C1QA is the A chain of the secreted complement recognition protein C1q. Six copies each of the A, B and C chains assemble into collagen-like stalks and heterotrimeric globular heads. The A-chain globular module binds immunoglobulins, and assembled C1q recognizes clustered IgG or IgM on target surfaces. Within the C1 complex, this recognition couples to activation of the associated C1r and C1s proteases and initiation of the classical complement cascade. C1QA also contributes to recognition of altered-self surfaces and receptor-mediated immune regulation by assembled C1q, including phosphatidylserine recognition and CD33 signaling. In mouse models, C1qa-dependent complement activity participates in synaptic remodeling and glial responses.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001540 amyloid-beta binding | TAS PMID:15269255 Absence of C1q leads to less neuropathology in transgenic mo... | KEEP AS NON CORE | Summary: C1q recognizes amyloid-associated material in a contextual neuroinflammatory setting. Reason: The cited PMID:15269255 mouse study discusses established whole-C1q binding to fibrillar amyloid and tests C1qa deletion in amyloid-transgenic animals. It does not isolate an A-chain amyloid-binding site. Recombinant-module work in PMID:12847249 reports the beta-amyloid peptide interaction particularly for ghB. Retain the existing statement-level assignment to C1QA in the assembled C1q context, without claiming autonomous A-chain peptide recognition or making this a core activity. |
| GO:0001774 microglial cell activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: C1qa influences microglial activation in an amyloid-associated mouse context. Reason: The donor is mouse C1qa/P98086. The official MGI homology table maps this experimental donor process to PMID:15269255; its actual Methods and Results compare C1qa-null and C1qa-sufficient APP transgenic mice and report reduced activated microglial markers without reduced amyloid burden. Retain the human orthology assertion as contextual, with no claim of a human perturbation assay or microglial-intrinsic A-chain signaling mechanism. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The donor is mouse C1qa/P98086. The official MGI homology table maps this experimental donor process to PMID:15269255; its actual Methods and Results compare C1qa-null and C1qa-sufficient APP transgenic mice and report reduced activated microglial markers without reduced amyloid burden. Retain the human orthology assertion as contextual, with no claim of a human perturbation assay or microglial-intrinsic A-chain signaling mechanism. Supporting Evidence: |
| GO:0001774 microglial cell activation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: C1qa influences microglial activation in an amyloid-associated mouse context. Reason: The donor is mouse C1qa/P98086. The official MGI homology table maps this experimental donor process to PMID:15269255; its actual Methods and Results compare C1qa-null and C1qa-sufficient APP transgenic mice and report reduced activated microglial markers without reduced amyloid burden. Retain the human orthology assertion as contextual, with no claim of a human perturbation assay or microglial-intrinsic A-chain signaling mechanism. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The donor is mouse C1qa/P98086. The official MGI homology table maps this experimental donor process to PMID:15269255; its actual Methods and Results compare C1qa-null and C1qa-sufficient APP transgenic mice and report reduced activated microglial markers without reduced amyloid burden. Retain the human orthology assertion as contextual, with no claim of a human perturbation assay or microglial-intrinsic A-chain signaling mechanism. Supporting Evidence: |
| GO:0001786 phosphatidylserine binding | IDA PMID:18250442 C1q binds phosphatidylserine and likely acts as a multiligan... | ACCEPT | Summary: C1QA contributes to phosphatidylserine recognition by assembled C1q. Reason: PMID:18250442 tests human serum C1q and its globular region on apoptotic HeLa cells and phosphatidylserine-containing surfaces by imaging, cosedimentation and surface plasmon resonance. Its structural Results place the principal phosphoserine site on the C subunit; an A-subunit contact is constrained by crystal packing. Accept the curated C1QA assertion in its heterotrimeric recognition-head context, while the core synthesis explicitly uses contributes_to rather than claiming an independently demonstrated A-chain phosphatidylserine site. Supporting Evidence: |
| GO:0001791 IgM binding | IDA PMID:12847249 Modular organization of the carboxyl-terminal, globular head... | ACCEPT | Summary: The recombinant human C1QA globular module binds IgM. Reason: The complete cached PMID:12847249 abstract reports human MBP-ghA expressed in E. coli, binding to heat-aggregated IgM in ELISA and competition with C1q-dependent hemolysis. This directly supports an A-chain recognition contribution; physiological multivalency belongs to the assembled C1q heads. Full Methods beyond the abstract were not inspected. Supporting Evidence: |
| GO:0001791 IgM binding | IDA PMID:19006321 Interaction of human C1q with IgG and IgM: revisited. | ACCEPT | Summary: A-chain residues contribute to C1q recognition of IgM. Reason: The complete cached PMID:19006321 abstract reports recombinant globular-module mutagenesis, including A-chain Lys200, affecting IgM and IgG binding. Retain the supported activity without extrapolating an isolated-module result to full physiological avidity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12960167 The crystal structure of the globular head of complement pro... | KEEP AS NON CORE | Summary: C1QA associates with C1QB within the C1q heterotrimeric recognition head. Reason: The complete cached abstract of PMID:12960167 directly describes the 1.9-angstrom heterotrimeric globular assembly. This is structural support for the annotated C1QB partner, corroborated by the exact UniProt SUBUNIT/interaction record. Retain the correct generic interaction as non-core under the standing task instruction; do not replace it with immunoglobulin binding, which concerns a different partner. |
| GO:0005515 protein binding | IPI PMID:21054788 CD91 interacts with mannan-binding lectin (MBL) through the ... | KEEP AS NON CORE | Summary: Retain C1QA-C1QB association with explicit independent structural support. Reason: PMID:21054788 is abstract-only and foregrounds MBL/CD91; its original C1QA-C1QB experiment was not independently inspected. This is not evidence of a wrong-gene annotation. The exact C1QB interaction is independently established by the C1q heterotrimer structure in PMID:12960167 and the A-B disulfide-linked fragment in PMID:7240, as well as the UniProt SUBUNIT and interaction entries. Retain the existing assertion with curator deference while preserving its original reference. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | KEEP AS NON CORE | Summary: Retain the curated C1QA-UBQLN2 screen interaction with assay-context limits. Reason: The complete PMID:21988832 abstract and the actual Y2H Methods describe human ORF/fragment constructs, self-activation exclusion, independent rescreening and sequence confirmation. The exact C1QA-UBQLN2 edge is present in GOA and the preserved UniProt interaction record. Retain this experimental binding assertion by qualified curator deference; the individual supplementary target row and an edge-specific orthogonal assay were not inspected. The interaction does not establish a native extracellular role, ubiquitin-transfer activity or a core function. The cache lists a 2017 erratum whose contents were not adjudicated. |
