme binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: This describes the heme/iron cofactor chemistry of a cytochrome P450 enzyme. It is valid supporting biology but is not a standalone core molecular function. Reason: Necessary cofactor binding but not informative as a core gene function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt COFACTOR: Name=heme |
| GO:0106256 hydroperoxy icosatetraenoate dehydratase activity | IEA GO_REF:0000003 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0001666 response to hypoxia | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0001676 long-chain fatty acid metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0001889 liver development | IEA GO_REF:0000107 | REMOVE | Summary: No reviewed mouse Cyp1a1 evidence supports a direct role for CYP1A1 in this developmental or cell-cycle process; the annotation likely reflects indirect expression or phenotype transfer rather than gene-product function. Reason: Unsupported developmental or cell-cycle role. |
| GO:0002933 lipid hydroxylation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0006631 fatty acid metabolic process | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0006778 porphyrin-containing compound metabolic process | IEA GO_REF:0000107 | REMOVE | Summary: This annotation does not match CYP1A1 biology. CYP1A1 uses heme and catalyzes monooxygenase reactions, but the reviewed evidence does not support this term as a process or activity of the gene product. Reason: Unsupported or chemically mismatched annotation for CYP1A1. |
| GO:0006805 xenobiotic metabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: This process captures the main biological role of CYP1A1: phase I metabolism of xenobiotics, especially PAHs and related aromatic toxicants. Mouse knockout and enzyme studies support detoxication and metabolic activation roles depending on substrate and tissue. Reason: Core biological process for CYP1A1 xenobiotic and toxin metabolism. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md Recent mouse work highlights polycyclic aromatic hydrocarbons (PAHs) as major CYP1A1 substrates/inducers; benzo[a]pyrene (B[a]P/BaP) is a prototypic example. PMID:16377763 inducible CYP1A1, probably in both intestine and liver, is most important in detoxication |
| GO:0008202 steroid metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0008210 estrogen metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0008391 arachidonate monooxygenase activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0008395 steroid hydroxylase activity | IEA GO_REF:0000107 | MODIFY | Summary: CYP1A1 has supported estrogen hydroxylase activities, but the broader steroid hydroxylase/steroid catabolism framing is not the best representation of the evidence and is not the core xenobiotic function. Reason: Prefer specific estrogen hydroxylase/metabolic terms where retained; do not treat broad steroid catabolism as core. Proposed replacements: estrogen 2-hydroxylase activity estrogen 16-alpha-hydroxylase activity Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0009410 response to xenobiotic stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The response annotation is consistent with CYP1A1 being an AHR-inducible xenobiotic-response gene, but it reflects regulatory context rather than the core enzymatic activity. Reason: Regulatory or exposure-response context rather than the enzyme activity itself. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md AHR is a ligand-activated transcription factor: ligand binding triggers AHR nuclear translocation and heterodimerization with ARNT, leading to binding at xenobiotic response elements (XREs) and induction of canonical target genes including Cyp1a1 and Ahrr. |
| GO:0009624 response to nematode | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0009635 response to herbicide | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0009804 coumarin metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0009812 flavonoid metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0010041 response to iron(III) ion | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0016491 oxidoreductase activity | IEA GO_REF:0000120 | MODIFY | Summary: The annotation captures CYP1A1 oxidoreductase chemistry but is less precise than the P450 paired-donor monooxygenase term supported by UniProt, Falcon, and mouse enzyme evidence. Reason: Replace with the more specific CYP monooxygenase/paired-donor oxidoreductase term. |
| GO:0016679 oxidoreductase activity, acting on diphenols and related substances as donors | IEA GO_REF:0000107 | REMOVE | Summary: This annotation does not match CYP1A1 biology. CYP1A1 uses heme and catalyzes monooxygenase reactions, but the reviewed evidence does not support this term as a process or activity of the gene product. Reason: Unsupported or chemically mismatched annotation for CYP1A1. |
