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Proteins/UNIPROT:Q7RTP6
Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Seems to act as Rab effector protein and plays a role in vesicle trafficking. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process and implicates RAB8A associated with exocytotic vesicles. Required for cytokinesis. Contributes to stabilization and/or maturation of the intercellular bridge independently of its monooxygenase activity. Promotes recruitment of Rab8 and ERC1 to the intercellular bridge, and together these proteins are proposed to function in timely abscission..
Function from UniProtKB (Q7RTP6), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
6 statements
6 statements · 2 reference databases · Subject: MICAL3 · Sources: Hetionet, UniProt
1 reaction
L-methionyl-[F-actin]+NADPH(4-)+dioxygen+hydronL-methionyl-(R)-S-oxide-[F-actin]+NADP(3-)+water
Catalysed by MICAL2 or MICAL3 or MICAL1
Reaction pageDirection not assertedBalance undeterminable
Rhea RHEA:51308CC BY 4.0Reference data
4 names
Resolves to: MICAL3