VPS45

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0016192 vesicle-mediated transport	IBA GO_REF:0000033	ACCEPT	Summary: Vesicle-mediated transport is consistent with the core biology of VPS45 as an SM-family protein that drives SNARE-dependent docking and fusion of transport vesicles in the endosomal/Golgi-to-vacuole system. Reason: Well-supported high-level process; Vps45p is required for fusion of Golgi-derived vesicles with the prevacuolar compartment. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000187655 · PANTHER:PTN000187655 SOURCE STALE OR MISSING The exact node is present in the pinned GOA WITH/FROM but absent from the current local PAINT snapshot. The transfer is independently supported by direct VPS45 trafficking evidence. SGD:S000003063 · VPS45 SUPPORTS TRANSFER The target's own experimentally grounded trafficking annotation is a valid descendant source, not circular evidence. Supporting Evidence: PMID:7720726 Fractionation studies show that Vps45p is a peripheral membrane protein that cofractionates with Golgi-like membranes, consistent with Vps45p functioning in membrane traffic between the Golgi and the vacuole. file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45 is an endosomal SM protein
GO:0000139 Golgi membrane	IBA GO_REF:0000033	ACCEPT	Summary: Golgi membrane localization is consistent with the role of Vps45p in Golgi(TGN)-to-prevacuolar transport and with its association with the late Golgi/early endosome syntaxin Tlg2p. Reason: Supported by IDA evidence (PMID:7720726) on this same term and by the VPS45-dependent Golgi-to-PVC trafficking step. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000187915 · PANTHER:PTN000187915 SOURCE STALE OR MISSING The exact ancestral node is recorded in GOA but cannot be recovered from the current local PAINT snapshot. MGI:MGI:891965 · MGI:MGI:891965 SUPPORTS TRANSFER The mammalian descendant source supports conserved Golgi/endosomal SM-protein localization. SGD:S000003063 · VPS45 SUPPORTS TRANSFER Direct yeast fractionation places Vps45 on Golgi-like membranes. Supporting Evidence: PMID:7720726 Fractionation studies show that Vps45p is a peripheral membrane protein that cofractionates with Golgi-like membranes, consistent with Vps45p functioning in membrane traffic between the Golgi and the vacuole. file:yeast/VPS45/VPS45-deep-research-falcon.md Sec1/Munc18-family SM protein required for docking/fusion of Golgi-derived vesicles with the prevacuolar compartment
GO:0006886 intracellular protein transport	IBA GO_REF:0000033	ACCEPT	Summary: Intracellular protein transport is consistent with the role of Vps45p in moving biosynthetic cargo from the Golgi/TGN into the prevacuolar compartment. Reason: High-level but accurate; Vps45p defines an intracellular route for biosynthetic cargo into the PVC. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000187655 · PANTHER:PTN000187655 SOURCE STALE OR MISSING The exact node is present in GOA but absent from the current local PAINT snapshot; target-specific experiments independently support the conserved transport process. SGD:S000003063 · VPS45 SUPPORTS TRANSFER The target's direct trafficking evidence appropriately grounds the IBA. Supporting Evidence: PMID:9650782 Here we demonstrate that the Sec1p-like protein Vps45p is required for the fusion of Golgi-derived vesicles with the prevacuolar compartment indicating that VPS45 functions before VPS27 in the vacuolar biogenesis pathway. file:yeast/VPS45/VPS45-deep-research-falcon.md A VPS45-dependent intracellular route (Golgi/TGN → PVC) for biosynthetic cargo
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: Cytoplasm localization is consistent with the cycling behavior of Vps45p, a peripheral membrane SM protein that exchanges between the cytosol and the cytoplasmic face of intracellular membranes. The vacuolar/Golgi membrane annotations capture the more specific membrane-associated compartments. Reason: Consistent with UniProt subcellular location and falcon synthesis; Vps45p becomes more cytosolic when its Tlg2 membrane anchor is removed. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md becomes more cytosolic when Tlg2 lacks its N-terminal Vps45-binding region
GO:0005774 vacuolar membrane	IEA GO_REF:0000044	ACCEPT	Summary: Vacuolar membrane is consistent with the experimentally documented cycling of Vps45p on and off the cytoplasmic side of the vacuolar membrane (UniProt; PubMed:12756236) and with its membrane association in wild-type contexts. Reason: Supported by UniProt subcellular location and falcon membrane-association evidence. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45p is predominantly membrane-associated in wild-type contexts
GO:0005794 Golgi apparatus	IEA GO_REF:0000117	ACCEPT	Summary: Golgi apparatus localization is consistent with the role of Vps45p at the late Golgi/TGN, where it associates with the Tlg2p syntaxin module and mediates Golgi-to-PVC transport. Reason: Plausible and corroborated by the more specific Golgi membrane (IDA) annotation; Vps45p acts at Tlg2-associated Golgi/endosomal membranes. Supporting Evidence: PMID:7720726 Fractionation studies show that Vps45p is a peripheral membrane protein that cofractionates with Golgi-like membranes, consistent with Vps45p functioning in membrane traffic between the Golgi and the vacuole. file:yeast/VPS45/VPS45-deep-research-falcon.md Golgi (TGN) → prevacuolar compartment/endosome (PVC)** transport in the CPY pathway