| GO:0016711 flavonoid 3'-monooxygenase activity | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0017143 insecticide metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0018894 dibenzo-p-dioxin metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0019341 dibenzo-p-dioxin catabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0019899 enzyme binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The binding annotation is supported mainly by homology to chaperone-assisted mitochondrial targeting. It is ancillary to CYP1A1 catalysis and should not be treated as a core function. Reason: Ancillary targeting/chaperone interaction rather than catalytic function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. |
| GO:0030544 Hsp70 protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The binding annotation is supported mainly by homology to chaperone-assisted mitochondrial targeting. It is ancillary to CYP1A1 catalysis and should not be treated as a core function. Reason: Ancillary targeting/chaperone interaction rather than catalytic function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. |
| GO:0032094 response to food | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The response annotation is consistent with CYP1A1 being an AHR-inducible xenobiotic-response gene, but it reflects regulatory context rather than the core enzymatic activity. Reason: Regulatory or exposure-response context rather than the enzyme activity itself. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md AHR is a ligand-activated transcription factor: ligand binding triggers AHR nuclear translocation and heterodimerization with ARNT, leading to binding at xenobiotic response elements (XREs) and induction of canonical target genes including Cyp1a1 and Ahrr. |
| GO:0032451 demethylase activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0032496 response to lipopolysaccharide | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0033189 response to vitamin A | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The response annotation is consistent with CYP1A1 being an AHR-inducible xenobiotic-response gene, but it reflects regulatory context rather than the core enzymatic activity. Reason: Regulatory or exposure-response context rather than the enzyme activity itself. |
| GO:0033595 response to genistein | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The response annotation is consistent with CYP1A1 being an AHR-inducible xenobiotic-response gene, but it reflects regulatory context rather than the core enzymatic activity. Reason: Regulatory or exposure-response context rather than the enzyme activity itself. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md AHR is a ligand-activated transcription factor: ligand binding triggers AHR nuclear translocation and heterodimerization with ARNT, leading to binding at xenobiotic response elements (XREs) and induction of canonical target genes including Cyp1a1 and Ahrr. |
| GO:0035902 response to immobilization stress | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0042359 vitamin D metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0042572 retinol metabolic process | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0042904 9-cis-retinoic acid biosynthetic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0043010 camera-type eye development | IEA GO_REF:0000107 | REMOVE | Summary: No reviewed mouse Cyp1a1 evidence supports a direct role for CYP1A1 in this developmental or cell-cycle process; the annotation likely reflects indirect expression or phenotype transfer rather than gene-product function. Reason: Unsupported developmental or cell-cycle role. |
| GO:0046209 nitric oxide metabolic process | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0046685 response to arsenic-containing substance | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0048565 digestive tract development | IEA GO_REF:0000107 | REMOVE | Summary: No reviewed mouse Cyp1a1 evidence supports a direct role for CYP1A1 in this developmental or cell-cycle process; the annotation likely reflects indirect expression or phenotype transfer rather than gene-product function. Reason: Unsupported developmental or cell-cycle role. |
| GO:0048771 tissue remodeling | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0051879 Hsp90 protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The binding annotation is supported mainly by homology to chaperone-assisted mitochondrial targeting. It is ancillary to CYP1A1 catalysis and should not be treated as a core function. Reason: Ancillary targeting/chaperone interaction rather than catalytic function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. |
| GO:0055093 response to hyperoxia | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0060137 maternal process involved in parturition | IEA GO_REF:0000107 | REMOVE | Summary: No reviewed mouse Cyp1a1 evidence supports a direct role for CYP1A1 in this developmental or cell-cycle process; the annotation likely reflects indirect expression or phenotype transfer rather than gene-product function. Reason: Unsupported developmental or cell-cycle role. |
