EMILIN1

Summary: EMILIN1 contributes to aortic-valve matrix homeostasis and morphology in the mouse model.

Reason: The exact mouse donor records cite the Emilin1-knockout study, which follows juvenile, adult and aged valves and documents progressive matrix and signaling abnormalities. This supports a contextual valve role, although the principal experiments address postnatal homeostasis and disease progression rather than a direct human developmental assay. The orthology transfer is retained as non-core with that organism and temporal boundary.

Summary: EMILIN1 contributes to aortic-valve matrix homeostasis and morphology in the mouse model.

Reason: The exact mouse donor records cite the Emilin1-knockout study, which follows juvenile, adult and aged valves and documents progressive matrix and signaling abnormalities. This supports a contextual valve role, although the principal experiments address postnatal homeostasis and disease progression rather than a direct human developmental assay. The orthology transfer is retained as non-core with that organism and temporal boundary.

Summary: EMILIN1 is a structural component of extracellular matrix.

Reason: The genuine 25037231 workbook contains EMILIN1 in sheets A and B at row 8: principal Q9Y6C2 in the Q9Y6C2|Q96IH6 group, 87 reported unique peptides and 16 positive sample-or-pool measurements. These are not 16 independent donors and do not distinguish the natural products. The RCA assignment is consistent with independent matrix-binding, deposition and assembly experiments; protein detection itself is not presented as a mechanical assay.

Summary: EMILIN1 and EMILIN2 C-terminal fragments interact in a controlled yeast two-hybrid assay.

Reason: The original used human EMILIN1 gC1q as bait against a human kidney cDNA library and recovered an EMILIN2 fragment containing its gC1q domain and part of the collagenous region. Reciprocal bait/prey orientation was positive, with empty-vector and unrelated-partner controls. This supports the curated interaction, although it does not establish a native full-length heterotrimer or a specific binding function. The generic binding annotation is retained as non-core.

Summary: The reported EMILIN1–NMI association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-758758) corroborate the human EMILIN1–NMI interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–MTMR9 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-754120) corroborate the human EMILIN1–MTMR9 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–MTMR9 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-2320570) corroborate the human EMILIN1–MTMR9 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–MTMR9 association is supported as a non-core interaction.

Reason: BioGRID interaction 1438356 corroborates the exact human EMILIN1–MTMR9 pair and PMID in a high-throughput two-hybrid assay. The original pair-level supplement was not inspected. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–BEX3 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10222334, EBI-10378784, EBI-10633356) corroborate the human EMILIN1–BEX3 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–NMI association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10276158, EBI-10430221, EBI-10633376) corroborate the human EMILIN1–NMI interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–ZC2HC1C association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10242463, EBI-10398039, EBI-10633366) corroborate the human EMILIN1–ZC2HC1C interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–BEX5 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10243767, EBI-10399233, EBI-10560696) corroborate the human EMILIN1–BEX5 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–PLAC9 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10244532, EBI-10399961, EBI-10489424, EBI-10490745, EBI-10562138) corroborate the human EMILIN1–PLAC9 interaction. The records include two-hybrid and mammalian validation assays (anti-tag coimmunoprecipitation and MAPPIT). Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–LAIR2 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10250506, EBI-10405702, EBI-10569410) corroborate the human EMILIN1–LAIR2 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–TAX1BP1 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10329690, EBI-10482257, EBI-10580026) corroborate the human EMILIN1–TAX1BP1 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–IFT20 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10262792, EBI-10329700, EBI-10417283, EBI-10482267, EBI-10490223, EBI-10583474) corroborate the human EMILIN1–IFT20 interaction. The records include two-hybrid and MAPPIT validation. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–RIBC1 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10265391, EBI-10419763, EBI-10587112) corroborate the human EMILIN1–RIBC1 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–MIA2 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10182673, EBI-10340600, EBI-10502148) corroborate the human EMILIN1–MIA2 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–MTMR9 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-10293032, EBI-10329712, EBI-10446484, EBI-10482279, EBI-10633386) corroborate the human EMILIN1–MTMR9 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–Efb association is supported as a non-core interaction.

Reason: The original Efb pull-down table explicitly lists EMILIN1 from human platelet lysate with added fibrinogen: 62 sample versus 21 control peptide hits, ratio 2.95. This supports association with the bacterial Efb preparation, but EMILIN1 was not among the interactions individually confirmed by the later immunoblot or SPR assays. Direct contact and an immune-function mechanism are not established. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–MTMR9 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-22271024) corroborate the human EMILIN1–MTMR9 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–BEX5 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-22145756) corroborate the human EMILIN1–BEX5 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–MTMR9 association is supported as a non-core interaction.

Reason: Exact PMID and accession matches in IntAct (EBI-22144642) corroborate the human EMILIN1–MTMR9 interaction. The curated assays are two-hybrid screens; individual mammalian validation is not inferred. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–TAX1BP1 association is supported as a non-core interaction.

Reason: Exact PMID/partner IntAct records corroborate EMILIN1–TAX1BP1 copurification. The author BioPlex3 HEK293T directed-edge data additionally contain EMILIN1 bait 11117 and TAX1BP1 prey 8887. Affinity-purification association need not represent direct binding. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: The reported EMILIN1–LAIR2 association is supported as a non-core interaction.

Reason: The original article identifies the U2OS AP-MS author network in Data Availability. That network contains LAIR2 and EMILIN1 nodes joined by edge 567376. This corroborates the reported association; endpoint ordering alone is not evidence of bait/prey direction or direct molecular contact. Retain the supported generic interaction as non-core without assigning the partner’s activity to EMILIN1 or identifying an unverified natural splice product.

Summary: Secreted human EMILIN1 is deposited in the extracellular matrix.

