COL6A3 encodes the alpha3 chain of collagen VI, an extracellular matrix protein with an extended array of N-terminal von Willebrand factor A domains, a short collagenous region and C-terminal globular domains. Long alpha3 products associate with alpha1 and alpha2 chains to form collagen VI units that assemble into dimers, tetramers and extracellular beaded microfibrils. Specific N- and C-terminal regions support higher-order assembly and matrix deposition. Human recombinant N-terminal domains bind heparin and hyaluronan. Proteolytic processing releases C-terminal fragments, including C5/endotrophin; experimentally studied fragments differ from the intact matrix chain. Alternative splicing produces five recorded human products, two of which lack the collagenous and C-terminal regions. Pathogenic COL6A3 variants cause collagen VI-related muscular dystrophies.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001527 microfibril | TAS PMID:16893474 Elastic fibres in health and disease. | ACCEPT | Summary: Collagen VI alpha3 is a constituent of extracellular beaded microfibrils. Reason: Retain the established microfibril location with direct alpha3 assembly and matrix-deposition support. The cited elastic-fibre review was available only as an abstract; its exact alpha3 passage remains unverified. The independent N5/C5 deletion studies support beaded collagen VI microfibrils, without identifying every short splice product as an incorporated chain. Supporting Evidence: PMID:11027693 cells that expressed alpha 3(VI) chains containing the N5 subdomain, alpha 3(VI) N9-C5, N6-C5, and N5-C5, formed microfibrils and deposited a collagen VI matrix. |
| GO:0004867 serine-type endopeptidase inhibitor activity | IEA GO_REF:0000002 | REMOVE | Summary: The native human C5 Kunitz fold does not justify this automatic inhibitor assignment. Reason: Current InterPro IPR002223 and IPR036880 map the fold to serine-type endopeptidase inhibitor activity. Original human recombinant C5 assays instead show no trypsin binding at 7 micromolar and no inhibition in peptide and nidogen-cleavage assays; engineered loop mutants and known inhibitors provide positive controls. This contradicts the electronic functional mapping at the tested native sequence. It neither negates all possible protease interactions nor claims that every splice product was tested. The successful engineered mutants are not native COL6A3 activity. Propagation Review Root cause: PROPAGATION BAD Sources checked: InterPro:IPR002223 SUPPORTS SOURCE BUT NOT TARGET The exact current InterPro record maps the Kunitz fold to GO:0004867, but native human C5 assays contradict that functional transfer under the tested conditions; fold membership itself is not disputed. InterPro:IPR036880 SUPPORTS SOURCE BUT NOT TARGET The exact current InterPro record maps the Kunitz fold to GO:0004867, but native human C5 assays contradict that functional transfer under the tested conditions; fold membership itself is not disputed. |
| GO:0005576 extracellular region | HDA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: Human aortic extracts contain the alpha3(VI) protein. Reason: Original Tables I-III identify CO6A3_HUMAN with 16, 164 and 57 unique peptides in NaCl, guanidine and SDS extracts, respectively. Actual extraction Methods and table headers were inspected. Retain extracellular detection without converting fraction identification into an isolated force, signaling or all-isoform assay. Supporting Evidence: |
| GO:0005576 extracellular region | HDA PMID:27068509 Extracellular matrix remodelling in response to venous hyper... | ACCEPT | Summary: Human-vein ECM analysis directly includes alpha3(VI). Reason: Actual human-vein extraction and MS Results were read. Figure 3 explicitly names CO6A3 and states that its spectral counts were scaled down fivefold for display. This supports the target-specific extracellular source link; it does not resolve each product or establish a separate regulatory mechanism. Supporting Evidence: |
| GO:0005576 extracellular region | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited extracellular-region assignment is consistent with direct target evidence. Reason: Current mouse Col6a3 alias resolution recovers a same-term IDA record, and the target itself has experimental extracellular records. This supports the present biological premise. The historical PAINT node/tree/MSA placement was not reconstructed; donor count and target self-inclusion are not treated as failures. The is_active_in qualifier is preserved without deriving an additional molecular activity from it. Propagation Review Root cause: NO FAILURE CORE Sources checked: MGI:MGI:88461 SUPPORTS TRANSFER Official MGI:88461-to-UniProt aliases resolve mouse Col6a3; current A0A087WS16!60049327 is a same-term IDA record from PMID:10444069. This is literal curator-record evidence, not a newly read original experiment. PANTHER:PTN002770434 UNRESOLVED Historical PAINT node/tree/MSA placement was not reconstructed; current descendant records do not establish the historical placement, and donor count/self-inclusion are not failure evidence. UniProtKB:P12111 SUPPORTS TRANSFER The target has current experimental extracellular records. Its self-inclusion is valid descendant evidence for PAINT, not circularity. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1564112 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: The degradation event places collagen VI outside cells as substrate material; MMP2, MMP9 and MMP11 perform the cleavage. