Gene Ontology annotation through association of InterPro records with GO terms
Mutations in PNKD causing paroxysmal dyskinesia alters protein cleavage and stability.
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Human PNKD-L has weak measurable S-D-lactoylglutathione hydrolysis in vitro, rather than the robust HAGH activity; no complete absence of hydrolysis is claimed.
"PNKD-L has extremely low but consistent SLG hydrolysis activity"
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Human PNKD-L does not restore lactoylglutathione metabolism in HAGH-null flies, arguing against physiological equivalence to glyoxalase II.
"introduction of a human PNKD-L transgene into the same null background shows no rescue of SLG metabolism"
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Tagged and untagged human PNKD-L in neuronal-derived cells support membrane association; this finding does not resolve localization of the altered rat B4F7D2 product.
"the results suggest that PNKD-L is a membrane-associated protein."
Reproducible comparison of two rat Pnkd products
Frozen exact-input ProtNLM output and UniProt sequence for B4F7D2
Protein mutated in paroxysmal dyskinesia interacts with the active zone protein RIM and suppresses synaptic vesicle exocytosis.
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Defined neuronal PNKD constructs and mouse knockout experiments support a synaptic-release regulatory role; this does not demonstrate that the alternative B4F7D2 rat product has the same activity.
"PNKD interacts with synaptic active zone proteins Rab3-interacting molecule (RIM)1 and RIM2, localizes to synapses, and modulates neurotransmitter release."