CELE_F58H1.1, F58H1.1

aman-2 encodes an alpha-mannosidase II, homologous to human MAN2A1 (OMIM:154582) and MAN2A2, that is required for normal N-glycan structures and predicted to act in the Golgi; AMAN-2 is predicted to mature glycoproteins by removing mannose residues from their N-linked oligosaccharides; translational fusions of AMAN-2 with GFP are subcellularly localized in a pattern consistent with Golgi function; aman-2 is broadly expressed in larvae; in adults, aman-2 is most strongly expressed in the digestive system (gut wall, pharynx and grinder), hypodermal cells, and neurons; aman-2 mutants have N-glycans not seen in normal worms, such as Hex5-7HexNAc2-3Fuc2Me, along with hybrid oligosaccharides, while having reduced paucimannosidic and trifucosylated glycans, and completely lacking tetrafucosylated ones; AMAN-2 contains three predicted N-glycosylation sites, one of which (Asn-320) is known to be occupied in vivo; Cu(II) was observed to completely inhibit AMAN-2, which it also does with mouse and Drosophila alpha-mannosidase II; the pH optimum of AMAN-2 is pH 5.5-6.0; several other ionic conditions (e.g., Co[II] or EDTA) have little effect on AMAN-2; aman-2(tm1078) mutants are superficially wild-type, but mutant extracts completely lack alpha-mannosidase II activity; aman-2(tm1078) mutants have reduced, but not absent, anti-horseradish peroxidase and phosphorylcholine epitopes.

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