ATL1

Summary: Retain Golgi membrane as contextual evidence.

Reason: The complete 2003 abstract reports Golgi/cis-Golgi localization in neuronal preparations. Retain this experimentally curated location as contextual, alongside the much better established ER fusion site. The original localization Methods and exact human-versus-rodent preparations were not independently read here; later human ATL1 ER evidence does not refute this Golgi observation.

Summary: Retain Golgi membrane as contextual evidence.

Reason: The 2007 abstract explicitly reports ER and Golgi localization and mutant effects at the ER/Golgi interface. Retain Golgi membrane localization as contextual; do not convert a historical compartment observation into a primary Golgi-fission mechanism. Detailed species and construct Methods remain uninspected.

Summary: Retain Golgi membrane as contextual evidence.

Reason: The UniProt Golgi-membrane mapping is consistent with the retained experimental Golgi observations. Keep as a contextual location; no evidence of an erroneous mapping or mutually exclusive ER/Golgi localization was found.

Summary: Retain supported GTPase activity.

Reason: GTP hydrolysis is a direct component of ATL1 membrane fusion. The 2003 source abstract and curated enzyme record are supported independently by later human ATL1 structural and biochemical studies. Retain the original broad catalytic annotation without replacing it with the already present fusogenic term; exact 2003 enzyme-assay Methods were not inspected.

Summary: Retain supported GTPase activity.

Reason: Human ATL1 cytosolic-fragment GTPase measurements and the conformational cycle support GTP hydrolysis. The selected 2024 Methods were independently examined; the lipid-mixing arm uses Drosophila ATL and must remain distinct from this human hydrolysis result.

Summary: Retain supported GTPase activity.

Reason: Retain the phylogenetic GTPase assertion because independent human ATL1 catalysis supports the same function. The PAINT node and alignment have not been replayed. The target in WITH/FROM is legitimate descendant evidence, not circularity, and the donor count is not an evidential score.

Summary: Retain supported GTPase activity.

Reason: The InterPro/Rhea mapping agrees with the measured GTP hydrolysis reaction. There is no biochemical basis to reject the electronic annotation; the more specific fusogenic activity already exists as separate source rows.

Summary: Retain protein binding as contextual evidence.

Reason: The 2006 abstract and selected indexed Results/Methods explicitly support physical interaction with spastin. Keep the generic interaction as non-core; the physical association is adjudicated, while its precise physiological contribution is less specific than ATL1 fusion. Do not infer that ATL1 activates spastin ATPase activity. Preserve the original partner and subject-isoform fields.

Summary: Retain protein binding as contextual evidence.

Reason: The 2009 Results directly demonstrate ATL1 association with DP1/REEP5 in coexpression/coimmunoprecipitation experiments. Retain the curated Q60870 heterologous partner as non-core. Mammalian assay-cell identity does not by itself determine the species of the expressed protein; the accession mapping is retained from the curator.

Summary: Retain protein binding as contextual evidence.

Reason: The 2009 Results demonstrate association with reticulon-3c, including reciprocal coimmunoprecipitation and controls. Retain the curator-mapped Q9ES97 interaction as non-core; it is not a new direct binding-domain activity. Do not erase species or conflate the unsuffixed partner with a different isoform row.

Summary: Retain protein binding as contextual evidence.

Reason: The source directly tests the Rtn3c interaction and retains strong control specificity. Keep this separate Q9ES97-3 assertion as non-core, with the curated isoform mapping unchanged. The mapping is not newly inferred from a protein name.

Summary: Retain protein binding as contextual evidence.

Reason: The 2009 source distinguishes native rat ATL1/Rtn4a coimmunoprecipitation from recombinant reticulon-domain experiments. Together with the positive curated heterologous Q9JK11-3 record, this supports retention as a non-core interaction; do not relabel the native rat experiment as an endogenous human pair.

Summary: Retain protein binding as contextual evidence.

