Cyp11b2 encodes mouse aldosterone synthase, a heme-containing mitochondrial cytochrome P450 expressed in adrenal zona glomerulosa cells. It converts deoxycorticosterone to aldosterone through 11-beta hydroxylation, corticosterone 18-hydroxylation and a final C18 oxidation. The reaction sequence uses molecular oxygen and electrons delivered through the mitochondrial adrenodoxin system. Aldosterone production supports electrolyte, water and blood-pressure homeostasis; Cyp11b2-deficient mice lack aldosterone and develop hypotension and compensatory activation of the renin-angiotensin system. Corticosterone is the principal mouse adrenal glucocorticoid, and is also an intermediate in the Cyp11b2 reaction sequence.
Definition: Catalysis of the reaction: 18-hydroxycorticosterone + 2 reduced adrenodoxin + O2 + 2 H+ = aldosterone + 2 oxidized adrenodoxin + 2 H2O. The C18 hydroxymethyl group is oxidized to the aldehyde group of aldosterone.
Justification: Mouse Cyp11b2 makes aldosterone and carries the curated orthology-supported RHEA:50792 reaction. GO:0047783 names the preceding hydroxylation rather than this oxidation. The same proposed term as the human CYP11B2 review represents this chemically distinct activity without inventing a GO identifier.
Parent term: oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
Mappings:
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001991 regulation of systemic arterial blood pressure by circulatory renin-angiotensin | IMP PMID:16118390 Kidney function in mice lacking aldosterone. | KEEP AS NON CORE | Summary: Aldosterone synthesis contributes to systemic blood-pressure control within the renin-angiotensin system. Reason: Cyp11b2 deletion causes hypotension and marked activation of the renin-angiotensin system. This physiological feedback role is secondary to the catalytic core; the enzyme is not an angiotensin receptor or renin-processing protease. Supporting Evidence: PMID:16118390 the AS-/- mice have low blood pressure, abnormal electrolyte homeostasis PMID:16118390 strong activation of the renin-angiotensin system. |
| GO:0002017 regulation of blood volume by renal aldosterone | IMP PMID:16118390 Kidney function in mice lacking aldosterone. | KEEP AS NON CORE | Summary: Aldosterone-dependent renal salt and water handling influences blood volume. Reason: The knockout study reports impaired distal-nephron sodium reabsorption, abnormal urine concentration and low blood pressure. This supports the existing systemic volume-homeostasis context; Cyp11b2 synthesizes the hormone rather than transporting renal ions itself. Supporting Evidence: PMID:16118390 absence of aldosterone in AS-/- mice results in impairment of Na+ reabsorption in the distal nephron, decreased blood pressure, and strong renin-angiotensin system activation. |
| GO:0004497 monooxygenase activity | IEA GO_REF:0000002 | MODIFY | Summary: Refine broad oxidative activity to the two specific hydroxylation reactions. Reason: Mouse aldosterone synthase executes both steroid 11-beta hydroxylation and corticosterone 18-hydroxylation. Both refinements are retained, rather than choosing one. The third C18 oxidation is represented separately by a proposed molecular function because the 18-hydroxylase term does not name the terminal reaction. Proposed replacements: steroid 11-beta-monooxygenase activity corticosterone 18-monooxygenase activity Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0004507 steroid 11-beta-monooxygenase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Mouse aldosterone synthase performs steroid 11-beta hydroxylation. Reason: The mouse expression study distinguishes Cyp11b2 from Cyp11b1 and demonstrates aldosterone formation from the deoxycorticosterone route. Curated catalytic reaction data support the initial corticosterone-producing hydroxylation. All repeated evidence rows represent the same supported gene-level activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0004507 steroid 11-beta-monooxygenase activity | IDA PMID:1686470 Different isozymes of mouse 11 beta-hydroxylase produce mine... | ACCEPT | Summary: Mouse aldosterone synthase performs steroid 11-beta hydroxylation. Reason: The mouse expression study distinguishes Cyp11b2 from Cyp11b1 and demonstrates aldosterone formation from the deoxycorticosterone route. Curated catalytic reaction data support the initial corticosterone-producing hydroxylation. All repeated evidence rows represent the same supported gene-level activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0004507 steroid 11-beta-monooxygenase activity | IDA PMID:8645611 The hamster adrenal cytochrome P450C11 has equipotent 11beta... | ACCEPT | Summary: Mouse aldosterone synthase performs steroid 11-beta hydroxylation. Reason: The mouse expression study distinguishes Cyp11b2 from Cyp11b1 and demonstrates aldosterone formation from the deoxycorticosterone route. Curated catalytic reaction data support the initial corticosterone-producing hydroxylation. All repeated evidence rows represent the same supported gene-level activity. The cited abstract explicitly concerns hamster enzymes; its full text was unavailable, so mouse comparative experiments cannot be excluded. Retention rests on the independent mouse study, not assumed mouse data in that abstract. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0004507 steroid 11-beta-monooxygenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Mouse aldosterone synthase performs steroid 11-beta hydroxylation. Reason: The mouse expression study distinguishes Cyp11b2 from Cyp11b1 and demonstrates aldosterone formation from the deoxycorticosterone route. Curated catalytic reaction data support the initial corticosterone-producing hydroxylation. All repeated evidence rows represent the same supported gene-level activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0004507 steroid 11-beta-monooxygenase activity | ISO GO_REF:0000096 | ACCEPT | Summary: Mouse aldosterone synthase performs steroid 11-beta hydroxylation. Reason: The mouse expression study distinguishes Cyp11b2 from Cyp11b1 and demonstrates aldosterone formation from the deoxycorticosterone route. Curated catalytic reaction data support the initial corticosterone-producing hydroxylation. All repeated evidence rows represent the same supported gene-level activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0004507 steroid 11-beta-monooxygenase activity | ISO GO_REF:0000096 | ACCEPT | Summary: Mouse aldosterone synthase performs steroid 11-beta hydroxylation. Reason: The mouse expression study distinguishes Cyp11b2 from Cyp11b1 and demonstrates aldosterone formation from the deoxycorticosterone route. Curated catalytic reaction data support the initial corticosterone-producing hydroxylation. All repeated evidence rows represent the same supported gene-level activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0004507 steroid 11-beta-monooxygenase activity | ISO GO_REF:0000119 | ACCEPT | Summary: Mouse aldosterone synthase performs steroid 11-beta hydroxylation. Reason: The mouse expression study distinguishes Cyp11b2 from Cyp11b1 and demonstrates aldosterone formation from the deoxycorticosterone route. Curated catalytic reaction data support the initial corticosterone-producing hydroxylation. All repeated evidence rows represent the same supported gene-level activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0004507 steroid 11-beta-monooxygenase activity | ISO GO_REF:0000119 | ACCEPT | Summary: Mouse aldosterone synthase performs steroid 11-beta hydroxylation. Reason: The mouse expression study distinguishes Cyp11b2 from Cyp11b1 and demonstrates aldosterone formation from the deoxycorticosterone route. Curated catalytic reaction data support the initial corticosterone-producing hydroxylation. All repeated evidence rows represent the same supported gene-level activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0005506 iron ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: The heme iron cofactor is integral to P450 catalysis. Reason: The curated cytochrome P450 family assignment, heme cofactor and axial iron-binding site support this mechanistic cofactor property. Iron binding describes the heme iron rather than a separate free-iron homeostatic function. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Belongs to the cytochrome P450 family. {ECO:0000305}. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Name=heme; Xref=ChEBI:CHEBI:30413; |
| GO:0005739 mitochondrion | HDA PMID:14651853 Integrated analysis of protein composition, tissue diversity... | ACCEPT | Summary: Cyp11b2 has supported mitochondrion localization, retained separately from its subcompartment annotations. Reason: The original HDA source combines mitochondrial proteomics from four mouse tissues with existing annotations. Its abstract does not expose a Cyp11b2-specific identification, and no target table was inspected here. Independently curated target mitochondrial localization supports retaining the organelle claim; this is not a new claim of direct detection or membrane-topology resolution in that study. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane |
| GO:0005739 mitochondrion | HDA PMID:18614015 A mitochondrial protein compendium elucidates complex I dise... | ACCEPT | Summary: Cyp11b2 has supported mitochondrion localization, retained separately from its subcompartment annotations. Reason: The original HDA source constructs a mitochondrial compendium using mass spectrometry, GFP tagging and computational integration across mouse tissues. No target-specific method or supplementary detection is assigned here. Curated Cyp11b2 mitochondrial localization corroborates the organelle claim without making the compendium an inner-membrane topology assay. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane |
| GO:0005739 mitochondrion | IEA GO_REF:0000002 | ACCEPT | Summary: Cyp11b2 has supported mitochondrion localization, retained separately from its subcompartment annotations. Reason: The InterPro IPR002399 source and independently curated mitochondrial P450 location support the organelle assignment. The target UniProt location is a similarity-based statement, not a direct mouse topology measurement. Mitochondrion is informative even though a separate inner-membrane annotation is retained. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane |
| GO:0005739 mitochondrion | ISO GO_REF:0000119 | ACCEPT | Summary: Cyp11b2 has supported mitochondrion localization, retained separately from its subcompartment annotations. Reason: The original ISO donor UniProtKB:P15538 supports mitochondrial localization, and curated target localization is consistent with the transfer. Retain the organelle claim rather than treating its granularity as a source failure. This follow-up does not independently reconstruct the orthology relationship or claim a direct mouse membrane-topology assay. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P15538 SUPPORTS TRANSFER The donor supports the conserved mitochondrial compartment and the curated target location is compatible. Retaining mitochondrion is a valid organelle-level transfer, not a specificity defect. No independent reconstruction of the donor relationship or target topology experiment is claimed here. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane |
| GO:0005739 mitochondrion | ISO GO_REF:0000119 | ACCEPT | Summary: Cyp11b2 has supported mitochondrion localization, retained separately from its subcompartment annotations. Reason: The original ISO donor UniProtKB:P19099 supports mitochondrial localization, and curated target localization is consistent with the transfer. Retain the organelle claim rather than treating its granularity as a source failure. This follow-up does not independently reconstruct the orthology relationship or claim a direct mouse membrane-topology assay. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P19099 SUPPORTS TRANSFER The donor supports the conserved mitochondrial compartment and the curated target location is compatible. Retaining mitochondrion is a valid organelle-level transfer, not a specificity defect. No independent reconstruction of the donor relationship or target topology experiment is claimed here. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane |
| GO:0005739 mitochondrion | ISO PMID:2738055 Isolation of aldosterone synthase cytochrome P-450 from zona... | ACCEPT | Summary: Cyp11b2 has supported mitochondrion localization, retained separately from its subcompartment annotations. Reason: The cited primary purified an aldosterone-producing P450 from rat zona-glomerulosa mitochondria; it is donor-species evidence, not a mouse localization experiment. The original ISO transfer through RGD:2454 and curated mouse mitochondrial location support the conserved organelle assignment, with inner-membrane detail retained separately. Under the root-organelle policy, retain this supported organelle assertion and its separate subcompartment claims. Propagation Review Root cause: NO FAILURE CORE Sources checked: RGD:2454 SUPPORTS TRANSFER The donor supports the conserved mitochondrial compartment and the curated target location is compatible. Retaining mitochondrion is a valid organelle-level transfer, not a specificity defect. No independent reconstruction of the donor relationship or target topology experiment is claimed here. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane PMID:2738055 The enzyme was present in the mitochondria of the zona glomerulosa |
| GO:0005743 mitochondrial inner membrane | IBA GO_REF:0000033 | ACCEPT | Summary: The inner mitochondrial membrane is the steroidogenic compartment. Reason: Retain the phylogenetic and independently curated mitochondrial membrane assignment. The UniProt statement is homology-based, so it is not represented as a new mouse membrane-fractionation assay. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane |
| GO:0005743 mitochondrial inner membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The inner mitochondrial membrane is the steroidogenic compartment. Reason: Retain the phylogenetic and independently curated mitochondrial membrane assignment. The UniProt statement is homology-based, so it is not represented as a new mouse membrane-fractionation assay. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane |
| GO:0005743 mitochondrial inner membrane | ISS GO_REF:0000024 | ACCEPT | Summary: The inner mitochondrial membrane is the steroidogenic compartment. Reason: Retain the phylogenetic and independently curated mitochondrial membrane assignment. The UniProt statement is homology-based, so it is not represented as a new mouse membrane-fractionation assay. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion inner membrane |
| GO:0006704 glucocorticoid biosynthetic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Corticosterone is a glucocorticoid as well as an intermediate of aldosterone synthesis. Reason: Cyp11b2 generates corticosterone during its multistep reaction. This is genuine glucocorticoid-producing chemistry, although its primary physiological role is aldosterone synthesis and Cyp11b1 supplies the major glucocorticoid branch. No predominant cortisol-producing role is inferred. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt = corticosterone + 2 oxidized [adrenodoxin] + H2O; |
