COL7A1 encodes the alpha1 chain of collagen VII, the principal structural protein of anchoring fibrils at epithelial basement membranes. Three alpha1(VII) chains form a long interrupted triple helix flanked by NC1 and NC2 regions. NC1 binds matrix ligands, including fibrillar collagen I, collagen IV and laminin 332; C-terminal interactions organize antiparallel assemblies that mature into anchoring fibrils linking the basement membrane to underlying connective tissue. Human skin and reconstituted matrix experiments support this mechanical attachment function. Pathogenic variants cause dystrophic epidermolysis bullosa, with fragile dermal–epidermal adhesion. The two annotated splice products differ by a 32-residue segment in the collagenous region; their individual assembly and binding properties have not been comprehensively compared.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0004867 serine-type endopeptidase inhibitor activity | IEA GO_REF:0000002 | REMOVE | Summary: The Kunitz-like region does not establish the transferred protease-inhibitor activity. Reason: Both cited InterPro entries genuinely carry the inhibitor mapping, but original human NC2/COL experiments contradict that transfer: the recombinant segment did not inhibit trypsin or chymotrypsin at the tested excesses, whereas aprotinin protected the substrate. Collagenase-isolated NC2 was also reported inactive, and thrombin/plasmin negatives were reported without displayed data. Remove this automatic activity inference without adding a universal NOT assertion or claiming that every protease, processed form or splice product was tested. The same region has positive assembly evidence. The public source-evidence index gives the original assay excerpt, construct composition, controls and external full-text access route; the preserved PMID cache remains abstract-only. Propagation Review Root cause: PROPAGATION BAD Sources checked: InterPro:IPR002223 SUPPORTS SOURCE BUT NOT TARGET The actual domain entry maps inhibitor activity, but target-specific NC2 assays contradict this automatic functional transfer at the tested scope. InterPro:IPR036880 SUPPORTS SOURCE BUT NOT TARGET The actual domain entry maps inhibitor activity, but target-specific NC2 assays contradict this automatic functional transfer at the tested scope. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19269366 TANGO1 facilitates cargo loading at endoplasmic reticulum ex... | KEEP AS NON CORE | Summary: Preserve the positive human MIA3 interaction as non-core binding. Reason: Two complete current IntAct records preserve co-immunoprecipitation and pull-down evidence for COL7A1–MIA3 from PMID:19269366, with exact reference-sequence ROGIDs. The reported MIA3 45–107 boundary is curator-inferred, not a paper-specified construct. A later structural study identifies this cargo-recognition region as the distinct MOTH domain family and explains the omitted terminal extensions; it does not justify forcing a SH3-domain-binding refinement. Absent classical PPII recognition is supporting context, not a requirement added to the GO definition. Retain the positive generic assertion under the supported-binding exception, without assigning MIA3 cargo-receptor activity to COL7A1 or relabeling the later collagen-IV assay as a COL7A1 experiment. |
| GO:0005576 extracellular region | HDA PMID:22664934 Comparison of tear protein levels in breast cancer patients ... | KEEP AS NON CORE | Summary: Original tear-fluid proteomics explicitly identifies COL7A1. Reason: Table II of the original human tear study contains CO7A1_HUMAN/COL7A1. Preserve extracellular detection as non-core sample context; the study pooled tear specimens for parts of its workflow, so this row does not establish a COL7A1-specific disease difference or a separate tear function. Supporting Evidence: |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1454757 | ACCEPT | Summary: Extracellular collagen fragments occur in a gelatin-degradation event. Reason: COL7A1-labelled fragments are represented in the inspected event graph. The MMPs perform proteolysis; this is a location assertion for substrate material, not a COL7A1 protease activity. Supporting Evidence: Reactome:R-HSA-1454757 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-1564120 | ACCEPT | Summary: Collagen VII is extracellular substrate in its degradation event. Reason: The actual event summary names collagen VII degradation by MMP1, MMP2 and MMP3, with target-labelled paths. Preserve extracellular location without assigning the enzymes’ cleavage activity to their substrate. Supporting Evidence: Reactome:R-HSA-1564120 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2089971 | ACCEPT | Summary: The secretion event places collagen VII products outside the cell. Reason: The inspected event connects ER-luminal precursors with extracellular