GO:0006886 intracellular protein transport	IEA GO_REF:0000117	ACCEPT	Summary: Duplicate of the IBA intracellular protein transport annotation; consistent with the biosynthetic Golgi-to-PVC route mediated by Vps45p. Reason: Same well-supported high-level process as the IBA annotation above. Supporting Evidence: PMID:9650782 Here we demonstrate that the Sec1p-like protein Vps45p is required for the fusion of Golgi-derived vesicles with the prevacuolar compartment indicating that VPS45 functions before VPS27 in the vacuolar biogenesis pathway. file:yeast/VPS45/VPS45-deep-research-falcon.md A VPS45-dependent intracellular route (Golgi/TGN → PVC) for biosynthetic cargo
GO:0015031 protein transport	IEA GO_REF:0000043	ACCEPT	Summary: Protein transport is a high-level keyword-derived term consistent with the role of Vps45p in vacuolar protein sorting; more specific child terms (Golgi to vacuole transport, Cvt pathway) better capture the biology. Reason: Accurate but general; retained as a parent of the specific transport processes Vps45p mediates. Supporting Evidence: PMID:9650782 Here we demonstrate that the Sec1p-like protein Vps45p is required for the fusion of Golgi-derived vesicles with the prevacuolar compartment indicating that VPS45 functions before VPS27 in the vacuolar biogenesis pathway. file:yeast/VPS45/VPS45-deep-research-falcon.md Sec1/Munc18-family SM protein required for docking/fusion of Golgi-derived vesicles with the prevacuolar compartment
GO:0016192 vesicle-mediated transport	IEA GO_REF:0000120	ACCEPT	Summary: Duplicate of the IBA vesicle-mediated transport annotation; consistent with the SNARE-dependent vesicle docking/fusion role of Vps45p. Reason: Same well-supported high-level process as the IBA annotation above. Supporting Evidence: PMID:9650782 Here we demonstrate that the Sec1p-like protein Vps45p is required for the fusion of Golgi-derived vesicles with the prevacuolar compartment indicating that VPS45 functions before VPS27 in the vacuolar biogenesis pathway. file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45 is an endosomal SM protein
GO:0031201 SNARE complex	IEA GO_REF:0000117	MARK AS OVER ANNOTATED	Summary: SNARE complex localization reflects the engagement of Vps45p with syntaxin SNAREs (Tlg2p/Pep12p) and its requirement for productive ternary SNARE complex formation (with Tlg1p and Vti1p for the Tlg2 module). Reason: Vps45p binds both individual SNAREs and assembled SNARE complexes, but it is an SM-family regulator rather than one of the SNARE proteins forming the core four-helix complex. SNARE binding and positive regulation of SNARE complex assembly capture the evidence without asserting membership. Supporting Evidence: PMID:11432826 First, SM proteins act as chaperone-like molecules for their cognate t-SNAREs. Secondly, SM proteins play an essential role in the activation process allowing their cognate t-SNARE to participate in ternary complex formation. file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45p is needed not just for Tlg2 stability but also for Tlg2 entry into ternary SNARE complexes
GO:0031338 regulation of vesicle fusion	IEA GO_REF:0000117	ACCEPT	Summary: Regulation of vesicle fusion is consistent with the SM-protein function of Vps45p in controlling SNARE-dependent docking and fusion; the mechanistically more specific term positive regulation of SNARE complex assembly (GO:0035543) is also annotated. Reason: Supported; Vps45p positively regulates productive SNARE complex assembly, a key control point for vesicle fusion. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Directly binds Tlg2p and positively regulates productive SNARE complex assembly
GO:0098588 bounding membrane of organelle	IEA GO_REF:0000117	ACCEPT	Summary: Bounding membrane of organelle is a high-level location term consistent with the peripheral association of Vps45p with the vacuolar/endosomal bounding membranes; more specific terms (vacuolar membrane, Golgi membrane) capture the biology. Reason: Plausible high-level location; Vps45p is membrane-associated on the cytoplasmic face of intracellular organelle membranes. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45p is membrane-associated when full-length Tlg2p is present
GO:0005515 protein binding	IPI PMID:10397773 A role for Tlg1p in the transport of proteins within the Gol...	MODIFY	Summary: Generic protein binding is uninformative. The biologically meaningful interaction in this row is with the syntaxin SNARE Tlg1p (UniProtKB:Q03322), so SNARE binding is the evidence-matched term. Reason: Replace generic GO:0005515 with GO:0000149 because the recorded partner is a SNARE protein. Proposed replacements: SNARE binding
GO:0005515 protein binding	IPI PMID:10978279 Pep3p/Pep5p complex: a putative docking factor at multiple s...	MARK AS OVER ANNOTATED	Summary: Generic protein binding is uninformative; the specific Vps45p-syntaxin and Vps45p-Vac1p interactions are better captured by SNARE binding and the docking/fusion process terms. Reason: Avoid GO:0005515; more specific terms capture the biology more accurately.
