The review covers all 12 normally fetched annotation identities and preserves their terms, qualifiers, original references, supporting entities and explicit isoform identifiers. Four UniProt products are retained at lengths 900, 872, 454 and 879 aa. The two HuRI interactions explicitly identify Q8NEL9-2; this does not establish equivalent functions for the other products.
The core is glycerophospholipid phospholipase A1 activity in the cytosolic pool, including direct participation in phosphatidylinositol metabolism. DDHD1 performs PI deacylation itself. The existing process term already covers this chemistry; a complete deacylation/re-acylation cycle is not established. No new annotation is proposed. The domain-to-metal-binding inference remains undecided because conserved residues and mutational sensitivity do not demonstrate metal occupancy [PMID:20359546; PMID:22922100].
The original COPII pull-down methods and Figure 7 identify p125/SEC23IP as the tested target, supporting correction of the two source-specific DDHD1 interaction rows PMID:17428803. The actual Results state: “p125 was also found to interact with GST-Sec24C as well as GST-Sec23A” (original, Figure 7B Results). HuRI's ZBTB24 partner has experimentally demonstrated sequence-specific DNA binding and transcriptional regulation, supporting a partner-class refinement; the CR1L interaction remains non-core [PMID:32296183; PMID:30085123].
Human FLAG-PA-PLA1 is cytosolic in the comparator experiment of the p125 localization paper PMID:15623529. Human DDHD1 also affects mitochondrial fragmentation in HeLa cells, with wild-type versus S537A rescue and two siRNAs; this context-dependent output is retained as non-core PMID:24599962. The SPG49/CYP2U1 fibroblast images in PMID:23176821 are not used as DDHD1 morphology experiments.
The source guide records access, construct and inference limits. The normal Falcon deep-research command failed authentication; its fallback failed with HTTP401 insufficient quota. No provider report was produced. These notes and the source guide are manually authored from the documented sources and independent consultation.
Positive generic interactions follow the user's project curation instructions. A supported partner-class refinement is preferred where available, and experimental source mismatches require actual assay evidence.
Main e32937e9a43d197137f795d76417027d318843f0 added the full-text PMID:23176821 cache with the CYP2U1 review. The new cache preserves the same article identity and the DDHD1/CYP2U1 distinctions documented above. It is protected in the publication plan; the initial abstract cache remains archived. Only access and provenance wording changed, with all annotation decisions and source fields preserved.
The biological summary now includes testis-rich expression, brain expression and autosomal recessive SPG28. The human UniProt record reports “Highly expressed in testis.” and “brain, spleen and lung.” [UniProtKB:Q8NEL9, TISSUE SPECIFICITY; PMID:9488669]. The accessible PMID:9488669 abstract concerns the bovine cloning work and does not independently identify the species of every tissue panel. The human expression statement is attributed to the curated human record, corroborated by the discussion of the full SPG28 study. Its Results section on SPG28/DDHD1 identifies segregating homozygous truncating/splice variants in affected families [PMID:23176821, “four truncating mutations in DDHD1”]. The French case’s two variants were not phased; the gene-level recessive disease conclusion does not require treating that individual as a fully resolved phase experiment.
The same curated record states “Forms homooligomers” and “heterooligomers with DDHD2” with experimental attribution to PMID:22922100 [UniProtKB:Q8NEL9, SUBUNIT, ECO:0000269]. The heterooligomeric association is described there as weaker. This evidence belongs in the biological record even though the accessible abstract does not present the oligomerization experiment and the full publisher text was not recovered. The protein products, assay species, oligomer stoichiometry and physiological consequences are not independently resolved here. An expert question now asks whether oligomerization affects catalysis or membrane access. No new GO assertion or additional core activity is inferred from this curated statement alone.
The CR1L binding decision remains KEEP_AS_NON_CORE under the user’s standing project instruction, an explicit departure from the skill’s generic-binding information-exclusion recommendation. The assay is positive and the partner class is unresolved; the gene’s receptor-like partner name does not establish a signal-initiating receptor activity. The ZBTB24 refinement describes a controlled qualitative binding capacity, not a demonstrated native neuronal complex or a transcriptional role for DDHD1.
The two COPII interaction removals still rest on the inspected original Methods and Figure 7B, which name p125/SEC23IP. The cached abstracts and the PTHR23509 membership table provide independent identity context, not a replacement for reading the actual experiments. The cytosolic pool is distinguished from the unresolved mechanism of access to membrane phospholipids. Product descriptions now state sequence facts; historical construct assignment, catalytic equivalence of shortened products and isoform-specific membrane access remain unestablished, as recorded above and in the existing product question. All twelve source assertions/actions and the single phospholipase core are unchanged.