output. This source object concerns the mature destination; it does not make COL7A1 secretion machinery. Supporting Evidence: Reactome:R-HSA-2089971 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2213192 | ACCEPT | Summary: The hemidesmosome-associated matrix model includes extracellular collagen VII material. Reason: The actual input names a collagen VII–laminin 332 complex; the event summary principally describes collagen XVII and integrin machinery. Preserve the collagen VII extracellular assertion without conflating the two collagen chains or claiming a newly reconstructed complete participant subgraph. Supporting Evidence: Reactome:R-HSA-2213192 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2213195 | ACCEPT | Summary: Anchoring-fibril formation places collagen VII in extracellular assemblies. Reason: The actual source describes antiparallel assembly followed by C-propeptide removal and lateral aggregation. COL7A1 contributes structure; BMP1 performs cleavage. Retain the extracellular location at this assembly stage. Supporting Evidence: Reactome:R-HSA-2213195 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2214324 | ACCEPT | Summary: Collagen VII dimerization is an extracellular structural assembly step. Reason: Actual event inputs and outputs identify collagen VII trimers and higher-order material. The current summary contains an amino-terminal wording inconsistency for the NC2 end; original target literature identifies NC2 as C-terminal. Preserve the source unchanged while using the experimentally supported orientation. Supporting Evidence: Reactome:R-HSA-2214324 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2214330 | ACCEPT | Summary: The BMP1 cleavage event contains extracellular collagen VII. Reason: The genuine summary states C-terminal NC2 processing of human procollagen VII by BMP1 and related enzymes. Retain substrate location, without assigning proteolytic catalysis to COL7A1. Supporting Evidence: Reactome:R-HSA-2214330 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2327733 | ACCEPT | Summary: Fibronectin association includes extracellular collagen VII material. Reason: The actual summary names collagen VII among FN1-binding collagens and the saved graph reaches target-labelled species. This supports location, not every listed collagen’s identical affinity or a new fibronectin-specific activity assertion. Supporting Evidence: Reactome:R-HSA-2327733 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2396234 | ACCEPT | Summary: Collagen VII matrix associations support extracellular localization. Reason: The actual event describes collagen VII binding to laminin 332, collagen IV and banded fibrils. Independent direct primary experiments support these matrix interactions; no direct integrin interaction is inferred from laminin bridging. Supporting Evidence: Reactome:R-HSA-2396234 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-3787997 | ACCEPT | Summary: Laminin 332 association occurs at the extracellular collagen VII NC1 region. Reason: The actual summary and input/output entities support extracellular matrix association. Original purified human NC1 experiments distinguish laminin binding from other matrix contacts and from cell-surface receptor activity. Supporting Evidence: Reactome:R-HSA-3787997 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-4086216 | ACCEPT | Summary: The integrin-association model contains extracellular collagen VII. Reason: The curated event names NC1 association with alpha2beta1 and a primary source not independently reread here. Preserve this location assertion without manufacturing an additional integrin-binding NEW from a pathway summary alone. Supporting Evidence: Reactome:R-HSA-4086216 |
| GO:0005590 collagen type VII trimer | IEA GO_REF:0000117 | ACCEPT | Summary: Retain the independently established collagen VII homotrimer. Reason: The exact current ARBA00098055 endpoint returned 404, so its present rule conditions were not recovered and no historical mapping failure is inferred. Human recombinant assembly evidence and the explicit alpha1(VII) homotrimer entry in the collagen-family review independently support the complex identity. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00098055 UNRESOLVED Current official endpoint returned 404; original rule identity preserved. This is not proof of historical failure or a denial of the independently established homotrimer. |
| GO:0005590 collagen type VII trimer | NAS PMID:29853175 Collagen Fibril Assembly and Function. | UNDECIDED | Summary: The exact type-VII premise of this NAS source remains unresolved. Reason: The genuine PMID:29853175 abstract discusses fibril assembly generally, and its target-specific full passage was not recovered. Preserve the source assertion as undecided rather than infer misattribution from its broad title or deny the independently established collagen VII homotrimer. Supporting Evidence: |
