Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods
Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2.
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Sulfatase activities are regulated by SUMF1-SUMF2 interaction; SUMF2 inhibits SUMF1-mediated sulfatase activation.
"Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2"
Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals.
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SUMF2 (paralog of FGE) is retained in the ER by canonical and non-canonical signals.
"Paralog of the formylglycine-generating enzyme--retention in the endoplasmic reticulum by canonical and noncanonical signals"
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Cysteine to formylglycine conversion (sulfatase maturation)
Glycosphingolipid metabolism / catabolism
Sulfatase activation by SUMF1 (FGE)
UniProt entry Q8NBJ7 (SUMF2)
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SUMF2 lacks formylglycine-generating activity and inhibits sulfatase activation by SUMF1.
"Inhibits the activation of sulfatases by SUMF1"
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SUMF2 forms a homodimer and a heterodimer with SUMF1.
"Homodimer and heterodimer with SUMF1"
Falcon deep research report for SUMF2
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SUMF2/pFGE binds sulfatase peptides but lacks formylglycine-generating catalytic activity; it acts as a negative regulator/antagonist of SUMF1-mediated sulfatase activation.
"Despite its structural similarity to SUMF1/FGE, SUMF2/pFGE completely lacks formylglycine-generating activity"
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Crystal structure shows a homodimer and structural similarity supporting possible FGE-pFGE heterodimers as the mechanism of antagonism.
"The asymmetric unit of the pFGE crystal contains a homodimer"