All 13 complete human QuickGO originals and all 16 exported columns were reconciled with the genuine 13-row native seed. The evidence map preserves the original contexts, seed and actual raw-to-native-to-reviewed joins; notes explain the synthesis and unresolved sources. All eleven qualified normal sources were genuinely acquired. The eight publication assessments distinguish cache availability from bibliographic verification, abstract access and selected original reading.
Current UniProt Q9P0K9 and HGNC:1362 identify human FRRS1L, formerly C9orf4/CG-6. The current reviewed reference is 293 residues and exactly matches the human leaf in the retained PTHR46902 tree/alignment. The native record declares no alternative products. Names suggesting a reductase do not establish an enzymatic activity.
The official UniSave history, entry 100 (2017; sequence version 2) and entry 128 (2022; sequence version 3), was compared with NM_014334.2, NM_014334.3 and NM_014334.4. The older NP_055149.2 sequence has 344 residues; the current NP_055149.3 sequence has 293. Old positions 52–344 match current positions 1–293 exactly. Historical K155/V195/W282/S317/Q321 therefore map to current K104/V144/W231/S266/Q270. Published labels remain tied to their original numbering. This is a reference-sequence revision, not evidence of a natural alternative product. The unversioned NM_014334 construct reported in PMID:28675162 was not resequenced here.
Official record; original article. Reading locators: PubMed title and bibliographic metadata.
Official PubMed identifier and title verified. The retained record has no abstract and the original text was not inspected. It provides cloning/mapping provenance by title; no AMPAR mechanism or expression assay detail is inferred from that title.
Official record; original article. Reading locators: PubMed abstract.
Official PubMed identifier/title and chromosome-9 sequence abstract verified. Relevant as genomic sequence/background provenance, not as an independent FRRS1L functional assay. Full text was not inspected.
Official record; original article. Reading locators: Functional human SH-SY5Y paragraph and Figure 4 caption; subsequent mechanism interpretation.
Official PubMed identity and selected original indexed main text/Figure 4 support the human SH-SY5Y knockdown and AMPA-response claim. Direct article/XML retrieval did not yield a complete article; selected browser-indexed original text was retained separately. No supplement-wide or figure-pixel inspection, direct assembly assay, or universal nonsense-mediated decay conclusion is claimed.
Official record; original article. Reading locators: PubMed title and bibliographic metadata.
Official PubMed identifier and title verified. The retained record has no abstract; the clinical mutation letter itself was not inspected. Its disease-association relevance is apparent from the title, but no unread molecular experiment is inferred.
Official record; original article. Reading locators: Results sec2/sec3/sec5-sec8; Discussion sec9; Methods sec11/sec12/sec15-sec17 and associated main captions.
Official PubMed identity and selected original XML Methods/Results/Discussion support selective native rat AMPAR complexes, reported human NM_014334 expression experiments, ER localization and receptor regulation. The construct accession is unversioned, and historical residue numbering must remain distinct from current-reference coordinates. Native AP/coassembly is not a purified pairwise contact map; no comprehensive supplement or raw-proteomics reanalysis is claimed.
Official record; original article. Reading locators: Plasmids; Co-immunoprecipitation and Western Blot in HEK Cells; Vesicle Immunoisolation; neuronal surface/deletion/rescue Results; Figures 1-2 and relevant main captions.
Official PubMed identity and selected original XML verify mouse FRRS1L constructs, GluA co-IP, intact DIC-positive vesicle immunoisolation, tagged surface localization and neuronal deletion/rescue. The HEK host does not make the tested mouse construct human. The DIC assay does not independently establish FRRS1L affinity for the intermediate chain; no full supplement or figure-pixel analysis is claimed.
Official record; original article. Reading locators: Results s2d/s2e and Figures 4-5; Discussion s3; Methods s4a/s4b12-s4b15.
Official PubMed identity and selected original mouse-null Results/Methods/Discussion support altered AMPAR abundance, Endo-H-sensitive receptor maturation and postsynaptic-fraction distribution. These receptor assays are not direct FRRS1L localization or glycosyltransferase measurements. The main text and Figure 4 caption differ in their summary of Gria transcript changes; no claim that every transcript is unchanged is used.
Official record; original article. Reading locators: PubMed/Europe PMC abstract; full-text route/access metadata.
Official PubMed/Europe PMC identifier, DOI and authentic abstract verified. The abstract supports an ER assembly model, but the original Methods, constructs and exact postsynaptic-ER localization experiment were not inspected. Attempted publisher routes returned 403 and the inspected institutional repository restricted article and supplement. These access limits leave the particular donor localization claim unverified; they do not refute it or establish global unavailability.
