DAG1 encodes dystroglycan, a cell-surface receptor that links extracellular matrix to the membrane-associated cytoskeleton. The 895-residue precursor enters the secretory pathway and undergoes SEA-domain self-processing into extracellular alpha-dystroglycan and transmembrane beta-dystroglycan, which remain noncovalently associated. Glycosylated alpha-dystroglycan binds laminins and other matrix ligands, including agrin and perlecan. Beta-dystroglycan anchors this ligand-binding surface in the membrane and engages cytoplasmic partners such as dystrophin, utrophin, ankyrin and CLASPs. This linkage supports basement-membrane organization and tissue integrity, with specialized roles at muscle membranes, glial interfaces and synapses. Glycan-dependent ligand binding, cytoplasmic-tail phosphorylation and proteolytic processing modify receptor behavior. Released alpha-derived material and intracellular beta-chain pools occur in specific contexts, including nuclear trafficking in cultured human cells.
Curated functional classes representing distinct biological activities. These may be splice variants, cleavage products, or other forms with different functions.
DAG1_ALPHAPRO_0000021065 (residues 30-653) DAG1_BETAPRO_0000021066 (residues 654-895) | GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-9913332 | KEEP AS NON CORE | Summary: Beta-dystroglycan passes through the Golgi membrane during complex assembly and delivery. Reason: The cited Reactome events contain the membrane-spanning beta chain, residues 654–895, in Golgi complexes or transport intermediates. This supports a biosynthetic location, distinct from the principal mature receptor function at the plasma membrane; it does not assign glycan-transfer activity to DAG1. |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-9913336 | KEEP AS NON CORE | Summary: Beta-dystroglycan passes through the Golgi membrane during complex assembly and delivery. Reason: The cited Reactome events contain the membrane-spanning beta chain, residues 654–895, in Golgi complexes or transport intermediates. This supports a biosynthetic location, distinct from the principal mature receptor function at the plasma membrane; it does not assign glycan-transfer activity to DAG1. |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-9913337 | KEEP AS NON CORE | Summary: Beta-dystroglycan passes through the Golgi membrane during complex assembly and delivery. Reason: The cited Reactome events contain the membrane-spanning beta chain, residues 654–895, in Golgi complexes or transport intermediates. This supports a biosynthetic location, distinct from the principal mature receptor function at the plasma membrane; it does not assign glycan-transfer activity to DAG1. |
| GO:0001618 virus receptor activity | IDA PMID:22156524 Identification of cell surface molecules involved in dystrog... | KEEP AS NON CORE | Summary: Dystroglycan can support Lassa-virus entry in susceptible cells. Reason: The original tests dystroglycan-positive controls as well as alternative entry routes: extracellular alpha-DG constructs inhibit susceptible-cell infection, and DAG1 expression restores entry into deficient cells. Its demonstration of dystroglycan-independent routes does not negate this positive receptor role. Dependence is cell-context and glycosylation dependent, not a universal requirement for Lassa entry. Supporting Evidence: |
| GO:0001954 positive regulation of cell-matrix adhesion | IEA GO_REF:0000107 | ACCEPT | Summary: Dystroglycan-mediated matrix attachment supports cell-matrix adhesion. Reason: The literal rat ortholog donor carries an experimental adhesion assertion (PMID:9153251). Conservation of the extracellular ligand-binding and membrane-linking architecture, together with direct human ligand-dependent adhesion evidence, supports this transfer. The term describes the receptor contribution to adhesion, not an enzymatic activity. |
| GO:0002009 morphogenesis of an epithelium | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Dystroglycan contributes to epithelial morphogenesis through basal matrix attachment. Reason: The actual PAINT assertion is on ancestral node PTN001090124 on the human lineage, with fly, mouse and worm descendants. Human receptor architecture and the chick epiblast perturbation study are compatible with this conserved developmental role. The epiblast study is comparative evidence, not a direct human embryogenesis experiment. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN001090124 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20260210. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. Supporting Evidence: |
| GO:0002162 dystroglycan binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Association of the two processed dystroglycan chains supports dystroglycan binding. Reason: The literal mouse ortholog has experimental support for this term. Alpha and beta chains derive from one precursor and remain noncovalently associated; this source-level association is retained without inventing a separate soluble-ligand receptor activity or treating the same-gene partner as a curation error. |
| GO:0003779 actin binding | IDA PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | UNDECIDED | Summary: The source-specific actin-binding experiment remains unresolved. Reason: The human platelet paper describes cytoskeletal interplay, but its operative actin-binding assay was not recovered. The broad abstract and independently supported indirect linkage through dystrophin or utrophin do not establish the specific actin interaction asserted here. Preserve the positive IDA assertion without inferring that DAG1 cannot bind actin. Supporting Evidence: |
| GO:0004252 serine-type endopeptidase activity | EXP PMID:17905726 SEA domain proteolysis determines the functional composition... | MODIFY | Summary: Dystroglycan undergoes intrinsic SEA-domain endoproteolytic self-processing. Reason: The original reports S654-dependent intramolecular processing, effects of hydroxyl/thiol substitutions and the neighboring loop, and ER-dependent folding. These experiments support self-cleavage of the precursor but do not establish the serine/acidic/basic catalytic triad required by GO:0004252. General endopeptidase activity preserves the demonstrated bond cleavage without assigning that specific enzyme mechanism. This is distinct from MMP-mediated ectodomain shedding; cleavage-defective constructs can still bind and assemble laminin. Proposed replacements: endopeptidase activity Supporting Evidence: |
| GO:0005055 laminin receptor activity | IBA GO_REF:0000033 | ACCEPT | Summary: Glycosylated alpha-dystroglycan acts as a laminin receptor. Reason: This is a defining function of the extracellular alpha chain in the membrane-associated alpha/beta complex. The mouse transfer and the actual on-lineage PAINT node PTN001090124 are consistent with human ligand-binding and matrix-attachment evidence. Ligand-binding competence depends on appropriate glycosylation; DAG1 is not the glycosyltransferase that produces that modification. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001090124 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20260129. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. |
| GO:0005055 laminin receptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: Glycosylated alpha-dystroglycan acts as a laminin receptor. Reason: This is a defining function of the extracellular alpha chain in the membrane-associated alpha/beta complex. The mouse transfer and the actual on-lineage PAINT node PTN001090124 are consistent with human ligand-binding and matrix-attachment evidence. Ligand-binding competence depends on appropriate glycosylation; DAG1 is not the glycosyltransferase that produces that modification. |
| GO:0005055 laminin receptor activity | ISS GO_REF:0000024 | ACCEPT | Summary: Glycosylated alpha-dystroglycan acts as a laminin receptor. Reason: This is a defining function of the extracellular alpha chain in the membrane-associated alpha/beta complex. The mouse transfer and the actual on-lineage PAINT node PTN001090124 are consistent with human ligand-binding and matrix-attachment evidence. Ligand-binding competence depends on appropriate glycosylation; DAG1 is not the glycosyltransferase that produces that modification. |
| GO:0005509 calcium ion binding | IEA GO_REF:0000002 | KEEP AS NON CORE | Summary: A recombinant human DAG1 structure directly supports calcium coordination. Reason: The actual 8UF4 deposit contains one modeled calcium ion coordinated by five native DAG1 residues in the human 491–748 IGL–SEA fragment. This independently supports the literal InterPro-derived calcium-binding assertion. Refolding used 50 mM calcium and purification used 10 mM calcium; native full-length occupancy, affinity and calcium-regulated physiological function remain unestablished. This is target coordination, not an inference from ligand-side calcium dependence. The paper’s wording about both molecules is not substituted for the single calcium atom modeled in the deposited structure. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10767429 Contribution of the different modules in the utrophin carbox... | MODIFY | Summary: Beta-dystroglycan binds the cytoskeletal protein utrophin. Reason: The source abstract explicitly examines the utrophin modules that bind beta-dystroglycan. The literal partner P46939 is utrophin, a cytoskeletal linker, so cytoskeletal protein binding is a supported narrower class. The original full text was not recovered; retain curator deference for the particular experimental assertion and do not claim a new direct human construct analysis. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10988290 Caveolin-3 directly interacts with the C-terminal tail of be... | KEEP AS NON CORE | Summary: The beta-dystroglycan cytoplasmic tail binds caveolin-3. Reason: The recovered original includes GST-tail binding, 293T association, C-terminal deletion and peptide experiments, with controls supporting the C-terminal PPxY region. Preserve this positive interaction under the supported-binding policy. The paper’s proposed WW-like classification of caveolin is not used to invent a modern domain-binding refinement, and heterologous assays do not by themselves establish every native membrane context. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:11495720 The interaction of dystrophin with beta-dystroglycan is regu... | MODIFY | Summary: Beta-dystroglycan binds the cytoskeletal linker dystrophin. Reason: The literal partner P11532 is dystrophin, and the complete abstract describes phosphorylation-dependent disruption of the beta-DG–dystrophin interaction using myotubes and peptide experiments. This supports the narrower cytoskeletal protein class. The original full text remains unavailable; the measured phosphorylation context is preserved without assigning identical binding to every phospho-state. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12592373 hAG-2 and hAG-3, human homologues of genes involved in diffe... | KEEP AS NON CORE | Summary: An alpha-dystroglycan fragment interacts with AGR2 in a yeast two-hybrid assay. Reason: The original used human AGR2 bait and identified DAG1 extracellular prey fragments from library screening. This is an explicit positive interaction, retained with its fragment and heterologous assay limits. It does not establish that DAG1 catalyzes AGR2 chemistry or mediates the tumor phenotype discussed in the paper. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12592373 hAG-2 and hAG-3, human homologues of genes involved in diffe... | KEEP AS NON CORE | Summary: An alpha-dystroglycan fragment interacts with AGR3 in a yeast two-hybrid assay. Reason: The original used human AGR3 bait and recovered DAG1 extracellular prey fragments. Retain the positive measured binding without inferring a native enzymatic or tumor-promoting role for DAG1 from the partner’s identity or expression correlation. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | MODIFY | Summary: A DAG1 peptide binds NCK1 SH3 domains in vitro. Reason: The literal curated records and original supplementary table identify NCK1 SH3-domain interactions with human DAG1 residues 300–313. SH3 domain binding is therefore more precise than generic protein binding for this assay. That peptide belongs to the extracellular alpha chain, whereas NCK1 is intracellular: these experiments do not establish accessibility or colocalization in a mature intact receptor. The paper’s validation percentage for a different partner subset is not transferred to this pair. Proposed replacements: SH3 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | UNDECIDED | Summary: The source-specific MAP2 interaction remains unresolved. Reason: The literal partner P11137 is MAP2. The platelet original was not recovered, and its general actin/microtubule discussion does not establish this individual pair. Preserve the positive IPI source object without substituting independently measured CLASP interactions or interpreting the absence of a current IntAct/MINT match as negative evidence. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19109891 An ankyrin-based mechanism for functional organization of dy... | MODIFY | Summary: The beta-dystroglycan cytoplasmic tail binds ankyrin-G. Reason: The exact records pair human DAG1 residues 776–895 with rat ankyrin-G Q3T1J5 and include tail-region perturbations. The source abstract distinguishes ankyrin-G-dependent dystroglycan trafficking from ankyrin-B-dependent dystrophin trafficking. Ankyrin binding is a justified narrower class; the original full text was not recovered, so detailed native-complex geometry is not inferred. Proposed replacements: ankyrin binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23940118 Epiblast integrity requires CLASP and Dystroglycan-mediated ... | MODIFY | Summary: Dystroglycan associates with the microtubule-associated protein CLASP1. Reason: The original includes human DAG1 and human CLASP1 constructs with reciprocal co-immunoprecipitation in HEK293 cells. CLASP1 is an established cytoskeletal protein, supporting this class refinement. Complex association is not equated with purified binary binding, and the accompanying chick epiblast perturbation is kept separate from the human interaction assay. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23940118 Epiblast integrity requires CLASP and Dystroglycan-mediated ... | MODIFY | Summary: Dystroglycan associates with the microtubule-associated protein CLASP2. Reason: Human DAG1 and CLASP2 constructs were tested by co-immunoprecipitation in the original. The established microtubule-associated identity of CLASP2 supports cytoskeletal protein binding. This does not assert isolated binary binding or turn the chick morphogenesis experiments into direct human developmental evidence. Proposed replacements: cytoskeletal protein binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:9417121 Agrin is a high-affinity binding protein of dystroglycan in ... | MODIFY | Summary: Dystroglycan binds agrin, a heparan sulfate proteoglycan. Reason: The complete abstract describes agrin affinity purification, co-precipitation and solid-phase binding in non-muscle tissues. The literal human partner O00468 is agrin, supporting refinement to the established proteoglycan-binding class already represented elsewhere. This means binding the proteoglycan, not a demonstrated interaction with its heparan-sulfate sugar alone. The abstract does not establish the species of every tissue preparation, and full-text assay details were not recovered. Proposed replacements: heparan sulfate proteoglycan binding Supporting Evidence: |
| GO:0005576 extracellular region | HDA PMID:16502470 Human colostrum: identification of minor proteins in the aqu... | KEEP AS NON CORE | Summary: DAG1-derived material was detected in the extracellular colostrum proteome. Reason: The source is a human aqueous-colostrum proteomics survey. Extracellular alpha-DG and released N-terminal material provide independent biological coherence, but the target-specific table and processed-chain identity were not recovered. Retain this contextual compartment observation with curator deference; do not infer secretion of intact membrane-spanning beta-DG or an extracellular catalytic function. |
| GO:0005576 extracellular region | HDA PMID:27068509 Extracellular matrix remodelling in response to venous hyper... | KEEP AS NON CORE | Summary: DAG1-derived material occurs in an extracellular-matrix proteomics context. Reason: The human varicose-vein study surveys extracellular matrix remodeling. The annotation is compatible with extracellular alpha-DG and its matrix associations. The target-specific quantitative table was not independently recovered, so the particular survey assignment is retained with curator deference rather than interpreted as a new molecular activity. Supporting Evidence: |
| GO:0005576 extracellular region | IDA PMID:18201566 Processing and secretion of the N-terminal domain of alpha-d... | KEEP AS NON CORE | Summary: An N-terminal alpha-dystroglycan product can be released extracellularly. Reason: The source abstract explicitly reports processing and secretion in cell culture and detection in normal human serum. This supports a released product context, not the inference that the entire 895-residue precursor or mature beta chain is freely secreted. Exact processing coordinates are not reconstructed from the abstract alone. Supporting Evidence: |
| GO:0005576 extracellular region | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Extracellular alpha-dystroglycan and released products support the broad compartment mapping. Reason: The actual ARBA00027128 condition branch matches the target, and the literal rat/UniProt location sources are preserved. This broad annotation encompasses released alpha-derived material as well as the extracellular receptor domain; it is not replaced solely by the more specific basement-membrane annotation, which does not capture every product context. Supporting Evidence: |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2396395 | KEEP AS NON CORE | Summary: The extracellular alpha chain participates in matrix-facing receptor complexes. Reason: The cited Reactome event contains processed alpha-DAG1, residues 30–653, in an extracellular ligand-bound or surface-associated complex. This supports extracellular exposure without asserting that the membrane-spanning beta chain is a soluble extracellular protein. The event’s particular ligand and complex role are retained as modeled context. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9010872 | KEEP AS NON CORE | Summary: The extracellular alpha chain participates in matrix-facing receptor complexes. Reason: The cited Reactome event contains processed alpha-DAG1, residues 30–653, in an extracellular ligand-bound or surface-associated complex. This supports extracellular exposure without asserting that the membrane-spanning beta chain is a soluble extracellular protein. The event’s particular ligand and complex role are retained as modeled context. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9913333 | KEEP AS NON CORE | Summary: The extracellular alpha chain participates in matrix-facing receptor complexes. Reason: The cited Reactome event contains processed alpha-DAG1, residues 30–653, in an extracellular ligand-bound or surface-associated complex. This supports extracellular exposure without asserting that the membrane-spanning beta chain is a soluble extracellular protein. The event’s particular ligand and complex role are retained as modeled context. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9913336 | KEEP AS NON CORE | Summary: The extracellular alpha chain participates in matrix-facing receptor complexes. Reason: The cited Reactome event contains processed alpha-DAG1, residues 30–653, in an extracellular ligand-bound or surface-associated complex. This supports extracellular exposure without asserting that the membrane-spanning beta chain is a soluble extracellular protein. The event’s particular ligand and complex role are retained as modeled context. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9913339 | KEEP AS NON CORE | Summary: The extracellular alpha chain participates in matrix-facing receptor complexes. Reason: The cited Reactome event contains processed alpha-DAG1, residues 30–653, in an extracellular ligand-bound or surface-associated complex. This supports extracellular exposure without asserting that the membrane-spanning beta chain is a soluble extracellular protein. The event’s particular ligand and complex role are retained as modeled context. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-9914537 | KEEP AS NON CORE | Summary: The extracellular alpha chain participates in matrix-facing receptor complexes. Reason: The cited Reactome event contains processed alpha-DAG1, residues 30–653, in an extracellular ligand-bound or surface-associated complex. This supports extracellular exposure without asserting that the membrane-spanning beta chain is a soluble extracellular protein. The event’s particular ligand and complex role are retained as modeled context. |
| GO:0005604 basement membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Alpha-dystroglycan occupies the basement-membrane–cell interface. Reason: Human inner-ear immunohistochemistry supports basement-membrane-associated DAG1, and the literal mouse/UniProt mappings agree. The PAINT assertion lies on the actual human lineage at PTN002727163; inclusion of human Q14118 among descendant evidence is legitimate, not circular. This location describes the extracellular receptor interface rather than secretion of the complete precursor. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN002727163 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20200421. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. Supporting Evidence: |
| GO:0005604 basement membrane | IDA PMID:19348877 Immunohistochemical distribution of basement membrane protei... | ACCEPT | Summary: Alpha-dystroglycan occupies the basement-membrane–cell interface. Reason: Human inner-ear immunohistochemistry supports basement-membrane-associated DAG1, and the literal mouse/UniProt mappings agree. The PAINT assertion lies on the actual human lineage at PTN002727163; inclusion of human Q14118 among descendant evidence is legitimate, not circular. This location describes the extracellular receptor interface rather than secretion of the complete precursor. Supporting Evidence: |
| GO:0005604 basement membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Alpha-dystroglycan occupies the basement-membrane–cell interface. Reason: Human inner-ear immunohistochemistry supports basement-membrane-associated DAG1, and the literal mouse/UniProt mappings agree. The PAINT assertion lies on the actual human lineage at PTN002727163; inclusion of human Q14118 among descendant evidence is legitimate, not circular. This location describes the extracellular receptor interface rather than secretion of the complete precursor. Supporting Evidence: |
| GO:0005654 nucleoplasm | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Human cell-atlas imaging supports a nucleoplasmic DAG1 pool. Reason: The current HPA record reports nucleoplasm as an additional location, including RT-4, HaCaT and U2OS observations. This is a contextual localization annotation, not evidence of a defined nuclear enzymatic or transcriptional function. The antibody-level readout does not by itself identify every processed molecular species. |
| GO:0005654 nucleoplasm | IDA PMID:18764929 Nuclear translocation of beta-dystroglycan reveals a distinc... | KEEP AS NON CORE | Summary: Beta-dystroglycan can accumulate in the nucleus in cultured human cells. Reason: The original combines cell fractionation with marker controls, microscopy and nuclear-localization-sequence constructs. It reports full-length beta-chain nuclear material, and an uncleavable precursor mutant can also enter the nucleus. Retain the compartment observation without making autoproteolysis an absolute prerequisite or assigning a nuclear function. Supporting Evidence: |
| GO:0005654 nucleoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The curated nucleoplasmic mapping reflects a context-dependent nuclear pool. Reason: The UniProt subcellular-location mapping is supported by the human cell study and HPA observations. Nuclear presence is secondary to the cell-surface matrix receptor role and does not establish transcription-factor or nuclear enzyme activity. Supporting Evidence: |
| GO:0005737 cytoplasm | IDA PMID:18764929 Nuclear translocation of beta-dystroglycan reveals a distinc... | KEEP AS NON CORE | Summary: The source reports cytoplasmic material during beta-dystroglycan trafficking. Reason: The original fractionation and localization experiments support a cytoplasmic pool in the studied human cells. This does not establish that normally glycosylated alpha-DG is a freely cytosolic protein, nor does it validate every independent cytosol annotation from a defective-glycosylation pathway model. Supporting Evidence: |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-5615637 | KEEP AS NON CORE | Summary: Alpha-dystroglycan occupies the ER lumen during precursor maturation. Reason: The source event places the luminal alpha-chain region, residues 30–653, or its glycosylated forms in the ER. The receptor is a substrate of the named glycosylation enzymes, while intrinsic SEA processing is a distinct reaction. Retain this biosynthetic compartment without assigning the modifying enzyme’s activity to DAG1. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8879117 | KEEP AS NON CORE | Summary: Alpha-dystroglycan occupies the ER lumen during precursor maturation. Reason: The source event places the luminal alpha-chain region, residues 30–653, or its glycosylated forms in the ER. The receptor is a substrate of the named glycosylation enzymes, while intrinsic SEA processing is a distinct reaction. Retain this biosynthetic compartment without assigning the modifying enzyme’s activity to DAG1. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8931648 | KEEP AS NON CORE | Summary: Alpha-dystroglycan occupies the ER lumen during precursor maturation. Reason: The source event places the luminal alpha-chain region, residues 30–653, or its glycosylated forms in the ER. The receptor is a substrate of the named glycosylation enzymes, while intrinsic SEA processing is a distinct reaction. Retain this biosynthetic compartment without assigning the modifying enzyme’s activity to DAG1. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-8931653 | KEEP AS NON CORE | Summary: Alpha-dystroglycan occupies the ER lumen during precursor maturation. Reason: The source event places the luminal alpha-chain region, residues 30–653, or its glycosylated forms in the ER. The receptor is a substrate of the named glycosylation enzymes, while intrinsic SEA processing is a distinct reaction. Retain this biosynthetic compartment without assigning the modifying enzyme’s activity to DAG1. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9913329 | KEEP AS NON CORE | Summary: Alpha-dystroglycan occupies the ER lumen during precursor maturation. Reason: The source event places the luminal alpha-chain region, residues 30–653, or its glycosylated forms in the ER. The receptor is a substrate of the named glycosylation enzymes, while intrinsic SEA processing is a distinct reaction. Retain this biosynthetic compartment without assigning the modifying enzyme’s activity to DAG1. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9913337 | KEEP AS NON CORE | Summary: Alpha-dystroglycan occupies the ER lumen during precursor maturation. Reason: The source event places the luminal alpha-chain region, residues 30–653, or its glycosylated forms in the ER. The receptor is a substrate of the named glycosylation enzymes, while intrinsic SEA processing is a distinct reaction. Retain this biosynthetic compartment without assigning the modifying enzyme’s activity to DAG1. |
| GO:0005788 endoplasmic reticulum lumen | TAS Reactome:R-HSA-9940714 | KEEP AS NON CORE | Summary: Alpha-dystroglycan occupies the ER lumen during precursor maturation. Reason: The source event places the luminal alpha-chain region, residues 30–653, or its glycosylated forms in the ER. The receptor is a substrate of the named glycosylation enzymes, while intrinsic SEA processing is a distinct reaction. Retain this biosynthetic compartment without assigning the modifying enzyme’s activity to DAG1. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9913329 | KEEP AS NON CORE | Summary: The precursor and beta chain are membrane-associated during ER maturation. Reason: The modeled precursor or beta-DG segment includes the transmembrane anchor and is located in the ER membrane during processing and export. This is a normal biosynthetic location, not the primary site of the mature extracellular-matrix receptor function. |