| GO:0006705 mineralocorticoid biosynthetic process | IDA PMID:1686470 Different isozymes of mouse 11 beta-hydroxylase produce mine... | MODIFY | Summary: Specify the experimentally established aldosterone-producing process. Reason: The expression and mouse genetic studies establish aldosterone biosynthesis as the specific process for this broad steroid/mineralocorticoid annotation. The original parent claim remains true. Proposed replacements: aldosterone biosynthetic process Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0006705 mineralocorticoid biosynthetic process | IMP PMID:18039983 Salt-sensitive blood pressure in mice with increased express... | MODIFY | Summary: Specify the experimentally established aldosterone-producing process. Reason: The expression and mouse genetic studies establish aldosterone biosynthesis as the specific process for this broad steroid/mineralocorticoid annotation. The original parent claim remains true. Proposed replacements: aldosterone biosynthetic process Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0008202 steroid metabolic process | IEA GO_REF:0000107 | MODIFY | Summary: Specify the experimentally established aldosterone-producing process. Reason: The expression and mouse genetic studies establish aldosterone biosynthesis as the specific process for this broad steroid/mineralocorticoid annotation. The original parent claim remains true. Proposed replacements: aldosterone biosynthetic process Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0008203 cholesterol metabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the broad cholesterol-derived steroid-pathway context. Reason: The inherited annotation describes a pathway context rather than direct cholesterol substrate recognition. Cyp11b2 performs downstream steroid-hormone chemistry; it does not cleave cholesterol. The same broad-boundary interpretation is retained in the independently curated human review, without recasting the IBA as a pairwise CYP11A1 transfer. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0008395 steroid hydroxylase activity | IDA PMID:1686470 Different isozymes of mouse 11 beta-hydroxylase produce mine... | MODIFY | Summary: Refine broad oxidative activity to the two specific hydroxylation reactions. Reason: Mouse aldosterone synthase executes both steroid 11-beta hydroxylation and corticosterone 18-hydroxylation. Both refinements are retained, rather than choosing one. The third C18 oxidation is represented separately by a proposed molecular function because the 18-hydroxylase term does not name the terminal reaction. Proposed replacements: steroid 11-beta-monooxygenase activity corticosterone 18-monooxygenase activity Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen | IEA GO_REF:0000002 | MODIFY | Summary: Refine broad oxidative activity to the two specific hydroxylation reactions. Reason: Mouse aldosterone synthase executes both steroid 11-beta hydroxylation and corticosterone 18-hydroxylation. Both refinements are retained, rather than choosing one. The third C18 oxidation is represented separately by a proposed molecular function because the 18-hydroxylase term does not name the terminal reaction. Proposed replacements: steroid 11-beta-monooxygenase activity corticosterone 18-monooxygenase activity Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. |
| GO:0020037 heme binding | IEA GO_REF:0000002 | ACCEPT | Summary: The heme iron cofactor is integral to P450 catalysis. Reason: The curated cytochrome P450 family assignment, heme cofactor and axial iron-binding site support this mechanistic cofactor property. Iron binding describes the heme iron rather than a separate free-iron homeostatic function. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Belongs to the cytochrome P450 family. {ECO:0000305}. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Name=heme; Xref=ChEBI:CHEBI:30413; |
| GO:0020037 heme binding | ISO GO_REF:0000119 | ACCEPT | Summary: The heme iron cofactor is integral to P450 catalysis. Reason: The curated cytochrome P450 family assignment, heme cofactor and axial iron-binding site support this mechanistic cofactor property. Iron binding describes the heme iron rather than a separate free-iron homeostatic function. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Belongs to the cytochrome P450 family. {ECO:0000305}. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Name=heme; Xref=ChEBI:CHEBI:30413; |
| GO:0020037 heme binding | ISS GO_REF:0000024 | ACCEPT | Summary: The heme iron cofactor is integral to P450 catalysis. Reason: The curated cytochrome P450 family assignment, heme cofactor and axial iron-binding site support this mechanistic cofactor property. Iron binding describes the heme iron rather than a separate free-iron homeostatic function. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Belongs to the cytochrome P450 family. {ECO:0000305}. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Name=heme; Xref=ChEBI:CHEBI:30413; |
