{"id":"2a40c298-3386-51c3-9cb9-557da9f9940a","stable_key":"research:selenon-serca-redox-control","predicate":"supports_redox_regulation_of","statement":"ER calcium depletion changes SELENON oligomerization and exposes reductase activity toward SERCA2 in the tested biochemical/cell systems.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"literature_reviewed:direct_experimental","direction":"positive","is_public":true,"mechanism_event_id":"fac6d8cd-24fa-552e-b56a-3543adcea79f","mechanism_event_label":"SELENON links low calcium inside the ER to regulation of its calcium-refilling pump.","subject":{"id":"3213fd02-a502-59ee-904c-4face633926b","slug":"selenon","display_name":"SELENON","entity_type_key":"protein"},"object":{"id":"d3d1a063-5164-5375-b200-917a8d69e0aa","slug":"atp2a2","display_name":"SERCA2","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"fac6d8cd-24fa-552e-b56a-3543adcea79f","stable_key":"research:selenon-serca-redox-control","event_type":"experimentally_scoped_interaction","label":"SELENON links low calcium inside the ER to regulation of its calcium-refilling pump.","description":"ER calcium depletion changes SELENON oligomerization and exposes reductase activity toward SERCA2 in the tested biochemical/cell systems.","status":"active","compartment":{"slug":"endoplasmic-reticulum","display_name":"Endoplasmic reticulum"},"participants":[{"entity":{"id":"3213fd02-a502-59ee-904c-4face633926b","slug":"selenon","display_name":"SELENON","entity_type_key":"protein"},"role":"regulator","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"d3d1a063-5164-5375-b200-917a8d69e0aa","slug":"atp2a2","display_name":"SERCA2","entity_type_key":"protein"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"e359bc15-e675-5d83-b0fe-1d70814e130b","slug":"calcium-ion","display_name":"Calcium ion","entity_type_key":"ion"},"role":"regulatory_input","stoichiometry":null,"state_label":"low ER luminal calcium","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Calcium-binding peptides and human cell experiments, including engineered SELENON variants.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Some assays use engineered Sec-to-Cys protein; these results do not define human nutrient-response thresholds.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Human cell systems and recombinant peptides","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"ca9f6a4d-4d77-5322-8f8f-b9e8277f8f50","evidence_kind":"curated_literature_summary","locator":"lines 1064-1073","start_line":1064,"end_line":1073,"excerpt":"## selenon-serca-redox-control\n\nSELENON links low calcium inside the ER to regulation of its calcium-refilling pump.\n\nER calcium depletion changes SELENON oligomerization and exposes reductase activity toward SERCA2 in the tested biochemical/cell systems.\n\nExperimental model: Calcium-binding peptides and human cell experiments, including engineered SELENON variants.\nOrganism: Human cell systems and recombinant peptides\nLimitations: Some assays use engineered Sec-to-Cys protein; these results do not define human nutrient-response thresholds.\nPrimary reference: [Selenoprotein N is an endoplasmic reticulum calcium sensor that links luminal calcium levels to a redox activity](https://pmc.ncbi.nlm.nih.gov/articles/PMC7474598/)","model_system":"Calcium-binding peptides and human cell experiments, including engineered SELENON variants.","directness":"author_interpretation","verification_status":"secondary_verified","notes":"Curated summary; inspect the linked primary papers for original methods and results.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"4f892f13-06ea-5199-a33c-a703f35c80ae","stable_key":"selenium-research-2026-09-17","title":"Selenium: literature corrections and mechanism additions","document_type":"curated_literature_review","citation_label":"Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually","file_path":"","sha256":"0b818b10c1c7120e5caf7f4d4019d7bd025d745692e424f515d3ef903c9ab7f3","revision_id":"80984e03-5f0f-5877-8094-afef7637444e","review_status":"secondary_verified","notes":"Secondary curated summaries of primary experiments, with explicit models and limitations. Not archived primary full text."}}],"relations":[],"conflicts":[],"corrections":[],"research":{"topic":"Calcium handling","plain_language":"SELENON links low calcium inside the ER to regulation of its calcium-refilling pump.","evidence_scope":"direct_experimental","papers":[{"key":"catalog-selenon-2020","title":"Selenoprotein N is an endoplasmic reticulum calcium sensor that links luminal calcium levels to a redox activity","url":"https://pmc.ncbi.nlm.nih.gov/articles/PMC7474598/","doi":"10.1073/pnas.2003847117","year":2020,"model":"Calcium-binding peptides and human cell experiments, including engineered SELENON variants.","summary":"Links ER calcium depletion, SELENON conformational state, and reductase activity toward SERCA2."}]}}