| GO:0005515 protein binding | IPI PMID:28018340 Analysis of the Interaction between Globular Head Modules of... | KEEP AS NON CORE | Summary: The human C1QA globular module binds mature gC1qR/C1QBP. Reason: PMID:28018340 Methods and Results directly test recombinant human ghA against mature human gC1qR residues 74-282 by ELISA and far-western, with MBP controls and ghA substitutions. This supports the exact processed partner UniProtKB:Q07021-PRO_0000018590; retain that identifier without replacing it by an unprocessed precursor. Physical recognition is supported, but these assays do not by themselves assign C1QA a catalytic or receptor-signaling mechanism. |
| GO:0005515 protein binding | IPI PMID:28325905 Evidence for C1q-mediated crosslinking of CD33/LAIR-1 inhibi... | KEEP AS NON CORE | Summary: Retain the C1QA-C1QB assembly interaction rather than substitute the CD33 partner from the paper title. Reason: PMID:28325905 tests intact C1q and globular/collagen fragments, and its Introduction explicitly describes A/B/C assembly. The source row names C1QB, not CD33. The original chain-specific assay in this paper is not separately verified here; independent PMID:12960167 structural and PMID:7240 A-B fragment evidence establish the interaction, with exact UniProt support. Retain the curator assertion in this assembly context. |
| GO:0005515 protein binding | IPI PMID:28325905 Evidence for C1q-mediated crosslinking of CD33/LAIR-1 inhibi... | MODIFY | Summary: C1q acts as a ligand for the CD33 inhibitory signaling receptor. Reason: PMID:28325905 directly reports purified whole-C1q/globular-fragment binding to CD33, binding to CD33-transfected cells, and increased CD33 ITIM phosphorylation in human monocytes. GO:0048018 receptor ligand activity therefore captures more of the established function than generic protein binding. The assays concern intact C1q or its heterotrimeric globular region, not isolated A-chain sufficiency; retain the curated assignment to C1QA in that complex context. This refines an existing binding assertion to GO:0048018, which is also supported by the independently reviewed receptor-ligand IBA annotation. Proposed replacements: receptor ligand activity |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Retain the curated C1QA-SGTB HuRI interaction with source-specific assay limits. Reason: The inspected PMID:32296183 Results describe three complementary Y2H versions, nine screens, quadruplicate pairwise retesting and sequence confirmation. The exact SGTB edge is present in GOA and the preserved UniProt interaction record. Retain the binary binding assertion with curator deference while disclosing that its individual supplementary row and any edge-specific orthogonal validation were not inspected. Framework validation and UniProt experiment counts are not claimed to verify a native C1q-SGTB mechanism. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | KEEP AS NON CORE | Summary: Retain the curated C1QA-UBQLN2 HuRI interaction with source-specific assay limits. Reason: The inspected PMID:32296183 Results establish the binary Y2H screen/retest framework; GOA and UniProt contain the exact UBQLN2 edge. Retain the correct generic binding assertion with qualified curator deference, independently corroborated as a curated interaction from PMID:21988832. Neither individual supplementary target table nor edge-specific orthogonal validation was inspected, and no native ubiquitin-related function is inferred for C1QA. |
| GO:0005515 protein binding | IPI PMID:34804054 SARS-CoV-2 Exacerbates COVID-19 Pathology Through Activation... | KEEP AS NON CORE | Summary: C1QA ghA binding to mature gC1qR is directly used as the assay positive control. Reason: Although PMID:34804054 focuses on viral proteins, its Results and Figure5 caption explicitly use recombinant C1QA ghA as a positive binding control for gC1qR. The Methods identify mature gC1qR; PMID:28018340 independently specifies residues74-282 and directly tests ghA binding. Preserve the processed partner UniProtKB:Q07021-PRO_0000018590 and retain non-core binding without transferring viral mechanisms or claiming the full precursor was tested. Text and caption were read, not the figure image. |
| GO:0005515 protein binding | IPI PMID:7240 Isolation, by partial pepsin digestion, of the three collage... | KEEP AS NON CORE | Summary: Retain C1QA-C1QB protein association with independent heterotrimer-interface evidence. Reason: The complete PMID:7240 abstract demonstrates an A-B disulfide-linked pepsin fragment. That covalent linkage establishes chain assembly but, by itself, does not demonstrate the noncovalent interaction meant by protein binding. Retain the existing curated generic binding assertion as non-core with independent heterotrimeric globular-interface support from PMID:12960167 and the exact UniProt interaction record. Preserve the original PMID and C1QB partner; do not treat the disulfide bond as a binding assay. |
| GO:0005576 extracellular region | EXP PMID:29449492 Structures of C1-IgG1 provide insights into how danger patte... | ACCEPT | Summary: C1QA acts extracellularly as part of soluble and surface-recruited C1q. Reason: The complete PMID:29449492 abstract describes purified C1-IgG1 assemblies and recognition on surfaces. This agrees with the secreted C1QA record and direct human-serum C1q experiments in PMID:18250442; no intracellular localization is inferred. |
| GO:0005576 extracellular region | IBA GO_REF:0000033 | ACCEPT | Summary: Extracellular function is a conserved feature of this C1q-family lineage. Reason: The exact PTHR15427 PAINT record places an extracellular-region IBD at PTN008355511 and includes human C1QA among its experimental descendants. Target self-evidence is legitimate grounding, not circularity. The cached node record and direct extracellular C1q studies agree; the full alignment and tree were not independently reconstructed. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008355511 SUPPORTS TRANSFER Exact non-negated PTHR15427 IBD row inspected. Target C1QA is a legitimate experimental descendant, not circular evidence. The preserved source list is phylogenetic grounding; full tree/MSA reconstruction was not performed. |
| GO:0005576 extracellular region | IDA PMID:18250442 C1q binds phosphatidylserine and likely acts as a multiligan... | ACCEPT | Summary: Purified human extracellular C1q recognizes apoptotic-cell surfaces. Reason: PMID:18250442 purifies C1q from human serum and tests its association with extracellularly exposed phosphatidylserine on apoptotic cells. This directly supports the extracellular location of its A-chain-containing assembly. Supporting Evidence: |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | ACCEPT | Summary: The UniProt secretion mapping correctly places C1QA extracellularly. Reason: The preserved UniProt SUBCELLULAR LOCATION entry and signal-peptide-bearing secreted product agree with direct serum-C1q experiments. The broad electronic location is accurate and need not be replaced by a context-specific surface location. |