| GO:0030325 adrenal gland development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Loss of Cyp11b2 alters adrenal organization and cell turnover. Reason: Target knockout produces a disorganized cortex, widened glomerulosa and altered turnover. These developmental/maintenance consequences provide independent mouse support beyond electronic transfer, but reflect endocrine feedback rather than a core developmental patterning function. Supporting Evidence: PMID:15731365 The adrenal cortex is disorganized and has cells that contain marked accumulations of lipid. The zona glomerulosa is widened |
| GO:0030425 dendrite | ISO GO_REF:0000096 | UNDECIDED | Summary: The transferred dendritic localization could not be verified. Reason: The source is rat RGD:2454. Mitochondrial localization does not exclude presence within neuronal dendrites, but no source-specific localization experiment was recovered. Neither adrenal expression nor lack of a cited neuronal assay establishes absence. Propagation Review Root cause: UNRESOLVED Sources checked: RGD:2454 UNRESOLVED Literal orthology donor preserved; target-specific dendritic evidence was not recovered. |
| GO:0032342 aldosterone biosynthetic process | IBA GO_REF:0000033 | ACCEPT | Summary: Aldosterone synthesis is the principal catalytic role. Reason: The cloned mouse AS protein synthesizes aldosterone, whereas Cyp11b1 forms corticosterone without completing aldosterone synthesis. Cyp11b2-null mice have undetectable plasma aldosterone. These independent target experiments support all rows, including those whose original comparative publication cannot be fully inspected. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. PMID:15731365 Aldosterone in plasma and AS mRNA in adrenal glands are undetectable in the null mice. |
| GO:0032342 aldosterone biosynthetic process | IDA PMID:1686470 Different isozymes of mouse 11 beta-hydroxylase produce mine... | ACCEPT | Summary: Aldosterone synthesis is the principal catalytic role. Reason: The cloned mouse AS protein synthesizes aldosterone, whereas Cyp11b1 forms corticosterone without completing aldosterone synthesis. Cyp11b2-null mice have undetectable plasma aldosterone. These independent target experiments support all rows, including those whose original comparative publication cannot be fully inspected. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. PMID:15731365 Aldosterone in plasma and AS mRNA in adrenal glands are undetectable in the null mice. |
| GO:0032342 aldosterone biosynthetic process | IDA PMID:8645611 The hamster adrenal cytochrome P450C11 has equipotent 11beta... | ACCEPT | Summary: Aldosterone synthesis is the principal catalytic role. Reason: The cloned mouse AS protein synthesizes aldosterone, whereas Cyp11b1 forms corticosterone without completing aldosterone synthesis. Cyp11b2-null mice have undetectable plasma aldosterone. These independent target experiments support all rows, including those whose original comparative publication cannot be fully inspected. The cited abstract explicitly concerns hamster enzymes; its full text was unavailable, so mouse comparative experiments cannot be excluded. Retention rests on the independent mouse study, not assumed mouse data in that abstract. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. PMID:15731365 Aldosterone in plasma and AS mRNA in adrenal glands are undetectable in the null mice. |
| GO:0032342 aldosterone biosynthetic process | IEA GO_REF:0000117 | ACCEPT | Summary: Aldosterone synthesis is the principal catalytic role. Reason: The cloned mouse AS protein synthesizes aldosterone, whereas Cyp11b1 forms corticosterone without completing aldosterone synthesis. Cyp11b2-null mice have undetectable plasma aldosterone. These independent target experiments support all rows, including those whose original comparative publication cannot be fully inspected. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. PMID:15731365 Aldosterone in plasma and AS mRNA in adrenal glands are undetectable in the null mice. |
| GO:0034650 cortisol metabolic process | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain secondary cortisol substrate chemistry by curated homology. Reason: The reviewed mouse UniProt record assigns cortisol conversion to 18-oxygenated derivatives by similarity to human CYP11B2, whose activity is experimentally established. Retain the broad inherited biochemical capability as non-core; mouse adrenal production of cortisol or its physiological importance is not established by this transfer. Supporting Evidence: file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Reaction=cortisol + 2 reduced [adrenodoxin] + O2 + 2 H(+) = 18- CC hydroxycortisol + 2 oxidized [adrenodoxin] + H2O; PMID:15356073 Both enzymes could synthesize 18-OHF from cortisol, but only AS could synthesize 18-oxoF. |
| GO:0042756 drinking behavior | IMP PMID:16118390 Kidney function in mice lacking aldosterone. | KEEP AS NON CORE | Summary: Altered Cyp11b2 activity changes water intake through endocrine physiology. Reason: Independent target overexpression experiments report altered water intake depending on salt diet. The outcome is downstream of aldosterone and volume homeostasis, not evidence that the enzyme acts as a neuronal behavioral regulator. Supporting Evidence: PMID:18039983 The AS(hi/hi) mice on a high-salt diet also had more water intake and urine volume and less urine osmolality than wild-type mice. |
