This review preserves the genuine 59-assertion seed, all 37 original reference identities and findings, and the absence of alternative-product records. Nine genuine load-bearing publications were added, giving 46 references. The official human product is P12109, 1,028 residues, with signal peptide 1–19 and mature chain 20–1028. No alternative product is invented. The fetched GOA, UniProt, family files, selected publication caches and Reactome files remain immutable.
The genuine default Falcon research attempt ended in a timeout; the configured Perplexity Lite fallback returned a 401 quota error. These are manual research notes; no provider-generated report is claimed.
Alpha1(VI) contributes structure to collagen VI trimers and beaded extracellular microfibrils. The core describes extracellular matrix structural contribution (GO:0005201), in canonical collagen VI trimers (GO:0005589), located in the extracellular matrix (GO:0031012). Existing GO:0030020 annotations follow the official collagen convention, but the author-chosen core does not assert a mechanically measured tensile property. Beaded collagen VI microfibrils are described biologically without requiring identity with the fibrillin/MFAP-focused GO:0001527 definition. No NEW annotation or additional process is proposed. PMID:2551668(https://pubmed.ncbi.nlm.nih.gov/2551668/) and PMID:23869615(https://pubmed.ncbi.nlm.nih.gov/23869615/).
The original 1989 sequence work uses human fibroblast/placental cDNA and amnion peptides. Its two C-terminal variants concern alpha2(VI), not alpha1(VI). Original scans were read by the independent core reviewer; canonical stoichiometry is contextual knowledge in that source. The 2008 experiment uses endogenous human alpha1/alpha2 in SaOS-2 cells with an engineered mouse alpha4 N6–C2 construct. It directly supports secreted disulfide-linked association of the tested alpha1/alpha2/alpha4 combination. Therefore row49 is refined from generic protein complex to GO:0140158, the VWA-rich collagen trimer class, rather than forcing the strictly alpha1/alpha2/alpha3 GO:0005589 definition. The experiment does not establish a native human alpha1/alpha2/alpha4 extracellular microfibril. PMID:18400749(https://pubmed.ncbi.nlm.nih.gov/18400749/).
The 1994 isolated human-chain experiments distinguish alpha1 and alpha2 ligand behavior. Alpha2, unlike alpha1, binds the tested perlecan/fibronectin/pepsin-VI preparations in the separate solid-phase assays. Both chains bind heparin-Sepharose; that purification observation is not treated as a universal negative or used to manufacture a NEW heparin annotation. Isolated non-triple-helical chains do not refute multichain coassembly. A listed erratum text was not recovered, so no correction scope is claimed. PMID:8168508(https://pubmed.ncbi.nlm.nih.gov/8168508/).
Three original IPI assertions were traced. Two exact current 42-field records support the COL9A1/COL6A1 association; the two 18400749 source assertions have no matching current pair in the bounded query, but original positive experiments independently support them. The BioPlex records map the canonical human products and use anti-tag co-IP/affinity purification in 293T and HCT116 cells. This supports co-complex association, not necessarily direct binary contact. The generic interaction is retained as KEEP_AS_NON_CORE. Partner identity does not identify which component makes a collagen-binding contact. The ClinGen curation instructions explicitly retain supported generic binding when no evidence-backed specific replacement is established. PMID:33961781(https://pubmed.ncbi.nlm.nih.gov/33961781/).
The original hMSC-TERT study uses calcitriol induction and a carbonate-treated membrane fraction. COL6A1 abundance rises, while the displayed collagen immunofluorescence is type I, not VI. Row30 retains genuine fraction association as non-core; row2 is MARK_AS_OVER_ANNOTATED because abundance during induction does not resolve the specific differentiation contribution. The endoderm study similarly measures COL6A1 expression but its collagen intervention screen uses I, III, IV and V. Row50 is MARK_AS_OVER_ANNOTATED while preserving the positive expression observation and a possible matrix contribution. PMID:16210410(https://pubmed.ncbi.nlm.nih.gov/16210410/), PMID:23154389(https://pubmed.ncbi.nlm.nih.gov/23154389/).
The broad tissue/morphogenesis assertions remain contextual, but row39 cell differentiation remains UNDECIDED: actual airway-cell spreading/barrier maturation does not resolve acquisition of a specialized fate, and the lung-study authors explicitly leave developmental ontogeny unresolved. Structural participation could qualify; no intrinsic fate-controller requirement is imposed. The skeletal-muscle IBA is judged as ancestral placement, not a donor vote. Official MGI mouse and ZFIN zebrafish identifiers resolve to Col6a1/col6a1, with current direct same-term records. Mouse autophagy/myofiber and zebrafish muscle perturbation/rescue studies support matrix-dependent muscle biology; they do not give collagen an autophagy catalytic activity. The historical PAINT tree/node was not reconstructed. PMID:21037586(https://pubmed.ncbi.nlm.nih.gov/21037586/), PMID:34992716(https://pubmed.ncbi.nlm.nih.gov/34992716/).
PDGF binding is positively reported for type VI and constituent chains in the complete authentic original abstract. The pooled affinity range and unspecified preparation species are not turned into a human alpha1(VI)-specific constant. This ligand context stays non-core. PMID:8900172(https://pubmed.ncbi.nlm.nih.gov/8900172/).
The lysosome assertion is retained as cargo context. Actual human RPE1/patient-fibroblast uptake and bafilomycin experiments support lysosomal degradation. The gifted uptake tetramers have unspecified species; the separate binding reagent is explicitly pepsinized human-tissue collagen VI. These reagents are not conflated. PMID:28604699(https://pubmed.ncbi.nlm.nih.gov/28604699/).