| GO:0005789 endoplasmic reticulum membrane | TAS Reactome:R-HSA-9913337 | KEEP AS NON CORE | Summary: The precursor and beta chain are membrane-associated during ER maturation. Reason: The modeled precursor or beta-DG segment includes the transmembrane anchor and is located in the ER membrane during processing and export. This is a normal biosynthetic location, not the primary site of the mature extracellular-matrix receptor function. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-5617037 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-5617096 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-5617143 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-8932427 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9638090 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9638097 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9913332 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9913336 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9913337 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9940714 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9940718 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9940735 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9940756 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005796 Golgi lumen | TAS Reactome:R-HSA-9940805 | KEEP AS NON CORE | Summary: The alpha chain undergoes Golgi luminal maturation and receptor-complex assembly. Reason: The exact Reactome event contains alpha-DAG1 residues 30–653 or a modified derivative in the Golgi lumen. Glycan extension, sulfation and related reactions are performed by the named enzymes; DAG1 supplies the modified receptor substrate. Complex assembly and transport events retain the same luminal orientation. This contextual compartment is supported without inventing DAG1 glycosyltransferase activity. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5615556 | UNDECIDED | Summary: Cytosolic localization of the modeled alpha-DAG1 species remains unresolved. Reason: The actual defective-POMT event uses an alpha-DAG1 entity spanning residues 30–653 labeled cytosol. Its summation concerns loss of glycosylation and disease, not a direct localization measurement of that alpha-chain species. Normal alpha-DG follows the secretory lumen, and separate beta-tail/cytoplasmic trafficking observations cannot resolve this particular model assignment. Preserve the TAS source without inferring that such mislocalization is impossible. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5615604 | UNDECIDED | Summary: Cytosolic localization of the modeled alpha-DAG1 species remains unresolved. Reason: The actual defective-POMT event uses an alpha-DAG1 entity spanning residues 30–653 labeled cytosol. Its summation concerns loss of glycosylation and disease, not a direct localization measurement of that alpha-chain species. Normal alpha-DG follows the secretory lumen, and separate beta-tail/cytoplasmic trafficking observations cannot resolve this particular model assignment. Preserve the TAS source without inferring that such mislocalization is impossible. |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Dystroglycan is associated with the membrane-linked cytoskeleton. Reason: The UniProt location mapping is consistent with beta-tail engagement of dystrophin, utrophin, ankyrin and CLASP-associated assemblies. It denotes association with a cytoskeletal compartment, not direct binding to every filament type or independent polymerization activity. |
| GO:0005886 plasma membrane | EXP PMID:26848865 CD93 and dystroglycan cooperation in human endothelial cell ... | ACCEPT | Summary: Human endothelial beta-dystroglycan is present at the cell surface. Reason: The original includes endogenous surface colocalization and proximity measurements in HUVECs, together with tagged human DAG1 constructs. These experiments support plasma-membrane localization; FRET/proximity evidence is not converted into an isolated binary binding claim. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA GO_REF:0000052 | ACCEPT | Summary: Human cell-atlas data support plasma-membrane localization. Reason: The actual HPA record lists plasma membrane as a main location in the examined cells, consistent with the beta-chain transmembrane anchor and the alpha/beta surface receptor. Additional nuclear or vesicular signals do not negate this principal location. |
| GO:0005886 plasma membrane | IDA PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | ACCEPT | Summary: The platelet annotation places beta-dystroglycan at the plasma membrane. Reason: The inaccessible original concerns human-adhered platelets, and the location is independently established for the membrane-spanning beta chain. Retain this correct compartment with explicit curator deference; this does not resolve the original’s individual cytoskeletal interactions or fine subcellular sites. |
| GO:0005886 plasma membrane | IDA PMID:18764929 Nuclear translocation of beta-dystroglycan reveals a distinc... | ACCEPT | Summary: The trafficking study retains a surface beta-dystroglycan pool. Reason: The original human-cell localization study compares plasma-membrane and intracellular pools and supports the canonical membrane location. Its nuclear observations describe additional trafficking contexts rather than replacement of the surface receptor role. Supporting Evidence: |
| GO:0005886 plasma membrane | IDA PMID:8017170 Immunogold localization of the 43-kDa dystroglycan at the pl... | ACCEPT | Summary: Human muscle immunogold microscopy locates 43-kDa dystroglycan at the plasma membrane. Reason: The source abstract explicitly identifies immunogold localization of the beta-chain-sized protein in control and dystrophic human muscle. This supports the cell-membrane anchor; source-specific ultrastructural details beyond the recovered abstract are left to the experimental curator. Supporting Evidence: |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: The beta-chain membrane anchor supports the conserved plasma-membrane location. Reason: Literal mouse ortholog and UniProt subcellular-location sources agree with direct human membrane evidence and the official transmembrane segment. The mapping does not require all processed DAG1 products to remain membrane attached. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-2396395 | ACCEPT | Summary: The mature alpha/beta receptor complex functions at the plasma membrane. Reason: The cited Reactome event explicitly places membrane-anchored beta-DAG1 with its extracellular alpha partner in a cell-surface complex or ligand-binding event. This agrees with the direct human membrane evidence and the receptor’s physical linkage role. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9010872 | ACCEPT | Summary: The mature alpha/beta receptor complex functions at the plasma membrane. Reason: The cited Reactome event explicitly places membrane-anchored beta-DAG1 with its extracellular alpha partner in a cell-surface complex or ligand-binding event. This agrees with the direct human membrane evidence and the receptor’s physical linkage role. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9913333 | ACCEPT | Summary: The mature alpha/beta receptor complex functions at the plasma membrane. Reason: The cited Reactome event explicitly places membrane-anchored beta-DAG1 with its extracellular alpha partner in a cell-surface complex or ligand-binding event. This agrees with the direct human membrane evidence and the receptor’s physical linkage role. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9913336 | ACCEPT | Summary: The mature alpha/beta receptor complex functions at the plasma membrane. Reason: The cited Reactome event explicitly places membrane-anchored beta-DAG1 with its extracellular alpha partner in a cell-surface complex or ligand-binding event. This agrees with the direct human membrane evidence and the receptor’s physical linkage role. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9913339 | ACCEPT | Summary: The mature alpha/beta receptor complex functions at the plasma membrane. Reason: The cited Reactome event explicitly places membrane-anchored beta-DAG1 with its extracellular alpha partner in a cell-surface complex or ligand-binding event. This agrees with the direct human membrane evidence and the receptor’s physical linkage role. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9914537 | ACCEPT | Summary: The mature alpha/beta receptor complex functions at the plasma membrane. Reason: The cited Reactome event explicitly places membrane-anchored beta-DAG1 with its extracellular alpha partner in a cell-surface complex or ligand-binding event. This agrees with the direct human membrane evidence and the receptor’s physical linkage role. Supporting Evidence: |
| GO:0005911 cell-cell junction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: A mouse ortholog experiment supports junctional localization in a specific cellular context. Reason: The exact donor record is an IDA cell-cell-junction assertion from PMID:23793062. Orthologous receptor architecture makes the transfer plausible, but the original junctional experiment was not independently recovered. Retain the contextual localization with curator deference rather than equating it with the principal basal cell-matrix attachment site. |
| GO:0005912 adherens junction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog provides contextual adherens-junction localization support. Reason: The literal donor has an IDA assertion for adherens junction from PMID:9117347. Preserve this conserved localization inference with its source limits; it does not make DAG1 a classical cadherin or establish a universal adherens-junction function. |