| GO:0070365 hepatocyte differentiation | IEA GO_REF:0000107 | REMOVE | Summary: No reviewed mouse Cyp1a1 evidence supports a direct role for CYP1A1 in this developmental or cell-cycle process; the annotation likely reflects indirect expression or phenotype transfer rather than gene-product function. Reason: Unsupported developmental or cell-cycle role. |
| GO:0070576 vitamin D 24-hydroxylase activity | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0071280 cellular response to copper ion | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:0101020 estrogen 16-alpha-hydroxylase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0101021 estrogen 2-hydroxylase activity | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0102033 long-chain fatty acid omega-hydroxylase activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0120319 long-chain fatty acid omega-1 hydroxylase activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:1900087 positive regulation of G1/S transition of mitotic cell cycle | IEA GO_REF:0000107 | REMOVE | Summary: No reviewed mouse Cyp1a1 evidence supports a direct role for CYP1A1 in this developmental or cell-cycle process; the annotation likely reflects indirect expression or phenotype transfer rather than gene-product function. Reason: Unsupported developmental or cell-cycle role. |
| GO:1901497 response to diphenyl ether | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This appears to be an inferred or expression-based response annotation. Available Cyp1a1 evidence supports AHR-regulated xenobiotic metabolism, not a direct mechanistic role in this specific response process. Reason: Likely over-propagated response annotation with insufficient direct support for CYP1A1 function. |
| GO:1904010 response to Aroclor 1254 | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The response annotation is consistent with CYP1A1 being an AHR-inducible xenobiotic-response gene, but it reflects regulatory context rather than the core enzymatic activity. Reason: Regulatory or exposure-response context rather than the enzyme activity itself. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md AHR is a ligand-activated transcription factor: ligand binding triggers AHR nuclear translocation and heterodimerization with ARNT, leading to binding at xenobiotic response elements (XREs) and induction of canonical target genes including Cyp1a1 and Ahrr. |
| GO:1904612 response to 2,3,7,8-tetrachlorodibenzodioxine | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The response annotation is consistent with CYP1A1 being an AHR-inducible xenobiotic-response gene, but it reflects regulatory context rather than the core enzymatic activity. Reason: Regulatory or exposure-response context rather than the enzyme activity itself. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md AHR is a ligand-activated transcription factor: ligand binding triggers AHR nuclear translocation and heterodimerization with ARNT, leading to binding at xenobiotic response elements (XREs) and induction of canonical target genes including Cyp1a1 and Ahrr. |
| GO:1904681 response to 3-methylcholanthrene | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The response annotation is consistent with CYP1A1 being an AHR-inducible xenobiotic-response gene, but it reflects regulatory context rather than the core enzymatic activity. Reason: Regulatory or exposure-response context rather than the enzyme activity itself. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md AHR is a ligand-activated transcription factor: ligand binding triggers AHR nuclear translocation and heterodimerization with ARNT, leading to binding at xenobiotic response elements (XREs) and induction of canonical target genes including Cyp1a1 and Ahrr. |
| GO:0001676 long-chain fatty acid metabolic process | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0002933 lipid hydroxylation | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0006631 fatty acid metabolic process | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0006805 xenobiotic metabolic process | ISO GO_REF:0000119 | ACCEPT | Summary: This process captures the main biological role of CYP1A1: phase I metabolism of xenobiotics, especially PAHs and related aromatic toxicants. Mouse knockout and enzyme studies support detoxication and metabolic activation roles depending on substrate and tissue. Reason: Core biological process for CYP1A1 xenobiotic and toxin metabolism. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md Recent mouse work highlights polycyclic aromatic hydrocarbons (PAHs) as major CYP1A1 substrates/inducers; benzo[a]pyrene (B[a]P/BaP) is a prototypic example. PMID:16377763 inducible CYP1A1, probably in both intestine and liver, is most important in detoxication |