| GO:0005576 extracellular region | NAS PMID:28104818 Structure and activation of C1, the complex initiating the c... | ACCEPT | Summary: The C1q recognition assembly operates in the extracellular C1 complex. Reason: PMID:28104818 Methods reconstitute purified plasma C1q with recombinant C1r/C1s and inspect the assembled C1 structure. This supports extracellular assembly and does not assign the proteases activities to C1QA. Supporting Evidence: |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-166753 | ACCEPT | Summary: The curated pathway event correctly places C1QA extracellularly. Reason: The cached C4-cleavage reaction occurs extracellularly; C1QA belongs to the recognition assembly while activated C1s performs proteolysis. Supporting Evidence: Reactome:R-HSA-166753 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-166792 | ACCEPT | Summary: The curated pathway event correctly places C1QA extracellularly. Reason: The cached C2-cleavage reaction is extracellular; the serine protease, not C1QA, cleaves C2. Supporting Evidence: Reactome:R-HSA-166792 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-173626 | ACCEPT | Summary: The curated pathway event correctly places C1QA extracellularly. Reason: The cached C1r-activation reaction locates the recognition/protease assembly extracellularly. C1r activation is not C1QA catalysis. Supporting Evidence: Reactome:R-HSA-173626 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-173631 | ACCEPT | Summary: The curated pathway event correctly places C1QA extracellularly. Reason: The cached C1s-activation reaction is extracellular; C1r cleaves C1s while C1QA supports the recognition assembly. Supporting Evidence: Reactome:R-HSA-173631 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-8852266 | ACCEPT | Summary: The curated pathway event correctly places C1QA extracellularly. Reason: The cached SERPING1-binding event acts on extracellular antigen-antibody-C1 assemblies. Supporting Evidence: Reactome:R-HSA-8852266 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-8852481 | ACCEPT | Summary: The curated pathway event correctly places C1QA extracellularly. Reason: The cached inhibitor-associated C1 disassembly event is extracellular. Supporting Evidence: Reactome:R-HSA-8852481 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9021306 | ACCEPT | Summary: The curated pathway event correctly places C1QA extracellularly. Reason: The cached C1 inhibitor reaction concerns extracellular C1r/C1s, consistent with the C1QA-containing assembly location. Supporting Evidence: Reactome:R-HSA-9021306 |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9920638 | ACCEPT | Summary: The curated pathway event correctly places C1QA extracellularly. Reason: The cached dengue NS1-C1q binding event is extracellular. Its uncertain effect on complement is not promoted to a C1QA catalytic or antiviral function. Supporting Evidence: Reactome:R-HSA-9920638 |
| GO:0005602 complement component C1 complex | IBA GO_REF:0000033 | ACCEPT | Summary: C1QA is a structural recognition-chain component of C1. Reason: The exact PAINT IBD at PTN008559546 is grounded by human C1QA itself, which is appropriate descendant experimental evidence. Recombinant C1q/C1r-C1s assembly and human C1 structure independently verify membership; no propagation failure or self-evidence circularity is inferred. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008559546 SUPPORTS TRANSFER Exact non-negated PTHR15427 IBD row inspected. Target C1QA is a legitimate experimental descendant, not circular evidence. The preserved source list is phylogenetic grounding; full tree/MSA reconstruction was not performed. |
| GO:0005602 complement component C1 complex | IDA PMID:23650384 Expression of recombinant human complement C1q allows identi... | ACCEPT | Summary: Recombinant human C1q assembles with the C1r-C1s protease tetramer. Reason: The complete PMID:23650384 abstract reports expression of full recombinant human C1q in HEK293-F cells, C-chain tagging, and C1r/C1s binding/activation experiments. A-chain Lys59 contributes to interaction, with stronger effects at B61/C58. This verifies C1 membership without claiming C1QA is the activating protease. Supporting Evidence: |
| GO:0005602 complement component C1 complex | IDA PMID:2988513 Molecular modelling of human complement subcomponent C1q and... | ACCEPT | Summary: Human C1q forms a complex with C1r2C1s2. Reason: The complete normal-source PMID:2988513 abstract compares C1q and C1q-C1r2C1s2 models with neutron-scattering and hydrodynamic data. Membership is supported even though later structural work refines the historical geometry. No full paper or exact historical model endorsement is claimed. |
| GO:0005602 complement component C1 complex | IDA PMID:34155115 C1q binding to surface-bound IgG is stabilized by C1r(2)s(2)... | ACCEPT | Summary: The A-chain-containing C1q assembly associates with C1r2s2. Reason: PMID:34155115 directly compares purified C1 and C1q, adds C1r2s2, and measures IgG-surface binding and complement-dependent uptake. C1 proteases stabilize C1q binding; membership does not confer serine-protease activity on C1QA. Supporting Evidence: |
| GO:0005602 complement component C1 complex | IDA PMID:6249812 Activation of a complex of C1r and C1s subcomponents of huma... | UNDECIDED | Summary: The specific historical C1-assembly experiment remains inaccessible. Reason: The PMID:6249812 cache contains bibliographic metadata but no abstract or experimental text. C1QA membership is independently established by PMID:23650384 and PMID:28104818, but this particular IDA source cannot be independently adjudicated from its title alone; retain the source assertion as UNDECIDED. |
| GO:0005602 complement component C1 complex | IDA PMID:6952210 Ultrastructure of the first component of human complement: e... | ACCEPT | Summary: Human C1q is part of the assembled first complement component. Reason: The complete PMID:6952210 abstract reports electron microscopy of carbodiimide-crosslinked human C1. It supports physical complex membership; detailed historical geometry is not treated as definitive in light of later structures. |
| GO:0005602 complement component C1 complex | NAS PMID:28104818 Structure and activation of C1, the complex initiating the c... | ACCEPT | Summary: C1QA participates in the C1q-C1r2s2 recognition-protease assembly. Reason: PMID:28104818 Results and Methods directly reconstitute and visualize C1. Proposed intercomplex versus intracomplex activation arrangements remain mechanistic models, but they do not weaken the demonstrated membership of the A-chain-containing C1q subcomplex. Supporting Evidence: |
| GO:0005602 complement component C1 complex | TAS PMID:9461517 C1q-mediated chemotaxis by human neutrophils: involvement of... | ACCEPT | Summary: The C1q A chain is a constituent of C1. Reason: The cited PMID:9461517 focuses on C1q-mediated chemotaxis rather than determining C1 stoichiometry. Retain its correct traceable membership statement with direct independent recombinant and structural support, while not presenting the chemotaxis assay as the original assembly experiment. |
| GO:0006956 complement activation | TAS PMID:9461517 C1q-mediated chemotaxis by human neutrophils: involvement of... | MODIFY | Summary: Refine complement activation to the experimentally supported classical pathway. Reason: The original broad complement-activation assertion is biologically valid. GO:0006958 complement activation, classical pathway is an is_a child of GO:0006956 and more precisely describes the established C1QA contribution. C1QA supplies part of the recognition assembly and helps couple bound ligands to C1r/C1s activation; it performs structural recognition work rather than proteolysis. The original PMID:9461517 chemotaxis paper is contextual, while independent human C1q assembly and activation evidence in PMID:23650384 and PMID:34155115 supports the classical-pathway refinement. This modification adds specificity to the existing assertion without proposing a new annotation or an additional core. Proposed replacements: complement activation, classical pathway |