Reason: The original compared sequence-confirmed human wild-type and A22T constructs. Human HEK293 conditioned-medium immunoblots demonstrate secretion; transfected mouse NIH3T3 cultures distinguish human from endogenous mouse EMILIN1, and human control fibroblasts and skin show extracellular matrix deposition. The mutant secretion defect does not negate wild-type localization. Extracellular matrix is the better resolved location. This is a compartment refinement through extracellular-structure part_of relationships, not a claim that GO:0031012 is an is_a descendant of GO:0005576.

Proposed replacements: extracellular matrix

Summary: The Reactome participant is EMILIN1 assembled within an elastic-fiber complex.

Reason: The captured event input contains an elastic-fiber/fibulin/emilin complex. Its Emilin set has a literal EMILIN1-polymer member, a trimer repeated unit, and three human Q9Y6C2 components modeled as residues 22–1016. Thus elastic fiber resolves the broad extracellular location more precisely. These are structural component edges, not evidence that EMILIN1 catalyzes crosslinking; the chain is not assigned to the short natural product.

Proposed replacements: elastic fiber

Summary: EMILIN1 promotes integrin-mediated cell adhesion.

Reason: The 1999 original directly tested a recombinant human gC1q fragment in cell-attachment assays, with fibronectin and albumin controls; adhesion was cell-line dependent and the receptor was not identified there. Subsequent direct purified alpha4beta1 binding, receptor blockade and ligand-mutant experiments establish integrin-mediated adhesion. GO:0033627 is a verified is_a descendant of cell adhesion. The refinement integrates that later evidence without recasting the 1999 experiment as an integrin-specific assay.

Proposed replacements: cell adhesion mediated by integrin

Summary: The EMILIN1 gC1q ligand directly supports cell-matrix adhesion.

Reason: Human recombinant gC1q supports Jurkat and EA.hy926 attachment, and selective ligand mutations impair this activity in the original assays. EMILIN1 supplies the adhesive contact itself, rather than merely being required for a downstream phenotype. Domain constructs and coated-substrate assays do not establish equal activity of both complete natural products.

Summary: EMILIN1 acts as an extracellular ligand in integrin-mediated signaling.

Reason: The current definition of signal transduction expressly includes ligand–receptor interaction. Human gC1q adhesion and integrin-blocking experiments, together with the contact-dependent proliferation and signaling study, support this broad context. Extracellular location does not exclude the ligand from signal transduction. The annotation is retained as non-core; no intracellular catalytic relay or autonomous kinase activity is attributed to EMILIN1.

Summary: Mouse EMILIN1 regulates vascular tone and blood pressure through a context-dependent matrix–signaling mechanism.

Reason: The exact mouse donor cites 22814752. Recovered original Methods and Results distinguish smooth-muscle from endothelial rescue, measure blood pressure and pressure-induced vascular responses, and show normalization of the excessive myogenic response by TGF-beta blockade. This provides more than an unqualified expression association, while the human transfer remains contextual and the recovered original is selected text rather than a complete PDF or supplement. No direct EMILIN1 ion-channel activity is inferred.

Summary: EMILIN1-dependent matrix signaling supports expression of selected valve-associated genes.

Reason: Mouse Emilin1 deficiency lowers selected transcripts, including endostatin and elastin, in the valve or adjacent vascular context. This supports positive regulation for those targets, while other transcripts change in the opposite direction. EMILIN1 is an extracellular regulator, not a demonstrated DNA-binding transcription factor; the gene-specific, age-dependent donor context is retained as non-core.

Summary: EMILIN1-dependent matrix signaling supports expression of selected valve-associated genes.

Reason: Mouse Emilin1 deficiency lowers selected transcripts, including endostatin and elastin, in the valve or adjacent vascular context. This supports positive regulation for those targets, while other transcripts change in the opposite direction. EMILIN1 is an extracellular regulator, not a demonstrated DNA-binding transcription factor; the gene-specific, age-dependent donor context is retained as non-core.

Summary: EMILIN1 restrains expression of selected profibrotic and angiogenic genes in the mouse valve model.

Reason: Emilin1-deficient valves show increased collagen I/III and VEGF-A/Flt1 transcript abundance in the original measurements. The negative-regulatory annotation therefore concerns these targets, not all gene expression. The study establishes a matrix-dependent signaling context without a direct transcriptional mechanism or a corresponding human perturbation experiment.

Summary: EMILIN1 restrains expression of selected profibrotic and angiogenic genes in the mouse valve model.

Reason: Emilin1-deficient valves show increased collagen I/III and VEGF-A/Flt1 transcript abundance in the original measurements. The negative-regulatory annotation therefore concerns these targets, not all gene expression. The study establishes a matrix-dependent signaling context without a direct transcriptional mechanism or a corresponding human perturbation experiment.

Summary: EMILIN1 positively regulates cell-substrate adhesion.

Reason: The literal PAINT node lies on the authenticated Q9Y6C2 path and its IBD matches the imported mouse donor. That donor currently carries IDA from 18757743 with an upstream-or-within qualifier; the recovered screen Methods describe mouse secreted proteins, but the exact EMILIN1 supplementary target entry remains unverified. Independent purified human ligand, receptor-blocking and ligand-mutant experiments directly establish adhesive activity. The positive inherited role is supported without pretending the mouse screen target table was read or treating donor count as evidence strength.

Summary: EMILIN1 supports cell migration in a defined haptotaxis assay.

Reason: The original measured EA.hy926 migration toward coated human gC1q and found that the E933A mutant impaired this response. The paper uses historical mature-protein numbering; E933 corresponds to residue 954 of the current 1,016-residue precursor. This is direct ligand-supported migration in the tested context, retained as a non-core process without extending it to all migration modes or developmental settings.

Summary: EMILIN1 restrains pathological angiogenesis in the mouse aortic-valve context.

Reason: The original shows increased provisional angiogenesis and later CD31-positive neovessels after Emilin1 deletion, accompanied by increased VEGF-A/Flt1 and reduced angiostatic factors. The exact BHF-UCL donor record is negative regulation of angiogenesis by IMP. The direction is supported, but this is a contextual matrix-dependent vascular effect rather than a universal antiangiogenic activity.

