PMID:15337741

Citation	Xin, X, Mains, RE and Eipper, BA (2004) Monooxygenase X, a member of the copper-dependent monooxygenase family localized to the endoplasmic reticulum. J. Biol. Chem. 279:48159-67
Abstract	Based on sequence comparisons, MOX (monooxygenase X), is a member of the copper monooxygenase family that includes dopamine beta-monooxygenase (DBM) and peptidylglycine alpha-hydroxylating monooxygenase (PHM). MOX has all of the residues expected to be critical for copper binding, and its cysteine residues can yield the intramolecular disulfide bond pattern observed in DBM. Although DBM and PHM function within the lumen of the secretory pathway, the published sequence for human MOX lacks a signal sequence, suggesting that it does not enter this compartment. We identified an upstream exon that encodes the signal sequence of human MOX. A retained intron yields minor amounts of transcript encoding MOX without a signal sequence. MOX transcripts are widely expressed, with the highest levels in the salivary gland and ovary and moderate levels in brain, pituitary, and heart. Despite the presence of a signal sequence, exogenous MOX is not secreted, and it localizes throughout the endoplasmic reticulum in both endocrine or nonendocrine cells. Neither appending green fluorescent protein to its C terminus nor deleting the hydrophobic domain near its C terminus facilitates secretion of MOX. MOX is N-glycosylated, is tightly membrane-associated, and forms oligomers that are not disulfide-linked. Based on its sequence and localization, MOX is predicted to hydroxylate a hydrophobic substrate in the endoplasmic reticulum.
Links	PubMed Online version:10.1074/jbc.M407486200
Keywords	Amino Acid Sequence; Animals; Cell Fractionation; Cell Line; Copper/metabolism; Endoplasmic Reticulum/enzymology; Exons; Humans; Introns; Isoenzymes/genetics; Isoenzymes/metabolism; Mice; Mixed Function Oxygenases/genetics; Mixed Function Oxygenases/metabolism; Molecular Sequence Data; Multigene Family; Protein Sorting Signals; Protein Structure, Quaternary; Sequence Alignment; Tissue Distribution
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
MOUSE:MOXD1		GO:0016020: membrane	ECO:0000255:	PMID:9051728	C		Fig. 3A	complete CACAO 5050
MOUSE:MOXD1	part_of	GO:0016020: membrane	ECO:0000255: match to sequence model evidence used in manual assertion		C		Seeded From UniProt	Missing: with/from
HUMAN:MOXD1		GO:0005789: endoplasmic reticulum membrane	ECO:0000314:		C		Fig. 6B	complete CACAO 5051
HUMAN:MOXD1	part_of	GO:0005789: endoplasmic reticulum membrane	ECO:0000314: direct assay evidence used in manual assertion		C		Seeded From UniProt	complete

References

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