| GO:0008202 steroid metabolic process | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0008210 estrogen metabolic process | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0008391 arachidonate monooxygenase activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0016491 oxidoreductase activity | ISO GO_REF:0000119 | MODIFY | Summary: The annotation captures CYP1A1 oxidoreductase chemistry but is less precise than the P450 paired-donor monooxygenase term supported by UniProt, Falcon, and mouse enzyme evidence. Reason: Replace with the more specific CYP monooxygenase/paired-donor oxidoreductase term. |
| GO:0042359 vitamin D metabolic process | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0042572 retinol metabolic process | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0070576 vitamin D 24-hydroxylase activity | ISO GO_REF:0000119 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0101020 estrogen 16-alpha-hydroxylase activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0101021 estrogen 2-hydroxylase activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0102033 long-chain fatty acid omega-hydroxylase activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0120319 long-chain fatty acid omega-1 hydroxylase activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0004497 monooxygenase activity | ISO GO_REF:0000096 | ACCEPT | Summary: Cyp1a1 encodes a CYP1-family heme monooxygenase. UniProt and the Falcon synthesis describe the canonical P450 paired-donor monooxygenase reaction, and mouse enzyme studies support CYP1A1-dependent oxidation of aromatic xenobiotic substrates. Reason: Core catalytic activity of CYP1A1. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md CYP1A1 is a membrane-associated heme-thiolate monooxygenase (cytochrome P450) classically found in microsomal/endoplasmic reticulum (ER) membranes as part of the mixed-function oxidase system. PMID:8274012 Kinetics of benzo[alpha]pyrene hydroxylase (AHH), 7-methoxyresorufin o-demethylase (MROD), and 7-ethoxyresorufin o-deethylase (EROD) were estimated in microsomes of Hep G2 cells infected with a recombinant vaccinia virus bearing mouse CYP1A1 or CYP1A2 cDNAs. |
| GO:0005743 mitochondrial inner membrane | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: The annotation has homology or database support but is not the primary catalytic site emphasized for mouse CYP1A1; the core location remains ER/microsomal membrane. Reason: Supported as a secondary or inferred localization, not the core catalytic compartment. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Mitochondrion inner membrane. Microsome membrane. Cytoplasm. |
| GO:0006778 porphyrin-containing compound metabolic process | ISO GO_REF:0000096 | REMOVE | Summary: This annotation does not match CYP1A1 biology. CYP1A1 uses heme and catalyzes monooxygenase reactions, but the reviewed evidence does not support this term as a process or activity of the gene product. Reason: Unsupported or chemically mismatched annotation for CYP1A1. |
| GO:0008395 steroid hydroxylase activity | ISO GO_REF:0000096 | MODIFY | Summary: CYP1A1 has supported estrogen hydroxylase activities, but the broader steroid hydroxylase/steroid catabolism framing is not the best representation of the evidence and is not the core xenobiotic function. Reason: Prefer specific estrogen hydroxylase/metabolic terms where retained; do not treat broad steroid catabolism as core. Proposed replacements: estrogen 2-hydroxylase activity estrogen 16-alpha-hydroxylase activity Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0009804 coumarin metabolic process | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0009812 flavonoid metabolic process | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0016491 oxidoreductase activity | ISO GO_REF:0000096 | MODIFY | Summary: The annotation captures CYP1A1 oxidoreductase chemistry but is less precise than the P450 paired-donor monooxygenase term supported by UniProt, Falcon, and mouse enzyme evidence. Reason: Replace with the more specific CYP monooxygenase/paired-donor oxidoreductase term. |
| GO:0016679 oxidoreductase activity, acting on diphenols and related substances as donors | ISO GO_REF:0000096 | REMOVE | Summary: This annotation does not match CYP1A1 biology. CYP1A1 uses heme and catalyzes monooxygenase reactions, but the reviewed evidence does not support this term as a process or activity of the gene product. Reason: Unsupported or chemically mismatched annotation for CYP1A1. |
| GO:0016711 flavonoid 3'-monooxygenase activity | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0017143 insecticide metabolic process | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0018894 dibenzo-p-dioxin metabolic process | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0019341 dibenzo-p-dioxin catabolic process | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0019899 enzyme binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: The binding annotation is supported mainly by homology to chaperone-assisted mitochondrial targeting. It is ancillary to CYP1A1 catalysis and should not be treated as a core function. Reason: Ancillary targeting/chaperone interaction rather than catalytic function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. |
