COL11A2

Summary: Human COL11A2 loss-of-function variants support skeletal development.

Reason: The original full PMID:10677296 reports seven human OSMED families, clinical and radiographic skeletal abnormalities, sequence segregation and RNA analysis. This supports the preserved developmental assertion through defective matrix structure; it does not establish a separate signaling or catalytic skeletal-development activity. Clinical measurements are distinguished from mouse compensation discussed by the authors.

Summary: Retain the skeletal role described for human collagen-XI disorders.

Reason: The complete PMID:7859284 abstract explicitly links COL11A2 splice and missense variants to dominant and recessive osteochondrodysplasias. Its skeletal-morphogenesis interpretation is consistent with the independently read human loss-of-function study. Preserve the original NAS assertion without claiming that the abstract contains a purified collagen mechanics assay.

Summary: The developmental annotation is consistent with COL11A2 matrix biology.

Reason: PMID:8838804 is a human COL11A2 sequence, gene-structure and splice-variant study. Its abstract explicitly gives the skeletal-integrity context of fibril-forming collagen XI, rather than a new developmental perturbation assay. Retain this NAS context alongside independent human genetic evidence.

Summary: Refine the structural constituent to the collagen tensile-strength class.

Reason: The InterPro-derived broad structural assertion is sound. Current GO:0030020 explicitly permits extracellular-matrix collagen proteins, and COL11A2 is an authentic fibrillar collagen-XI chain with target-specific cartilage/fibril evidence. The refinement follows this ontology convention and assembled-matrix role, not a claim that PMID:28344315 directly measures the tensile modulus of isolated COL11A2.

Proposed replacements: extracellular matrix structural constituent conferring tensile strength

Summary: The COL11A2-specific attribution of the recorded DDR2 interaction remains unresolved.

Reason: Full publisher text is available and its assays were inspected, but the participant mapping needed to adjudicate this COL11A2 assertion remains unresolved. Two positive MINT records map P13942 to DDR2 and are preserved literally. The original experiments use human DDR2 residues 26–186, commercial collagen type II in SPR and TCS, explicitly bovine nasal-septum type II for the TCS preparation, and a generic GPO-repeat computational docking model; they do not identify a tested COL11A2 chain. The campaign policy retains UNDECIDED when the relevant evidence cannot be adjudicated and does not remove a positive generic-binding assertion merely for lack of specificity. Full-text access therefore does not justify REMOVE or establish this exact interaction. Preserve the source pending substrate/mapping clarification, without retargeting it, denying possible DDR2–COL11A2 biology, or promoting an unsupported partner-class refinement.

Summary: COL11A2 is an extracellular collagen matrix component.

Reason: The ARBA location is consistent with the signal-bearing secreted collagen chain, collagen-XI assembly and direct human ECM-enriched target proteomics. This extracellular-region annotation remains valid at its stated breadth; it does not mean every recorded short alternative product was localized independently.

Summary: Retain the source-specific extracellular collagen location.

Reason: The actual model traces cleaved collagen-XI alpha-2 material to P13942 in the extracellular substrate set. MMPs perform gelatin degradation; COL11A2 is not assigned protease activity or a new degradation process.

Summary: Retain the source-specific extracellular collagen location.

Reason: The actual model traces COL11A2-containing type-XI tropocollagen and fibrillar material in the extracellular region. Model membership supports location and is not an independent biophysical measurement.

Summary: Retain the source-specific extracellular collagen location.

Reason: COL11A2-containing procollagen is represented as an extracellular substrate during N-propeptide removal. This supports the location, not protease activity or a new protein-processing annotation.

Summary: Retain the source-specific extracellular collagen location.

Reason: The extracellular procollagen and processed collagen hierarchy contains the exact P13942 entity. C-propeptide-cleaving enzymes perform the proteolysis; the collagen location does not assign that chemistry to COL11A2.

Summary: Retain the source-specific extracellular collagen location.