Summary: EMILIN1 restrains pathological angiogenesis in the mouse aortic-valve context.

Reason: The original shows increased provisional angiogenesis and later CD31-positive neovessels after Emilin1 deletion, accompanied by increased VEGF-A/Flt1 and reduced angiostatic factors. The exact BHF-UCL donor record is negative regulation of angiogenesis by IMP. The direction is supported, but this is a contextual matrix-dependent vascular effect rather than a universal antiangiogenic activity.

Summary: The established structural contribution is broader than a resolved recoil-specific activity.

Reason: The exact mouse Q99K41 donor has genuine IMP evidence from 14701737, including abnormal elastic-fiber architecture after Emilin1 loss. The orthology transfer is not rejected because it is mouse evidence. Independent mechanistic studies support matrix-component binding, deposition, fiber integrity and anchorage. These justify the structural-integrity parent GO:0005201, while the more specific contribution to reversible elastic recoil remains unresolved. The 2022 study does include femur three-point bending and altered stiffness; those measurements are not dismissed as absent, but do not isolate elastic-fiber recoil. This is a proportionate generalization, not a claim that EMILIN1 has no mechanical role.

Proposed replacements: extracellular matrix structural constituent

Summary: Human aortic matrix proteomics supports EMILIN1 detection; structural integrity is the proportionate function.

Reason: Original Table II identifies EMILIN-1/EMIL1_HUMAN with eight unique peptides, eight unique spectra, 3.0% sequence coverage and 30 total spectra in the sequentially extracted human aortic matrix preparation. The paper uses NaCl, SDS and guanidine extraction; its orthogonal imaging targets are other proteins, so no EMILIN1-specific image is claimed. Independent mechanistic studies support matrix-component binding, deposition, fiber integrity and anchorage. These justify the structural-integrity parent GO:0005201, while the more specific contribution to reversible elastic recoil remains unresolved. The 2022 study does include femur three-point bending and altered stiffness; those measurements are not dismissed as absent, but do not isolate elastic-fiber recoil. This is a proportionate generalization, not a claim that EMILIN1 has no mechanical role.

Proposed replacements: extracellular matrix structural constituent

Summary: Deposited endothelial-matrix proteomics supports EMILIN1; the function is generalized to matrix structural integrity.

Reason: The original explicitly deposits its MaxQuant outputs in PXD000359. The genuine txtECM.zip proteinGroups.txt line 2296 contains Q9Y6C2;H0Y7A0;Q96IH6, majority Q9Y6C2, 47 unique peptides overall and positive intensity in all three ECM experiments; reverse, contaminant and site-only flags are blank. The group contains 1016- and 347-residue sequences and is not an isoform-specific assignment. This is an author-output check, not raw-spectra reanalysis or a claim to have recovered published Table S6. Independent mechanistic studies support matrix-component binding, deposition, fiber integrity and anchorage. These justify the structural-integrity parent GO:0005201, while the more specific contribution to reversible elastic recoil remains unresolved. The 2022 study does include femur three-point bending and altered stiffness; those measurements are not dismissed as absent, but do not isolate elastic-fiber recoil. This is a proportionate generalization, not a claim that EMILIN1 has no mechanical role.

Proposed replacements: extracellular matrix structural constituent

Summary: The detected EMILIN1 group supports a general matrix structural role.

Reason: The authentic 25037231 A8/B8 record is positive in all 16 sample-or-pool measurements and reports 87 unique peptides for Q9Y6C2|Q96IH6. Its ECM-enrichment and protein-group assignment support detection but neither natural-product specificity nor a direct elasticity measurement. Independent mechanistic studies support matrix-component binding, deposition, fiber integrity and anchorage. These justify the structural-integrity parent GO:0005201, while the more specific contribution to reversible elastic recoil remains unresolved. The 2022 study does include femur three-point bending and altered stiffness; those measurements are not dismissed as absent, but do not isolate elastic-fiber recoil. This is a proportionate generalization, not a claim that EMILIN1 has no mechanical role.

Proposed replacements: extracellular matrix structural constituent

Summary: The recovered human-vein matrix detections support a general structural function.

Reason: The genuine OUP supplement identifies Q9Y6C2/EMIL1_HUMAN in guanidine extracts: Table S4 reports 24 unique peptides and 246 peptide-spectrum matches in solution, and 11 unique peptides and 128 matches in gel. These complementary workflows are not independent donors and their counts are not added. The two reported normal-versus-varicose quantifications do not establish differential EMILIN1 abundance. Together with independent matrix-binding, deposition and fiber-integrity evidence, these detections support generalization to GO:0005201. Neither this proteomics experiment nor the separate bone-stiffness assay isolates reversible elastic-fiber recoil; elasticity is not declared biologically false. Natural-product equivalence and EMILIN1 protease activity are not inferred.

Proposed replacements: extracellular matrix structural constituent

Summary: The cell-derived matrix detections support EMILIN1 structural integrity rather than a resolved recoil-specific activity.

Reason: The genuine workbook has EMILIN1 in Table I row 10 for all six bone-marrow stromal-cell donors and Table II row 9 for adipose and dermal matrices. The fractional peptide summaries are preserved as reported, not converted into counts of distinct peptide sequences. Decellularization, serum carryover and human/bovine shared-peptide limits remain relevant; the adjacent ITIH2 row is not part of the target. Independent mechanistic studies support matrix-component binding, deposition, fiber integrity and anchorage. These justify the structural-integrity parent GO:0005201, while the more specific contribution to reversible elastic recoil remains unresolved. The 2022 study does include femur three-point bending and altered stiffness; those measurements are not dismissed as absent, but do not isolate elastic-fiber recoil. This is a proportionate generalization, not a claim that EMILIN1 has no mechanical role.