The lysosomal-membrane proteomics study identifies human placental COL6A1-associated peptides and discusses terminal-domain/degradation material. Positive fraction presence remains non-core, without integral topology. The captured target row lacks complete column headers, so its unlabeled numeric columns are not interpreted. PMID:17897319(https://pubmed.ncbi.nlm.nih.gov/17897319/).
Actual mouse bronchial epithelial immunogold and secretion work supports WT vesicular collagen VI, with KO accumulation and tested mouse Col6a1-GFP secretion. Row57 retains this real intracellular cargo location. In contrast, the SR donor source shows organelle dilation after knockout and the myofibril source measures tropomyosin oxidation/MAO/contractile damage. These positive pathology findings were overextended into specific protein locations. The human electronic transfers in rows31/32 are removed because the affected organelle or contractile apparatus is not established as a collagen VI site. Broad ER/ER-lumen assembly and observed intracellular cargo locations remain separately supported. PMID:24357721(https://pubmed.ncbi.nlm.nih.gov/24357721/), PMID:22024752(https://pubmed.ncbi.nlm.nih.gov/22024752/), PMID:20716577(https://pubmed.ncbi.nlm.nih.gov/20716577/).
Sarcolemma has an explicit covering basement-membrane/collagen-network definition. The mouse source is preserved at abstract/current-donor scope, without claiming an independently inspected COL6A1 image or plasma-membrane insertion. Broad ER and ER-lumen assignments concern precursor modification/assembly before secretion and remain non-core locations. PMID:16810681(https://pubmed.ncbi.nlm.nih.gov/16810681/).
Actual target records were read from the original human-aortic Table II, feeder-matrix Table1, and two views of the human colon/liver workbook. The feeder table detects COL6A1 in hPSF/ihPSF, while HUES1 MS is ND. Original human-atrial Table1 marks alpha1(VI) positive in GuHCl input and glycopeptide analysis, with the glycoprotein-enrichment column blank. Cell-derived ECM Table1 groups COL6A1/2/3; it does not individually quantify each alpha chain. PMID:20551380(https://pubmed.ncbi.nlm.nih.gov/20551380/), PMID:23658023(https://pubmed.ncbi.nlm.nih.gov/23658023/), PMID:25037231(https://pubmed.ncbi.nlm.nih.gov/25037231/), PMID:27559042(https://pubmed.ncbi.nlm.nih.gov/27559042/), PMID:28327460(https://pubmed.ncbi.nlm.nih.gov/28327460/).
Original human vein Figure3 text explicitly names CO6A1; scaling intensity down fivefold is a plotting convention, not a biological fold change. Genuine full HTML also recovered actual tissue-proteomics and urinary/salivary/EPS-vesicle Methods. Exact supplementary target rows for the latter studies remain uninspected: nominal XLS/XLSX downloads are preserved HTML challenge responses, not workbooks. This limitation is confined to target-table verification rather than falsely claiming unavailable full Methods. Existing positive curator observations remain scoped non-core exosome detections. PMID:27068509(https://pubmed.ncbi.nlm.nih.gov/27068509/), PMID:28675934(https://pubmed.ncbi.nlm.nih.gov/28675934/), PMID:19056867(https://pubmed.ncbi.nlm.nih.gov/19056867/), PMID:19199708(https://pubmed.ncbi.nlm.nih.gov/19199708/), PMID:23533145(https://pubmed.ncbi.nlm.nih.gov/23533145/).
All 13 current Reactome summaries and actual target paths were inspected. Degradation distinguishes substrate collagen from metalloproteinases; ER association/dimerization/tetramerization distinguishes structural assembly from modifying enzymes; secretion bridges precursor and extracellular stages. Broad collagen-set ligand events do not demonstrate every isolated alpha-chain contact. The NCAM summary foregrounds other types while the graph reaches COL6A1; extracellular location is retained without adding a direct NCAM-binding claim. No NEW process is inferred from pathway membership. The cached GO-CAM index is checked at its authenticated bytes.
The revised actions distinguish three kinds of evidence. Mouse muscle pathology supports matrix-dependent muscle homeostasis, but not a human collagen-chain location in the myofibril or sarcoplasmic reticulum. Positive BioPlex co-complex association supports non-core generic binding; it does not establish the specific collagen contact. Differentiation-associated expression is a real observation, but its conversion into a specific differentiation function is over-annotation while the matrix contribution remains unresolved. These changes supersede the initial action choices without changing the experimental observations or manufacturing a negative biological result.
ARBA00027429 condition set 214 matches all three recorded human COL6A1 FunFams (3.40.50.410:FF:000026, :000050 and :000060). The published rule match verifies provenance. It does not add a COL6A1-specific mechanistic differentiation experiment. The broad transfer remains UNDECIDED: its historical premise is unavailable, and it is not necessarily confined to the two expression studies. Positive matrix effects leave a differentiation contribution unresolved, without proving either the transferred function or its over-annotation. ARBA00027429, PMID:31837950(https://pubmed.ncbi.nlm.nih.gov/31837950/).
The assembly evidence supports an integrated extracellular structural role and anchoring context. Core GO:0005201 and GO:0031012 express that demonstrated role directly. Existing source annotations to the more specific tensile-strength and microfibril terms are retained at their separately assessed scopes. Open questions concern how induced collagen VI contributes to osteoblast/endoderm differentiation and how native chain combinations distribute mechanical and ligand-retention roles. PMID:22024752(https://pubmed.ncbi.nlm.nih.gov/22024752/), PMID:16210410(https://pubmed.ncbi.nlm.nih.gov/16210410/), PMID:23154389(https://pubmed.ncbi.nlm.nih.gov/23154389/).