Reason: The event represents COL11A2-containing collagen moving from an ER-luminal complex to extracellular collagen. Preserve the extracellular output location without converting secretory cargo status into an autonomous secretion activity.

Summary: Retain the source-specific extracellular collagen location.

Reason: The extracellular collagen-XI fibril/fibre hierarchy contains P13942. Retain the spatial assertion without treating a generic fibre-formation model as a tissue-specific COL11A2 mechanical experiment.

Summary: Retain the source-specific extracellular collagen location.

Reason: The model explicitly places COL11A2-containing type-XI fibrils in extracellular cross-linked assemblies with type-II fibrils. This is curated structural context; it does not make COL11A2 the lysyl oxidase that generates cross-links.

Summary: COL11A2 is a constituent of the collagen type XI heterotrimer.

Reason: The exact target passage in the PMID:17876790 family review was not recovered beyond its complete abstract. The assertion is nevertheless independently supported by the human COL11A2 identity, the explicit collagen-XI chain composition in PMID:10677296, and the target-resolved Reactome procollagen-XI assembly. The original NAS source remains intact; this is not a claim of reading that review in full.

Summary: Retain alpha-2(XI) membership in collagen XI.

Reason: The complete PMID:7859284 abstract explicitly identifies COL11A2 as the alpha-2 chain of minor fibrillar collagen XI. Independent source and official complex definition identify the heterotrimeric composition; no COL11A2 homotrimer or activity of every splice product is inferred.

Summary: Human COL11A2 encodes a collagen-XI constituent chain.

Reason: PMID:8838804 establishes the human alpha-2(XI) coding and splice organization. Its identity context and the separately supported heterotrimer composition justify this NAS component annotation; gene-sequence determination is not recast as a new purified trimer-reconstitution assay.

Summary: The ER lumen is a valid precursor biosynthesis compartment.

Reason: The ARBA assignment agrees with the secretory signal and the curated luminal procollagen-XI assembly pathway. It is retained as a biosynthetic location distinct from the extracellular site of matrix work; there is no claim that every alternative product was directly localized.

Summary: Retain the ER-luminal precursor location.

Reason: COL11A2-containing procollagen is present in the luminal C-linked-trimer and triple-helix assembly hierarchy, with chaperones acting on it. This is a precursor location, not an independent chaperone or folding-catalyst activity of COL11A2.

Summary: Retain the ER-luminal precursor location.

Reason: The exact target is in an ER-luminal collagen/SERPINH1 input before extracellular delivery. This is a precursor location, not an independent chaperone or folding-catalyst activity of COL11A2.

Summary: Retain the ER-luminal precursor location.

Reason: The association event explicitly includes luminal alpha-2(XI) procollagen chains and the collagen-XI trimer, with a recursive chain to P13942. This is a precursor location, not an independent chaperone or folding-catalyst activity of COL11A2.

Summary: The inherited hearing role is supported by target and ortholog evidence.

Reason: Current exact-term tracing resolves mouse Col11a2 and human COL11A2 experimental grounding, including legitimate target self-evidence. PMID:10581026 separates human DFNA13 genetics from mouse knockout hearing and tectorial-fibril assays. The role follows matrix organization, not a sensory receptor or channel activity. The historical PAINT node placement is not reconstructed.

Summary: Retain the electronically inferred contribution to hearing.

Reason: The ARBA assertion agrees with independent human COL11A2 hearing-loss genetics and mouse tectorial-matrix organization. This process-level role is retained without making COL11A2 an autonomous auditory transducer.

Summary: COL11A2 contributes the matrix organization needed for hearing.

Reason: PMID:10581026 reports human DFNA13 families separately from targeted mouse Col11a2 disruption, auditory brainstem responses and disorganized tectorial collagen fibrils. The mouse experiment supplies the structural mechanism; it is not presented as a human inner-ear knockout experiment or direct receptor activity.

Summary: Human OSMED hearing loss supports the original process annotation.