| GO:0006958 complement activation, classical pathway | IBA GO_REF:0000033 | ACCEPT | Summary: Classical complement initiation is a conserved function of the C1q recognition lineage. Reason: The exact PTN008559546 PAINT IBD lists mouse, zebrafish and human C1QA descendants for classical complement activation. The target appears among genuine experimental sources and is not circular evidence. Human recombinant C1q and surface-recruited C1 experiments establish the function directly; no target-specific loss or divergence is evident. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008559546 SUPPORTS TRANSFER Exact non-negated PTHR15427 IBD row inspected. Target C1QA is a legitimate experimental descendant, not circular evidence. The preserved source list is phylogenetic grounding; full tree/MSA reconstruction was not performed. |
| GO:0006958 complement activation, classical pathway | IDA PMID:12847249 Modular organization of the carboxyl-terminal, globular head... | ACCEPT | Summary: C1QA ligand recognition contributes directly to classical complement initiation. Reason: PMID:12847249 reports human recombinant ghA binding immunoglobulins and competing with C1q-dependent lysis of IgG/IgM-sensitized sheep erythrocytes. This establishes a recognition contribution, not a catalytic cleavage activity of the isolated chain. Supporting Evidence: |
| GO:0006958 complement activation, classical pathway | IDA PMID:19006321 Interaction of human C1q with IgG and IgM: revisited. | ACCEPT | Summary: C1QA contributes to antibody-dependent complement recognition. Reason: The PMID:19006321 abstract reports A-chain globular-module substitutions affecting IgG/IgM binding. Classical activation is the established function of the assembled C1q recognition system; retain the source assignment with independent direct assembly/activation evidence from PMID:23650384. |
| GO:0006958 complement activation, classical pathway | IDA PMID:23650384 Expression of recombinant human complement C1q allows identi... | ACCEPT | Summary: Recombinant human C1q supports C1 protease activation. Reason: The PMID:23650384 abstract directly reports C1r/C1s binding and activation using recombinant human C1q. Recognition-chain substitutions alter recruitment. The chemistry is performed by C1r/C1s; C1QA contributes structural binding sites within the activating assembly. Supporting Evidence: |
| GO:0006958 complement activation, classical pathway | IDA PMID:24626930 Complement is activated by IgG hexamers assembled at the cel... | ACCEPT | Summary: Antigen-bound IgG clustering recruits C1q and initiates classical complement. Reason: The inspected PMID:24626930 main narrative combines human IgG Fc-interface mutagenesis, target-cell complement-dependent cytotoxicity and C1-IgG cryoelectron tomography. It supports the A-chain-containing recognition complex as a direct participant. Supplementary target data and high-resolution chain-specific contacts were not independently read. Supporting Evidence: |
| GO:0006958 complement activation, classical pathway | IDA PMID:29449492 Structures of C1-IgG1 provide insights into how danger patte... | ACCEPT | Summary: C1q recognition of antibody assemblies couples to C1 activation. Reason: The complete PMID:29449492 abstract reports C1-IgG1 cryo-EM, functional IgG1-mutant analysis and conformational rearrangements of C1q and C1r2s2. This supports classical initiation by the assembled complex without deciding between intra- and intercomplex protease-activation models. Supporting Evidence: |
| GO:0006958 complement activation, classical pathway | IDA PMID:3258649 The binding site for C1q on IgG. | ACCEPT | Summary: C1q-immunoglobulin recognition is required for antibody-triggered complement lysis. Reason: The complete PMID:3258649 abstract reports mouse IgG2b Fc substitutions and a peptide mimic that inhibits complement lysis. The antibody reagent is explicitly mouse; the abstract does not establish the species of every C1q preparation. Retain the human curator assignment with direct human C1q corroboration, without claiming a human-antibody assay in this paper. |
| GO:0006958 complement activation, classical pathway | IDA PMID:34155115 C1q binding to surface-bound IgG is stabilized by C1r(2)s(2)... | ACCEPT | Summary: C1q surface recognition supports classical complement deposition and phagocytic clearance. Reason: PMID:34155115 directly tests human antibody-coated Staphylococcus aureus, purified C1/C1q and human serum complement. Reconstitution and blocking experiments establish the recognition assembly in complement-dependent C3 deposition and neutrophil uptake. This does not assign downstream cleavage or cellular engulfment machinery to C1QA. Supporting Evidence: |
| GO:0006958 complement activation, classical pathway | IDA PMID:6249812 Activation of a complex of C1r and C1s subcomponents of huma... | UNDECIDED | Summary: The specific historical activation experiment cannot be read from this cache. Reason: PMID:6249812 currently has only bibliographic metadata. The overall classical complement function is well established by independent sources, but the original IDA assay cannot be adjudicated from the title, so the source-specific row remains UNDECIDED rather than removed. |
| GO:0006958 complement activation, classical pathway | IDA PMID:6776418 The Clq receptor site on immunoglobulin G. | ACCEPT | Summary: C1q recognition of immunoglobulin participates in classical activation. Reason: The complete PMID:6776418 abstract reports chemical and inhibitor evidence for a C1q-interaction site on IgG. Retain the curated functional link, corroborated by modern IgG-interface mutagenesis and C1 activation studies, without treating the historical contact proposal as a current atomic structure. |
| GO:0006958 complement activation, classical pathway | NAS PMID:11527969 Substrate specificities of recombinant mannan-binding lectin... | ACCEPT | Summary: The stated classical-pathway role of C1q is correct despite the cited paper focusing on MASPs. Reason: The complete PMID:11527969 abstract assays recombinant human MASP-1/MASP-2 and contrasts them with C1r/C1s. It does not make C1QA a serine protease. Retain the correct nontraceable classical-pathway statement using independent direct human C1q assembly/activation evidence; a MASP-focused title is not proof of a wrong-gene curation error. |
| GO:0007165 signal transduction | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: C1q receptor engagement can trigger cellular signaling. Reason: This logical inference derives from GO:0048018 receptor ligand activity, whose official relation includes participation in signal transduction. Human C1q-CD33 binding and ITIM phosphorylation support the biological link. Retain the broad signaling term as contextual rather than implying C1QA is a kinase, G protein or intracellular signal transducer. Supporting Evidence: |
| GO:0007267 cell-cell signaling | TAS PMID:9461517 C1q-mediated chemotaxis by human neutrophils: involvement of... | KEEP AS NON CORE | Summary: Extracellular C1q can elicit leukocyte responses. Reason: The complete PMID:9461517 abstract reports chemotaxis of human neutrophils in response to C1q and its collagen-like tail, with receptor and G-protein-pathway dependence. This supports contextual intercellular signaling by the complex; downstream G-protein/PI3K activities are not properties of C1QA. Supporting Evidence: |
| GO:0009986 cell surface | EXP PMID:34155115 C1q binding to surface-bound IgG is stabilized by C1r(2)s(2)... | ACCEPT | Summary: C1q is recruited to antibody-coated target-cell surfaces. Reason: PMID:34155115 directly measures C1q binding on IgG-coated Staphylococcus aureus and model surfaces. The A-chain-containing complex is a peripheral extracellular occupant, not an integral membrane protein. A cell-surface annotation does not require membrane insertion. Supporting Evidence: |
