Generated by resolve_iba_sources.py. Accessions are read from this gene's own
ABHD8-goa.tsv; all protein data is fetched from the UniProt REST API at run time.
The rows do not share a source set, which matters: a propagation_review copied from
one row to another will misstate what was inspected.
| GO term | WITH/FROM sources |
|---|---|
| GO:0004620 | AGI_LocusCode:AT4G24160, FB:FBgn0033226, MGI:MGI:1915938, PANTHER:PTN008676419, SGD:S000003342 |
| GO:0006654 | PANTHER:PTN008676419, SGD:S000004089, UniProtKB:Q8WTS1 |
| GO:0042171 | AGI_LocusCode:AT4G24160, PANTHER:PTN008676419, SGD:S000004089, UniProtKB:Q8WTS1 |
| GO:0052689 | AGI_LocusCode:AT4G24160, FB:FBgn0033226, MGI:MGI:1915938, PANTHER:PTN008676419, SGD:S000003342 |
| GO:0055088 | AGI_LocusCode:AT4G24160, PANTHER:PTN008676419 |
For each source: what protein it is, and what evidence it carries for the terms
propagated to ABHD8. IBA WITH/FROM is supposed to list experimentally-annotated
members, so 'this source only carries the same family-level inference' is a testable
claim rather than a safe hedge - and the table below is what settles it.
| WITH/FROM | protein | UniProt status | organism | own evidence for the propagated terms |
|---|---|---|---|---|
AGI_LocusCode:AT4G24160 |
O22975 (LPAAT_ARATH) — 1-acylglycerol-3-phosphate O-acyltransferase | Swiss-Prot (reviewed) | Arabidopsis thaliana | 0004620=IBA/IDA; 0006654=IBA; 0042171=IBA/IDA/IEA; 0052689=IBA/IDA; 0055088=IBA/IMP |
FB:FBgn0033226 |
Q5U191 (puml) — 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 | TrEMBL (UNREVIEWED); 4 entries for this id - including A1Z753 "Pummelig, isoform A" | Drosophila melanogaster | 0004620=IBA/IMP; 0006654=IBA; 0042171=IBA/IEA; 0052689=IBA/IDA; 0055088=IBA |
MGI:MGI:1915938 |
Q8VD66 (Abhd4) — (Lyso)-N-acylphosphatidylethanolamine lipase | Swiss-Prot (reviewed) | Mus musculus | 0004620=IBA/IDA; 0006654=IBA; 0042171=IBA; 0052689=IBA/IDA; 0055088=IBA |
PANTHER:PTN008676419 |
PANTHER family/subfamily node - an internal tree node, not a protein | — | — | not applicable |
SGD:S000003342 |
P53264 (CLD1) — Cardiolipin-specific deacylase 1, mitochondrial | Swiss-Prot (reviewed) | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 0004620=IBA/IDA/IMP; 0006654=IBA; 0042171=IBA; 0052689=IBA/IDA/IMP; 0055088=IBA |
SGD:S000004089 |
Q12385 (ICT1) — 1-acylglycerol-3-phosphate O-acyltransferase ICT1 | Swiss-Prot (reviewed) | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | 0004620=IBA; 0006654=IBA/IMP; 0042171=IBA/IDA/IEA; 0052689=IBA; 0055088=IBA |
UniProtKB:Q8WTS1 |
Q8WTS1 (ABHD5) — 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 | Swiss-Prot (reviewed) | Homo sapiens | 0004620=IBA; 0006654=IBA/IDA; 0042171=IBA/IDA/IEA; 0052689=IBA/ISS; 0055088=IBA |
Term ids are abbreviated to their digits; each entry lists the evidence codes that
source carries for that term or any of its descendants.
6 of the 7 sources carry experimental evidence of
their own for at least one propagated term: AGI_LocusCode:AT4G24160, FB:FBgn0033226, MGI:MGI:1915938, SGD:S000003342, SGD:S000004089, UniProtKB:Q8WTS1.
But 1 of the 6 protein sources (FB:FBgn0033226) has no reviewed UniProt entry. Its GO
annotations are real curated annotations, but its protein NAME in the column above is
an automatic by-similarity label, not a characterisation - so it must not be counted
alongside the Swiss-Prot recommended names as independent evidence of what the family
does. Evidence provenance and name provenance are separate questions, and only the
former is settled here for all 6 sources; the latter for 5.
SGD:S000004089 resolves to ICT1_YEAST (Q12385, gene ICT1), whose UniProt recommended name is "1-acylglycerol-3-phosphate O-acyltransferase ICT1".
The acyltransferase activity therefore sits in a named, reviewed member of this family
in another organism, so the two acyltransferase-branch IBAs are propagating from a real
annotated activity. They are marked over-annotated rather than removed because what is
absent is a demonstration in ABHD8, not an activity in the family.
Q8WTS1 — ABHD5_HUMAN, Homo sapiens: 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- annotated active-site residues: 0
- FUNCTION: Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfer of an acyl group on a lysophosphatidic acid (PubMed:18606822). Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-ara
Q96I13 — ABHD8_HUMAN, Homo sapiens: Protein ABHD8
- annotated active-site residues: 3
- FUNCTION: Negatively regulates NLRP3-driven inflammation (PubMed:39225180). Promotes NLRP3 degradation through the chaperone-mediated autophagy (CMA) pathway, hence attenuating inflammasome activation and IL1B secretion. Acts by recruiting palmitoyltransferase ZDHHC12 to NLRP3, facilitating NLRP3 palmitoylati
Read those two blocks together, because they cut in opposite directions and both
matter to this review.
ABHD5 is not the pseudoenzyme it is usually invoked as. It is routinely cited as the
family's fold-without-catalysis case - its nucleophilic serine is replaced, which is why
no active site is annotated - yet UniProt records a demonstrated CoA-dependent
lysophosphatidic acid acyltransferase activity for it, with substrate preferences and a
primary reference. So Q8WTS1, the source of ABHD8's GO:0006654 and GO:0042171 IBAs,
carries a measured acyl-transfer activity and not merely a fold.
The analogy cannot be run the other way either. The active-site counts show ABHD8 has
a full annotated charge-relay triad where ABHD5 has none, so ABHD8 cannot be dismissed as
an ABHD5-type catalytically dead fold. Both the case for the lipid IBAs and the case
against them are weaker than the ABHD5 comparison is usually made to carry. The
defensible position is the narrow one: ABHD8's triad is intact and untested.