Reason: The original full PMID:10677296 directly reports audiometry and COL11A2 loss-of-function genotypes in affected human families. Retain the process outcome in the collagen-matrix context, without inferring a separately demonstrated molecular auditory-transduction mechanism.

Summary: Retain the human recessive hearing-loss evidence.

Reason: The complete PMID:16033917 abstract reports a consanguineous Iranian family, homozygous COL11A2 P621T in deaf relatives and absence from 269 controls. This is positive human genetic evidence for the original hearing role; no full-paper protein assay or unique activity of a current splice product is claimed.

Summary: Retain the hearing phenotype associated with human OSMED.

Reason: PMID:9188673 explicitly describes three human siblings homozygous for a COL11A2 missense variant, with non-progressive sensorineural deafness and cartilage abnormalities. This is human clinical evidence, not the mouse Col11a2 knockout study. Retain the existing process annotation as an outcome of the structural role.

Summary: Retain the collagen tensile-strength structural class.

Reason: PMID:28344315 directly identifies P13942/COL11A2 in human bone-marrow ECM-enriched preparations; original S3 records seven distinct peptides across the complete data set. Proteomics establishes target presence, not tensile mechanics. Retention combines that collagen identity with the explicit current GO:0030020 convention for ECM collagens and independent fibril/structural evidence.

Summary: Retain the inherited extracellular collagen structural role.

Reason: Current source tracing resolves human COL4A1 and C. elegans LET-2 with matching experimental functional grounding. These current records do not reconstruct historical PTN001166351 placement, and donor number is not a quality measure. Target-specific collagen-XI matrix evidence and the official GO:0030020 collagen convention support retention.

Summary: COL11A2 contributes structure as an assembled collagen-XI chain.

Reason: The complete PMID:7859284 abstract identifies the fibrillar alpha-2(XI) chain and human matrix-related skeletal disease. This NAS tensile-class annotation follows the official convention for ECM collagens and target structural biology; the abstract does not measure an isolated-chain elastic modulus.

Summary: Retain the structural role of the human fibrillar collagen chain.

Reason: The PMID:8838804 abstract establishes human alpha-2(XI) sequence identity and the fibril-forming skeletal-integrity context. Combined with target fibril findings and the explicit GO collagen convention, this supports the structural class. No mechanical measurement is attributed to the sequencing study.

Summary: Retain the collagen structural class independently of a tensile assay.

Reason: PMID:28675934 is an ECM proteomics and matrisome-annotation methods paper. Its full Methods and Results distinguish protein detection/classification from function; its exact original COL11A2 table entry remains uninspected after supplement-download challenges. The structural term is retained on the independently verified collagen identity, human ECM target evidence and GO collagen convention, without claiming this RCA source directly measures tensile work.

Summary: COL11A2 contributes the structure that organizes collagen fibrils.

Reason: Human COL11A2 cartilage ultrastructure and mouse Col11a2 tectorial-membrane disruption support a performed structural contribution to fibril size and arrangement. Current source tracing resolves the listed COL11/COL5 collagen donors and legitimate target experimental grounding. It does not reconstruct the historical PAINT node or establish loss from current donor counts.

Summary: Human COL11A2-associated cartilage shows altered fibril organization.

Reason: The complete PMID:9188673 abstract explicitly reports increased fibril diameter and aggregation in cartilage from human siblings homozygous for a COL11A2 mutation. This directly supports the original organization assertion in its stated structural context. Preserve the curator evidence code; do not reclassify it mechanically from the shorter cache or present it as a purified-protein assay.

Summary: Retain the electronically inferred fibril-organizing role.

Reason: The ARBA assertion is consistent with human COL11A2 cartilage ultrastructure and the independently tested mouse tectorial-matrix phenotype. COL11A2 supplies a component of the organizing collagen structure, rather than merely serving as an enzyme substrate. No additional process assertion is needed.

Summary: The cited clinical study does not establish macromolecule-adaptor activity.