| GO:0009986 cell surface | IEA GO_REF:0000044 | ACCEPT | Summary: The mapped surface location reflects extracellular ligand-dependent recruitment. Reason: UniProt maps the direct PMID:34155115 surface-binding evidence to its cell-surface vocabulary. Retain this broad location with the explicit antibody-coated target-surface context, not an unsupported plasma-membrane topology. |
| GO:0016322 neuron remodeling | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: C1q-dependent synaptic elimination contributes to neuronal remodeling in mouse models. Reason: The donor is mouse C1qa/P98086. The official MGI homology graph maps neuron remodeling to PMID:18083105. The complete normal PMID:18083105 abstract reports C1q/C3-deficient mice with failed retinogeniculate refinement and excess retinal innervation, alongside postnatal synaptic C1q localization. Retain the human assignment as contextual orthology, not a directly assayed human developmental mechanism; full Methods were not available in this cache. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The donor is mouse C1qa/P98086. The official MGI homology graph maps neuron remodeling to PMID:18083105. The complete normal PMID:18083105 abstract reports C1q/C3-deficient mice with failed retinogeniculate refinement and excess retinal innervation, alongside postnatal synaptic C1q localization. Retain the human assignment as contextual orthology, not a directly assayed human developmental mechanism; full Methods were not available in this cache. Supporting Evidence: |
| GO:0016322 neuron remodeling | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: C1q-dependent synaptic elimination contributes to neuronal remodeling in mouse models. Reason: The donor is mouse C1qa/P98086. The official MGI homology graph maps neuron remodeling to PMID:18083105. The complete normal PMID:18083105 abstract reports C1q/C3-deficient mice with failed retinogeniculate refinement and excess retinal innervation, alongside postnatal synaptic C1q localization. Retain the human assignment as contextual orthology, not a directly assayed human developmental mechanism; full Methods were not available in this cache. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The donor is mouse C1qa/P98086. The official MGI homology graph maps neuron remodeling to PMID:18083105. The complete normal PMID:18083105 abstract reports C1q/C3-deficient mice with failed retinogeniculate refinement and excess retinal innervation, alongside postnatal synaptic C1q localization. Retain the human assignment as contextual orthology, not a directly assayed human developmental mechanism; full Methods were not available in this cache. Supporting Evidence: |
| GO:0019864 IgG binding | IDA PMID:24626930 Complement is activated by IgG hexamers assembled at the cel... | ACCEPT | Summary: C1q recognizes clustered IgG Fc regions. Reason: PMID:24626930 directly tests human IgG Fc-interface mutations, C1 binding and complement-dependent cytotoxicity. It supports multivalent IgG recognition by assembled C1q; independent recombinant ghA binding in PMID:12847249 supports the A-chain contribution without assigning every head contact to chain A. |
| GO:0019864 IgG binding | IDA PMID:29449492 Structures of C1-IgG1 provide insights into how danger patte... | ACCEPT | Summary: C1QA contributes to IgG recognition by the heterotrimeric C1q heads. Reason: The original contributes_to qualifier is preserved. The PMID:29449492 abstract reports C1-IgG1 structures and functional antibody substitutions, establishing recognition by the assembled complex rather than autonomous sufficiency of one chain. Supporting Evidence: |
| GO:0019864 IgG binding | IDA PMID:3258649 The binding site for C1q on IgG. | ACCEPT | Summary: C1q binds the antibody Fc region. Reason: The PMID:3258649 abstract identifies a C1q-binding surface by mouse IgG2b mutagenesis and peptide inhibition of lysis. Retain the human C1QA annotation with explicit reagent-species limits and independent human ghA/IgG evidence; do not claim the abstract tested human IgG or purified A chain. |
| GO:0019864 IgG binding | IDA PMID:6776418 The Clq receptor site on immunoglobulin G. | ACCEPT | Summary: C1q interacts with the IgG constant-region surface. Reason: The complete PMID:6776418 abstract supports C1q-IgG binding through inhibitory and chemical-modification experiments. The interaction itself is independently confirmed by human recombinant-module and modern complex studies, even though exact historical residue models have evolved. |
| GO:0031012 extracellular matrix | HDA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | UNDECIDED | Summary: The specific extracellular-matrix proteomic assignment remains unverified. Reason: The actual PMID:28675934 cache includes the matrisome extraction/proteomics framework and narrative, but the relevant individual protein table is not present in the material inspected. Secreted C1q can associate with extracellular structures, yet that general plausibility does not independently verify this HDA tissue-matrix entry. Preserve the original assertion as UNDECIDED; no wrong-gene or contamination claim is made. Supporting Evidence: |
| GO:0045202 synapse | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: C1q can localize at synapses in rodent neural contexts. Reason: The source is the inspected PTN008559546 IBD for the IBA row, or the exact mouse/rat ortholog for the transfer rows. The official MGI homology graph links experimental synaptic localization to PMID:18083105 and PMID:27033548. The complete PMID:18083105 abstract describes postnatal synaptic C1q localization; the actual PMID:27033548 main narrative directly reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain contextual orthology rather than claiming human imaging. The rat-specific culture experiment is not separately described in the accessible abstract and is retained with curator deference to the mapped rat donor record. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN008559546 SUPPORTS TRANSFER Exact non-negated PTHR15427 IBD row inspected. The preserved source list is phylogenetic grounding; full tree/MSA reconstruction was not performed. |
| GO:0045202 synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: C1q can localize at synapses in rodent neural contexts. Reason: The source is the inspected PTN008559546 IBD for the IBA row, or the exact mouse/rat ortholog for the transfer rows. The official MGI homology graph links experimental synaptic localization to PMID:18083105 and PMID:27033548. The complete PMID:18083105 abstract describes postnatal synaptic C1q localization; the actual PMID:27033548 main narrative directly reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain contextual orthology rather than claiming human imaging. The rat-specific culture experiment is not separately described in the accessible abstract and is retained with curator deference to the mapped rat donor record. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The source is the inspected PTN008559546 IBD for the IBA row, or the exact mouse/rat ortholog for the transfer rows. The official MGI homology graph links experimental synaptic localization to PMID:18083105 and PMID:27033548. The complete PMID:18083105 abstract describes postnatal synaptic C1q localization; the actual PMID:27033548 main narrative directly reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain contextual orthology rather than claiming human imaging. The rat-specific culture experiment is not separately described in the accessible abstract and is retained with curator deference to the mapped rat donor record. |