| GO:0005590 collagen type VII trimer | TAS PMID:21421911 The collagen family. | ACCEPT | Summary: The original review table explicitly lists the collagen VII homotrimer. Reason: Actual archived Table 1 identifies collagen VII, alpha1(VII), and three alpha1(VII) chains. Retain the type-VII trimer assertion, distinguishing that directly inspected review entry from the unchanged abstract-only cache and from a new experimental measurement. |
| GO:0005590 collagen type VII trimer | TAS PMID:9375848 Molecular basis of dystrophic epidermolysis bullosa: mutatio... | ACCEPT | Summary: Retain collagen VII homotrimer membership with independent assembly support. Reason: The cited clinical abstract identifies type VII collagen as the principal anchoring-fibril protein, while independent human assembly and sequence evidence establishes the homotrimer. The original clinical full text was not recovered; no new trimer experiment is attributed to that abstract. |
| GO:0005604 basement membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Retain inherited basement-membrane/interface localization. Reason: Exact current mouse Col15a1 and Col7a1 identities have same-term experimental localization records, and independent human anchoring-complex experiments support the target location. Historical PAINT node placement and MSA were not reconstructed. Neither donor count nor the presence of a target-like donor is evidence of propagation failure. Propagation Review Root cause: NO FAILURE CORE Sources checked: MGI:MGI:88449 SUPPORTS TRANSFER Exact current identity and same-term curator records include IBA, IDA. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. MGI:MGI:88462 SUPPORTS TRANSFER Exact current identity and same-term curator records include IBA, IDA, IEA. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. PANTHER:PTN002770818 UNRESOLVED Historical PAINT node/tree/MSA placement remains uninspected; current descendant records do not reconstruct that judgment, and no donor-count or self-source failure is inferred. |
| GO:0005604 basement membrane | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt subcellular mapping agrees with the basement-membrane interface. Reason: SL-0025 is a location vocabulary source, not a donor protein. Current official target localization and human matrix experiments support basement-membrane-associated anchoring fibrils; the term does not require insertion into a lipid bilayer. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0025 SUPPORTS TRANSFER This is the official subcellular-location vocabulary mapping, not a donor organism. Target localization and direct matrix evidence support the mapped term. |
| GO:0005604 basement membrane | TAS PMID:9375848 Molecular basis of dystrophic epidermolysis bullosa: mutatio... | ACCEPT | Summary: The clinical source places collagen VII at the cutaneous basement-membrane zone. Reason: The complete original abstract explicitly describes tissue separation below the lamina densa at anchoring fibrils. Retain this structural-interface location with independent human matrix evidence, without converting disease severity into another molecular activity. |
| GO:0005788 endoplasmic reticulum lumen | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Retain ER-luminal precursor localization as non-core biosynthetic context. Reason: ARBA00028691 currently matches the target through its InterPro/Hominidae and FunFam/Homo branches. The original MIA3 abstract and exact interaction records independently place collagen VII cargo on the luminal side of the secretory pathway. This precursor location is distinct from the mature extracellular structural core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: ARBA:ARBA00028691 SUPPORTS TRANSFER Current exact InterPro/Hominidae and FunFam/Homo condition branches match; independent secretory-cargo evidence supports the luminal precursor location. Supporting Evidence: |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-2022073 | KEEP AS NON CORE | Summary: Procollagen triple-helix formation places the precursor in the ER lumen. Reason: The event describes ER folding initiated at collagen C termini. Retain the inherited COL7A1 precursor location as biosynthetic context; the event summary is general collagen biology, and the bounded graph did not establish a complete target-reference path. COL7A1 is the chain being assembled, not the chaperone or isomerase. Supporting Evidence: Reactome:R-HSA-2022073 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-203973 | KEEP AS NON CORE | Summary: ER budding retains a luminal cargo context for the collagen precursor. Reason: The budding summary describes SAR1-dependent vesicle release without naming COL7A1. Retain the inherited ER-luminal cargo location, supported by