ABHD14A is a metabolic serine hydrolase of the α/β-hydrolase superfamily, closely related at the sequence level to ABHD14B, from which it is distinguished by defined sequence determinants PMID:37974539. A soluble N-terminally truncated form is an active enzyme that preferentially hydrolyzes short-chain esters, and its p-nitrophenyl-acetate hydrolysis is enhanced by CoA, consistent with a ping-pong type acetyltransferase mechanism analogous to ABHD14B [PMID:bio_10.1101_2025.11.28.691245]. Heterologously expressed full-length protein localizes to the Golgi apparatus, while endogenous protein is undetectable across immortalized cell lines and adult mouse tissues despite transcriptomic predictions [PMID:bio_10.1101_2025.11.28.691245]. At the transcriptional level, ABHD14A (Dorz1) is positively regulated by the zinc-finger transcription factor Zic1 in cerebellar granule neuron precursors PMID:14667578. Beyond these findings, the physiological substrates and in vivo role of ABHD14A have not been characterized in the available corpus.
| Year | Confidence | Finding | PMIDs | Journal |
|---|---|---|---|---|
| 2023 | Medium | ABHD14A is a member of the metabolic serine hydrolase superfamily with high sequence similarity to ABHD14B; bioinformatics coupled with biochemical experiments identified key sequence determinants distinguishing ABHD14A from ABHD14B, enabling better classification of each enzyme. ABHD14A still lacked functional annotation at the time of this study. | PMID:37974539 | Proteins |
| 2025 | Medium | ABHD14A is an active serine hydrolase enzyme that preferentially hydrolyzes short-chain esters, as demonstrated by gel-based activity-based protein profiling (ABPP) and p-nitrophenyl-ester hydrolysis assays using a soluble N-terminally truncated variant. ABHD14A exhibits CoA-dependent enhancement of p-nitrophenyl-acetate hydrolysis, indicative of a ping-pong type acetyltransferase mechanism similar to ABHD14B. | PMID:bio_10.1101_2025.11.28.691245 | bioRxiv |
| 2025 | Medium | Upon heterologous expression in HEK293T cells, full-length ABHD14A localizes specifically to the Golgi apparatus, suggesting a specialized role in secretory pathway biology. Endogenous ABHD14A protein is undetectable across a panel of immortalized mammalian cell lines and adult mouse tissues, contradicting transcriptomic database predictions. | PMID:bio_10.1101_2025.11.28.691245 | bioRxiv |
| 2003 | Medium | Dorz1 (ABHD14A) expression in cerebellar granule neuron precursors is positively regulated by the transcription factor Zic1; Dorz1 was identified as one of the most significantly down-regulated genes in Zic1-deficient cerebellum, and Dorz1 expression was up-regulated in cultured cells overexpressing Zic1. | PMID:14667578 | Brain research. Molecular brain research |
| 2018 | Low | Abhd14a mRNA expression is enzymatically upregulated in some tissues of Bphl knockout mice, indicating that ABHD14A expression can be compensatorily induced in the absence of the related serine hydrolase BPHL. | PMID:30121252 | Biochemical pharmacology |