| GO:0005925 focal adhesion | HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome... | KEEP AS NON CORE | Summary: Focal-adhesion localization is supported in a defined human cell context, while the original proteomics assignment remains unresolved. Reason: Retain the contextual compartment with independent positive corroboration and curator deference. The complete PMID:9117347 abstract explicitly reports recruitment to focal adhesions in human aortic smooth-muscle cells and rat REF52 fibroblasts, with ligand and cell-type dependence; several other cell lines fail to recruit dystroglycan even on laminin. The PMID:21423176 DAG1 target row or peptide assignment was not recovered, so this corroboration does not verify that particular HDA experiment or establish universal focal-adhesion residence. |
| GO:0005925 focal adhesion | IDA PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | KEEP AS NON CORE | Summary: Contextual focal-adhesion localization has independent human support; the specific platelet observation remains unverified. Reason: The full PMID:18341635 platelet original and its localization panel remain unavailable. Independently, the complete PMID:9117347 abstract reports dystroglycan at focal adhesions of human aortic smooth-muscle cells and rat REF52 fibroblasts, with cell-type and ligand dependence. Retain the contextual location with curator deference, explicitly separating that human corroboration from the unrecovered platelet assay. Neither a universal compartment nor a negative platelet result is inferred. |
| GO:0005925 focal adhesion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat focal-adhesion donor is experimentally grounded and has separate human contextual corroboration. Reason: The literal rat donor includes an IDA focal-adhesion assertion from PMID:9117347, alongside propagated records. The same complete abstract also explicitly reports human aortic smooth-muscle focal localization; this human observation is independent corroboration and does not change the imported rat source. Recruitment is ligand- and cell-type-dependent, with negative observations in some other lines. This supports a contextual location, without verifying the separate unresolved human proteomics or platelet experiments or making DAG1 an integrin-family receptor. Supporting Evidence: |
| GO:0006509 membrane protein ectodomain proteolysis | IDA PMID:19946898 Enzymatic processing of beta-dystroglycan recombinant ectodo... | MARK AS OVER ANNOTATED | Summary: Dystroglycan is the substrate in the cited MMP-9 ectodomain-cleavage experiment. Reason: The recovered original tests a murine beta-DG ectodomain fragment with human MMP-9 and maps cleavage at His715/Leu716. MMP-9 performs the proteolytic step; being the cleaved membrane protein does not establish that DAG1 participates as a protease or other performer of that process. This source-specific overannotation is separate from DAG1’s experimentally supported intrinsic SEA self-processing. |
| GO:0007411 axon guidance | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Dystroglycan contributes to axon guidance through extracellular and cellular organization. Reason: The actual PAINT node PTN000490290 lies on the human lineage and preserves the curated fly, mouse and worm descendant context. The conserved extracellular receptor architecture is compatible with a developmental guidance contribution, including the modeled SLIT2 interaction; no direct human axon-guidance assay or catalytic signaling activity is claimed. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000490290 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20260218. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. |
| GO:0007416 synapse assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog supports a conserved contribution to synapse assembly. Reason: Retain the orthology-based developmental process as a contextual consequence of dystroglycan-mediated synaptic organization. The transfer is not a direct human assay, and it is not expanded to every synapse subtype or every molecular step of synaptogenesis. |
| GO:0008307 structural constituent of muscle | IMP PMID:18691338 A comparative study of alpha-dystroglycan glycosylation in d... | ACCEPT | Summary: Dystroglycan provides a structural membrane–matrix linkage in muscle. Reason: The cited clinical study concerns defects in alpha-DG glycosylation and muscle pathology; it does not test a panel of DAG1 mutations. Its structural interpretation is supported by the established extracellular ligand-binding/cytoplasmic-linker architecture and direct human sarcolemmal localization. Retain the annotation with the clinical assay scope explicit, without treating phenotype severity as a quantitative measure of receptor function. |
| GO:0009897 external side of plasma membrane | IEA GO_REF:0000107 | ACCEPT | Summary: The alpha chain forms an external cell-surface receptor component. Reason: The mouse ortholog IDA source and the official alpha/beta topology support the extracellular, membrane-associated alpha chain. This does not place the beta-chain cytoplasmic tail outside the cell. |
| GO:0009986 cell surface | IEA GO_REF:0000107 | ACCEPT | Summary: Dystroglycan is active as a receptor at the cell surface. Reason: The literal mouse IDA donor and human ligand-binding and membrane-localization evidence support the surface receptor. This cell-surface assignment does not imply that every released or intracellular processed DAG1 product occupies that location. |
| GO:0014037 Schwann cell differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Schwann-cell differentiation is a conserved contextual role supported by the rat ortholog. Reason: The literal rat evidence includes expression-pattern assertions from PMID:11869039 and PMID:16228655. Retain the established lineage-associated role with those evidence limits; expression dynamics alone do not specify a direct differentiation-switch mechanism or a new core molecular activity. |
| GO:0014044 Schwann cell development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse perturbation supports a contribution to Schwann-cell development. Reason: The exact mouse donor includes IMP support from PMID:12797959. Conservation of the basal-lamina receptor supports transfer of this contextual developmental role; no direct human developmental perturbation or cell-autonomous pathway mechanism is inferred. |
| GO:0014894 response to denervation involved in regulation of muscle adaptation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog changes in the context of denervation-associated muscle adaptation. Reason: The literal donor is an IEP assertion from PMID:8906620. Retain the restricted response context rather than converting an expression-associated adaptation into a direct force-generating or denervation-sensing activity. |
| GO:0015631 tubulin binding | IDA PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | UNDECIDED | Summary: The source-specific tubulin interaction remains unresolved. Reason: The platelet original was not recovered. Its abstract concerns microtubules but does not establish a direct tubulin-binding assay, and independent CLASP association cannot substitute for tubulin binding. Preserve the IDA assertion without inferring that the interaction is absent. Supporting Evidence: |
| GO:0016010 dystrophin-associated glycoprotein complex | IDA PMID:17993586 Expression of the dystrophin-glycoprotein complex is a marke... | ACCEPT | Summary: Dystroglycan is a component of the dystrophin-associated glycoprotein complex. Reason: The source examines the complex during human airway-smooth-muscle maturation, including increased beta-DG expression. Complex membership is independently consistent with the receptor’s alpha/beta architecture and membrane–cytoskeleton linkage. Full source-specific assembly details were not recovered, so the claim does not go beyond membership. Supporting Evidence: |
| GO:0016010 dystrophin-associated glycoprotein complex | IEA GO_REF:0000120 | ACCEPT | Summary: Domain, rule and ortholog evidence support dystrophin-associated complex membership. Reason: The target meets actual ARBA00028743 condition branches 1 and 4; its InterPro member match and literal rat experimental donor agree. These are reconstructed sources rather than a family-name guess. The broader complex includes the smaller alpha/beta dystroglycan unit, so neither membership assertion is discarded merely because the other exists. |
| GO:0016011 dystroglycan complex | IBA GO_REF:0000033 | ACCEPT | Summary: The processed alpha and beta chains constitute the dystroglycan complex. Reason: Both the literal mouse transfer and the actual on-lineage PAINT node PTN000490290 support the conserved alpha/beta complex. Its noncovalent association and complementary extracellular/membrane topology are established; this is not a claim of multiple alternatively spliced proteins. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000490290 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20260218. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. Supporting Evidence: |
| GO:0016011 dystroglycan complex | IEA GO_REF:0000107 | ACCEPT | Summary: The processed alpha and beta chains constitute the dystroglycan complex. Reason: Both the literal mouse transfer and the actual on-lineage PAINT node PTN000490290 support the conserved alpha/beta complex. Its noncovalent association and complementary extracellular/membrane topology are established; this is not a claim of multiple alternatively spliced proteins. Supporting Evidence: |
| GO:0016020 membrane | IDA PMID:17628813 MLC1 is associated with the dystrophin-glycoprotein complex ... | TOO GENERAL | Summary: The observed membrane association is represented by supported specific membrane locations. Reason: The human brain source places beta-DG in astrocytic endfoot-associated membranes. Its broad membrane annotation is true but is covered more informatively by the existing plasma-membrane and biosynthetic membrane annotations. The paper’s MLC1–Kir4.1 co-immunoprecipitation is not recast as a direct DAG1 interaction. Supporting Evidence: |