GO:0005515 protein binding	IPI PMID:12553664 A novel phospholipid-binding protein from the yeast Saccharo...	MARK AS OVER ANNOTATED	Summary: Generic protein binding is uninformative for Vps45p; its functional partnerships (syntaxins, Vac1p) are represented by more specific terms. Reason: Avoid GO:0005515; more specific terms capture the biology more accurately.
GO:0005515 protein binding	IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine...	MODIFY	Summary: This proteome-survey row records the syntaxin SNARE Tlg1p (UniProtKB:Q03322) as the partner; generic protein binding loses that specificity. Reason: Replace GO:0005515 with GO:0000149 because the recorded partner is a SNARE. Proposed replacements: SNARE binding
GO:0005515 protein binding	IPI PMID:16429126 Proteome survey reveals modularity of the yeast cell machine...	MODIFY	Summary: The second physical GOA row from this proteome-scale affinity-purification study has a distinct WITH/FROM partner (UniProtKB:Q08144). Generic protein binding remains uninformative relative to the established syntaxin/SNARE interactions. Reason: Replace GO:0005515 with GO:0000149 because the recorded partner Tlg2p is a syntaxin SNARE. Proposed replacements: SNARE binding
GO:0005515 protein binding	IPI PMID:18719252 High-quality binary protein interaction map of the yeast int...	MARK AS OVER ANNOTATED	Summary: Generic protein binding from a binary interactome map; not informative about the specific molecular function of Vps45p. Reason: Avoid GO:0005515; high-throughput interaction without a specific functional term.
GO:0005515 protein binding	IPI PMID:18719252 High-quality binary protein interaction map of the yeast int...	MODIFY	Summary: The second binary-interactome row has a distinct WITH/FROM partner (UniProtKB:Q08144). The interaction may be useful evidence, but the generic molecular-function term adds no biological specificity. Reason: Replace GO:0005515 with GO:0000149 because the recorded partner Tlg2p is a syntaxin SNARE. Proposed replacements: SNARE binding
GO:0005515 protein binding	IPI PMID:19667197 The N-terminal peptide of the syntaxin Tlg2p modulates bindi...	MODIFY	Summary: This study characterizes how the N-terminal peptide of Tlg2p modulates binding of its closed conformation to Vps45p — a SNARE-binding interaction. Generic protein binding is over-annotated; SNARE binding (GO:0000149) captures it specifically. Reason: Replace GO:0005515 with GO:0000149; the interaction is specifically with the syntaxin SNARE Tlg2p. Proposed replacements: SNARE binding
GO:0005515 protein binding	IPI PMID:27107014 An inter-species protein-protein interaction network across ...	MARK AS OVER ANNOTATED	Summary: Generic protein binding from a large-scale inter-species interaction network; not informative about Vps45p molecular function. Reason: Avoid GO:0005515; high-throughput interaction without a specific functional term.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	MARK AS OVER ANNOTATED	Summary: Generic protein binding from a global interactome study; not informative about Vps45p molecular function. Reason: Avoid GO:0005515; high-throughput interaction without a specific functional term.