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-1564112 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2089971 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: The secretion event connects ER-luminal collagen precursors with extracellular output; this row records the destination. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-2089971 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2213207 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: The network event explicitly describes collagen VI tetramers joining into beaded filaments and lateral associations. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-2213207 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2327695 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: The integrin event contains collagen VI within a broader collagen set; it does not isolate an alpha3-specific interface for every listed integrin. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-2327695 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2327909 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: Decorin association includes extracellular collagen VI material, without isolating an alpha3-decorin contact. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-2327909 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2466106 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: Biglycan association includes extracellular collagen VI material, without a purified alpha3-specific affinity measurement. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-2466106 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-375151 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: The NCAM1 summary names other collagen types, while its participant graph also reaches COL6A3 through a collagen set. The independently established extracellular location is retained without inventing an alpha3-NCAM1 assay. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-375151 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-382054 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: The PDGF event contains extracellular collagen material; it does not assign PDGF receptor activity or intracellular signaling to alpha3. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-382054 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-4084903 | ACCEPT | Summary: The event places COL6A3-containing material in the extracellular region. Reason: The alpha10beta1 event includes collagen VI and IX material, supporting extracellular location without identifying a universal alpha3-only integrin contact. The actual current summary and complete target-membership paths were inspected. This remains a location assertion. Supporting Evidence: Reactome:R-HSA-4084903 |
| GO:0005589 collagen type VI trimer | IEA GO_REF:0000117 | ACCEPT | Summary: Retain canonical alpha1/alpha2/alpha3 collagen VI trimer membership. Reason: The official term explicitly specifies the canonical three chains. Current ARBA00093710 matches COL6A3 through the exact FunFam condition set 000003/000004/000021 plus Metazoa; the separate PANTHER SF90 branch does not match the target SF13. Independent alpha3 assembly experiments support the complex. This does not establish incorporation of the two products lacking a collagenous region. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00093710 SUPPORTS TRANSFER Current exact target FunFam branch 000003/000004/000021 and Metazoa match; the alternative SF90 branch does not. Canonical complex biology is independently supported. |
| GO:0005589 collagen type VI trimer | TAS PMID:23869615 The expanded collagen VI family: new chains and new question... | ACCEPT | Summary: The family review supports the canonical collagen VI trimer. Reason: The selected full review describes alpha1/alpha2/alpha3 stoichiometry, intracellular assembly and extracellular beaded microfibrils. Its discussion of alternative long chains is distinguished from direct testing of every native combination or every modern alpha3 product. Supporting Evidence: |
| GO:0005589 collagen type VI trimer | TAS PMID:8782832 Type VI collagen mutations in Bethlem myopathy, an autosomal... | ACCEPT | Summary: Canonical alpha3 complex membership is retained with independent assembly evidence. Reason: The genuine Bethlem abstract concerns collagen VI-related myopathy and reports variants in alpha1 and alpha2 with prior linkage near alpha3. Its complete alpha3 text was not recovered. This does not justify a wrong-gene accusation or overturn established alpha3 trimer membership; direct alpha3 assembly sources independently support the term. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-1614460 | KEEP AS NON CORE | Summary: Retain the source-specific biosynthetic ER-lumen location. Reason: Dimerization of collagen VI precursor units is an intracellular luminal assembly stage. Actual event membership was traced to P12111. This transient precursor location is outside the principal mature extracellular structural core and does not assign collagen synthesis, transport or protease activity to the chain. Supporting Evidence: Reactome:R-HSA-1614460 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-1614461 | KEEP AS NON CORE | Summary: Retain the source-specific biosynthetic ER-lumen location. Reason: Tetramerization of collagen VI dimers occurs before secretion. Actual event membership was traced to P12111. This transient precursor location is outside the principal mature extracellular