Proposed replacements: extracellular matrix structural constituent

Summary: EMILIN1 detection in breast and omental matrix supports a general structural function.

Reason: The authentic 28675934 workbook contains 20 target protein-summary records across the breast, unfractionated omentum and fractionated omentum analyses. Nineteen name Q9Y6C2 alone; D2164 is a mixed Q9Y6C2;Q8IUD2 group and is kept separate. Alternate-search F50/F66 entries are not counted as additional biological observations. No isoform-specific identification, tumor-causal effect or recoil measurement follows from those detections. Independent mechanistic studies support matrix-component binding, deposition, fiber integrity and anchorage. These justify the structural-integrity parent GO:0005201, while the more specific contribution to reversible elastic recoil remains unresolved. The 2022 study does include femur three-point bending and altered stiffness; those measurements are not dismissed as absent, but do not isolate elastic-fiber recoil. This is a proportionate generalization, not a claim that EMILIN1 has no mechanical role.

Proposed replacements: extracellular matrix structural constituent

Summary: The EMILIN1-specific basis for positive regulation of coagulation is unresolved.

Reason: The literal source CPX-438 describes mouse EMILIN2 and is inferred from human EMILIN1 complex CPX-421. Both captured records carry a broad family-level functional description and cite 22566882 plus the EMILIN1 self-assembly paper. The inspected review attributes its platelet/coagulation mechanism to multimerin-1, whereas the self-assembly original does not establish this process. This is a concrete provenance concern requiring clarification of the EMILIN1 assay, not evidence that EMILIN1 cannot influence coagulation. The source and positive assertion are preserved pending that clarification.

Summary: EMILIN1 restrains TGF-beta receptor signaling in defined mouse tissue contexts.

Reason: The exact donor study reports increased pSMAD2/3 and related valve abnormalities after Emilin1 deletion. The earlier authenticated 16530041 abstract supplies a precursor-binding mechanism that limits furin-dependent TGF-beta maturation, but its complete original and human preparation were not recovered. Together these support contextual negative regulation; EMILIN1 is not the processing protease and no direct receptor-enzyme inhibition is inferred.

Summary: EMILIN1 restrains TGF-beta receptor signaling in defined mouse tissue contexts.

Reason: The exact donor study reports increased pSMAD2/3 and related valve abnormalities after Emilin1 deletion. The earlier authenticated 16530041 abstract supplies a precursor-binding mechanism that limits furin-dependent TGF-beta maturation, but its complete original and human preparation were not recovered. Together these support contextual negative regulation; EMILIN1 is not the processing protease and no direct receptor-enzyme inhibition is inferred.

Summary: EMILIN1 limits a VEGF-receptor-associated angiogenic context in mouse valves.

Reason: The donor original measures increased VEGF-A and Flt1 abundance and pathological neovascularization in Emilin1-deficient valves; Flk1 abundance is unchanged. This supports the curated negative-regulatory context, while it does not directly measure receptor phosphorylation or prove EMILIN1 binding to a VEGF receptor. The broad source assertion is retained as non-core with that distinction.

Summary: EMILIN1 limits a VEGF-receptor-associated angiogenic context in mouse valves.

Reason: The donor original measures increased VEGF-A and Flt1 abundance and pathological neovascularization in Emilin1-deficient valves; Flk1 abundance is unchanged. This supports the curated negative-regulatory context, while it does not directly measure receptor phosphorylation or prove EMILIN1 binding to a VEGF receptor. The broad source assertion is retained as non-core with that distinction.

Summary: EMILIN1 is detected with the human aortic extracellular matrix fraction.

Reason: Original Table II directly identifies EMILIN-1 with eight unique peptides and 30 total spectra after the documented sequential extraction. The imported colocalizes_with relation is retained exactly; fraction-level proteomics does not imply target-specific microscopy or a particular mature fiber position. Independent matrix-localization evidence is compatible with this broad, assay-bounded location.

Summary: Human cell-derived extracellular matrices contain EMILIN1.

Reason: Original Table 1 explicitly reports EMILIN1 across the displayed ECM preparations. The genuine supplementary Protein Report tables independently contain human IPI00013079 in both HUES1 replicates, both ihPSF replicates and the recovered hPSF replicate 2 record. HUES1 has two and eleven unique peptides in its respective replicates. Mouse IPI00115516 records are distinguished from these human records; hPSF replicate 1 detection is not invented. Decellularization and protein-group evidence support broad ECM localization without resolving natural products.

Summary: EMILIN1 is present in the matrix produced by human endothelial cells.

Reason: The original describes purified HUVEC-derived ECM and requires intensity in all three replicates for its ECM dataset. The author-deposited PXD000359 txtECM proteinGroups.txt record has positive intensity in Exp1, Exp2 and Exp3, with 47, 44 and 45 unique peptides respectively and blank reverse/contaminant flags. Q9Y6C2 is the majority accession of a three-sequence group, so the observation is not assigned to a single natural product. Published Table S6 itself remains unrecovered; the independently authenticated author output supplies the target-specific evidence.

Summary: The EMILIN1 protein group is detected in enriched human tissue matrix.

Reason: The exact 25037231 workbook row is positive across 16 tumor, metastasis and normal-tissue sample-or-pool measurements. The principal Q9Y6C2 and Q96IH6 group and 87 reported unique peptides are retained. These enriched fraction observations support the broad ECM term, without assigning every molecule to a mature elastic fiber, inferring disease causation or resolving the two natural products.

Summary: EMILIN1 is detected in the extracellular matrix of human saphenous veins.

Reason: The authentic supplement resolves the source-specific target: Table S4 explicitly identifies Q9Y6C2/EMIL1_HUMAN with multiple unique peptides in both guanidine-extract workflows, distinct from the adjacent EMILIN2 row. The original uses six normal and six varicose vein samples with sequential saline, SDS and guanidine extraction. This supports broad ECM localization without target-specific microscopy, natural-product assignment or a disease-dependent abundance claim. Earlier failed supplement routes remain preserved but no longer justify uncertainty after the successful independent recovery.