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	MODIFY	Summary: A distinct physical GOA row from the quantitative interactome has WITH/FROM UniProtKB:Q03322. Co-enrichment supports association, but generic protein binding is not an informative Vps45 molecular function. Reason: Replace GO:0005515 with GO:0000149 because the recorded partner Tlg1p is a syntaxin SNARE. Proposed replacements: SNARE binding
GO:0005515 protein binding	IPI PMID:37968396 The social and structural architecture of the yeast protein ...	MODIFY	Summary: A third physical GOA row from the quantitative interactome has WITH/FROM UniProtKB:Q08144. The underlying association is plausible, but GO:0005515 is too generic to describe the SM-syntaxin relationship. Reason: Replace GO:0005515 with GO:0000149 because the recorded partner Tlg2p is a syntaxin SNARE. Proposed replacements: SNARE binding
GO:0000011 vacuole inheritance	IMP PMID:1493335 Morphological classification of the yeast vacuolar protein s...	KEEP AS NON CORE	Summary: Vacuole inheritance defects are part of the broad class-D/class-E vps mutant phenotype rather than a direct molecular function of Vps45p. The core role of Vps45p is SNARE-dependent vesicle docking/fusion in the Golgi-to-vacuole/endosomal system; defective vacuole inheritance is an indirect downstream consequence of impaired trafficking. Reason: Pleiotropic/indirect phenotype of disrupted vacuolar trafficking, not the core direct function; retained as non-core. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45 is an endosomal SM protein that couples signaling-defined membrane identity (Vac1–Vps21–PI3P) to the formation and maintenance of a fusion-competent syntaxin/SNARE state
GO:0000139 Golgi membrane	IDA PMID:7720726 Yeast Vps45p is a Sec1p-like protein required for the consum...	ACCEPT	Summary: Direct evidence places Vps45p at Golgi membranes, consistent with its role in the consumption (fusion) of vacuole-targeted, post-Golgi transport vesicles and its association with the Tlg2p syntaxin at late Golgi/early endosome membranes. Reason: IDA-supported localization concordant with the Golgi-to-PVC trafficking function of Vps45p. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Sec1/Munc18-family SM protein required for docking/fusion of Golgi-derived vesicles with the prevacuolar compartment
GO:0000149 SNARE binding	IPI PMID:16769821 The Sec1p/Munc18 protein Vps45p binds its cognate SNARE prot...	ACCEPT	Summary: SNARE binding is a core molecular function of Vps45p. As an SM protein it binds cognate SNAREs and is required for productive ternary SNARE complex assembly. PMID:16769821 shows that L117R abolishes the Sly1p-Sed5p-type Tlg2 N-terminal interaction, assembled Tlg2-containing complex binding, and membrane association, yet still rescues CPY sorting; this interaction mode is therefore dispensable for trafficking. The paper also identifies an N-terminus-independent mode through direct Snc2 binding and a W244R-locked conformation that the authors propose wild-type Vps45 adopts transiently during its functional cycle. Reason: Direct interaction (IPI) with cognate syntaxins; this is the defining molecular activity of the SM protein and is strongly corroborated by the falcon synthesis. Supporting Evidence: PMID:16769821 Our finding that the disruption of Vps45p binding to Tlg2p through L117 of the SM protein had no effect on CPY sorting (Fig. 1 D) and the finding that the analogous binding of Sly1p to Sed5p is not required for membrane traffic (Peng and Gallwitz, 2004) implies that the hydrophobic pocket mode of interaction between SM proteins and their Sxs is not critical. file:yeast/VPS45/VPS45-deep-research-falcon.md physically associates with the syntaxin-like t-SNARE Tlg2p and also forms a separate complex with the endosomal t-SNARE Pep12p
GO:0000149 SNARE binding	IPI PMID:16769821 The Sec1p/Munc18 protein Vps45p binds its cognate SNARE prot...	ACCEPT	Summary: The second physical SNARE-binding row records the distinct WITH/FROM partner SGD:S000005854. Full-text experiments show that Vps45 binds both Tlg2 and the v-SNARE Snc2 through distinct modes. Reason: This physical row is retained separately because it represents a distinct SNARE partner and directly supports the core SNARE-binding function. Supporting Evidence: PMID:16769821 Fig. 2 A demonstrates that His6-Vps45p interacts directly with the cytosolic domains of both Tlg2p and the v-SNARE Snc2p (Snc2p-PrA).