| GO:0045202 synapse | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: C1q can localize at synapses in rodent neural contexts. Reason: The source is the inspected PTN008559546 IBD for the IBA row, or the exact mouse/rat ortholog for the transfer rows. The official MGI homology graph links experimental synaptic localization to PMID:18083105 and PMID:27033548. The complete PMID:18083105 abstract describes postnatal synaptic C1q localization; the actual PMID:27033548 main narrative directly reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain contextual orthology rather than claiming human imaging. The rat-specific culture experiment is not separately described in the accessible abstract and is retained with curator deference to the mapped rat donor record. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P31720 SUPPORTS TRANSFER The source is the inspected PTN008559546 IBD for the IBA row, or the exact mouse/rat ortholog for the transfer rows. The official MGI homology graph links experimental synaptic localization to PMID:18083105 and PMID:27033548. The complete PMID:18083105 abstract describes postnatal synaptic C1q localization; the actual PMID:27033548 main narrative directly reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain contextual orthology rather than claiming human imaging. The rat-specific culture experiment is not separately described in the accessible abstract and is retained with curator deference to the mapped rat donor record. |
| GO:0045202 synapse | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: C1q can localize at synapses in rodent neural contexts. Reason: The source is the inspected PTN008559546 IBD for the IBA row, or the exact mouse/rat ortholog for the transfer rows. The official MGI homology graph links experimental synaptic localization to PMID:18083105 and PMID:27033548. The complete PMID:18083105 abstract describes postnatal synaptic C1q localization; the actual PMID:27033548 main narrative directly reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain contextual orthology rather than claiming human imaging. The rat-specific culture experiment is not separately described in the accessible abstract and is retained with curator deference to the mapped rat donor record. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The source is the inspected PTN008559546 IBD for the IBA row, or the exact mouse/rat ortholog for the transfer rows. The official MGI homology graph links experimental synaptic localization to PMID:18083105 and PMID:27033548. The complete PMID:18083105 abstract describes postnatal synaptic C1q localization; the actual PMID:27033548 main narrative directly reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain contextual orthology rather than claiming human imaging. The rat-specific culture experiment is not separately described in the accessible abstract and is retained with curator deference to the mapped rat donor record. |
| GO:0048018 receptor ligand activity | IBA GO_REF:0000033 | ACCEPT | Summary: The C1q recognition complex can act as an extracellular signaling-receptor ligand. Reason: The exact PAINT IBD at PTN008355511 derives this activity from adiponectin-family experimental descendants. This is a phylogenetic node assertion, not a pairwise similarity transfer. Direct C1q-CD33 binding and CD33 ITIM activation independently support the target complex activity. No target-specific loss is established, and the full family alignment was not independently reconstructed. Accept the receptor-recognition activity consistently with the independent target evidence and the contributed receptor-ligand core. The documented example is CD33 signaling in human monocytes; neither isolated C1QA sufficiency nor universal CD33 dependence is claimed. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008355511 SUPPORTS TRANSFER Exact non-negated PTHR15427 IBD row inspected. The preserved source list is phylogenetic grounding; full tree/MSA reconstruction was not performed. Supporting Evidence: |
| GO:0048143 astrocyte activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: C1qa-dependent complement influences astrocyte activation in a mouse disease model. Reason: The mouse C1qa donor is traced through the official MGI homology record to PMID:15269255. In the actual paper, C1qa deletion reduces plaque-associated GFAP/astrocyte activation in APP-transgenic mice without decreasing amyloid burden. Retain a contextual human orthology annotation; neither a human intervention nor a cell-autonomous astrocyte receptor mechanism is claimed. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The mouse C1qa donor is traced through the official MGI homology record to PMID:15269255. In the actual paper, C1qa deletion reduces plaque-associated GFAP/astrocyte activation in APP-transgenic mice without decreasing amyloid burden. Retain a contextual human orthology annotation; neither a human intervention nor a cell-autonomous astrocyte receptor mechanism is claimed. Supporting Evidence: |
| GO:0048143 astrocyte activation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: C1qa-dependent complement influences astrocyte activation in a mouse disease model. Reason: The mouse C1qa donor is traced through the official MGI homology record to PMID:15269255. In the actual paper, C1qa deletion reduces plaque-associated GFAP/astrocyte activation in APP-transgenic mice without decreasing amyloid burden. Retain a contextual human orthology annotation; neither a human intervention nor a cell-autonomous astrocyte receptor mechanism is claimed. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The mouse C1qa donor is traced through the official MGI homology record to PMID:15269255. In the actual paper, C1qa deletion reduces plaque-associated GFAP/astrocyte activation in APP-transgenic mice without decreasing amyloid burden. Retain a contextual human orthology annotation; neither a human intervention nor a cell-autonomous astrocyte receptor mechanism is claimed. Supporting Evidence: |
| GO:0050808 synapse organization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: C1q-dependent synaptic elimination can alter synapse organization in mouse models. Reason: The preserved source is mouse C1qa/P98086. The official MGI homology graph maps the experimental donor association to PMID:27033548. The complete available main narrative reports C1q synaptic localization plus C1qa knockout and anti-C1q interventions preserving synaptic puncta and LTP after oligomeric amyloid challenge. Retain this contextual organization role, not a claim that C1QA is a structural synaptic scaffold or that the experiment was performed in humans. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The preserved source is mouse C1qa/P98086. The official MGI homology graph maps the experimental donor association to PMID:27033548. The complete available main narrative reports C1q synaptic localization plus C1qa knockout and anti-C1q interventions preserving synaptic puncta and LTP after oligomeric amyloid challenge. Retain this contextual organization role, not a claim that C1QA is a structural synaptic scaffold or that the experiment was performed in humans. Supporting Evidence: |