Summary: EMILIN1 is detected in human stromal-cell-derived extracellular matrix.

Reason: The exact target rows in Tables I and II identify EMILIN1 in all six bone-marrow donor matrices and the adipose/dermal preparations. The original decellularization and proteomic thresholds were assessed; residual cellular material and possible serum/shared-peptide contributions are reported limits, not evidence that this established matrix constituent is a false hit. The location remains broad and no isoform assignment is made.

Summary: EMILIN1 occurs in the analyzed human breast and omental matrix fractions.

Reason: The genuine workbook contains nineteen Q9Y6C2-only protein records plus one explicitly mixed Q9Y6C2/ERC1 group. The latter is not used to relabel the neighboring single-target record or to create another donor. The ECM-enrichment workflow and exact target detections support broad extracellular-matrix localization; no direct imaging, natural-product specificity or physiological tumor effect is inferred.

Summary: EMILIN1 is an active extracellular matrix component.

Reason: The target has an exact 1,016-residue MSA match and descends from the literal ECM IBD node; all imported donor identifiers match the saved IBD. Current donor records provide ECM or EMILIN-complex grounding across the family, including experimental evidence on human EMILIN1 itself. The EMILIN3 donor has a complex-location annotation rather than an exact current ECM row; the complex has an authenticated is_a/part_of path to ECM. This does not invalidate the historical placement. Human secretion, matrix deposition and adhesion experiments independently establish the target role; self-donor evidence is valid and no short-product equivalence is inferred.

Summary: EMILIN1 localizes to the extracellular matrix.

Reason: Mouse immunofluorescence and cultured-fibroblast experiments directly place Emilin1 in matrix networks and elastic-fiber-associated structures. Independent human wild-type secretion and matrix-deposition experiments support transfer of this broad compartment. The source organism is retained and mutant trafficking phenotypes are not substituted for normal localization.

Summary: Human EMILIN1 is an extracellular matrix component.

Reason: The original documents wild-type secretion and matrix deposition using human constructs in HEK293 and NIH3T3 cells, and confirms an extracellular network in human control fibroblasts and skin. Human and mouse proteins are distinguished in the transfected mouse-cell experiment. A22T retention and reduced deposition are mutant effects; no ER-resident normal function or short-product equivalence is inferred.

Summary: EMILIN1 is a documented extracellular matrix glycoprotein.

Reason: The cited family review explicitly discusses EMILIN1 in extracellular matrix and elastic-fiber-associated assemblies. This broad location is independently supported by human secretion/deposition and mouse tissue experiments, rather than inferred solely from the review title or from other family members.

Summary: EMILIN1 limits collagen production in mouse valve disease and human dermal fibroblast contexts.

Reason: Emilin1-deficient mouse aortic valves show increased collagen I/III transcript abundance and deposition (PMID:25056700, Figure 5). Independent human evidence in PMID:36351433, Figure 6A and the accompanying Results, shows increased COL1A1 transcripts and intracellular collagen I in EMILIN1-deficient dermal fibroblasts; the Results also report elevated collagen protein in culture supernatants. These production readouts support contextual negative regulation of collagen biosynthesis, while Figure 5 and the collagen-network Results separately show impaired fibril assembly and crosslinking. Increased production must therefore not be equated with increased successful matrix assembly. The signaling route varies among patient cell lines and is not resolved by these assays; this remains a non-core regulatory effect rather than collagen-synthetic activity performed by EMILIN1.

Summary: EMILIN1 limits collagen production in mouse valve disease and human dermal fibroblast contexts.

Reason: Emilin1-deficient mouse aortic valves show increased collagen I/III transcript abundance and deposition (PMID:25056700, Figure 5). Independent human evidence in PMID:36351433, Figure 6A and the accompanying Results, shows increased COL1A1 transcripts and intracellular collagen I in EMILIN1-deficient dermal fibroblasts; the Results also report elevated collagen protein in culture supernatants. These production readouts support contextual negative regulation of collagen biosynthesis, while Figure 5 and the collagen-network Results separately show impaired fibril assembly and crosslinking. Increased production must therefore not be equated with increased successful matrix assembly. The signaling route varies among patient cell lines and is not resolved by these assays; this remains a non-core regulatory effect rather than collagen-synthetic activity performed by EMILIN1.

Summary: EMILIN1 directly supports integrin-mediated adhesion.

Reason: The literal IBD at PTN002692991 lies on the target path and matches both imported donors. Current mouse EMILIN1 and human multimerin-1 records retain experimental integrin-adhesion grounding. More decisively for the target, purified human EMILIN1/gC1q binding, blocking and ligand-mutant experiments establish its adhesive ligand role. The PAINT placement is evaluated phylogenetically, not as a pairwise similarity score or donor-count argument.

Summary: EMILIN1 is an adhesive integrin ligand.

Reason: The mouse donor annotation is experimentally grounded in 21949412, which also contains human cell-line experiments with integrin blockade. Earlier purified human alpha4beta1 binding and ligand-mutant adhesion assays independently establish the target function. Mouse tissue phenotypes and human ligand assays remain separate evidence streams.

Summary: EMILIN1 is a ligand of alpha4beta1 integrin, not a constituent of its alpha4/beta1 heterodimer.

Reason: GO:0034668 denotes the receptor complex comprising one alpha4 and one beta1 integrin subunit. The recovered original characterizes the extracellular EMILIN1 gC1q ligand and its cell-adhesion determinants; it does not identify EMILIN1 as either receptor subunit. Thus the literal part_of assertion is a term-to-role mismatch. The positive integrin interaction and adhesive function remain supported and are retained in the separate integrin-binding and adhesion annotations.

