Amontillado is the Drosophila PC2-like serine endopeptidase that matures neuropeptide and peptide-hormone precursors in the secretory pathway. Productive maturation and secretion require the helper protein 7B2 and an insect-cell processing context. Its substrates include the adipokinetic hormone precursor, linking peptide processing to sugar homeostasis, developmental transitions and behavior.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002165 instar larval or pupal development | IMP PMID:19559693 The proprotein convertase amontillado (amon) is required dur... | KEEP AS NON CORE | Summary: Pupal and larval developmental progression depends on amon. Reason: Conditional rescue establishes stage-specific requirements for developmental transitions mediated by peptide processing. Supporting Evidence: PMID:19559693 amon is required during pupal development for head eversion, leg and wing disc extension, and abdominal differentiation. |
| GO:0004252 serine-type endopeptidase activity | EXP PMID:10749852 Interaction of Drosophila melanogaster prohormone convertase... | ACCEPT | Summary: Amontillado is a catalytically active prohormone-processing serine endopeptidase. Reason: Activity appears when fly PC2 matures and is secreted from S2 cells with 7B2. The active-site-mutant rescue and mature-hormone loss experiments independently connect serine proteolysis to biological function. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. |
| GO:0004252 serine-type endopeptidase activity | IBA GO_REF:0000033 | ACCEPT | Summary: Amontillado is a catalytically active prohormone-processing serine endopeptidase. Reason: Activity appears when fly PC2 matures and is secreted from S2 cells with 7B2. The active-site-mutant rescue and mature-hormone loss experiments independently connect serine proteolysis to biological function. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. |
| GO:0004252 serine-type endopeptidase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Amontillado is a catalytically active prohormone-processing serine endopeptidase. Reason: Activity appears when fly PC2 matures and is secreted from S2 cells with 7B2. The active-site-mutant rescue and mature-hormone loss experiments independently connect serine proteolysis to biological function. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. |
| GO:0005576 extracellular region | IBA GO_REF:0000033 | ACCEPT | Summary: The processed enzyme can be secreted. Reason: The primary S2-cell experiment directly detects active dPC2 in conditioned medium. The lack of secretion in heterologous HEK cells reflects maturation requirements and does not contradict secretion from insect cells. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. |
| GO:0005576 extracellular region | IDA PMID:10749852 Interaction of Drosophila melanogaster prohormone convertase... | ACCEPT | Summary: The processed enzyme can be secreted. Reason: The primary S2-cell experiment directly detects active dPC2 in conditioned medium. The lack of secretion in heterologous HEK cells reflects maturation requirements and does not contradict secretion from insect cells. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | ACCEPT | Summary: The processed enzyme can be secreted. Reason: The primary S2-cell experiment directly detects active dPC2 in conditioned medium. The lack of secretion in heterologous HEK cells reflects maturation requirements and does not contradict secretion from insect cells. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. |
| GO:0006508 proteolysis | IDA PMID:10749852 Interaction of Drosophila melanogaster prohormone convertase... | ACCEPT | Summary: Proteolysis is directly demonstrated in peptide-precursor processing. Reason: Amontillado supplies prohormone-convertase activity, and loss of mature AKH in mutants links proteolysis to its in-vivo substrate processing. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. |
| GO:0006508 proteolysis | IEA GO_REF:0000002 | ACCEPT | Summary: Proteolysis is directly demonstrated in peptide-precursor processing. Reason: Amontillado supplies prohormone-convertase activity, and loss of mature AKH in mutants links proteolysis to its in-vivo substrate processing. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. |
| GO:0008233 peptidase activity | IDA PMID:10749852 Interaction of Drosophila melanogaster prohormone convertase... | MODIFY | Summary: Serine endopeptidase activity specifies generic peptidase activity. Reason: The characterized PC2-like enzyme performs endoproteolytic precursor processing and is not merely an unspecified peptide-binding protein. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. |
| GO:0008236 serine-type peptidase activity | IEA GO_REF:0000002 | MODIFY | Summary: The relevant serine peptidase reaction is endoproteolysis. Reason: PC2 cleavage of prohormones establishes the endopeptidase subclass. Proposed replacements: serine-type endopeptidase activity Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. |
| GO:0016020 membrane | IBA GO_REF:0000033 | UNDECIDED | Summary: Membrane association is not established by secretion or a signal peptide. Reason: The exact protein has a cleavable N-terminal signal peptide and a soluble secretory convertase architecture. The direct experiment establishes secretion; it does not distinguish transient membrane association or provide an anchor. The inherited membrane assertion therefore needs target-specific support. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. |
| GO:0016486 peptide hormone processing | IBA GO_REF:0000033 | ACCEPT | Summary: Peptide hormone processing is the central biological function. Reason: Mass spectrometry detects loss of mature AKH and other neuropeptide signals in amon mutants. These are direct fly data rather than a transfer from mammalian PC2. Supporting Evidence: PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. PMID:21138435 A loss of amon correlates with a loss of neuropeptide hormone signals from the larval ring gland and perisympathetic organs. |
