Component
SERCA2
Independent protein record for Sarcoplasmic/endoplasmic reticulum calcium ATPase 2.
2 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What it acts on
Human SERCA2b couples its ATPase cycle to sequestration of cytosolic calcium into the ER.
Experimental context and source evidence
- compartment_description
- ER membrane
- experimental_model
- Purified recombinant human SERCA2b; cryo-EM and ATPase characterization
- limitations
- Evidence specifies ATP2A2 splice isoform SERCA2b; kinetic properties should not be assigned to every SERCA isoform.
- nutrient_topic
- Calcium research collection; topical membership is not evidence of a direct dietary effect. · Calcium
- organism
- Homo sapiens
- plain_language
- SERCA2b uses ATP to refill ER calcium stores.
- primary_references
- [ca-zhang2020] Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail (2020). https://pubmed.ncbi.nlm.nih.gov/32851169/ DOI: 10.1126/sciadv.abb0147
- research_relationship_category
- transport
- tissue_or_cell_type
- Recombinant SERCA2b
- transport_effect
- lowers Recorded as sequestration of cytosolic calcium into the ER.
- transport_or_reaction_direction
- Cytosol to ER lumen
- transport_pool
- cytosolic calcium Recorded as sequestration of cytosolic calcium into the ER.
Calcium: mechanism-first literature curation (2026-09-17) · lines 571–583
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human SERCA2b; cryo-EM and ATPase characterization · source_derived_draft · unverified_draft
### ca-serca2b-er-uptake Human SERCA2b couples its ATPase cycle to sequestration of cytosolic calcium into the ER. Condition category: normal nutrient_topic: Calcium research collection; topical membership is not evidence of a direct dietary effect. plain_language: SERCA2b uses ATP to refill ER calcium stores. organism: Homo sapiens tissue_or_cell_type: Recombinant SERCA2b experimental_model: Purified recombinant human SERCA2b; cryo-EM and ATPase characterization limitations: Evidence specifies ATP2A2 splice isoform SERCA2b; kinetic properties should not be assigned to every SERCA isoform. research_relationship_category: transport transport_or_reaction_direction: Cytosol to ER lumen compartment_description: ER membrane [ca-zhang2020] Cryo-EM structures of SERCA2b reveal the mechanism of regulation by the luminal extension tail (2020). https://pubmed.ncbi.nlm.nih.gov/32851169/ DOI: 10.1126/sciadv.abb0147
Complete structured claim and evidence
What acts on it
ER calcium depletion changes SELENON oligomerization and exposes reductase activity toward SERCA2 in the tested biochemical/cell systems.
Experimental context and source evidence
- experimental_model
- Calcium-binding peptides and human cell experiments, including engineered SELENON variants.
- limitations
- Some assays use engineered Sec-to-Cys protein; these results do not define human nutrient-response thresholds.
- organism
- Human cell systems and recombinant peptides
Selenium: literature corrections and mechanism additions · lines 1064–1073
Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually · supports · Calcium-binding peptides and human cell experiments, including engineered SELENON variants. · secondary_verified · secondary_verified
## selenon-serca-redox-control SELENON links low calcium inside the ER to regulation of its calcium-refilling pump. ER calcium depletion changes SELENON oligomerization and exposes reductase activity toward SERCA2 in the tested biochemical/cell systems. Experimental model: Calcium-binding peptides and human cell experiments, including engineered SELENON variants. Organism: Human cell systems and recombinant peptides Limitations: Some assays use engineered Sec-to-Cys protein; these results do not define human nutrient-response thresholds. Primary 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/)
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.