Summary: EMILIN1 negatively regulates proliferation in the tested integrin-contact contexts.

Reason: The original uses human cell lines, receptor-blocking and proliferation assays as well as distinct mouse skin experiments. These resolve the direction of the broad proliferation-regulation annotation: EMILIN1–integrin contact restrains proliferation in the tested settings. GO:0008285 is an authenticated is_a descendant of GO:0042127. This refinement does not claim a universal antiproliferative response across all tissues or products.

Proposed replacements: negative regulation of cell population proliferation

Summary: EMILIN1 self-association supports its matrix assemblies.

Reason: The current mouse donor includes a 14701737 self-binding record, while that original also uses human recombinant EMILIN1 and references earlier oligomerization work. The human target is independently and directly supported by controlled C-terminal interaction assays, trimer measurements and full-length recombinant assemblies in 10821830 and 18463100. Thus the target function is retained without recasting every donor experiment as an isolated mouse-protein self-binding assay.

Summary: EMILIN1 self-association supports homotrimeric and larger assemblies.

Reason: Human EMILIN1 C-terminal constructs interact in controlled yeast co-transformation and mating assays. Biochemical experiments support gC1q trimers, and full-length human recombinant protein secreted from 293-EBNA cells forms larger disulfide-linked assemblies. This establishes self-association, while the original explicitly leaves the detailed architecture of native tissue assemblies unresolved.

Summary: The human EMILIN1 gC1q domain self-associates.

Reason: The original provides biochemical trimer evidence and an NMR-constrained homology model of the recombinant human gC1q domain. The deposited construct contains 12 tag/cloning residues followed by a 150-residue natural segment mapping to precursor residues 867–1016. The same segment occurs in the short natural product, but a shared domain does not establish that either complete isoform was assayed or functions equivalently.

Summary: The interaction screen independently corroborates EMILIN1 self-association.

Reason: IntAct EBI-10488347 / IM-23318-29257 records the exact human EMILIN1 self-pair in the cited two-hybrid array screen. This supports self-association in conjunction with the independent domain and full-length assembly experiments. The screen does not determine native stoichiometry or establish that both natural splice products were assayed.

Summary: The resolved angiogenic effect in the cited mouse evidence is negative regulation.

Reason: The PAINT node and IBD for the positive annotation are genuine and lie on the target path. However, the current mouse donor has conflicting signed records from the same paper: a ComplexPortal IDA positive record and a BHF-UCL IMP negative record. The operative original shows increased angiogenesis after Emilin1 loss, not suppression of angiogenesis by the knockout. Negative regulation therefore preserves the observed contextual effect. This is an explicit sign correction, not an ancestor refinement, a rejection based on donor count, or a claim of universal antiangiogenic function. The imported source dictionaries remain unchanged for curator reconciliation.

Proposed replacements: negative regulation of angiogenesis

Summary: The resolved angiogenic effect in the cited mouse evidence is negative regulation.

Reason: The PAINT node and IBD for the positive annotation are genuine and lie on the target path. However, the current mouse donor has conflicting signed records from the same paper: a ComplexPortal IDA positive record and a BHF-UCL IMP negative record. The operative original shows increased angiogenesis after Emilin1 loss, not suppression of angiogenesis by the knockout. Negative regulation therefore preserves the observed contextual effect. This is an explicit sign correction, not an ancestor refinement, a rejection based on donor count, or a claim of universal antiangiogenic function. The imported source dictionaries remain unchanged for curator reconciliation.

Proposed replacements: negative regulation of angiogenesis

Summary: The demonstrated human receptor-ligand activity is integrin binding that mediates cell-matrix adhesion.

Reason: Human purified-receptor binding and ligand-dependent adhesion establish the specific integrin-ligand role. The inherited IBA names PTN002692991 and MMRN2; the saved current IBD with that ligand term and donor instead lies at PTN000396133 in the MMRN2 branch, outside the target path. This is a version/placement discrepancy, not evidence that human EMILIN1 lacks ligand activity. GO:0098640 captures the demonstrated interaction as an explicit lateral replacement; it is not an is_a descendant of receptor ligand activity.

Proposed replacements: integrin binding involved in cell-matrix adhesion

Summary: EMILIN1 participates structurally in elastic-fiber assembly.

Reason: The mouse study documents altered fiber architecture and fibulin-5 deposition after Emilin1 loss. Independent recombinant human EMILIN1–elastin interaction and later EMILIN1-dependent fibulin-4 deposition experiments establish physical matrix-organizing work, beyond necessity alone. The protein provides an organizing matrix component; LOX-family enzymes perform crosslink chemistry. This assembly role does not require treating EMILIN1 itself as a recoil-producing elastin polymer.

Summary: EMILIN1 participates structurally in elastic-fiber assembly.

Reason: The mouse study documents altered fiber architecture and fibulin-5 deposition after Emilin1 loss. Independent recombinant human EMILIN1–elastin interaction and later EMILIN1-dependent fibulin-4 deposition experiments establish physical matrix-organizing work, beyond necessity alone. The protein provides an organizing matrix component; LOX-family enzymes perform crosslink chemistry. This assembly role does not require treating EMILIN1 itself as a recoil-producing elastin polymer.

Summary: EMILIN1 restrains valve-interstitial-cell activation in the mouse model.

Reason: The donor original identifies increased SMemb, alpha-SMA and proliferative markers in Emilin1-deficient valve tissue, supporting a transition toward activated/myofibroblastic states. This contextual negative regulation is retained without extending the broad term to all cell activation or assigning a direct intracellular activation enzyme to EMILIN1.

Summary: EMILIN1 restrains valve-interstitial-cell activation in the mouse model.

Reason: The donor original identifies increased SMemb, alpha-SMA and proliferative markers in Emilin1-deficient valve tissue, supporting a transition toward activated/myofibroblastic states. This contextual negative regulation is retained without extending the broad term to all cell activation or assigning a direct intracellular activation enzyme to EMILIN1.