independent collagen VII secretion evidence, as non-core context. Incomplete participant expansion prevents claiming a newly traced COL7A1 path. Supporting Evidence: Reactome:R-HSA-203973 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-204008 | KEEP AS NON CORE | Summary: Outer-coat and v-SNARE recruitment provides an ER-export context. Reason: This source describes SEC13/SEC31 recruitment and v-SNARE incorporation, not a COL7A1-specific assay. Retain the inherited luminal precursor location without assigning coat or SNARE activity; its target membership was not fully reconstructed from the partial graph. Supporting Evidence: Reactome:R-HSA-204008 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-2089971 | KEEP AS NON CORE | Summary: Collagen secretion distinguishes ER precursor input from extracellular output. Reason: The collagen-secretion summary explicitly separates ER processing from extracellular secretion. Retain the ER-luminal stage as non-core precursor context, distinct from the mature anchoring-fibril location; a complete COL7A1 reference-entity path was not recovered. Supporting Evidence: Reactome:R-HSA-2089971 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-5694417 | KEEP AS NON CORE | Summary: ER-exit-site organization accompanies export of luminal collagen cargo. Reason: SEC16, SAR1 and SEC23/SEC24 organize the export machinery in this summary. The inherited COL7A1 assertion concerns luminal cargo rather than those coat components. Independent secretory biology supports retaining the location, while unresolved graph expansion limits target-specific source tracing. Supporting Evidence: Reactome:R-HSA-5694417 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-5694427 | KEEP AS NON CORE | Summary: MIA3 recognizes procollagen VII on the luminal side of the ER. Reason: The event explicitly names MIA3 binding to procollagen VII, supporting the precursor location. Its historical SH3 designation is qualified by the later MOTH-domain study; neither that label nor cargo recognition assigns MIA3 activity to COL7A1. The event text was read, but the full target-reference graph remains incomplete. Supporting Evidence: Reactome:R-HSA-5694427 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-5694435 | KEEP AS NON CORE | Summary: MIA2 and MIA3 concentrate procollagen VII at ER exit sites. Reason: This source explicitly names procollagen VII loading by the MIA2/MIA3 machinery. Retain the luminal cargo location as biosynthetic context, not a transmembrane-receptor function. The named event supports this scope despite incomplete expansion of its compound participants. Supporting Evidence: Reactome:R-HSA-5694435 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-5694436 | KEEP AS NON CORE | Summary: Cargo-receptor dissociation separates the departing procollagen from ER receptors. Reason: The procollagen VII event retains MIA2 and MIA3 in the ER membrane while cargo proceeds through export. The inherited ER-luminal annotation concerns the precursor stage, not receptor recycling by COL7A1. Source text was read; full participant tracing remains incomplete. Supporting Evidence: Reactome:R-HSA-5694436 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-5694522 | KEEP AS NON CORE | Summary: Inner-coat assembly selects soluble cargo through receptors. Reason: The generic summary distinguishes direct coat contacts from receptor-mediated loading of soluble cargo. Retain the inherited COL7A1 luminal precursor context, supported by independent secretion evidence, without inferring direct cytosolic coat binding. The partial graph does not newly prove target membership. Supporting Evidence: Reactome:R-HSA-5694522 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-5694527 | KEEP AS NON CORE | Summary: SAR1 nucleotide cycling checks cargo loading before export. Reason: The event assigns GTP hydrolysis to SAR1 and stimulation to SEC23; it does not name COL7A1. Retain the inherited ER cargo location as non-core, not a GTPase activity. Target-specific participant tracing remains unresolved after the recorded source-access failures. Supporting Evidence: Reactome:R-HSA-5694527 |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8944255 | KEEP AS NON CORE | Summary: Procollagen VII chain association occurs during ER trimer assembly. Reason: The event title identifies procollagen VII association, while its summary explains general C-terminal chain alignment. Retain the inherited ER-luminal precursor location with independent collagen VII assembly evidence. This does not turn structural association into enzymatic processing, and a complete reference-entity path was not recovered. Supporting Evidence: Reactome:R-HSA-8944255 |