| GO:0050808 synapse organization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: C1q-dependent synaptic elimination can alter synapse organization in mouse models. Reason: The preserved source is mouse C1qa/P98086. The official MGI homology graph maps the experimental donor association to PMID:27033548. The complete available main narrative reports C1q synaptic localization plus C1qa knockout and anti-C1q interventions preserving synaptic puncta and LTP after oligomeric amyloid challenge. Retain this contextual organization role, not a claim that C1QA is a structural synaptic scaffold or that the experiment was performed in humans. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The preserved source is mouse C1qa/P98086. The official MGI homology graph maps the experimental donor association to PMID:27033548. The complete available main narrative reports C1q synaptic localization plus C1qa knockout and anti-C1q interventions preserving synaptic puncta and LTP after oligomeric amyloid challenge. Retain this contextual organization role, not a claim that C1QA is a structural synaptic scaffold or that the experiment was performed in humans. Supporting Evidence: |
| GO:0062167 complement component C1q complex | IDA PMID:24626930 Complement is activated by IgG hexamers assembled at the cel... | ACCEPT | Summary: C1QA is one of the three distinct chains in the C1q recognition complex. Reason: PMID:24626930 examines the C1q-containing recognition assembly recruited to IgG hexamers. Independent heterotrimer structural evidence in PMID:12960167 establishes A/B/C composition, and the source complex term accurately captures membership. |
| GO:0062167 complement component C1q complex | IPI PMID:29449492 Structures of C1-IgG1 provide insights into how danger patte... | ACCEPT | Summary: C1QA contributes to the C1q subcomplex within C1. Reason: The PMID:29449492 C1-IgG1 structural study directly analyzes the C1q recognition subcomplex. Preserve membership rather than replacing it with a binding term or assigning C1r/C1s catalysis. |
| GO:0098794 postsynapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Postsynaptic C1q localization is supported in the mouse donor context. Reason: The source is mouse C1qa/P98086. MGI traces the donor postsynapse annotation to PMID:27033548. The actual paper reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain this contextual location without inferring membrane insertion, a resolved membrane leaflet, or human-cell imaging. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The source is mouse C1qa/P98086. MGI traces the donor postsynapse annotation to PMID:27033548. The actual paper reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain this contextual location without inferring membrane insertion, a resolved membrane leaflet, or human-cell imaging. Supporting Evidence: |
| GO:0098794 postsynapse | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Postsynaptic C1q localization is supported in the mouse donor context. Reason: The source is mouse C1qa/P98086. MGI traces the donor postsynapse annotation to PMID:27033548. The actual paper reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain this contextual location without inferring membrane insertion, a resolved membrane leaflet, or human-cell imaging. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The source is mouse C1qa/P98086. MGI traces the donor postsynapse annotation to PMID:27033548. The actual paper reports C1q colocalization with PSD95-positive puncta by structured illumination microscopy in mouse hippocampus. Retain this contextual location without inferring membrane insertion, a resolved membrane leaflet, or human-cell imaging. Supporting Evidence: |
| GO:0098883 synapse pruning | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: C1q-dependent recognition contributes to synapse pruning in mouse models. Reason: The source is mouse C1qa/P98086. MGI links synapse-pruning evidence to PMID:27033548. Its actual main narrative combines C1qa knockout/anti-C1q blockade, downstream C3 deposition, synaptic puncta loss and CR3-dependent microglial engulfment. Retain the existing contextual orthology assertion: C1q supplies recognition/complement initiation while microglia execute engulfment. No new process assertion or human assay is implied. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The source is mouse C1qa/P98086. MGI links synapse-pruning evidence to PMID:27033548. Its actual main narrative combines C1qa knockout/anti-C1q blockade, downstream C3 deposition, synaptic puncta loss and CR3-dependent microglial engulfment. Retain the existing contextual orthology assertion: C1q supplies recognition/complement initiation while microglia execute engulfment. No new process assertion or human assay is implied. Supporting Evidence: |
| GO:0098883 synapse pruning | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: C1q-dependent recognition contributes to synapse pruning in mouse models. Reason: The source is mouse C1qa/P98086. MGI links synapse-pruning evidence to PMID:27033548. Its actual main narrative combines C1qa knockout/anti-C1q blockade, downstream C3 deposition, synaptic puncta loss and CR3-dependent microglial engulfment. Retain the existing contextual orthology assertion: C1q supplies recognition/complement initiation while microglia execute engulfment. No new process assertion or human assay is implied. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The source is mouse C1qa/P98086. MGI links synapse-pruning evidence to PMID:27033548. Its actual main narrative combines C1qa knockout/anti-C1q blockade, downstream C3 deposition, synaptic puncta loss and CR3-dependent microglial engulfment. Retain the existing contextual orthology assertion: C1q supplies recognition/complement initiation while microglia execute engulfment. No new process assertion or human assay is implied. Supporting Evidence: |
| GO:0098888 extrinsic component of presynaptic membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The precise presynaptic membrane association remains unresolved. Reason: The exact mouse C1qa/P98086 source is preserved. An extrinsic membrane component is loosely associated with a membrane surface; the term does not demand membrane insertion or resolved leaflet topology. Nevertheless, secretion and general synaptic localization in the accessible PMID:18083105 abstract do not alone identify a presynaptic membrane association. The inspected MGI donor table did not expose the direct experiment for this exact transfer. Retain UNDECIDED for that source-specific access gap, without alleging incorrect orthology or absence of synaptic C1q. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P98086 UNRESOLVED The exact mouse C1qa/P98086 source is preserved. An extrinsic membrane component is loosely associated with a membrane surface; the term does not demand membrane insertion or resolved leaflet topology. Nevertheless, secretion and general synaptic localization in the accessible PMID:18083105 abstract do not alone identify a presynaptic membrane association. The inspected MGI donor table did not expose the direct experiment for this exact transfer. Retain UNDECIDED for that source-specific access gap, without alleging incorrect orthology or absence of synaptic C1q. |