The two incoming IBA rows use AN1/PTN002930507 in the actual PTHR46902 topology; both nodes are on the human AN10/PTN002508553 path. Literal descendant evidence is RGD:1309978 for receptor-level regulation and UniProtKB:Q9P0K9 for glutamate-signaling regulation. The human self donor is valid experimental grounding for an ancestral inference, not circularity. The full retained tree, alignment, AN/PTN lookup and literal IBD joins support this statement; a short donor list is not the reason for acceptance.
Current official mouse B1AXV0 and rat D3ZE85 records were joined by exact term to the incoming human transfers. Mouse complex binding and DIC binding trace to PMID:29276473. Rat receptor-level regulation traces to PMID:28675162. Mouse ER/postsynapse records trace to PMID:31604597; their donor-only extensions remain separate from the unextended human originals. The current mouse synapse row is electronic. A mouse plasma-membrane ISO record points back to human PR:Q9P0K9; this literal chain is neither independent human experimental confirmation nor proof of a historical circular error.
GO:0035255 identifies ionotropic glutamate receptor binding and supports the specific replacement for raw 0. Co-IP and selective coassembly justify receptor association without claiming purified binary affinity. GO:0045505 is more specific than association with DIC-positive vesicles; raw 1 remains unresolved. The single core combines receptor binding with the existing receptor-level process, glutamate-signaling regulation and ER membrane location. No equivalence or unverified ancestor relationship between the two process terms is asserted.
The precise biochemical assembly mechanism remains open. No folding, carrier-delivery, integral-scaffold, reductase, glycosyltransferase or channel-gating MF is substituted merely because FRRS1L is an assembly factor. No new assembly process annotation is proposed. Receptor-level regulation does not itself locate FRRS1L at a synapse. Postsynapse and broad synapse remain unresolved because the relevant later localization experiments were not accessible. Contextual plasma-membrane evidence is retained separately from the ER-centered core.
All eight publication caches and three PTHR46902 files are present and retain their native machine metadata. The two-row normal PAINT slice matches both incoming IBD assertions and their literal donors; the separately retained target topology establishes ancestry. Publication titles use the genuine fetched records. Cache availability is distinct from the actual selected reading described above: acquiring full text does not imply that every section, supplement or figure was read. The review adds no supporting-text quotation, natural alternative product or annotation. Manual primary research was used under the existing provider credential hold; no provider run is claimed. Actual checks and history outcomes are recorded in the notes.
For the two GO:0045202 synapse rows, the human IEA from GO_REF:0000044 and the human ISS from GO_REF:0000024 are different evidence routes. ISS is a curator-mediated sequence transfer, even though the current same-term mouse B1AXV0 row is itself electronic. Both remain UNDECIDED. The exact original/native indices are defined by index_scheme and the complete joins in the public evidence map.
The negative result in PMID:28675162 must be stated explicitly: its Results section “FRRS1l-containing AMPARs in brain neurons localize to the ER” and Figure 5 report 815/848 immunoparticles at ER membranes across 29 sampled rat neurons, with 33 at or near plasma membrane and no observed staining in the sampled synaptic compartment. The described distribution is mainly somatic/proximal-dendritic. Its immunohistochemistry Methods specify 3–4-week-old Wistar rats; electron-microscopy Methods separately name two Wistar rats without giving age in that sentence. These observations strongly favor ER localization in the inspected preparations. PMID:29276473 Figure 1F, neuronal immunocytochemistry Methods and Discussion report minor rather than absent PSD-95 overlap for expressed mouse HA-FRRS1L. Neither assay is a human endogenous localization experiment. The broad located_in annotation is nonexclusive and does not require dominant or constitutive residence; conversely, MARK_AS_OVER_ANNOTATED does not require proof of universal absence. The sampled negative and distinct partial-positive contexts leave the transferred scope unresolved. The still-uninspected PMID:31604597 donor experiment consequently matters to both postsynapse and its broader synapse location. The positive plasma-membrane observations are retained in their specific experimental contexts and do not imply that lack of signal in one preparation settles every other compartment.
The GO:0044877→GO:0035255 MODIFY names the identified receptor partner rather than asserting that the replacement is an is_a child of complex binding. The current UniProt SUBUNIT statement is by similarity to B1AXV0, including its direct-binding language; it is not a new human binary-binding experiment. Its separate FUNCTION statement has experimental provenance to PMID:27236917. That original was inspected externally at the selected Figure 4/Methods/Results scope recorded above, while its normal cache remains abstract-only. An optional in_complex addition of GO:0032281 is outside this focused amendment. The existing core already describes nascent ER receptor association; this does not imply that GO:0032281 excludes transient assemblies. Historical reference-sequence differences remain separate from natural isoforms.