Reason: The 2009 source uses human RTN4a-derived cytoplasmic and membrane-domain constructs and supports association through the membrane-containing region. Retain the Q9NQC3 record as non-core; a positive coimmunoprecipitation is not a claim that a purified full-length binary complex was reconstituted.

Summary: Retain protein binding as contextual evidence.

Reason: Retain this separate Q9NQC3-1 interaction as non-core. The relevant reticulon/ATL1 experiments were inspected, and UniProt reports positive experiments for this exact partner. The original isoform assignment is curator-supplied and remains unchanged.

Summary: Retain protein binding as contextual evidence.

Reason: Indexed original Results/Figure 7 and construct Methods show human REEP1 and ATL1 coimmunoprecipitation in transfected COS7 cells, with the ATL1 membrane-containing region sufficient for association. Keep this binding record as non-core. Rat-neuron colocalization and REEP1 microtubule binding are distinct experiments, not direct ATL1 microtubule activity.

Summary: Retain protein binding as contextual evidence.

Reason: Original indexed Results/Figure 2F identify all three human atlastins with endogenous protrudin, with recombinant interaction experiments also described. The ATL1-protrudin association is supported and retained as non-core; the broader ER-shaping context does not establish an additional specific ATL1 molecular activity.

Summary: Retain protein binding as contextual evidence.

Reason: The source abstract plus original indexed Results/Figure 3 explicitly show tagged CPT1C and ATL1 coimmunoprecipitation and colocalization in COS7 cells. Retain this supported generic association as non-core, without claiming that all lipid-droplet or mouse-neuron phenotypes in the paper are direct ATL1 activities.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact O00628-2 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P02545 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P04156 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P19404 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P35240 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P41219 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P42858 interaction with positive NbExp=18; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P50570-2 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P50897 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P51149 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact P54577 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact Q16637 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact Q7Z699 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact Q86WV8 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact Q8N5K1 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact Q8WXH2 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact Q96CV9 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: The source-specific interaction remains unresolved.

Reason: UniProt records the exact Q9BZ23-2 interaction with positive NbExp=3; this is not evidence of an absent or refuted interaction. The complete PMID32814053 abstract describes a systematic interaction screen, but the pair-level original dataset, construct and validation result for this row were not inspected. Publisher/DOI access did not supply that evidence. Use UNDECIDED under the user enum, preserve the partner/isoform and revisit if the exact source record is read; do not REMOVE or call it nonspecific merely because it is high throughput.

Summary: Retain supported GTP binding.

Reason: GTP binding is an experimentally established prerequisite of ATL1 catalysis, independently corroborating the IBA function. Keep the original phylogenetic source object; the PAINT ancestral placement itself has not been replayed and the donor list is not graded by length.

Summary: Retain supported GTP binding.

Reason: The InterPro GTP-binding inference agrees with the experimentally characterized ATL1 G domain and nucleotide-bound human structures. Retain the functional mapping; no additional binding core is needed alongside the fusogenic core.

Summary: Retain supported GTP binding.

Reason: Retain the curator transfer of GTP binding from rat ATL1 Q6PST4, independently corroborated by human ATL1 nucleotide-bound structures and biochemical work. The source remains ISS rather than being rewritten as a new human experiment.

Summary: Retain cytoplasm as contextual evidence.

Reason: Cytoplasm is a broad compartment containing the cytoplasmic ER network, not a synonym for free cytosol. Retain the mouse-ortholog transfer as non-core location context; ATL1 is membrane-associated and should not be described as a soluble cytosolic enzyme.

Summary: Retain supported endoplasmic reticulum.

Reason: The 2009 Results localize low/moderate recombinant Myc-ATL1 primarily to tubular ER in COS7 cells. This supports the ER compartment as part of the core localization; no requirement to replace the valid parent term with an already existing child.

Summary: Retain supported endoplasmic reticulum membrane.

Reason: The original integral-membrane/topology observation and reviewed ER membrane annotation are coherent with multiple independent human ATL1 localization studies. Retain the experimental source; the 2003 detailed ER assay was not independently replayed.

