The exact selected A1Z8G0 is Metro isoform A (595 residues), with two L27 domains, PDZ, SH3, and a guanylate-kinase-like domain. PMID:20427642(https://pubmed.ncbi.nlm.nih.gov/20427642/) directly identifies junctional localization and L27-dependent DlgS97/DLin-7 complex organization: “Metro stabilizes junctional DlgS97 in a complex with the highly conserved adaptor protein DLin-7.” These findings validate the broad cell-junction prediction (LSP relative to cell-cell junction). The standard cache is abstract-only. The author-institution full PDF was retrieved from https://publications.mpi-cbg.de/Bachmann_2010_4293.pdf and retained with unmodified pdftotext extraction in metro-publication-artifacts. Figure2G explicitly places Metro in the SSR, so the gene-level IDA is accepted. The paper reports Metro-B556aa as the predominant muscle form; the selected A595aa retains the same named scaffold domains. The reproducible target-specific analysis identifies Pro422/His488 at conserved GMP-pocket sites and a remodeled ATP loop, with two independent alignments and active-enzyme/MAGUK controls. Primary mutagenesis and MPP-family structural work support an enzyme-to-scaffold transition. Consequently the electronic kinase and transferase annotations are removed; nucleotide/ATP binding remain separate unresolved questions. No generic MAGUK domain is counted as proof of kinase activity.
The selected frozen UniProt record is retained in metro-uniprot-source.json, with the complete original prediction metadata in metro-predictions-source.json. It maps the exact accession to this FlyBase gene; current sequence identity does not establish the historical predictor input. Gene-level experiments support conserved functions unless a relevant isoform difference is established. Falcon research was requested with perplexity-lite fallback alongside publication caching. Primary publications and sequence observations, rather than AI summaries or ARBA assertions, support the curated conclusions.
Falcon report read: it correctly identifies the scaffold complex, the experimentally predominant Metro-B isoform and SSR localization. Its lack-of-catalysis caveat is retained as a knowledge gap; no bare report verdict is used to prove catalytic inactivity.
The catalytic inference uses primary comparator studies PMID:12482754(https://pubmed.ncbi.nlm.nih.gov/12482754/) and PMID:22117215(https://pubmed.ncbi.nlm.nih.gov/22117215/), with exact Metro residue observations. It does not require a separate Metro enzyme assay to recognize the established family transition, and does not assert absence of all residual chemistry.