| GO:0030544 Hsp70 protein binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: The binding annotation is supported mainly by homology to chaperone-assisted mitochondrial targeting. It is ancillary to CYP1A1 catalysis and should not be treated as a core function. Reason: Ancillary targeting/chaperone interaction rather than catalytic function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. |
| GO:0032451 demethylase activity | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. |
| GO:0042904 9-cis-retinoic acid biosynthetic process | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: This substrate/process annotation is too specific for the available mouse Cyp1a1 evidence and likely reflects broad CYP-family or orthology transfer rather than a demonstrated CYP1A1 function. Reason: Too specific or pathway-like for the available Cyp1a1 evidence. |
| GO:0051879 Hsp90 protein binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: The binding annotation is supported mainly by homology to chaperone-assisted mitochondrial targeting. It is ancillary to CYP1A1 catalysis and should not be treated as a core function. Reason: Ancillary targeting/chaperone interaction rather than catalytic function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. |
| GO:1900087 positive regulation of G1/S transition of mitotic cell cycle | ISO GO_REF:0000096 | REMOVE | Summary: No reviewed mouse Cyp1a1 evidence supports a direct role for CYP1A1 in this developmental or cell-cycle process; the annotation likely reflects indirect expression or phenotype transfer rather than gene-product function. Reason: Unsupported developmental or cell-cycle role. |
| GO:0042572 retinol metabolic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0008210 estrogen metabolic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0101020 estrogen 16-alpha-hydroxylase activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0101021 estrogen 2-hydroxylase activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt 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 C15alpha and C16alpha positions. Displays different regioselectivities for polyunsaturated fatty acids (PUFA) hydroxylation. |
| GO:0005743 mitochondrial inner membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The annotation has homology or database support but is not the primary catalytic site emphasized for mouse CYP1A1; the core location remains ER/microsomal membrane. Reason: Supported as a secondary or inferred localization, not the core catalytic compartment. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane. Mitochondrion inner membrane. Microsome membrane. Cytoplasm. |
| GO:0030544 Hsp70 protein binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The binding annotation is supported mainly by homology to chaperone-assisted mitochondrial targeting. It is ancillary to CYP1A1 catalysis and should not be treated as a core function. Reason: Ancillary targeting/chaperone interaction rather than catalytic function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. |
| GO:0051879 Hsp90 protein binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: The binding annotation is supported mainly by homology to chaperone-assisted mitochondrial targeting. It is ancillary to CYP1A1 catalysis and should not be treated as a core function. Reason: Ancillary targeting/chaperone interaction rather than catalytic function. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt Interacts with cytosolic chaperones HSP70 and HSP90; this interaction is required for initial targeting to mitochondria. |
| GO:0009636 response to toxic substance | IMP PMID:16377763 Oral benzo[a]pyrene in Cyp1 knockout mouse lines: CYP1A1 imp... | KEEP AS NON CORE | Summary: The response annotation is consistent with CYP1A1 being an AHR-inducible xenobiotic-response gene, but it reflects regulatory context rather than the core enzymatic activity. Reason: Regulatory or exposure-response context rather than the enzyme activity itself. Supporting Evidence: PMID:16377763 inducible CYP1A1, probably in both intestine and liver, is most important in detoxication |
| GO:0009308 amine metabolic process | IMP PMID:17052995 Mouse lung CYP1A1 catalyzes the metabolic activation of 2-am... | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: PMID:17052995 These results reveal that mouse lung has basal and inducible PhIP N(2)-hydroxylase activity predominantly catalyzed by CYP1A1. |