GO:0005829 cytosol	IDA PMID:9624182 The vesicle transport protein Vps33p is an ATP-binding prote...	UNDECIDED	Summary: Cytosol localization is plausible for Vps45p, a peripheral SM protein that cycles between the cytosol and the cytoplasmic face of intracellular membranes. However, the cited reference PMID:9624182 (Gerhardt et al. 1998) is titled and abstracted as a study of the SM protein Vps33p, not Vps45p; its cytosol/membrane cycling data concern Vps33p. The full text is not available in the publication cache, so it cannot be confirmed whether the paper contains a direct IDA observation of Vps45p cytosol localization, and the GOA IDA attribution may be a mis-annotation conflating two SM-family proteins. Reason: Cannot verify the IDA: the cited PMID:9624182 is a Vps33p study (Vps45p does not appear in the abstract) and the full text is not accessible to confirm any direct Vps45p cytosol observation. Per curation guidelines, mark UNDECIDED when the relevant publication cannot be accessed/verified rather than ACCEPT.
GO:0006623 protein targeting to vacuole	IMP PMID:7628704 STT10, a novel class-D VPS yeast gene required for osmotic i...	ACCEPT	Summary: Protein targeting to the vacuole is a core process for Vps45p; vps45/stt10 mutants show a class-D vacuolar protein sorting defect, mis-sorting biosynthetic cargo (e.g., CPY) that depends on the VPS45-mediated Golgi-to-PVC route. Reason: Core vacuolar protein sorting function; strong CPY mis-sorting in vps45 mutants. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md strong CPY mis-sorting, with ~70% CPY secretion versus ~2–4% in wild type
GO:0006895 Golgi to endosome transport	IGI PMID:9335586 Genetic interactions between a pep7 mutation and the PEP12 a...	ACCEPT	Summary: Golgi to endosome transport captures the VPS45-dependent intracellular route by which biosynthetic cargo moves from the Golgi/TGN to the prevacuolar/endosomal compartment (PVC). Genetic interactions with PEP12 and PEP7 place Vps45p in this Golgi-to-endosome SNARE module. Reason: Supported by genetic interaction (IGI) and by the falcon-defined VPS45-dependent biosynthetic route into the PVC. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md A VPS45-dependent intracellular route (Golgi/TGN → PVC) for biosynthetic cargo
GO:0006896 Golgi to vacuole transport	IMP PMID:7720726 Yeast Vps45p is a Sec1p-like protein required for the consum...	ACCEPT	Summary: Golgi to vacuole transport is a core biological process for Vps45p, which is required for the consumption (docking/fusion) of vacuole-targeted, post-Golgi transport vesicles with the prevacuolar compartment en route to the vacuole. Reason: IMP-supported core trafficking step; central to the function of this SM protein. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Sec1/Munc18-family SM protein required for docking/fusion of Golgi-derived vesicles with the prevacuolar compartment
GO:0007033 vacuole organization	IMP PMID:9650782 Traffic into the prevacuolar/endosomal compartment of Saccha...	KEEP AS NON CORE	Summary: Altered vacuole organization/morphology in vps45 mutants is a downstream consequence of impaired delivery of biosynthetic cargo and membrane to the vacuole, rather than a direct molecular function. The core role of Vps45p is SNARE-mediated docking/fusion at the Golgi-to-PVC step. Reason: Indirect/pleiotropic organelle-morphology phenotype of disrupted trafficking; retained as non-core. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md A VPS45-dependent intracellular route (Golgi/TGN → PVC) for biosynthetic cargo
GO:0007035 vacuolar acidification	IMP PMID:7628704 STT10, a novel class-D VPS yeast gene required for osmotic i...	KEEP AS NON CORE	Summary: Defective vacuolar acidification in vps45/stt10 mutants is an indirect consequence of the class-D vps trafficking defect; the source paper reports vacuoles with normal vacuolar H(+)-ATPase activity but defective acidification, indicating mis-delivery of components rather than a direct role of Vps45p in acidification. Reason: Indirect/pleiotropic phenotype; vacuolar H(+)-ATPase activity is normal, so Vps45p does not directly mediate acidification. Retained as non-core. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45 is an endosomal SM protein that couples signaling-defined membrane identity (Vac1–Vps21–PI3P) to the formation and maintenance of a fusion-competent syntaxin/SNARE state