| GO:0007155 cell adhesion | NAS PMID:29853175 Collagen Fibril Assembly and Function. | UNDECIDED | Summary: The exact adhesion premise of this NAS citation remains unresolved. Reason: The target-specific passage in PMID:29853175 was not recovered. Keep this source-scoped annotation undecided while preserving established positive collagen VII matrix attachment and adhesion biology from independent sources. No intrinsic signaling or receptor requirement is imposed on structural participation in adhesion. |
| GO:0008544 epidermis development | TAS PMID:8170945 Dominant dystrophic epidermolysis bullosa: identification of... | MARK AS OVER ANNOTATED | Summary: The source establishes inherited skin fragility rather than a demonstrated epidermis-development step. Reason: Actual original human pedigree Methods, mutation analysis, Results and Discussion identify a COL7A1 glycine substitution associated with dominant dystrophic epidermolysis bullosa. These positive genotype and anchoring-fibril findings do not independently show the protein performing the formation-to-maturity process specified by epidermis development. Mark this source-specific process interpretation over-annotated, without denying mechanical attachment or a possible developmental contribution. Supporting Evidence: |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | HDA PMID:28344315 Proteomic characterization of human multiple myeloma bone ma... | ACCEPT | Summary: Original marrow ECM workbooks identify the collagen VII group. Reason: The authentic target rows in S2 and S3 include COL7A1 and the Q02388/Q02388-2 group across the recorded donor and disease subsets. Retain the collagen structural class under the current term’s explicit collagen convention and independent attachment/assembly evidence. Protein-group detection is not isoform resolution or an isolated tensile-force assay. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | IBA GO_REF:0000033 | ACCEPT | Summary: Retain the inherited extracellular tensile structural class. Reason: Current same-term records include experimental evidence on human COL4A1 and worm let-2, while the target’s own human anchoring-fibril attachment and assembly experiments support the biological class. The historical PTN001166351 placement remains uninspected; no transfer failure follows from sparse donors or a nonfibrillar comparator. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001166351 UNRESOLVED Historical PAINT node/tree/MSA placement remains uninspected; current descendant records do not reconstruct that judgment, and no donor-count or self-source failure is inferred. UniProtKB:P02462 SUPPORTS TRANSFER Exact current identity and same-term curator records include HDA, IBA, IMP, RCA. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. WB:WBGene00002280 SUPPORTS TRANSFER Exact current identity and same-term curator records include IBA, IMP. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | ISS GO_REF:0000024 | ACCEPT | Summary: The exact pig COL7A1 donor supports the conserved structural class. Reason: Current F1SKM1 is pig COL7A1 and carries the same term by RCA from PMID:22261194. Its genuine abstract describes cardiac ECM proteomics rather than a direct force measurement. Retain the homologous structural role with independent human attachment evidence, while leaving the original pig target table and historical curator transfer procedure unclaimed. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:F1SKM1 SUPPORTS TRANSFER The authenticated pig COL7A1 identity has current same-term IBA and RCA records, including RCA from PMID:22261194. The original pig target table and historical manual transfer were not independently reconstructed. |
| GO:0030020 extracellular matrix structural constituent conferring tensile strength | RCA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: Human colon/liver ECM proteomics detects a COL7A1 protein group. Reason: Both original workbook sheets report the same COL7A1 group containing Q02388 and Q02388-2; the sheets are views of one dataset. The study’s extraction/MS Methods and exact target group were inspected. Retain the established tensile structural class without treating group detection as a force assay or resolving the two splice products. |
| 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 VII structural class with an explicit source-access limit. Reason: The selected protocol cache provides partial ECM proteomics text, but supplementary retrievals returned challenge HTML and the exact COL7A1 row was not recovered. The citation’s target link therefore remains unverified. Independent human attachment/assembly evidence and the official collagen convention support this existing structural assertion; no newly inspected target table or mechanical measurement is attributed to the inaccessible supplement. |