structural core and does not assign collagen synthesis, transport or protease activity to the chain. Supporting Evidence: Reactome:R-HSA-1614461 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-2022073 | KEEP AS NON CORE | Summary: Retain the source-specific biosynthetic ER-lumen location. Reason: The triple-helix event contains alpha3 as a structural chain being assembled; chaperones and isomerases perform their own activities. Actual event membership was traced to P12111. This transient precursor location is outside the principal mature extracellular structural core and does not assign collagen synthesis, transport or protease activity to the chain. Supporting Evidence: Reactome:R-HSA-2022073 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-2089971 | KEEP AS NON CORE | Summary: Retain the source-specific biosynthetic ER-lumen location. Reason: The secretion event has ER-luminal input and extracellular output at different stages; this row preserves the former. Actual event membership was traced to P12111. This transient precursor location is outside the principal mature extracellular structural core and does not assign collagen synthesis, transport or protease activity to the chain. Supporting Evidence: Reactome:R-HSA-2089971 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8944247 | KEEP AS NON CORE | Summary: Retain the source-specific biosynthetic ER-lumen location. Reason: The association event aligns collagen VI chains in the ER-luminal pathway before higher-order assembly. Actual event membership was traced to P12111. This transient precursor location is outside the principal mature extracellular structural core and does not assign collagen synthesis, transport or protease activity to the chain. Supporting Evidence: Reactome:R-HSA-8944247 |
| GO:0007517 muscle organ development | TAS PMID:8782832 Type VI collagen mutations in Bethlem myopathy, an autosomal... | UNDECIDED | Summary: The cited clinical source does not resolve the muscle-development assertion at the available access level. Reason: The authentic abstract establishes collagen VI-related myopathy, but does not establish what alpha3 itself does during progression of muscle from formation to maturity. Full original recovery was unsuccessful. Preserve the TAS assertion and positive disease context as UNDECIDED; neither clinical necessity alone nor an abstract naming other chains settles this source-specific process assignment. Supporting Evidence: |
| GO:0009749 response to glucose | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the inherited glucose-response context at the actual rat expression scope. Reason: The exact rat Col6a3 donor A0A8I6AHL9 carries GO:0009749 by IEP from PMID:8494053. Its complete abstract reports increased collagen VI-chain transcripts and fibrils in rat nerve connective-tissue cultures exposed to high glucose; observations in two human diabetic nerves are separate. The current definition includes gene-expression changes. Retain non-core response context, without asserting glucose sensing, metabolism or a human alpha3-specific intervention. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:A0A8I6AHL9 SUPPORTS TRANSFER Exact rat Col6a3 record254016058 carries response-to-glucose IEP from8494053; the complete abstract supports expression response, without reconstructing historical Compara internals. ensembl:ENSRNOP00000093441 UNRESOLVED The historical Ensembl mapping is not reconstructed; the paired current rat UniProt donor and its exact same-term IEP record are verified separately. Supporting Evidence: PMID:8494053 exposed to high glucose |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | ISS GO_REF:0000024 | ACCEPT | Summary: Retain the transferred collagen VI structural class. Reason: The exact porcine COL6A3 donor Q1T7A5 has the same structural term by RCA from cardiac ECM proteomics. The abstract and literal donor record were checked, but its exact target table was not recovered. Independent human alpha3 assembly evidence and the current collagen annotation comment support this class; the pig proteomics is not relabeled as an isolated tensile test in humans. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q1T7A5 SUPPORTS TRANSFER Exact porcine COL6A3 record58826684(RCA structural) or58826683(HDA ECM), selected by the source term, supports the ortholog premise; full target proteomics table was not recovered. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: Retain the established collagen VI structural class with the source-specific detection limits. Reason: Original aortic tables identify alpha3 in all three extracellular extraction fractions. The current GO:0030020 comment expressly permits extracellular matrix collagens. Direct alpha3 assembly/deposition evidence supports that class; proteomic classification alone is not an isolated longitudinal-force measurement. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: Retain the established collagen VI structural class with the source-specific detection limits. Reason: Original human colon/liver workbook sheets A and B both contain the same COL6A3 protein group at row95. These are two views of one dataset, not independent experiments or isoform-resolved detection. The current GO:0030020 comment expressly permits extracellular matrix collagens. Direct alpha3 assembly/deposition evidence supports that class; proteomic classification alone is not an isolated longitudinal-force measurement. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: Retain the established collagen VI structural class with the source-specific detection limits. Reason: Original human atrial Methods and Table1 identify alpha3(VI) in GuHCl input, glycoprotein enrichment and glycopeptide detection. The current GO:0030020 comment expressly permits extracellular matrix collagens. Direct alpha3 assembly/deposition evidence supports that class; proteomic classification alone is not an isolated longitudinal-force measurement. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: Retain the established collagen VI structural class with the source-specific detection limits. Reason: Original human cell-derived ECM Methods and Table1 classify COL6A1/2/3 together as beaded-filament collagen VI. The grouped entry is not individual-chain quantitation. The current GO:0030020 comment expressly permits extracellular matrix collagens. Direct alpha3 assembly/deposition evidence supports that class; proteomic classification alone is not an isolated longitudinal-force measurement. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: Retain the established collagen VI structural class with the source-specific detection limits. Reason: The selected source contains authentic human-tissue extraction comparisons and Results, but attempted supplementary spreadsheets were HTML challenges. Its exact alpha3 target row remains unverified. The current GO:0030020 comment expressly permits extracellular matrix collagens. Direct alpha3 assembly/deposition evidence supports that class; proteomic classification alone is not an isolated longitudinal-force measurement. |
| GO:0031012 extracellular matrix | HDA PMID:20551380 Proteomics characterization of extracellular space component... | ACCEPT | Summary: Human aortic proteomics directly identifies alpha3 in extracellular matrix extracts. Reason: All three original target table rows and extraction Methods were inspected. The 16/164/57 unique-peptide counts support matrix-fraction detection, not an alpha3-specific vascular signaling process or equal detection of all five products. Supporting Evidence: |
| GO:0031012 extracellular matrix | HDA PMID:23658023 Comparative proteomic analysis of supportive and unsupportiv... | ACCEPT | Summary: Human placental stromal-cell matrices contain alpha3(VI). Reason: Original Table1 identifies COL6A3 in hPSF and immortalized hPSF ECM at normalized counts 1.25 and 8.41; all four mouse feeder columns and HUES1 are ND. Actual culture and matrix-denudation Methods were read. Retain human placental stromal-cell ECM detection without claiming ESC-matrix positivity or target-specific stem-cell induction. Supporting Evidence: |
| GO:0031012 extracellular matrix | HDA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: Retain extracellular matrix localization at the inspected sample and source scope. Reason: Original human colon/liver workbook sheets A and B both contain the same COL6A3 protein group at row95. These are two views of one dataset, not independent experiments or isoform-resolved detection. This is consistent with direct alpha3 matrix-deposition evidence; any unrecovered source-specific target table is explicitly distinguished from independent support. |
| GO:0031012 extracellular matrix | HDA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: Retain extracellular matrix localization at the inspected sample and source scope. Reason: Original human atrial Methods and Table1 identify alpha3(VI) in GuHCl input, glycoprotein enrichment and glycopeptide detection. This is consistent with direct alpha3 matrix-deposition evidence; any unrecovered source-specific target table is explicitly distinguished from independent support. |
| GO:0031012 extracellular matrix | HDA PMID:28327460 Comprehensive proteomic characterization of stem cell-derive... | ACCEPT | Summary: Retain extracellular matrix localization at the inspected sample and source scope. Reason: Original human cell-derived ECM Methods and Table1 classify COL6A1/2/3 together as beaded-filament collagen VI. The grouped entry is not individual-chain quantitation. This is consistent with direct alpha3 matrix-deposition evidence; any unrecovered source-specific target table is explicitly distinguished from independent support. |
| GO:0031012 extracellular matrix | HDA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: Retain extracellular matrix localization at the inspected sample and source scope. Reason: The selected source contains authentic human-tissue extraction comparisons and Results, but attempted supplementary spreadsheets were HTML challenges. Its exact alpha3 target row remains unverified. This is consistent with direct alpha3 matrix-deposition evidence; any unrecovered source-specific target table is explicitly distinguished from independent support. |
| GO:0031012 extracellular matrix | IDA PMID:18400749 Three novel collagen VI chains, alpha4(VI), alpha5(VI), and ... | ACCEPT | Summary: The original study directly localizes human alpha3(VI) in extracellular matrix. Reason: Results and Figure7 explicitly use alpha3-specific 3C4 monoclonal staining in human skeletal muscle, cardiac muscle, lung and liver, with antibody controls. Preserve this target-specific IDA; it is not inferred from the paper title or transferred from its engineered alternative-chain assembly assays. No new figure-pixel or all-product claim is made. Supporting Evidence: |