| GO:0016020 membrane | IEA GO_REF:0000120 | TOO GENERAL | Summary: Broad membrane localization adds no specificity beyond the supported membrane compartments. Reason: The exact mouse and InterPro sources agree with a membrane-spanning beta chain. Existing plasma-membrane, ER-membrane and Golgi-membrane assertions provide the relevant compartment detail. The evidence is retained; this is a specificity decision, not a rejection of membrane association. |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog supports basolateral receptor localization in epithelial cells. Reason: The exact donor is an IDA basolateral-plasma-membrane assertion from PMID:11416038. Retain this tissue-dependent polarity context with curator deference, without extending it to all DAG1-expressing cells. |
| GO:0016340 calcium-dependent cell-matrix adhesion | IEA GO_REF:0000107 | ACCEPT | Summary: Dystroglycan-mediated matrix adhesion can depend on calcium. Reason: The literal rat IMP source supports calcium-dependent cell-matrix adhesion. This is compatible with ligand-binding and receptor-mediated attachment, but calcium dependence of the adhesion assay alone does not identify a calcium-binding site in DAG1 or the ligand. The process and the separate molecular-binding annotation are assessed independently. |
| GO:0017166 vinculin binding | IPI PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | UNDECIDED | Summary: The source-specific vinculin interaction remains unresolved. Reason: The literal partner P18206 is vinculin, but the platelet original was not recovered and no current literal pair from the inspected IntAct/MINT records resolves it. Preserve the positive IPI assertion; missing recovery is neither proof of nonbinding nor a basis for substituting another cytoskeletal interaction. Supporting Evidence: |
| GO:0021675 nerve development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT supports a conserved contribution to nerve development. Reason: PTN000490290 is on the actual human lineage. Mouse and rat descendant evidence supports the ancestral developmental assignment, including source-specific expression evidence rather than a direct human developmental assay. Retain the conserved biological context without inferring a new catalytic or signaling mechanism. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000490290 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20260218. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. |
| GO:0021675 nerve development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog supports a contextual nerve-development association. Reason: The literal rat donor has an IEP nerve-development assertion from PMID:16228655. Retain this orthologous developmental context while preserving the distinction between expression-pattern evidence and a mechanistically resolved developmental step. |
| GO:0021682 nerve maturation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse perturbation supports a contribution to nerve maturation. Reason: The exact mouse donor includes IMP evidence from PMID:12797959. Dystroglycan’s basal-lamina attachment role provides a coherent conserved context, but the original experiment is not presented as a direct human maturation assay. |
| GO:0022011 myelination in peripheral nervous system | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Dystroglycan contributes to peripheral myelination in the mouse donor model. Reason: The literal mouse IMP source supports the peripheral-nervous-system myelination term. Retain the orthologous developmental contribution without assigning myelin lipid synthesis or claiming that this same experiment tests human DAG1. |
| GO:0030027 lamellipodium | IDA PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | UNDECIDED | Summary: The platelet lamellipodium localization remains unresolved. Reason: The operative full text and localization panel were not recovered. General cytoskeletal interplay or independent cell-migration phenotypes do not establish this specific structure in that source. Preserve the positive annotation with its access limit. Supporting Evidence: |
| GO:0030175 filopodium | IDA PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | UNDECIDED | Summary: The platelet filopodium localization remains unresolved. Reason: The inaccessible original’s abstract does not resolve the specific filopodial localization experiment. No absence claim is made, and lamellipodial or generic membrane evidence is not substituted for the requested compartment. Supporting Evidence: |
| GO:0030198 extracellular matrix organization | TAS Reactome:R-HSA-3000171 | ACCEPT | Summary: Dystroglycan participates in organizing the extracellular matrix at the cell surface. Reason: DAG1 supplies a ligand-binding, membrane-anchored surface that supports matrix attachment and assembly, so it performs a structural part of this process rather than merely being a glycosylation substrate. The cited Reactome pathway provides context; direct receptor and assembly evidence supports the biological judgment independently of pathway breadth. |
| GO:0030336 negative regulation of cell migration | IMP PMID:19587235 Tumor suppressor function of laminin-binding alpha-dystrogly... | KEEP AS NON CORE | Summary: Ligand-competent alpha-dystroglycan can restrain cell migration. Reason: The original human-cell experiments combine DAG1 depletion, ligand-blocking antibody and laminin-fragment conditions with migration measurements. They support negative regulation in that glycosylation and ligand context, not a universal antimigratory effect in all tissues. Supporting Evidence: |
| GO:0031012 extracellular matrix | HDA PMID:27559042 Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin... | ACCEPT | Summary: The extracellular alpha chain associates with matrix at the cell surface. Reason: The glycoproteomics source supplies a human extracellular-matrix annotation. The exact target quantitative table was not recovered, so its survey assignment is retained with curator deference and independently established alpha-DG matrix association. Neither the study’s decorin mechanism nor a freely secreted beta chain is attributed to DAG1. |
| GO:0031103 axon regeneration | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog is associated with axon-regeneration contexts. Reason: The literal donor evidence is IEP from PMID:16228655. Retain the restricted orthologous response context without treating changing expression as a demonstrated direct axon-growth mechanism. |
| GO:0031643 positive regulation of myelination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Rat perturbation supports a positive contribution to myelination. Reason: The exact donor carries IMP support from PMID:17395644. This is a conserved contextual role of the receptor and its cellular environment, not an additional molecular enzyme activity or evidence of direct human myelin production. |
| GO:0033268 node of Ranvier | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Dystroglycan localizes in the nodal organization context in the mouse donor. Reason: The literal mouse assertion derives from PMID:12797959. Retain the conserved node-of-Ranvier compartment with curator deference, while distinguishing the glial/membrane receptor location from an ion-channel activity. |
| GO:0034399 nuclear periphery | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog provides evidence for a nuclear-peripheral pool. Reason: The literal rat IDA record is PMID:21668890. This is compatible with independently observed human beta-DG nuclear trafficking, but it does not establish an identical human nuclear-envelope mechanism or a nuclear core function. Supporting Evidence: |
| GO:0034453 microtubule anchoring | IMP PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | UNDECIDED | Summary: The platelet microtubule-anchoring mechanism remains unresolved. Reason: The full platelet original was not recovered, so its perturbation and anchoring endpoints cannot be independently adjudicated. A separate CLASP/chick epiblast study supports related biology but does not resolve the assay attributed to this PMID. Preserve the source-specific IMP assertion without a false negative conclusion. Supporting Evidence: |
| GO:0035022 positive regulation of Rac protein signal transduction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Dystroglycan engagement can enhance Rac signaling in a defined context. Reason: The literal mouse IMP and rabbit IDA donors cite PMID:16475793. Retain this conserved receptor-associated signaling response with the measured-species and source limits explicit. DAG1 is not inferred to be a Rac guanine-nucleotide exchange factor or to activate Rac in every cell type. |
| GO:0035022 positive regulation of Rac protein signal transduction | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Dystroglycan engagement can enhance Rac signaling in a defined context. Reason: The literal mouse IMP and rabbit IDA donors cite PMID:16475793. Retain this conserved receptor-associated signaling response with the measured-species and source limits explicit. DAG1 is not inferred to be a Rac guanine-nucleotide exchange factor or to activate Rac in every cell type. |
| GO:0035418 protein localization to synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog contributes to organizing proteins at synapses. Reason: The exact donor records include IMP evidence from PMID:11157973 and PMID:22553019. Retain the conserved synaptic organization role; this does not identify DAG1 as a general intracellular protein transporter. |