| GO:0043434 response to peptide hormone | IEA GO_REF:0000107 | MODIFY | Summary: Cyp11b2 participates in the cellular steroidogenic response to peptide-hormone signaling. Reason: Angiotensin II-dependent endocrine regulation and compensatory renin-angiotensin activation after Cyp11b2 loss support the inherited response context. This is a regulated steroidogenic output, not peptide-hormone receptor activity. The broader response-to-peptide-hormone row is refined to its already present cellular counterpart. Proposed replacements: cellular response to peptide hormone stimulus Supporting Evidence: PMID:18039983 AS(hi/hi) mice were more susceptible than wild-type mice to infusion of angiotensin II PMID:15731365 Their plasma renin and angiotensin II concentrations are 45x and 4x wild type. |
| GO:0047783 corticosterone 18-monooxygenase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Corticosterone 18-hydroxylation is the second aldosterone-producing reaction. Reason: This activity converts corticosterone to 18-hydroxycorticosterone. Mouse aldosterone synthase activity is established by expression and loss-of-function experiments; the curated orthology-based reaction assignment identifies the step. The subsequent 18-oxidation is a different activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Reaction=corticosterone + 2 reduced [adrenodoxin] + O2 + 2 H(+) = 18- CC hydroxycorticosterone + 2 oxidized [adrenodoxin] + H2O; |
| GO:0047783 corticosterone 18-monooxygenase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Corticosterone 18-hydroxylation is the second aldosterone-producing reaction. Reason: This activity converts corticosterone to 18-hydroxycorticosterone. Mouse aldosterone synthase activity is established by expression and loss-of-function experiments; the curated orthology-based reaction assignment identifies the step. The subsequent 18-oxidation is a different activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Reaction=corticosterone + 2 reduced [adrenodoxin] + O2 + 2 H(+) = 18- CC hydroxycorticosterone + 2 oxidized [adrenodoxin] + H2O; |
| GO:0047783 corticosterone 18-monooxygenase activity | ISO GO_REF:0000096 | ACCEPT | Summary: Corticosterone 18-hydroxylation is the second aldosterone-producing reaction. Reason: This activity converts corticosterone to 18-hydroxycorticosterone. Mouse aldosterone synthase activity is established by expression and loss-of-function experiments; the curated orthology-based reaction assignment identifies the step. The subsequent 18-oxidation is a different activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Reaction=corticosterone + 2 reduced [adrenodoxin] + O2 + 2 H(+) = 18- CC hydroxycorticosterone + 2 oxidized [adrenodoxin] + H2O; |
| GO:0047783 corticosterone 18-monooxygenase activity | ISO GO_REF:0000096 | ACCEPT | Summary: Corticosterone 18-hydroxylation is the second aldosterone-producing reaction. Reason: This activity converts corticosterone to 18-hydroxycorticosterone. Mouse aldosterone synthase activity is established by expression and loss-of-function experiments; the curated orthology-based reaction assignment identifies the step. The subsequent 18-oxidation is a different activity. Supporting Evidence: PMID:1686470 the product of the AS gene efficiently synthesized aldosterone. file:mouse/Cyp11b2/Cyp11b2-uniprot.txt Reaction=corticosterone + 2 reduced [adrenodoxin] + O2 + 2 H(+) = 18- CC hydroxycorticosterone + 2 oxidized [adrenodoxin] + H2O; |
| GO:0050801 monoatomic ion homeostasis | IMP PMID:16118390 Kidney function in mice lacking aldosterone. | KEEP AS NON CORE | Summary: Cyp11b2-dependent aldosterone maintains systemic electrolyte balance. Reason: Mouse knockout directly disturbs multiple plasma ions, including potassium, calcium and magnesium. This collective physiological endpoint is retained outside the catalytic core; narrowing to potassium alone would omit supported effects. Supporting Evidence: PMID:16118390 the AS-/- mice have low blood pressure, abnormal electrolyte homeostasis |
| GO:0071375 cellular response to peptide hormone stimulus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Cyp11b2 participates in the cellular steroidogenic response to peptide-hormone signaling. Reason: Angiotensin II-dependent endocrine regulation and compensatory renin-angiotensin activation after Cyp11b2 loss support the inherited response context. This is a regulated steroidogenic output, not peptide-hormone receptor activity. The broader response-to-peptide-hormone row is refined to its already present cellular counterpart. Supporting Evidence: PMID:18039983 AS(hi/hi) mice were more susceptible than wild-type mice to infusion of angiotensin II PMID:15731365 Their plasma renin and angiotensin II concentrations are 45x and 4x wild type. |
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