| GO:0009404 toxin metabolic process | IMP PMID:17166882 7H-dibenzo[c,g]carbazole metabolism by the mouse and human C... | ACCEPT | Summary: This process captures the main biological role of CYP1A1: phase I metabolism of xenobiotics, especially PAHs and related aromatic toxicants. Mouse knockout and enzyme studies support detoxication and metabolic activation roles depending on substrate and tissue. Reason: Core biological process for CYP1A1 xenobiotic and toxin metabolism. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md Recent mouse work highlights polycyclic aromatic hydrocarbons (PAHs) as major CYP1A1 substrates/inducers; benzo[a]pyrene (B[a]P/BaP) is a prototypic example. PMID:17166882 the major CYP1 enzymes that metabolize DBC are CYP1A1 in beta-naphthoflavone (BNF)-induced liver, CYP1A2 in non-induced liver, CYP1B1 and CYP1A1 in induced lung and none in non-induced lung. |
| GO:0018958 phenol-containing compound metabolic process | IMP PMID:17052995 Mouse lung CYP1A1 catalyzes the metabolic activation of 2-am... | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: PMID:17052995 These results reveal that mouse lung has basal and inducible PhIP N(2)-hydroxylase activity predominantly catalyzed by CYP1A1. |
| GO:0016712 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen | IDA PMID:8274012 Enzyme-kinetic and immunochemical characteristics of mouse c... | ACCEPT | Summary: Cyp1a1 encodes a CYP1-family heme monooxygenase. UniProt and the Falcon synthesis describe the canonical P450 paired-donor monooxygenase reaction, and mouse enzyme studies support CYP1A1-dependent oxidation of aromatic xenobiotic substrates. Reason: Core catalytic activity of CYP1A1. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md CYP1A1 is a membrane-associated heme-thiolate monooxygenase (cytochrome P450) classically found in microsomal/endoplasmic reticulum (ER) membranes as part of the mixed-function oxidase system. PMID:8274012 Kinetics of benzo[alpha]pyrene hydroxylase (AHH), 7-methoxyresorufin o-demethylase (MROD), and 7-ethoxyresorufin o-deethylase (EROD) were estimated in microsomes of Hep G2 cells infected with a recombinant vaccinia virus bearing mouse CYP1A1 or CYP1A2 cDNAs. |
| GO:0050665 hydrogen peroxide biosynthetic process | IMP PMID:14980704 Cyp1a2 protects against reactive oxygen production in mouse ... | KEEP AS NON CORE | Summary: The annotation is biologically plausible from UniProt/homology evidence because CYP1A1 can oxidize endogenous lipids, retinoids, and estrogens, but these are secondary substrate classes relative to the canonical xenobiotic/PAH monooxygenase role. Reason: Valid secondary substrate/process context, not the central evolved role emphasized by mouse literature. Supporting Evidence: PMID:14980704 Cyp1a1(-/-) microsomes displayed markedly lower levels of H(2)O(2) production in both induced and noninduced microsomes, compared with those in wild-type and Cyp1a2(-/-) microsomes. |
| GO:0004497 monooxygenase activity | IDA PMID:14642533 Upregulation of CYP2e1 and CYP3a activities in histamine-def... | ACCEPT | Summary: Cyp1a1 encodes a CYP1-family heme monooxygenase. UniProt and the Falcon synthesis describe the canonical P450 paired-donor monooxygenase reaction, and mouse enzyme studies support CYP1A1-dependent oxidation of aromatic xenobiotic substrates. Reason: Core catalytic activity of CYP1A1. Supporting Evidence: file:mouse/Cyp1a1/Cyp1a1-uniprot.txt A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, steroid hormones and vitamins. 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 (CPR; NADPH-ferrihemoprotein reductase). file:mouse/Cyp1a1/Cyp1a1-deep-research-falcon.md CYP1A1 is a membrane-associated heme-thiolate monooxygenase (cytochrome P450) classically found in microsomal/endoplasmic reticulum (ER) membranes as part of the mixed-function oxidase system. PMID:8274012 Kinetics of benzo[alpha]pyrene hydroxylase (AHH), 7-methoxyresorufin o-demethylase (MROD), and 7-ethoxyresorufin o-deethylase (EROD) were estimated in microsomes of Hep G2 cells infected with a recombinant vaccinia virus bearing mouse CYP1A1 or CYP1A2 cDNAs. PMID:14642533 ethoxyresorufin O-dealkylase activity of CYP1A |
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Download this section (compressed HTML)Q: Should mouse Cyp1a1 retain mitochondrial inner membrane and HSP70/HSP90 binding annotations when the cited support is primarily homology to rat CYP1A1 rather than direct mouse localization evidence?
Q: Should highly specific dioxin, vitamin D, flavonoid, and stress-response annotations be narrowed to xenobiotic metabolism/response terms unless direct mouse Cyp1a1 substrate evidence is available?
Experiment: Perform direct mouse CYP1A1 substrate assays with purified enzyme or Cyp1a1-null rescue microsomes for vitamin D, retinoid, flavonoid, coumarin, and eicosanoid substrates to separate true CYP1A1 activities from broad CYP-family transfer.
Experiment: Use induced mouse tissues with fractionation or targeted proteomics to test whether mitochondrial CYP1A1 localization is reproducible and functionally significant relative to ER/microsomal CYP1A1.
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