SERCA (Ca-P60A, CG3725; UniProt P22700) - manual literature synthesis

No deep-research API was available for this session. This file is a manual synthesis written by
the reviewer from the cached publications in publications/ and the UniProt record
(SERCA-uniprot.txt). Every assertion carries provenance.

Identity and family

• Drosophila SERCA (FlyBase FBgn0263006, GeneID 49297; synonyms Ca-P60A, CaP60A, CG3725) is the
  single sarco/endoplasmic reticulum Ca2+-ATPase of the fly. Cloned by Magyar and Varadi:
  PMID:2148477
• It is the only SERCA expressed in flies: PMID:23434461.
• UniProt: [UniProt P22700 "Belongs to the cation transport ATPase (P-type) (TC 3.A.3)"];
  NCBIfam TIGR01116 (ATPase-IIA1_Ca, the SERCA-type P2A calcium ATPase family); 10 TM helices
  (UniProt TRANSMEM features), catalytic phospho-Asp at residue 351 (FT ACT_SITE 351), Ca2+ site
  residues in TM4-TM8 (FT BINDING).
• Reaction: [UniProt P22700 "Reaction=Ca(2+)(in) + ATP + H2O = Ca(2+)(out) + ADP + phosphate + H(+);"] (EC 7.2.2.10).

Molecular function: P-type Ca2+ pump into the ER/SR

• PMID:15520268
• PMID:24807223
• Activity assays in flies: Ca2+-dependent, thapsigargin-sensitive ATP hydrolysis
  PMID:28399403;
  reduced SERCA activity in DJ-1beta PD-model flies PMID:33892078.
• Thapsigargin binding site conserved PMID:22952921.

Regulators / partners

• Sarcolamban peptides SclA/SclB (smORF peptides; phospholamban/sarcolipin-like) regulate cardiac
  Ca2+ uptake PMID:23970561;
  UniProt [UniProt P22700 "Interacts with SclA and SclB."].
• Seipin binds and promotes SERCA activity in fat body PMID:24807223.
• THADA binds SERCA and acts as an uncoupler PMID:28399403.

Localization

• ER membrane and SR membrane [UniProt P22700 "Endoplasmic reticulum membrane"; "Sarcoplasmic reticulum membrane"], colocalizing with SclA/SclB at diads (PMID:23970561 via UniProt).
• Used as an ER marker in fat body and salivary gland PMID:28399403.
• LOPIT organelle proteomics of embryos (PMID:19317464).

Physiological roles (downstream of ER/SR Ca2+ uptake)

• Neuromuscular: conditional (kum) paralytic alleles PMID:15520268; muscle relaxation PMID:15520268.
• Photoreceptor synaptic exocytosis in the lamina depends partly on ER Ca2+ stores filled by SERCA PMID:22952921.
• Heart: PMID:24098595; RyR mutation rescues kum170 cardiac phenotype PMID:24098595.
• Flight circuit: InsP3R deficits compensated by reduced SERCA PMID:16899722.
• Lipid storage in fat body PMID:24807223.
• Thermogenesis: in mammals uncoupled SERCA ATP hydrolysis generates heat; fly evidence is via THADA
  mutants PMID:28399403.
• Notch signalling: SERCA loss impairs Notch receptor maturation/trafficking, affecting midgut stem
  cell differentiation and follicle cell programmes PMID:23434461;
  PMID:26205122.