Reference protein: Q8IYP9. This is a manual literature synthesis using fetched primary-publication text and the reviewed human UniProt record.
The strongest direct functional source is the substrate-focused BK-channel study. It identifies zDHHC22 and zDHHC23 among the mammalian DHHC enzymes as controllers of palmitoylation of the intracellular BK S0–S1 loop. Efficient surface expression depends on this lipidation. This supports protein-cysteine S-palmitoyltransferase activity and protein localization to the plasma membrane; the transport channel is the substrate, so the enzyme should not itself be described as a potassium channel. PMID:22399288(https://pubmed.ncbi.nlm.nih.gov/22399288/)
The human reviewed record describes Golgi and trans-Golgi-network membrane localization and a multipass membrane architecture. The conserved DHHC catalytic cysteine provides a mechanism-specific sequence anchor. The ER IBA need not be discarded because Golgi localization is also observed: the two membrane pools are not inherently incompatible. Exact subcellular residence should be distinguished from the destination of the lipidated cargo. PMID:22399288(https://pubmed.ncbi.nlm.nih.gov/22399288/)
The BK-channel experiments support the measured substrate relationship. They do not establish unrestricted palmitoylation of every protein, direct NOS1 regulation, or disease-level mechanisms. High-throughput protein-binding annotations are retained as non-core interactions rather than used to define catalysis. PMID:22399288(https://pubmed.ncbi.nlm.nih.gov/22399288/)
The source caches distinguish full text from abstract-only access; unresolved experimental annotations should remain UNDECIDED until their supporting material is available. This synthesis focuses on the biochemical mechanism, localization, and evidence needed for the paired horse prediction assessment; it does not certify every existing GO annotation.