K9IJK6

Summary: Mark full-length tPA smooth-muscle migration transfer as over-annotation.

Reason: The focused OpenScientist report retains the secreted serine-protease/plasminogen-activation core but finds no positive evidence that compact salivary DSPA-gamma executes the downstream cellular smooth-muscle roles inherited from full-length mammalian tPA. K9IJK6 lacks the finger and EGF domains that mediate several noncatalytic tPA receptor/cofactor interactions, so this process should not be treated as a core target function.

Summary: The tPA-like secreted serine protease retains the inferred plasminogen-activating catalytic function.

Reason: Plasminogen activation is the specific proteolytic function inferred for this salivary plasminogen-activator homolog; it names conversion of the zymogen rather than a generic vascular phenotype. The previous UNDECIDED treated the PRU00121 warning as loss of catalytic residues. The actual rule concerns kringle-domain disulfide features, not the protease catalytic triad. UniProt identifies trypsin His/Ser signatures and a Peptidase S1 region; PMID:23411029 describes the corresponding salivary DSPA-gamma architecture. The TreeGrafter source PTN000667065 descends from the plasminogen-activation IBD PTN002799995 and broad protease IBD PTN001208002. PMID:7592732 reports substantial amidolytic activity and fibrin-stimulated plasminogen activation for DSPA-gamma directly, so retain the conserved catalytic inference without importing DSPA-alpha1-specific activity measurements.

Summary: Mark full-length tPA PDGFR-signaling transfer as over-annotation.

Reason: The focused OpenScientist report retains the secreted serine-protease/plasminogen-activation core but finds no positive evidence that compact salivary DSPA-gamma executes inherited platelet-derived growth factor receptor signaling biology. K9IJK6 lacks full-length tPA exosites and acts in saliva rather than the mammalian vessel-wall contexts that underlie this downstream signaling term.

Summary: The tPA-like secreted serine protease retains the inferred plasminogen-activating catalytic function.

Reason: Serine-type endopeptidase activity describes internal peptide-bond cleavage by the trypsin-family catalytic machinery, which is the proposed plasminogen-activating reaction. The previous UNDECIDED treated the PRU00121 warning as loss of catalytic residues. The actual rule concerns kringle-domain disulfide features, not the protease catalytic triad. UniProt identifies trypsin His/Ser signatures and a Peptidase S1 region; PMID:23411029 describes the corresponding salivary DSPA-gamma architecture. The TreeGrafter source PTN000667065 descends from the plasminogen-activation IBD PTN002799995 and broad protease IBD PTN001208002. PMID:7592732 reports substantial amidolytic activity and fibrin-stimulated plasminogen activation for DSPA-gamma directly, so retain the conserved catalytic inference without importing DSPA-alpha1-specific activity measurements.

Summary: The N-terminal secretion signal and salivary-protein context support extracellular localization.

Reason: UniProt predicts an N-terminal signal peptide at residues 1-21. The primary transcriptome/proteome study identifies abundant salivary plasminogen activators. Extracellular region and extracellular space are compatible core locations; neither is weakened by a kringle disulfide propagation warning.

Summary: The N-terminal secretion signal and salivary-protein context support extracellular localization.

Reason: UniProt predicts an N-terminal signal peptide at residues 1-21. The primary transcriptome/proteome study identifies abundant salivary plasminogen activators. Extracellular region and extracellular space are compatible core locations; neither is weakened by a kringle disulfide propagation warning.

Summary: The tPA-like secreted serine protease retains the inferred plasminogen-activating catalytic function.

Reason: Proteolysis is direct peptide-bond cleavage performed by the enzyme during plasminogen activation, so it is part of its core work. The previous UNDECIDED treated the PRU00121 warning as loss of catalytic residues. The actual rule concerns kringle-domain disulfide features, not the protease catalytic triad. UniProt identifies trypsin His/Ser signatures and a Peptidase S1 region; PMID:23411029 describes the corresponding salivary DSPA-gamma architecture. The TreeGrafter source PTN000667065 descends from the plasminogen-activation IBD PTN002799995 and broad protease IBD PTN001208002. Retain the conserved catalytic inference with direct DSPA-gamma biochemical support rather than DSPA-alpha1-specific activity measurements.

Summary: The tPA-like secreted serine protease retains the inferred plasminogen-activating catalytic function.

Reason: Peptidase activity identifies peptide-bond hydrolysis in the proposed plasminogen-activating reaction; this is intrinsic catalytic work rather than a secondary consequence. The previous UNDECIDED treated the PRU00121 warning as loss of catalytic residues. The actual rule concerns kringle-domain disulfide features, not the protease catalytic triad. UniProt identifies trypsin His/Ser signatures and a Peptidase S1 region; PMID:23411029 describes the corresponding salivary DSPA-gamma architecture. The TreeGrafter source PTN000667065 descends from the plasminogen-activation IBD PTN002799995 and broad protease IBD PTN001208002. Retain the conserved catalytic inference with direct DSPA-gamma biochemical support rather than DSPA-alpha1-specific activity measurements.

Summary: The tPA-like secreted serine protease retains the inferred plasminogen-activating catalytic function.

Reason: Serine-type peptidase activity captures the catalytic serine mechanism supported by the trypsin-family active-site signatures. The previous UNDECIDED treated the PRU00121 warning as loss of catalytic residues. The actual rule concerns kringle-domain disulfide features, not the protease catalytic triad. UniProt identifies trypsin His/Ser signatures and a Peptidase S1 region; PMID:23411029 describes the corresponding salivary DSPA-gamma architecture. The TreeGrafter source PTN000667065 descends from the plasminogen-activation IBD PTN002799995 and broad protease IBD PTN001208002. Retain the conserved catalytic inference with direct DSPA-gamma biochemical support rather than DSPA-alpha1-specific activity measurements.

Summary: The tPA-like secreted serine protease retains the inferred plasminogen-activating catalytic function.

Reason: Hydrolase activity describes the hydrolytic chemistry of the peptide-bond cleavage itself; it is broad but still represents the core catalytic reaction. The previous UNDECIDED treated the PRU00121 warning as loss of catalytic residues. The actual rule concerns kringle-domain disulfide features, not the protease catalytic triad. UniProt identifies trypsin His/Ser signatures and a Peptidase S1 region; PMID:23411029 describes the corresponding salivary DSPA-gamma architecture. The TreeGrafter source PTN000667065 descends from the plasminogen-activation IBD PTN002799995 and broad protease IBD PTN001208002. Retain the conserved catalytic inference with direct DSPA-gamma biochemical support rather than DSPA-alpha1-specific activity measurements.

Summary: Mark the inherited lipid-response row as salivary tPA over-annotation.

Reason: The focused DSPA-gamma report treats cellular response to lipid as an electronic carry-over from full-length mammalian tPA's indirect, context-specific cell biology. The salivary K9IJK6 core remains plasminogen activation; no direct DSPA-gamma evidence supports retaining this generic ARBA response process as a target function.

Summary: Mark the inherited oxygen-compound response row as salivary tPA over-annotation.

Reason: The focused DSPA-gamma report treats cellular response to oxygen-containing compound as an electronic carry-over from full-length mammalian tPA's indirect, context-specific cell biology. The salivary K9IJK6 core remains plasminogen activation; no direct DSPA-gamma evidence supports retaining this generic ARBA response process as a target function.