| GO:0016486 peptide hormone processing | IEA GO_REF:0000117 | ACCEPT | Summary: Peptide hormone processing is the central biological function. Reason: Mass spectrometry detects loss of mature AKH and other neuropeptide signals in amon mutants. These are direct fly data rather than a transfer from mammalian PC2. Supporting Evidence: PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. PMID:21138435 A loss of amon correlates with a loss of neuropeptide hormone signals from the larval ring gland and perisympathetic organs. |
| GO:0016486 peptide hormone processing | IMP PMID:20523747 The proprotein convertase encoded by amontillado (amon) is r... | ACCEPT | Summary: Peptide hormone processing is the central biological function. Reason: Mass spectrometry detects loss of mature AKH and other neuropeptide signals in amon mutants. These are direct fly data rather than a transfer from mammalian PC2. Supporting Evidence: PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. PMID:21138435 A loss of amon correlates with a loss of neuropeptide hormone signals from the larval ring gland and perisympathetic organs. |
| GO:0016486 peptide hormone processing | IMP PMID:21138435 Deficiency of prohormone convertase dPC2 (AMONTILLADO) resul... | ACCEPT | Summary: Peptide hormone processing is the central biological function. Reason: Mass spectrometry detects loss of mature AKH and other neuropeptide signals in amon mutants. These are direct fly data rather than a transfer from mammalian PC2. Supporting Evidence: PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. PMID:21138435 A loss of amon correlates with a loss of neuropeptide hormone signals from the larval ring gland and perisympathetic organs. |
| GO:0016486 peptide hormone processing | IMP PMID:21214272 Peptidomics and peptide hormone processing in the Drosophila... | ACCEPT | Summary: Peptide hormone processing is the central biological function. Reason: Mass spectrometry detects loss of mature AKH and other neuropeptide signals in amon mutants. These are direct fly data rather than a transfer from mammalian PC2. Supporting Evidence: PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. PMID:21138435 A loss of amon correlates with a loss of neuropeptide hormone signals from the larval ring gland and perisympathetic organs. |
| GO:0017171 serine hydrolase activity | HDA PMID:33827210 A Superfamily-wide Activity Atlas of Serine Hydrolases in &l... | KEEP AS NON CORE | Summary: Serine hydrolase is a supported broad catalytic class. Reason: The independent direct PC2 activity experiment supports the broad HDA class, but the specific endopeptidase term carries the physiological mechanism. Supporting Evidence: PMID:10749852 when dPC2 and either d7B2 or r7B2 were coexpressed in Drosophila S2 cells, abundant immunoreactive dPC2 was secreted into the medium, coincident with the appearance of PC2 activity. |
| GO:0030537 larval behavior | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Larval behavior depends on processed peptide hormones. Reason: The experimentally defined wandering defect supports this broad larval-behavior parent; it is secondary to neuropeptide maturation. Supporting Evidence: PMID:21138435 The lack of AMON activity resulted in a deficiency of L3 larva to enter the wandering phase. |
| GO:0033500 carbohydrate homeostasis | IMP PMID:20523747 The proprotein convertase encoded by amontillado (amon) is r... | KEEP AS NON CORE | Summary: Sugar homeostasis depends on AKH precursor processing. Reason: Cell-specific inactivation and rescue link amon to endocrine AKH production and circulating sugar concentrations. Supporting Evidence: PMID:20523747 mass spectrometric profiling shows that the production of mature AKH is inhibited in amon mutants. |
| GO:0035180 larval wandering behavior | IMP PMID:21138435 Deficiency of prohormone convertase dPC2 (AMONTILLADO) resul... | KEEP AS NON CORE | Summary: Larval wandering requires amon-dependent neuropeptide production. Reason: The direct peptide-profiling study reports failure of deficient L3 larvae to enter the wandering stage. Supporting Evidence: PMID:21138435 The lack of AMON activity resulted in a deficiency of L3 larva to enter the wandering phase. |
| GO:0035187 hatching behavior | IMP PMID:10436051 A role for amontillado, the Drosophila homolog of the neurop... | KEEP AS NON CORE | Summary: Hatching behavior requires active amontillado. Reason: Restoration by wild-type enzyme, but not a catalytic-histidine mutant, links the behavior to proteolytic processing. Supporting Evidence: PMID:10436051 Ubiquitous expression of amontillado can restore near wild-type levels of this behavior, whereas expression of amontillado with an alanine substitution for the catalytic histidine cannot. |
| GO:0043005 neuron projection | IBA GO_REF:0000033 | ACCEPT | Summary: The protein acts in neurosecretory projections. Reason: Target-specific immunolocalization places amon in neurons innervating the ring gland, and neurohemal peptide-processing defects fit this cellular location. Supporting Evidence: PMID:19559693 The amon protein is expressed in neuronal cells that innervate the corpus allatum and corpora cardiaca of the ring gland PMID:21138435 A loss of amon correlates with a loss of neuropeptide hormone signals from the larval ring gland and perisympathetic organs. |
| GO:0045464 R8 cell fate specification | IMP PMID:28853393 Parallel Activin and BMP signaling coordinates R7/R8 photore... | KEEP AS NON CORE | Summary: R8 subtype specification is a context-specific consequence of peptide processing. Reason: The retinal study places the processing factor upstream of TGF-beta pathway components in pale R7, influencing R8 identity through intercellular signaling. Supporting Evidence: PMID:28853393 The Amon TGFΞ² processing factor appears to regulate components of the TGFΞ² pathway specifically in pale R7. |
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