Summary: Retain supported endoplasmic reticulum membrane.

Reason: The inspected 2006 Results show N- and C-terminally tagged full-length atlastin in a reticular ER pattern in HeLa cells, colocalizing with calreticulin/PDI/Sec61 markers. Retain ER membrane localization; mouse NSC34 observations are a separate model and tags/overexpression remain explicit.

Summary: Retain supported endoplasmic reticulum membrane.

Reason: The complete 2007 abstract identifies ER as well as Golgi localization. Retain the core ER membrane location with corroborating later direct ATL1 imaging, without claiming the uninspected detailed Methods were read.

Summary: Retain supported endoplasmic reticulum membrane.

Reason: The inspected 2009 Results support ATL1 localization through its membrane-anchoring region to the tubular ER. Retain the core membrane compartment, keeping the original assay evidence type unchanged.

Summary: Retain supported endoplasmic reticulum membrane.

Reason: The inspected 2016 live-cell Results/Figure 1 show tagged ATL1 throughout the tubular ER in U2OS cells. Preserve this direct location evidence while distinguishing it from ATL2/3 punctate junctional enrichment and the separate Xenopus extract assays.

Summary: Retain supported endoplasmic reticulum membrane.

Reason: UniProt ER membrane mapping agrees with the direct localization and membrane anchoring evidence. Retain this electronic row without modifying its source term or evidence.

Summary: Retain supported endoplasmic reticulum membrane.

Reason: The rat-ortholog ER membrane transfer is independently consistent with human ATL1 localization. Retain ISS and its donor rather than fabricating a different original experiment.

Summary: Retain Golgi apparatus as contextual evidence.

Reason: Retain the rat ATL1 Golgi transfer as contextual non-core localization. Earlier Golgi/cis-Golgi observations are not disproven by the current ER fusion model; the source remains orthology-based.

Summary: Retain supported endoplasmic reticulum organization.

Reason: ER organization is a direct consequence of ATL1 performing membrane fusion and is experimentally supported in human ATL1 expression/perturbation studies. Retain the IBA claim, with the node/MSA unexamined. The target among descendants is not circular evidence.

Summary: Retain axonogenesis as contextual evidence.

Reason: Retain the curated rat-ortholog axonogenesis transfer as a non-core developmental outcome. It is compatible with neuronal ER-network function and is not contradicted by the present evidence; no new broad neuronal process is proposed.

Summary: Retain supported endoplasmic reticulum membrane fusion.

Reason: Retain ER membrane fusion as the process directly performed by ATL1. The 2024 evidence combines human cytosolic mechanism/yeast complementation with Drosophila lipid mixing, and independent selected primary-source reading supports direct human ATL1 lipid mixing in PMID:34817557. These experimental arms must be described separately.

Summary: Retain supported endoplasmic reticulum membrane fusion.

Reason: The ARBA ER fusion inference matches the experimentally established ATL1 fusogenic activity. Retain the existing process term; do not add redundant membrane-fusion ancestors or another NEW copy.

Summary: Retain supported endoplasmic reticulum membrane fusion.

Reason: The inspected 2016 ATL1 dominant-negative and dimerization-control experiments in live U2OS cells support the requirement for ATL1-mediated ER fusion in maintaining network connectivity. Accept with independent direct fusogenic evidence; the Xenopus reconstitution arm is not a purified human ATL1 fusion assay.

Summary: Retain axon as contextual evidence.

Reason: Axonal localization is compatible with the transferred rat neuronal distribution. Retain as non-core cell-type context, without adding an unverified isoform-specific or axon-only requirement.

Summary: Retain supported identical protein binding.

Reason: Self-association is mechanistically relevant to the fusion cycle and is reported by the 2003 abstract and independently established by later human ATL1 structures/biochemistry. Accept identical-protein binding, while avoiding a fixed physiological tetramer claim based solely on the early size estimates.

Summary: Retain supported identical protein binding.