| GO:0030134 COPII-coated ER to Golgi transport vesicle | TAS Reactome:R-HSA-203973 | KEEP AS NON CORE | Summary: Vesicle budding carries the inherited secretory-cargo location. Reason: The summary describes SAR1-dependent budding and partial uncoating, without naming COL7A1. Retain the inherited carrier location, consistent with collagen VII secretion, as non-core. The incomplete target graph does not establish a new COL7A1 path or a role in budding machinery. Supporting Evidence: Reactome:R-HSA-203973 |
| GO:0030134 COPII-coated ER to Golgi transport vesicle | TAS Reactome:R-HSA-5694409 | KEEP AS NON CORE | Summary: RAB1 activation provides a transport context for inherited cargo localization. Reason: TRAPPC performs nucleotide exchange on RAB1 in this generic event. The retained COL7A1 assertion concerns carrier cargo, not exchange activity; independent secretory biology supports its non-core location. The summary does not name COL7A1 and unresolved graph expansion prevents a complete target-reference trace. Supporting Evidence: Reactome:R-HSA-5694409 |
| GO:0030134 COPII-coated ER to Golgi transport vesicle | TAS Reactome:R-HSA-5694418 | KEEP AS NON CORE | Summary: RAB1-dependent docking places inherited cargo in an ER-derived carrier. Reason: The summary concerns RAB1, USO1 and Golgi tether interactions. Retain COL7A1 as inherited secretory cargo without assigning tether activity. COL7A1 is not named in the summary, and its precise participant path remains incomplete. Supporting Evidence: Reactome:R-HSA-5694418 |
| GO:0030134 COPII-coated ER to Golgi transport vesicle | TAS Reactome:R-HSA-5694439 | KEEP AS NON CORE | Summary: Coat recruitment of TRAPPC and RAB1 accompanies transport of cargo. Reason: This source describes TRAPPC3 contact with SEC23 and recruitment of transport machinery. Retain the inherited COL7A1 carrier location as non-core secretory context, not a coat or nucleotide-exchange function. The generic summary and partial graph do not independently resolve target membership. Supporting Evidence: Reactome:R-HSA-5694439 |
| GO:0030134 COPII-coated ER to Golgi transport vesicle | TAS Reactome:R-HSA-5694441 | KEEP AS NON CORE | Summary: Coat phosphorylation provides the inherited carrier-location context. Reason: CSNK1D-dependent SEC23/SEC24 phosphorylation promotes coat release in this summary. The COL7A1 annotation is inherited cargo localization, consistent with secretion, not kinase activity. Its target-specific path remains unresolved and the summary does not name COL7A1. Supporting Evidence: Reactome:R-HSA-5694441 |
| GO:0030134 COPII-coated ER to Golgi transport vesicle | TAS Reactome:R-HSA-5694446 | KEEP AS NON CORE | Summary: SNARE-mediated fusion releases cargo into the acceptor compartment. Reason: The summary assigns membrane fusion to the SNARE machinery and describes generic cargo release. Retain the inherited COL7A1 carrier location as non-core without assigning fusion activity. COL7A1 is not named in the summary, and the incomplete graph does not newly establish its full participant path. Supporting Evidence: Reactome:R-HSA-5694446 |
| GO:0030198 extracellular matrix organization | IBA GO_REF:0000033 | ACCEPT | Summary: Retain ECM organization through collagen VII assembly and matrix attachment. Reason: Collagen VII performs structural work by organizing antiparallel assemblies and binding matrix constituents; this is more than a requirement inferred from loss of skin integrity. Exact current descendant identities and same-term curator records were inspected, with experimental records distinguished from inferred ones. Historical PTN002770636 placement was not reconstructed and no donor-count or circularity claim is made. Propagation Review Root cause: NO FAILURE CORE Sources checked: FB:FBgn0000299 UNRESOLVED Exact current identity and same-term curator records include IBA. The historical premise remains unresolved; no biological absence or circularity is inferred. FB:FBgn0016075 UNRESOLVED Exact current identity and same-term curator records include IBA. The historical premise remains unresolved; no biological absence or circularity is inferred. FB:FBgn0260660 UNRESOLVED Exact current identity and same-term curator records include IBA. The historical premise remains unresolved; no biological absence or circularity is inferred. MGI:MGI:104687 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. MGI:MGI:104688 UNRESOLVED Exact current identity and same-term curator records include IBA. The historical premise remains unresolved; no biological absence or circularity is inferred. MGI:MGI:1095415 SUPPORTS TRANSFER Exact current identity and same-term curator records include IBA, IMP. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. MGI:MGI:2152695 SUPPORTS TRANSFER Exact current identity and same-term curator records include IBA, IDA. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. MGI:MGI:2672118 SUPPORTS TRANSFER Exact current identity and same-term curator records include IBA, IMP. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. MGI:MGI:88446 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. MGI:MGI:88447 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. MGI:MGI:88451 SUPPORTS TRANSFER Exact current identity and same-term curator records include IBA, IMP. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. MGI:MGI:88452 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. MGI:MGI:88453 SUPPORTS TRANSFER Exact current identity and same-term curator records include IMP. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. MGI:MGI:88457 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. MGI:MGI:88458 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. MGI:MGI:88468 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. PANTHER:PTN002770636 UNRESOLVED Historical PAINT node/tree/MSA placement remains uninspected; current descendant records do not reconstruct that judgment, and no donor-count or self-source failure is inferred. RGD:61817 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. RGD:621351 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. UniProtKB:P02458 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. UniProtKB:P02461 UNRESOLVED Exact current identity and same-term curator records include IEA. The historical premise remains unresolved; no biological absence or circularity is inferred. UniProtKB:P02462 UNRESOLVED Exact current identity and same-term curator records include IBA. The historical premise remains unresolved; no biological absence or circularity is inferred. UniProtKB:P05997 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. UniProtKB:P08123 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. UniProtKB:P13942 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. UniProtKB:P20908 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. UniProtKB:P53420 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. WB:WBGene00001263 SUPPORTS TRANSFER Exact current identity and same-term curator records include IBA, IMP. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. ZFIN:ZDB-GENE-030131-9102 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. ZFIN:ZDB-GENE-101001-1 UNRESOLVED Exact current identity and same-term curator records include IBA. The historical premise remains unresolved; no biological absence or circularity is inferred. ZFIN:ZDB-GENE-101001-2 UNRESOLVED No same-term current record was returned for the authenticated alias query. The historical premise remains unresolved; no biological absence or circularity is inferred. |
| GO:0030199 collagen fibril organization | IEA GO_REF:0000107 | ACCEPT | Summary: Retain collagen-fibril organization with target assembly evidence. Reason: The exact rat Col7a1 donor D3ZE04 carries the same process by IMP; the paired historical Ensembl accession is retained without a new independent mapping claim. Human C-terminal assembly and anchoring-fibril studies support COL7A1 structural participation. The donor activity paper and historical Compara transfer were not independently reconstructed. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:D3ZE04 SUPPORTS TRANSFER The authenticated rat Col7a1 identity has a current same-term IMP record. This supports the ortholog-transfer premise; the donor paper and historical Ensembl Compara mapping were not newly verified. ensembl:ENSRNOP00000027994 UNRESOLVED The historical mapping was not independently reconstructed. |
| GO:0031012 extracellular matrix | HDA PMID:25037231 Extracellular matrix signatures of human primary metastatic ... | ACCEPT | Summary: Original colon/liver ECM data identifies the collagen VII protein group. Reason: The authentic COL7A1 target group occurs in both original workbook views. Retain matrix location at the human tissue and protein-group scope; neither isoform-specific deposition nor a separate signaling activity follows. Supporting Evidence: |
| GO:0031012 extracellular matrix | HDA PMID:28344315 Proteomic characterization of human multiple myeloma bone ma... | ACCEPT | Summary: Original marrow ECM workbooks identify COL7A1 in the reported sample groups. Reason: The actual target rows and headers in S2/S3 were inspected. Preserve matrix detection and sample-specific criteria without treating ND threshold cells as proof of absolute absence or collapsing distinct donor/disease columns. Supporting Evidence: |
| GO:0031012 extracellular matrix | HDA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | ACCEPT | Summary: Retain established extracellular matrix localization with the exact protocol-access limitation. Reason: The available protocol text is partial and the attempted supplementary files are HTML challenges. Its exact COL7A1 target link remains unverified; human anchoring-complex experiments independently establish ECM location. This is not a claim of a recovered protocol target row. |