| GO:0042169 SH2 domain binding | IDA PMID:11724572 Tyrosine phosphorylation of beta-dystroglycan at its WW doma... | KEEP AS NON CORE | Summary: Phosphorylated beta-dystroglycan tail can bind SH2-domain proteins. Reason: The complete abstract describes phosphorylated tail GST assays and association of SH2-containing proteins. This supports a phosphorylation-dependent interaction rather than constitutive recruitment by all DAG1 products. Full-text details were not recovered, and no kinase or phosphatase catalytic activity is assigned to DAG1. Supporting Evidence: |
| GO:0042383 sarcolemma | IBA GO_REF:0000033 | ACCEPT | Summary: The dystroglycan receptor links matrix and cytoskeleton at the sarcolemma. Reason: The actual PAINT node PTN000490290 is on the human lineage, and the literal mammalian experimental donors and UniProt location mapping agree. Direct human immunogold evidence supports this muscle membrane location. The broader plasma-membrane annotation remains useful across non-muscle tissues. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000490290 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20260828. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. Supporting Evidence: |
| GO:0042383 sarcolemma | IEA GO_REF:0000120 | ACCEPT | Summary: The dystroglycan receptor links matrix and cytoskeleton at the sarcolemma. Reason: The actual PAINT node PTN000490290 is on the human lineage, and the literal mammalian experimental donors and UniProt location mapping agree. Direct human immunogold evidence supports this muscle membrane location. The broader plasma-membrane annotation remains useful across non-muscle tissues. Supporting Evidence: |
| GO:0043034 costamere | IEA GO_REF:0000107 | ACCEPT | Summary: Dystroglycan participates in costameric membrane–cytoskeleton linkage. Reason: The literal rat IDA donor PMID:10531619 supports the costamere location, coherent with beta-tail binding to cytoskeletal linkers and extracellular matrix attachment. Retain this structural muscle context without assigning force generation to the receptor. |
| GO:0043236 laminin binding | IEA GO_REF:0000120 | ACCEPT | Summary: Glycosylated alpha-dystroglycan binds laminins. Reason: Literal mouse and rat experimental donor records support the ligand-binding class, which is directly coherent with human glycosylation-dependent receptor evidence. Binding and receptor activity express related aspects of the same performed core function; no novel separate activity is manufactured. |
| GO:0043237 laminin-1 binding | IEA GO_REF:0000120 | ACCEPT | Summary: Alpha-dystroglycan binds laminin-1 in the supported ligand context. Reason: The actual rat, mouse and rabbit donor evidence supports this narrower laminin specificity. Preserve the source-specific biochemical ligand claim without implying that laminin-1 is the only recognized laminin or that all DAG1 glycoforms bind equally. Supporting Evidence: |
| GO:0043237 laminin-1 binding | ISS GO_REF:0000024 | ACCEPT | Summary: Alpha-dystroglycan binds laminin-1 in the supported ligand context. Reason: The actual rat, mouse and rabbit donor evidence supports this narrower laminin specificity. Preserve the source-specific biochemical ligand claim without implying that laminin-1 is the only recognized laminin or that all DAG1 glycoforms bind equally. Supporting Evidence: |
| GO:0043395 heparan sulfate proteoglycan binding | IEA GO_REF:0000107 | ACCEPT | Summary: Alpha-dystroglycan binds extracellular heparan sulfate proteoglycan ligands. Reason: The literal mouse donor evidence is compatible with established binding of agrin and perlecan. This term describes binding a proteoglycan ligand, not proof that the heparan-sulfate chain alone is the contact determinant. The agrin source provides additional direct ligand-class support. Supporting Evidence: |
| GO:0043403 skeletal muscle tissue regeneration | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog is associated with skeletal-muscle regeneration. Reason: The literal source is an IEP assertion from PMID:12086334. Retain the response and tissue context without treating expression changes as proof that DAG1 executes a myogenic transcriptional program. |
| GO:0043409 negative regulation of MAPK cascade | IMP PMID:19587235 Tumor suppressor function of laminin-binding alpha-dystrogly... | KEEP AS NON CORE | Summary: Ligand-competent dystroglycan can attenuate ERK/MAPK signaling in the studied cells. Reason: The original DAG1 siRNA and ligand-blocking/ligand-fragment experiments measure phosphorylated relative to total ERK. These results support a negative pathway response in that context, not direct enzymatic inhibition of MEK or ERK by DAG1. Supporting Evidence: |
| GO:0043434 response to peptide hormone | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog responds in a peptide-hormone experimental context. Reason: The exact donor is an IEP assertion from PMID:11416038. Retain the response term with its expression-based scope; it does not identify DAG1 as the peptide-hormone receptor or a universal hormone-response effector. |
| GO:0044853 plasma membrane raft | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog localizes in plasma-membrane raft preparations. Reason: The literal rat IDA record PMID:22613990 supports this contextual membrane microdomain. Retain the compartment inference without equating a biochemical raft fraction with fixed nanoscale organization in every cell. |
| GO:0044877 protein-containing complex binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse donor supports association with a protein-containing complex. Reason: The literal mouse IDA source is PMID:19494113. Keep the positive complex-binding assertion under the supported-binding policy. The available donor record does not justify inventing a unique adaptor mechanism or a more specific binding class for this particular source. |
| GO:0045121 membrane raft | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog has a contextual membrane-raft association. Reason: The literal mouse IDA source PMID:11259414 supports this compartment. Retain it independently of the rat plasma-membrane-raft source, preserving source-specific location breadth and without asserting that all DAG1 molecules reside in rafts. |
| GO:0045202 synapse | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Dystroglycan has synaptic localization in addition to its broader matrix-receptor role. Reason: The UniProt location mapping is consistent with curated mouse synaptic localization and the conserved postsynaptic organizing function. This broad label spans different synaptic contexts; it is not treated as proof of every subtype-specific localization. |
| GO:0045202 synapse | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mouse experimental evidence supports a synaptic DAG1 pool. Reason: The exact mouse donor includes an experimental synapse assertion from PMID:40473926. Retain the orthologous location with curator deference and preserve the distinction from direct human synaptic imaging. |
| GO:0045211 postsynaptic membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Dystroglycan occupies postsynaptic membrane-associated assemblies. Reason: The UniProt mapping and manual mouse transfer agree with the established membrane-anchored postsynaptic role. The current literal donor query did not recover an exact experimental GO:0045211 row, which is an access/provenance limit rather than disproof of the historical manual transfer. The broader on-lineage postsynapse evidence remains separately recorded. |
| GO:0045211 postsynaptic membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Dystroglycan occupies postsynaptic membrane-associated assemblies. Reason: The UniProt mapping and manual mouse transfer agree with the established membrane-anchored postsynaptic role. The current literal donor query did not recover an exact experimental GO:0045211 row, which is an access/provenance limit rather than disproof of the historical manual transfer. The broader on-lineage postsynapse evidence remains separately recorded. |
| GO:0046718 symbiont entry into host cell | IEA GO_REF:0000108 | KEEP AS NON CORE | Summary: The logical entry-process mapping follows the demonstrated virus-receptor activity. Reason: Dystroglycan provides a binding/entry receptor in susceptible cells, performing a step rather than serving only as a passive intracellular cargo. The implication from the existing virus-receptor annotation is appropriate within the same cell and glycosylation limits; alternative entry routes remain possible. Supporting Evidence: |
| GO:0048714 positive regulation of oligodendrocyte differentiation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Rat perturbation supports a contribution to oligodendrocyte differentiation. Reason: The literal rat IMP source is PMID:17395644. Preserve this developmental context as a conserved receptor-associated function without promoting a particular differentiation signaling mechanism to a core activity. |
| GO:0050807 regulation of synapse organization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog regulates synaptic organization. Reason: The exact donor includes IMP and IDA records from PMID:27707967. Retain the conserved organization role with curator deference, without treating every downstream synaptic phenotype as an independent molecular activity. |
| GO:0051124 synaptic assembly at neuromuscular junction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Dystroglycan contributes to neuromuscular-junction assembly in the mouse model. Reason: The literal mouse IMP donor PMID:11157973 supports the process. The receptor’s matrix-binding and membrane scaffold roles provide a coherent conserved contribution, but this is not a direct human developmental assay. |