Reason: The human ATL1 cytosolic 1–446 structures and solution dimerization measurements directly support self-association. Accept as a component of the fusion mechanism, not as a second independent binding core. The transmembrane segments are absent from these structural constructs.

Summary: Retain supported identical protein binding.

Reason: The complete original abstract explicitly identifies the human ATL1 cytosolic segment and dimer structures; full-length Drosophila protein supplies the fusion assay. Accept human self-association while preserving this construct/species distinction.

Summary: Retain supported identical protein binding.

Reason: Indexed original Results and Methods use human ATL1 cytosolic fragments, nucleotide-dependent oligomer measurements and conformational assays. Accept the self-interaction component of the fusion mechanism; these experiments do not themselves assay a purified full-length human membrane-fusion reaction.

Summary: Retain supported protein homooligomerization.

Reason: Human biochemical and structural self-association independently corroborates the IBA homooligomerization claim. Retain the original ancestral node; no node/MSA replay is claimed and the single descendant donor is not a weakness. Do not infer a constant oligomer stoichiometry.

Summary: Retain supported endoplasmic reticulum tubular network.

Reason: The mouse-ortholog tubular-network location is independently corroborated by direct human ATL1 imaging. Retain the original electronic transfer; use the membrane child for the synthesized core location.

Summary: Retain supported endoplasmic reticulum tubular network.

Reason: Retain the curator mouse-ortholog tubular-network transfer because direct human ATL1 imaging independently supports this compartment. No new human evidence type is substituted into the source object.

Summary: Retain supported endoplasmic reticulum tubular network membrane.

Reason: The 2016 Results/Figure 1 place active membrane-anchored ATL1 throughout ER tubules, supporting the tubular-network membrane as the precise core site. ATL1 need not be as concentrated at junctions as ATL2/3 to be active there.

Summary: Retain supported endoplasmic reticulum tubular network membrane.

Reason: The ARBA tubular ER membrane location agrees with direct localization evidence. Retain the current term and use it as the core location; no redundant new location is needed.

Summary: Retain supported GTPase-dependent fusogenic activity.

Reason: This is the specific molecular function of ATL1: GTP hydrolysis coupled to membrane fusion. Retain the curated IDA assertion holistically, with the 2024 human/Drosophila/yeast assay limits and independently examined human lipid-mixing evidence made explicit.

Summary: Retain supported GTPase-dependent fusogenic activity.

Reason: The ARBA fusogenic activity is consistent with independent human ATL1 biochemistry and the conserved mechanism. Retain it without adding another identical NEW molecular-function row.

Summary: Retain Golgi cis cisterna membrane as contextual evidence.

Reason: Retain cis-Golgi membrane localization as an orthology-based, non-core neuronal/secretory context. Do not reassign it to ER simply because ER fusion is the current core model.

Summary: Retain supported endoplasmic reticulum tubular network membrane organization.

Reason: Tubular ER network membrane organization is the direct biological role supported by ATL1 fusion and network-connectivity experiments. Retain the electronic inference; it is not merely an indirect disease association.

Summary: Retain supported endoplasmic reticulum tubular network membrane organization.

Reason: The inspected 2009 Myc-ATL1 WT/K80A and membrane-domain expression experiments support ER-network organization. Keep ATL1 perturbation distinct from the paper’s ATL2/3 depletion experiments and Xenopus in-vitro system; do not label those arms human ATL1 knockdown.

Summary: Retain supported endoplasmic reticulum tubular network membrane organization.

Reason: The 2016 live-cell ATL1 WT/K80A/dimerization-control studies support formation and maintenance of connected ER tubules. Retain the direct process assertion, separating the human-cell and Xenopus extract arms and noting overexpression dependence.

Summary: Retain supported endoplasmic reticulum tubular network membrane organization.

Reason: Retain the 2024 human ATL1 complementation/mechanistic support for ER network organization. Selected source Methods establish human full-length expression in yeast and cytosolic single-molecule assays separately from Drosophila lipid mixing; H443P is engineered, whereas S398Y/N440T are the disease variants.