Summary: The demonstrated EMILIN1 activity is integrin binding that mediates cell-matrix adhesion.

Reason: The source tests a homotrimeric extracellular ligand, its integrin-dependent adhesion and its ligand determinants. It does not demonstrate a selective bridge bringing two distinct partner molecules together for coordinated function; the proposed multi-contact receptor geometry remains hypothetical. GO:0098640 captures the experimentally established interaction. This is an explicit lateral replacement of molecular adaptor activity, not an is_a descendant refinement or an assertion of novel integrin-receptor membership.

Proposed replacements: integrin binding involved in cell-matrix adhesion

Summary: EMILIN1 restrains SMAD signaling in the studied mouse valve context.

Reason: The original measures increased pSMAD2/3 in deficient valves at the investigated ages. This supports negative regulation downstream of extracellular matrix/TGF-beta control, not direct SMAD binding or dephosphorylation by EMILIN1. Contextual signaling participation is retained as non-core.

Summary: EMILIN1 restrains SMAD signaling in the studied mouse valve context.

Reason: The original measures increased pSMAD2/3 in deficient valves at the investigated ages. This supports negative regulation downstream of extracellular matrix/TGF-beta control, not direct SMAD binding or dephosphorylation by EMILIN1. Contextual signaling participation is retained as non-core.

Summary: EMILIN1 is associated with extracellular vesicles released by cultured trabecular-meshwork cells.

Reason: The original human trabecular-meshwork study identifies Q9Y6C2 in its exosome proteomic table and specifically detects EMILIN1 by immunoblot after density-gradient fractionation near 1.10 g/ml. This is stronger than an unverified generic fraction hit and is retained as a contextual location. The study does not detect EMILIN1 in the corresponding aqueous-humor or urinary exosome blots, and the cultured-cell observation is not generalized to every extracellular vesicle or bodily fluid. Figure captions and operative text were read; figure pixels were not inspected.

Summary: EMILIN1 restrains ERK signaling in defined tissue and integrin-contact contexts.

Reason: The mouse valve study finds elevated pERK1/2 in adult and aged deficiency, whereas juvenile stages and other signaling measures differ. Human integrin-contact experiments provide additional context-specific regulation. The annotation is retained without a universal sign claim or attribution of kinase/phosphatase activity to EMILIN1.

Summary: EMILIN1 restrains ERK signaling in defined tissue and integrin-contact contexts.

Reason: The mouse valve study finds elevated pERK1/2 in adult and aged deficiency, whereas juvenile stages and other signaling measures differ. Human integrin-contact experiments provide additional context-specific regulation. The annotation is retained without a universal sign claim or attribution of kinase/phosphatase activity to EMILIN1.

Summary: EMILIN1 is associated with elastic fibers.

Reason: The actual current ARBA rule contains a condition set satisfied by the target FunFam 2.60.120.40:FF:000010 and Euarchontoglires lineage. Its output is GO:0071953. Independent tissue/deposition experiments and the literal Reactome assembly chain support the same location; rule applicability is verified rather than inferred from the accession alone.

Summary: EMILIN1 is an elastic-fiber-associated matrix component.

Reason: The original TAS citation is a review of elastic fibers. Its complete operative text was not recovered here, but the location is independently established by the mouse tissue/fibroblast original and the explicit human Reactome fiber-assembly chain. The sound broad location is retained with curator deference; no claim is made to have inspected the unavailable 2006 review body or to have assigned every short splice product to mature fibers.

Summary: EMILIN1 binds integrins to mediate cell-matrix adhesion.

Reason: Ligand mutations and cellular adhesion assays in the original establish the functional gC1q interface; the earlier purified human alpha4beta1 solid-phase binding assay provides complementary direct interaction evidence. The receptor is distinct from the extracellular EMILIN1 ligand. No purified alpha9beta1 affinity measurement or solved ligand–integrin co-complex is implied.

Summary: A reported antibacterial toxin-inhibition role remains unresolved at the operative assay level.

Reason: The authenticated abstract reports EMILIN interactions with anthrax protective antigen and inhibition of toxin action in vitro. GO:1900426 can include enhancement of host defense and does not require direct bacterial killing. However, the original Methods and Results were not recovered, leaving the exact EMILIN1 preparation, toxin-inhibition assay and controls unverified. The positive report and curated IDA assertion are preserved without a wrong-gene claim.

Summary: EMILIN1 limits VEGF-associated signaling and neovascularization in mouse valve disease.

Reason: The source records increased VEGF-A/Flt1 expression and progressive angiogenesis after Emilin1 deletion. This supports the curated negative-regulatory context, but neither an EMILIN1–VEGF binary interaction nor direct VEGF-receptor inhibition was demonstrated by those measurements. The source remains non-core and organism-specific.

Summary: EMILIN1 limits VEGF-associated signaling and neovascularization in mouse valve disease.

Reason: The source records increased VEGF-A/Flt1 expression and progressive angiogenesis after Emilin1 deletion. This supports the curated negative-regulatory context, but neither an EMILIN1–VEGF binary interaction nor direct VEGF-receptor inhibition was demonstrated by those measurements. The source remains non-core and organism-specific.

Summary: EMILIN1 promotes extracellular matrix assembly through matrix-component interactions.

Reason: The donor phenotype includes disrupted matrix architecture. Independent positive mechanistic evidence includes recombinant EMILIN1–elastin association and direct human EMILIN1 binding to murine fibulin-4, with supplementation restoring fibulin-4 deposition in depleted mouse osteoblast cultures. Thus EMILIN1 performs matrix-organizing work rather than merely being a disease-associated requirement. The species combinations and cell-type dependence remain explicit.

Summary: EMILIN1 promotes extracellular matrix assembly through matrix-component interactions.