GO:0031201 SNARE complex	IPI PMID:10397773 A role for Tlg1p in the transport of proteins within the Gol...	MARK AS OVER ANNOTATED	Summary: Vps45p is part of the SNARE machinery, engaging the Tlg2p syntaxin module (with Tlg1p and Vti1p) required for productive SNARE complex formation in the Golgi/endosomal system. Reason: Interaction with a SNARE complex does not make the SM regulator a core SNARE-complex subunit. PMID:10397773 says Vps45 enters a complex with Tlg1/Tlg2/Vti1, but mechanistic work distinguishes Vps45 from the SNARE proteins and supports binding/regulation rather than `part_of` membership. Supporting Evidence: PMID:10397773 Tlg1p is able to bind His6-tagged Sec17p (yeast alpha-SNAP) in a dose-dependent manner and enters into a SNARE complex with Vti1p, Tlg2p, and Vps45p. file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45p is needed not just for Tlg2 stability but also for Tlg2 entry into ternary SNARE complexes
GO:0032258 cytoplasm to vacuole targeting by the Cvt pathway	IMP PMID:10545112 Cytoplasm to vacuole trafficking of aminopeptidase I require...	ACCEPT	Summary: Vps45p, together with the syntaxin Tlg2p, forms a t-SNARE-Sec1p module required for the constitutive cytoplasm-to-vacuole targeting (Cvt) pathway of aminopeptidase I. vps45 mutants fail to mature API and phenocopy tlg2 deletion, while starvation-induced macroautophagy remains intact. Reason: Directly demonstrated (Abeliovich et al. 1999); a core Vps45p-dependent membrane-fusion process. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Vps45p and Tlg2p are required for maturation/processing of API via the constitutive Cvt route
GO:0035543 positive regulation of SNARE complex assembly	IMP PMID:11432826 Vps45p stabilizes the syntaxin homologue Tlg2p and positivel...	ACCEPT	Summary: Vps45p positively regulates SNARE complex formation: it stabilizes the syntaxin homologue Tlg2p (preventing rapid proteasomal degradation) and is required for Tlg2p to enter productive ternary SNARE complexes with its cognate partners Tlg1p and Vti1p. This is a defining molecular role of the SM protein. Reason: Directly demonstrated (Bryant & James 2001); core regulatory function. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Directly binds Tlg2p and positively regulates productive SNARE complex assembly
GO:0048210 Golgi vesicle fusion to target membrane	IMP PMID:9650782 Traffic into the prevacuolar/endosomal compartment of Saccha...	ACCEPT	Summary: Golgi vesicle fusion to target membrane reflects the core SM-protein role of Vps45p in promoting SNARE-dependent docking and fusion of Golgi-derived transport vesicles with the prevacuolar compartment. Reason: Core trafficking function; Vps45p enables docking/fusion of Golgi-derived vesicles with the PVC. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md Sec1/Munc18-family SM protein required for docking/fusion of Golgi-derived vesicles with the prevacuolar compartment
GO:0051082 unfolded protein binding	IMP PMID:11432826 Vps45p stabilizes the syntaxin homologue Tlg2p and positivel...	MARK AS OVER ANNOTATED	Summary: The chaperone-like activity of Vps45p is specific to SNARE complex assembly (it stabilizes the Tlg2p syntaxin and promotes productive SNARE pairing), not generic binding of unfolded proteins. Modern consensus frames SM proteins as active chaperones for productive trans-SNARE complex assembly rather than general protein-folding chaperones, so unfolded protein binding over-extends the function. Reason: GO:0051082 is obsolete. The chaperone activity is SNARE-assembly-specific; positive regulation of SNARE complex assembly (GO:0035543) and SNARE binding (GO:0000149) capture it more accurately than generic unfolded protein binding. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md SM proteins as active chaperones for productive trans-SNARE complex assembly, rather than passive syntaxin binders
GO:0051082 unfolded protein binding	IPI PMID:11432826 Vps45p stabilizes the syntaxin homologue Tlg2p and positivel...	MARK AS OVER ANNOTATED	Summary: Duplicate (IPI) of the unfolded protein binding annotation. As above, the chaperone activity of Vps45p is SNARE-assembly-specific rather than generic unfolded protein binding. Reason: GO:0051082 is obsolete. SNARE-assembly-specific chaperone activity is better captured by GO:0035543 and GO:0000149 than by generic unfolded protein binding. Supporting Evidence: file:yeast/VPS45/VPS45-deep-research-falcon.md SM proteins as active chaperones for productive trans-SNARE complex assembly, rather than passive syntaxin binders

Gene Description

Existing Annotations Review

Core Functions

References

Deep Research

Falcon

📚 Additional Documentation

Notes

📄 View Raw YAML