| GO:0098890 extrinsic component of postsynaptic membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The precise postsynaptic membrane association remains unresolved. Reason: The exact mouse C1qa/P98086 source is preserved. PMID:27033548 directly shows C1q colocalization with PSD95-positive puncta in mouse hippocampus and supports the broader postsynaptic annotation. Extrinsic membrane association does not require insertion or leaflet-level proof, but punctum colocalization alone does not resolve association with the postsynaptic membrane itself. The inspected donor table did not expose the direct experiment underlying this exact transfer. Retain UNDECIDED for the unavailable source-specific localization evidence, not because extracellular C1q cannot associate with a membrane. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P98086 UNRESOLVED The exact mouse C1qa/P98086 source is preserved. PMID:27033548 directly shows C1q colocalization with PSD95-positive puncta in mouse hippocampus and supports the broader postsynaptic annotation. Extrinsic membrane association does not require insertion or leaflet-level proof, but punctum colocalization alone does not resolve association with the postsynaptic membrane itself. The inspected donor table did not expose the direct experiment underlying this exact transfer. Retain UNDECIDED for the unavailable source-specific localization evidence, not because extracellular C1q cannot associate with a membrane. |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | UNDECIDED | Summary: The exact glutamatergic-synapse donor assignment remains unresolved. Reason: The exact mouse C1qa/P98086 source is preserved. A glutamatergic synapse uses glutamate as its neurotransmitter. The inspected mouse studies establish synaptic localization and include PSD95-positive puncta and hippocampal physiology, making this neuronal context plausible. However, the direct experiment mapped to this particular fine donor term was not exposed in the inspected MGI table, and the accessible 2007 source is abstract-only. Retain UNDECIDED for that source-specific access limit without asserting that the biological localization is contradicted. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P98086 UNRESOLVED The exact mouse C1qa/P98086 source is preserved. A glutamatergic synapse uses glutamate as its neurotransmitter. The inspected mouse studies establish synaptic localization and include PSD95-positive puncta and hippocampal physiology, making this neuronal context plausible. However, the direct experiment mapped to this particular fine donor term was not exposed in the inspected MGI table, and the accessible 2007 source is abstract-only. Retain UNDECIDED for that source-specific access limit without asserting that the biological localization is contradicted. |
| GO:0106139 symbiont cell surface | IDA PMID:34155115 C1q binding to surface-bound IgG is stabilized by C1r(2)s(2)... | ACCEPT | Summary: Human C1q acts on antibody-coated bacterial surfaces. Reason: The actual PMID:34155115 Methods and Results demonstrate C1q/C1 binding on Staphylococcus aureus bearing human anti-wall-teichoic-acid antibodies, with downstream human-complement deposition. This directly supports the host recognition complex on a symbiont cell surface; it does not imply bacterial synthesis of C1QA or membrane insertion. Supporting Evidence: |
| GO:0150062 complement-mediated synapse pruning | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Classical complement recognition by C1q contributes to developmental synaptic pruning. Reason: The mouse C1qa source is traced by MGI to PMID:18083105 for complement-mediated pruning. The complete source abstract reports C1q/C3-deficient mice with impaired synaptic elimination and retinogeniculate refinement. Retain this existing contextual orthology annotation; C1q supplies recognition/complement initiation while cellular engulfment is executed by phagocytes. Human developmental timing and autonomous A-chain sufficiency are not demonstrated. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The mouse C1qa source is traced by MGI to PMID:18083105 for complement-mediated pruning. The complete source abstract reports C1q/C3-deficient mice with impaired synaptic elimination and retinogeniculate refinement. Retain this existing contextual orthology annotation; C1q supplies recognition/complement initiation while cellular engulfment is executed by phagocytes. Human developmental timing and autonomous A-chain sufficiency are not demonstrated. Supporting Evidence: |
| GO:0150062 complement-mediated synapse pruning | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Classical complement recognition by C1q contributes to developmental synaptic pruning. Reason: The mouse C1qa source is traced by MGI to PMID:18083105 for complement-mediated pruning. The complete source abstract reports C1q/C3-deficient mice with impaired synaptic elimination and retinogeniculate refinement. Retain this existing contextual orthology annotation; C1q supplies recognition/complement initiation while cellular engulfment is executed by phagocytes. Human developmental timing and autonomous A-chain sufficiency are not demonstrated. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The mouse C1qa source is traced by MGI to PMID:18083105 for complement-mediated pruning. The complete source abstract reports C1q/C3-deficient mice with impaired synaptic elimination and retinogeniculate refinement. Retain this existing contextual orthology annotation; C1q supplies recognition/complement initiation while cellular engulfment is executed by phagocytes. Human developmental timing and autonomous A-chain sufficiency are not demonstrated. Supporting Evidence: |
| GO:0150064 vertebrate eye-specific patterning | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: C1qa-dependent complement contributes to eye-specific neural pattern refinement in mice. Reason: The official MGI homology table maps the mouse C1qa donor assertion to PMID:18083105. The complete source abstract explicitly reports failure of retinogeniculate connection refinement and excess retinal innervation in C1q-deficient mice. Retain the existing developmental orthology assignment as non-core, without treating it as general eye morphogenesis or a directly assayed human phenotype. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The official MGI homology table maps the mouse C1qa donor assertion to PMID:18083105. The complete source abstract explicitly reports failure of retinogeniculate connection refinement and excess retinal innervation in C1q-deficient mice. Retain the existing developmental orthology assignment as non-core, without treating it as general eye morphogenesis or a directly assayed human phenotype. Supporting Evidence: |
| GO:0150064 vertebrate eye-specific patterning | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: C1qa-dependent complement contributes to eye-specific neural pattern refinement in mice. Reason: The official MGI homology table maps the mouse C1qa donor assertion to PMID:18083105. The complete source abstract explicitly reports failure of retinogeniculate connection refinement and excess retinal innervation in C1q-deficient mice. Retain the existing developmental orthology assignment as non-core, without treating it as general eye morphogenesis or a directly assayed human phenotype. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P98086 SUPPORTS TRANSFER The official MGI homology table maps the mouse C1qa donor assertion to PMID:18083105. The complete source abstract explicitly reports failure of retinogeniculate connection refinement and excess retinal innervation in C1q-deficient mice. Retain the existing developmental orthology assignment as non-core, without treating it as general eye morphogenesis or a directly assayed human phenotype. Supporting Evidence: |
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Download this section (compressed HTML)Q: Which C1QA residues make physiological contributions to phosphatidylserine recognition independently of the established C-chain site, beyond crystal-packing contacts?
Q: Which exact donor experiments support the fine presynaptic/post-synaptic membrane and glutamatergic-synapse transfers to human C1QA?
Q: Can the original PMID:6249812 experimental text and the C1QA extracellular-matrix target table in PMID:28675934 be inspected to resolve their source-specific UNDECIDED rows?
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