Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniPathway vocabulary mapping.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Molecular cloning and functional analysis of zebrafish neutral ceramidase.
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The zebrafish cDNA confers neutral-pH ceramidase activity on transfected cells.
"The enzyme activity at neutral pH increased markedly after transformation of Chinese hamster CHOP and zebrafish BRF41 cells with the cDNA"
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Overexpressed zebrafish enzyme localizes to ER/Golgi and plasma membrane.
"The overexpressed enzyme was found to be distributed in endoplasmic reticulum/Golgi compartments as well as the plasma membranes"
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Knockdown raises embryonic ceramide levels.
"The ceramide level in AMO-injected embryos increased significantly compared with that in control embryos"
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Co-injected mRNA rescues enzyme activity and circulation, showing specificity of the knockdown.
"Simultaneous injection of both AMO and synthetic znCD mRNA into one-cell-stage embryos rescued znCD activity and blood cell circulation"
Structural Basis for Ceramide Recognition and Hydrolysis by Human Neutral Ceramidase.
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Human neutral ceramidase is a Zn2+-dependent amidase converting ceramide to sphingosine.
"Neutral ceramidase (nCDase) catalyzes conversion of the apoptosis-associated lipid ceramide to sphingosine, the precursor for the proliferative factor sphingosine-1-phosphate"
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The catalytic mechanism is a Zn2+-dependent amidase strategy.
"Our results suggest that nCDase uses a new catalytic strategy for Zn(2+)-dependent amidases"
UniProtKB entry Q5W7F1 for Danio rerio asah2
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Asah2 is a plasma membrane neutral ceramidase.
"Plasma membrane ceramidase that hydrolyzes sphingolipid ceramides into sphingosine and free fatty acids at neutral pH (PubMed:15271994)"
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The physiological direction is hydrolysis; the condensation reaction is by similarity only.
"PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20857"
Falcon (Edison) deep research report on Danio rerio asah2 (Q5W7F1) neutral ceramidase
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Golgi and mitochondrial localizations have been reported only in specific contexts, including
overexpression studies that can confound steady-state localization.
"reports of **mitochondrial** localization in overexpression studies (noting that overexpression can confound steady-state localization)"