Reason: The donor phenotype includes disrupted matrix architecture. Independent positive mechanistic evidence includes recombinant EMILIN1–elastin association and direct human EMILIN1 binding to murine fibulin-4, with supplementation restoring fibulin-4 deposition in depleted mouse osteoblast cultures. Thus EMILIN1 performs matrix-organizing work rather than merely being a disease-associated requirement. The species combinations and cell-type dependence remain explicit.

Summary: EMILIN1 regulates collagen fibril organization; the unsigned term captures the established matrix role.

Reason: The mouse donor study, PMID:25056700, documents increased collagen deposition together with randomly arranged, heterogeneous aortic fibrils (Results and Supplementary Figure S2M), not a resolved inhibitory effect on organization itself. PMID:36351433 provides direct human and mouse evidence for altered fibril architecture and reduced crosslinking: cultured deficient fibroblasts produce abnormal fibrils, whereas skin contains larger, more variable fibrils without a significant change in the area occupied by fibrils (Figures 5 and 7; Figure S11 for area measurements). The paper separately reports increased collagen synthesis and disorganized aortic deposits (Figure 6). The GO organization process concerns fibril size and arrangement; collagen abundance, fibril diameter and successful network assembly are distinct readouts and do not select one signed rate or extent across these contexts. Generalize to GO:1904026, regulation of collagen fibril organization. This is supported beyond a loss-of-function requirement: EMILIN1 binds EFEMP2/fibulin-4 and promotes its matrix deposition (PMID:28717224, Figure 5), while the human and mouse study connects deficient EFEMP2 deposition with reduced LOX function and collagen crosslinking. EMILIN1 supplies matrix-organizing interactions; LOX performs the crosslinking chemistry. The positive contribution to stable assembly is retained without claiming that all tissue-specific collagen responses have the same regulatory sign.

Proposed replacements: regulation of collagen fibril organization

Summary: EMILIN1 regulates collagen fibril organization; the unsigned term captures the established matrix role.

Reason: The mouse donor study, PMID:25056700, documents increased collagen deposition together with randomly arranged, heterogeneous aortic fibrils (Results and Supplementary Figure S2M), not a resolved inhibitory effect on organization itself. PMID:36351433 provides direct human and mouse evidence for altered fibril architecture and reduced crosslinking: cultured deficient fibroblasts produce abnormal fibrils, whereas skin contains larger, more variable fibrils without a significant change in the area occupied by fibrils (Figures 5 and 7; Figure S11 for area measurements). The paper separately reports increased collagen synthesis and disorganized aortic deposits (Figure 6). The GO organization process concerns fibril size and arrangement; collagen abundance, fibril diameter and successful network assembly are distinct readouts and do not select one signed rate or extent across these contexts. Generalize to GO:1904026, regulation of collagen fibril organization. This is supported beyond a loss-of-function requirement: EMILIN1 binds EFEMP2/fibulin-4 and promotes its matrix deposition (PMID:28717224, Figure 5), while the human and mouse study connects deficient EFEMP2 deposition with reduced LOX function and collagen crosslinking. EMILIN1 supplies matrix-organizing interactions; LOX performs the crosslinking chemistry. The positive contribution to stable assembly is retained without claiming that all tissue-specific collagen responses have the same regulatory sign.

Proposed replacements: regulation of collagen fibril organization

Summary: Macrophage accumulation is supported, but the migration-specific inference remains unresolved.

Reason: PMID:25056700, Figure 5C-D and the associated Results, detects increased Mac-3-positive cells in aged Emilin1-deficient valves, with unchanged CD45 staining. These are endpoint tissue-abundance measurements. The Discussion proposes several explanations involving systemic TGF-beta signaling, cells entering from the adventitia, new vessels and endothelial disruption; it does not resolve which route contributes. GO:1905522 concerns a reduction in the frequency, rate or extent of macrophage movement between sites. The operative Methods and Results do not separately measure that movement or exclude altered local retention, survival or proliferation as contributors to accumulation. The donor observation and its possible migration interpretation are retained, but inflammation alone does not settle the process-specific inference. This is scientific uncertainty despite accessible evidence, not an access failure or a claim that the curator annotated the wrong gene.

Summary: Macrophage accumulation is supported, but the migration-specific inference remains unresolved.

Reason: PMID:25056700, Figure 5C-D and the associated Results, detects increased Mac-3-positive cells in aged Emilin1-deficient valves, with unchanged CD45 staining. These are endpoint tissue-abundance measurements. The Discussion proposes several explanations involving systemic TGF-beta signaling, cells entering from the adventitia, new vessels and endothelial disruption; it does not resolve which route contributes. GO:1905522 concerns a reduction in the frequency, rate or extent of macrophage movement between sites. The operative Methods and Results do not separately measure that movement or exclude altered local retention, survival or proliferation as contributors to accumulation. The donor observation and its possible migration interpretation are retained, but inflammation alone does not settle the process-specific inference. This is scientific uncertainty despite accessible evidence, not an access failure or a claim that the curator annotated the wrong gene.

Summary: EMILIN1 participates in homotrimeric EMILIN assemblies.

Reason: The 2008 domain study directly supports the gC1q homotrimeric assembly mechanism. Its fragment lacks the N-terminal EMI domain and is not a complete native matrix complex by itself. The earlier full-length human recombinant study independently demonstrates homotrimeric and disulfide-linked higher assemblies, supporting the broader EMILIN-complex annotation with that distinction retained.

Summary: Human EMILIN1 forms homotrimeric and higher-order assemblies.

Reason: The source combines controlled C-terminal self-interaction assays, biochemical gC1q trimer measurements and analysis of full-length human recombinant protein secreted from 293-EBNA cells. Full-length protein forms high-molecular-mass disulfide-linked assemblies, whereas the engineered C-terminally truncated construct does not form comparable large assemblies. The natural 347-residue splice product is not that engineered truncation, and native tissue architecture was not directly resolved.