| GO:0031012 extracellular matrix | ISS PMID:22261194 Proteomics analysis of cardiac extracellular matrix remodeli... | ACCEPT | Summary: The exact porcine COL7A1 source carries matrix-fraction localization. Reason: Current F1SKM1 has the same-term HDA record from PMID:22261194, with colocalizes_with preserved in the donor record. The complete abstract establishes pig cardiac ECM proteomics but does not enumerate the target; no full target table or human alpha1(VII)-specific experiment is claimed. Independent human matrix evidence supports the existing homologous location. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:F1SKM1 SUPPORTS TRANSFER Exact current identity and same-term curator records include HDA. These support the current transfer premise; underlying primary papers and historical PAINT placement are not newly claimed as read. |
| GO:0033116 endoplasmic reticulum-Golgi intermediate compartment membrane | TAS Reactome:R-HSA-5694446 | MODIFY | Summary: Refine the compound membrane location to the ER–Golgi intermediate compartment. Reason: The actual source models SNARE-mediated fusion with membrane-associated cargo/receptor complexes and release of cargo into the acceptor compartment. COL7A1 is secretory collagen cargo, not a demonstrated constituent of the lipid bilayer specified by GO:0033116. Use the encompassing ER–Golgi intermediate compartment for this contextual transit; its current children are the membrane and TRAPPI complex, neither a more accurate COL7A1 class here. Preserve the original TAS source and qualifier. The full target subgraph remains unexpanded, so this is a term-scope judgment on the inherited cargo assertion rather than a claimed new topology assay. Proposed replacements: endoplasmic reticulum-Golgi intermediate compartment |
| GO:0035987 endodermal cell differentiation | IEP PMID:23154389 Regulation of endodermal differentiation of human embryonic ... | MARK AS OVER ANNOTATED | Summary: The study reports COL7A1 expression during differentiation, not a demonstrated target-performed differentiation step. Reason: Actual hESC Methods and Results show COL7A1 transcript upregulation during definitive-endoderm induction. The tested matrices were collagens I, III, IV and V, fibronectin, laminin and vitronectin; the integrin perturbations concern ITGA5/ITGAV and other matrix interactions. Preserve the positive expression result, but mark the inference to COL7A1 performing endodermal-cell differentiation over-annotated for this source. No global absence of developmental function is asserted. Supporting Evidence: |
| GO:0005518 collagen binding | IDA PMID:18599485 Supramolecular interactions in the dermo-epidermal junction ... | NEW | Summary: Human collagen VII directly binds reconstituted collagen I fibrils. Reason: Recombinant human full-length 2,944-aa COL7A1 and an NC1-containing mini-collagen bound embryonic-chicken collagen I fibrils in dose-dependent assays; a shortened NC1 construct lacking the relevant von Willebrand A segment did not. Selective tag-transfer cross-linking corroborates binding. Separate purified human NC1 assays support collagen IV binding. Current typed ancestry of collagen binding does not include GO:0005515 and its ancestors/descendants overlap no retained source term; neither collagen-V-specific binding nor the cell-matrix-adhesion-specific child is established by these matrix-to-matrix assays. This adds an observed MF within the structural account, not a new process, receptor claim, native cross-link chemistry or equal activity of both splice products. |
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Download this section (compressed HTML)Q: How does the 32-residue collagenous deletion alter collagen VII assembly, fibril attachment and tissue distribution compared with the displayed product?
Q: What chemical interactions account for the exceptional stability of native collagen VII–banded-fibril connections?
Q: Does a defined endogenous NC2 processing state inhibit a protease not addressed by the original negative assays, or is its principal role structural?
Q: Which steps of collagen VII trafficking depend directly on the complete MIA3 MOTH region, and how do those contacts change during cargo release?
Experiment: Compare both sequence-verified human products in matched secretion, matrix-binding and anchoring-fibril reconstitution assays, with product-specific peptides.
Hypothesis: The central deletion alters assembly or mechanical attachment without necessarily removing the conserved NC1/NC2 interactions.
Experiment: Analyze purified native collagen VII–collagen I complexes by sensitive cross-link mass spectrometry and selective bond-cleavage controls.
Hypothesis: Specific covalent or unusually stable noncovalent contacts explain the resistance observed in human skin extracts.
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