| GO:0031012 extracellular matrix | ISS PMID:22261194 Proteomics analysis of cardiac extracellular matrix remodeli... | ACCEPT | Summary: Retain the porcine-to-human extracellular matrix transfer. Reason: Exact Q1T7A5 is porcine COL6A3 and carries the same ECM term by HDA/colocalizes_with from the cited cardiac proteomics source. The genuine abstract and literal record support the transfer premise. No newly inspected pig target-table row or human alpha3 intervention is claimed; human matrix evidence independently supports the location. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:Q1T7A5 SUPPORTS TRANSFER Exact porcine COL6A3 record58826684(RCA structural) or58826683(HDA ECM), selected by the source term, supports the ortholog premise; full target proteomics table was not recovered. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: Preserve alpha3 detection in a human urinary exosome preparation as non-core. Reason: The original public NHLBI companion database row287 assigns one peptide to COL6A3, historical isoform5/RefSeq NP_476508, and explicitly cites this study. Actual pooled-urine isolation/MS Methods were read. This positive historical protein assignment is retained without equating its isoform label to current P12111-5, asserting a unique peptide sequence that was not recovered, or assigning vesicle biogenesis. Supporting Evidence: |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | UNDECIDED | Summary: The exact COL6A3 target entry in the EPS-urine exosome study remains unverified. Reason: The selected full article describes pooled prostate-cancer/control EPS-urine exosome proteomics and possible soluble extracellular contaminants. Genuine supplementary-file requests returned HTML challenges, not readable spreadsheets, so the source-specific alpha3 row could not be inspected. Preserve the HDA assertion as UNDECIDED; independent urinary or CSF detection does not substitute for this missing target record. Supporting Evidence: |
| GO:1903561 extracellular vesicle | HDA PMID:24769233 Proteomic analysis of cerebrospinal fluid extracellular vesi... | KEEP AS NON CORE | Summary: Retain positive human CSF extracellular-vesicle fraction detection. Reason: Original PXD000608 MaxQuant proteinGroups row315 identifies a COL6A3 group containing P12111, P12111-2, P12111-3 and legacy entries. It reports 70 group-unique peptides, 55 and 56 in the two EV pools, and 14 and 4 in the matched supernatants, with no reverse/contaminant flag. The parameters specify 1% peptide and protein FDR. This supports fraction detection without resolving all products, vesicle topology or a vesicle-production function. Supporting Evidence: |
| GO:0008201 heparin binding | IDA PMID:1425570 Structure of recombinant N-terminal globule of type VI colla... | NEW | Summary: Human alpha3 N-terminal domains bind heparin. Reason: Original human recombinant N9-N2 affinity chromatography and domain mapping demonstrate heparin binding; N9/N6/N3-derived fragments bind while N4/N5/N7 fragments do not. The measured interaction is salt-sensitive; the tested large basement-membrane heparan-sulfate proteoglycan was not an active ligand. This IDA is scoped to the sequence-defined historical N-terminal preparation, not every complete modern product, a native heparan-sulfate complex or a new signaling process. Current typed coverage has no seed or co-proposed ancestor/descendant and no more-specific child. Supporting Evidence: PMID:1425570 Fragment N9-N2 showed binding to heparin |
| GO:0005540 hyaluronic acid binding | IDA PMID:1425570 Structure of recombinant N-terminal globule of type VI colla... | NEW | Summary: Human alpha3 N-terminal domains bind hyaluronan. Reason: The same authentic human recombinant N9-N2 study directly tests hyaluronan affinity chromatography, with bound material resisting high salt and requiring urea for most elution. This supports a distinct ligand-binding MF at the tested N-terminal construct scope; it does not establish a measured binding site in every splice product or a physiological receptor mechanism. Current typed coverage has no seed or co-proposed ancestor/descendant and no more-specific child. Supporting Evidence: PMID:1425570 N9-N2 showed strong binding to hyaluronan |
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Download this section (compressed HTML)Q: Which native assemblies or matrix functions, if any, contain the two short alpha3 products lacking the collagenous and C-terminal regions?
Q: How should GO microfibril assembly distinguish the directly demonstrated collagen VI interfaces from the current fibrillin-associated annotation convention?
Q: Does sequence-defined human free C5 reproduce the mouse endothelial migration response, and what receptor or relay and directional-migration mechanism mediates it?
Q: How do the N-terminal heparin and hyaluronan interactions change after native collagen VI assembly and alpha3 processing?
Experiment: Compare all five sequence-defined human products with alpha1/alpha2 using pulse-chase secretion, chain-specific peptides and matrix electron microscopy.
Hypothesis: Products retaining the collagenous/C-terminal regions differ from the two short products in incorporation and beaded-microfibril assembly.
Experiment: Test purified sequence-defined human C5 alongside the published mouse construct in concentration-gradient and checkerboard migration assays, with matched fold/purity controls.
Hypothesis: Fragment sequence, processing state or an indirect relay determines the migration response independently of the disputed ANTXR-binding model.
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