Reason: The complete original PMID:10677296 Methods and Results concern human family phenotypes, variants and RNA analysis; its collagen-XI heterotrimer and fibril discussion does not demonstrate COL11A2 bringing distinct macromolecules together for coordinated action as required by GO:0030674. Matrix incorporation is real, but is already represented by the supported collagen structural and fibril annotations. Mark this NAS adaptor specificity as over-annotated without denying interactions or inventing a separate scaffold mechanism.

Summary: Human COL11A2 is detected in ECM-enriched bone-marrow material.

Reason: Original PMID:28344315 Tables S2 and S3 identify COL11A2/P13942 in the collagen class. S3 detects it in four healthy donors plus one newly diagnosed and one relapsed myeloma preparation; S2 uses a different cohort-signature classification. Preserve the positive localization without claiming absence in disease, a cell-specific producer, or isoform-resolved protein detection.

Summary: Retain extracellular matrix localization with explicit source limits.

Reason: The original PMID:28675934 full methods establish ECM enrichment and human proteomics, but its exact COL11A2 supplement row could not be inspected. The location is independently supported by the original human target table in PMID:28344315 and collagen-XI biology, so retain the annotation with curator deference rather than overrule it from unavailable target-table evidence.

Summary: Retain the inherited extracellular matrix localization.

Reason: Current official identities and complete exact-term queries trace all listed source entities, including inferred-only current records where applicable. These are present-day provenance, not a reconstruction of PTN008390299. Human target proteomics and collagen-XI structural evidence independently support the matrix location; no target-specific loss is established.

Summary: The collagen-XI chain acts in extracellular matrix.

Reason: The exact target passage in the family review PMID:17876790 is unavailable beyond its complete abstract. Independent human ECM target detection and the authentic collagen-XI identity establish the location. Preserve the NAS assertion and reference identity while making the source-specific access limit explicit.

Summary: Retain the inherited skeletal morphogenesis role.

Reason: Current source tracing resolves mouse Col11a1 and Col11a2 with experimental grounding for the exact term. Human COL11A2 loss-of-function skeletal phenotypes support the corresponding structural developmental role. Historical PTN008601449 placement is not independently reconstructed, and no donor-count argument is used.

Summary: Retain the inherited cartilage-development context.

Reason: Current exact-term records include legitimate human COL11A2 grounding and zebrafish col11a2 perturbation evidence; mouse Col11a2 current matches are inferred and recorded as such. This does not establish a PAINT-node defect. Human cartilage and skeletal findings support the role as a structural matrix component rather than a new signaling activity.

Summary: The cartilage-development inference fits collagen-XI biology.

Reason: Human COL11A2-associated cartilage ultrastructure and skeletal dysplasia support the preserved ARBA process annotation. The protein contributes matrix structure; no distinct cartilage-patterning signal or enzyme is inferred.

Summary: Retain the cartilage phenotype in human COL11A2 disease.

Reason: The PMID:9188673 complete abstract explicitly reports cartilage histology, severe osteoarthritis and abnormal collagen fibrils in three homozygous human siblings. This is positive target-specific evidence for the existing IMP developmental context, with no complete original Methods or direct chondrogenesis assay claim.

Summary: Human COL11A2 variants support the original palate-development context.

Reason: The PMID:12673280 complete abstract reports targeted analysis of Robin-sequence, cleft-palate and micrognathia cohorts, including a COL11A2 stop variant in Robin sequence. Retain this original IMP annotation with the structural craniofacial context and curator deference; the source does not by itself establish a separate palate-specific molecular mechanism.

Summary: Retain the soft-palate phenotype associated with COL11A2 deficiency.

Reason: The original full PMID:10677296 includes posterior medial palatal clefting and related craniofacial findings among human OSMED cases. These support the preserved developmental outcome, not a demonstrated autonomous palate-patterning activity. Its scope remains within the collagen-matrix disease phenotype.