| GO:0051393 alpha-actinin binding | IDA PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | KEEP AS NON CORE | Summary: Curated interaction evidence supports alpha-actinin association in the platelet source. Reason: The original platelet full text remains unavailable, but an independently inspected BioGRID record identifies the human ACTN1–DAG1 pair with affinity-capture Western and linked FRET evidence. Retain this positive interaction with explicit curator deference; the record does not establish an isolated binary interface or every other cytoskeletal interaction attributed to that paper. Supporting Evidence: |
| GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog can support PI3K/AKT signaling in a defined context. Reason: The literal mouse IMP record PMID:12402286 supports a positive signaling contribution. This contextual effect need not match the negative direction measured in a different human ligand/glycosylation system. DAG1 is not assigned PI3K catalytic activity or a context-independent direction of signaling. |
| GO:0051898 negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction | IMP PMID:19587235 Tumor suppressor function of laminin-binding alpha-dystrogly... | KEEP AS NON CORE | Summary: Ligand-competent alpha-dystroglycan can attenuate PI3K/AKT pathway output. Reason: The original human-cell perturbation and ligand experiments measure phosphorylated relative to total AKT and support a negative response in that system. This does not establish direct inhibition of PI3K enzyme activity and does not contradict a positive receptor-associated effect in another cellular context. Supporting Evidence: |
| GO:0055001 muscle cell development | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT supports an ancestral contribution to muscle-cell development. Reason: The actual PTN000490290 assertion lies on the human lineage. Current IBD evidence includes the historical fly context and an additional mapped zebrafish descendant, while the historical source tuple is preserved. The conserved receptor role supports the developmental inference; donor count or changes in the current experimental record are not treated as evidence of loss. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000490290 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20260828. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. |
| GO:0060055 angiogenesis involved in wound healing | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog is associated with angiogenesis during wound repair. Reason: The literal donor is an IEP assertion from PMID:21192954. Retain this restricted response context and its weaker expression-based causal resolution. It is not expanded to a direct angiogenic enzyme activity or to all vascular development. |
| GO:0060077 inhibitory synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog localizes at inhibitory synapses. Reason: The exact mouse IDA source PMID:40473926 supports this compartment. Retain the conserved synaptic location with curator deference without claiming direct human subtype-specific imaging. |
| GO:0070062 extracellular exosome | HDA PMID:19199708 Proteomic analysis of human parotid gland exosomes by multid... | KEEP AS NON CORE | Summary: Alpha-chain peptides were detected in a human parotid exosome preparation. Reason: The actual supplementary workbooks identify IPI00028911.1/DAG1 with two sequences and two spectra. The two target peptides map to residues 262 and 283 in the human alpha chain. This supports the measured extracellular-vesicle preparation, with the source’s contamination limits; it does not identify intact beta-DG cargo, vesicle membrane orientation or a dedicated exosomal function. Supporting Evidence: |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | KEEP AS NON CORE | Summary: The human prostatic-secretion survey provides a contextual exosome annotation. Reason: The source describes vesicles isolated from pooled expressed-prostatic-secretion urine, with fractionation and mass-spectrometry criteria. Its target-specific supplemental workbook was not recovered as a valid spreadsheet, so retain the positive HDA assertion with curator deference and independent evidence that alpha-DG material can occur in extracellular-vesicle preparations. That corroboration does not replace the source-specific quantitative assignment. |
| GO:0070938 contractile ring | IDA PMID:18341635 beta-Dystroglycan modulates the interplay between actin and ... | UNDECIDED | Summary: The platelet contractile-ring localization remains unresolved. Reason: The original full text and operative localization panel were not recovered. General actin–microtubule interplay in adhered platelets does not establish this precise compartment, but the positive IDA assertion is preserved without an absence claim. Supporting Evidence: |
| GO:0071260 cellular response to mechanical stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Rat perturbation supports a cellular response to mechanical stimulation. Reason: The exact donor carries IMP evidence from PMID:18556591. The membrane–matrix linkage provides a coherent context for this response, but the transfer does not establish a direct force-sensing molecular mechanism in human DAG1. |
| GO:0071397 cellular response to cholesterol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog responds to cholesterol-related membrane conditions. Reason: The literal donor evidence is IEP from PMID:22613990. Preserve the response context without assigning cholesterol-binding, sterol metabolism or direct cholesterol sensing to DAG1. |
| GO:0071711 basement membrane organization | IMP PMID:23940118 Epiblast integrity requires CLASP and Dystroglycan-mediated ... | ACCEPT | Summary: Dystroglycan helps maintain basal attachment and basement-membrane organization. Reason: The original uses chick epiblast perturbations to establish basal cortical and matrix organization, alongside separate human DAG1–CLASP association experiments. The conserved structural receptor contribution supports the process annotation with curator deference; the developmental experiment is not mislabeled as a direct human embryonic assay. Supporting Evidence: |
| GO:0085029 extracellular matrix assembly | IEA GO_REF:0000107 | ACCEPT | Summary: Dystroglycan provides a cell-surface platform for extracellular-matrix assembly. Reason: The literal mouse IMP donor PMID:10366602 agrees with laminin-binding/assembly experiments. DAG1 performs a receptor/scaffold contribution to matrix assembly, distinct from being modified by glycosylation enzymes. The source supports assembly rather than synthesis of the matrix ligands themselves. |
| GO:0098684 photoreceptor ribbon synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog is active at photoreceptor ribbon synapses. Reason: The exact mouse donor records include IDA evidence from PMID:21129441 and PMID:22553019. Retain this specialized synaptic location with curator deference and without inferring that the same assays were performed on human retinal DAG1. |
| GO:0098696 regulation of neurotransmitter receptor localization to postsynaptic specialization membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse evidence supports regulation of receptor localization at postsynaptic specializations. Reason: The literal donor from PMID:27707967 supports the conserved synaptic-organizing contribution. This is not a claim that DAG1 transports neurotransmitter receptors autonomously or acts as a neurotransmitter receptor itself. |
| GO:0098794 postsynapse | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: PAINT supports a conserved postsynaptic site of action. Reason: The actual PTN002727163 assertion is on the human lineage, with the historical mouse and rat sources preserved. Retain the conserved compartment and distinguish the phylogenetic inference from direct human imaging or a universal presynaptic role. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002727163 SUPPORTS TRANSFER Actual PTHR21559 ancestor on the human PTN002502358 path; literal IBD date 20260224. The ungapped target matches the official 895-residue sequence. Biological and assay limitations remain in the source-specific reason; no target loss is established. |
| GO:0098794 postsynapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog has experimentally supported postsynaptic activity. Reason: The literal mouse donor has IDA evidence from PMID:24753587. Retain the source-specific postsynaptic context, consistent with the separate PAINT inference but not a duplicate claim of direct human experimental localization. |
| GO:0098942 retrograde trans-synaptic signaling by trans-synaptic protein complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog contributes to retrograde signaling through a trans-synaptic complex. Reason: The literal donor is from PMID:27707967 and supports a contextual synaptic signaling role. Conservation of the membrane receptor architecture makes the transfer coherent; no intracellular catalytic activity or universally bidirectional signaling mechanism is inferred. |
| GO:0098978 glutamatergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The rat ortholog has a glutamatergic-synapse localization assertion. Reason: The exact rat IDA donor PMID:9446825 supports this synaptic context. Retain the curated transfer without claiming that it excludes inhibitory-synapse pools or directly establishes the human subtype distribution. |
| GO:0098982 GABA-ergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog has a GABA-ergic-synapse localization assertion. Reason: The literal mouse source PMID:27707967 supports this specific compartment. Retain the contextual transfer and preserve the distinct glutamatergic and inhibitory-synapse source scopes. |
| GO:0099524 postsynaptic cytosol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The cytoplasmic side of dystroglycan can contribute within a postsynaptic assembly. Reason: The literal rat IDA source PMID:9446825 supports this postsynaptic-cytosol context. The beta-chain cytoplasmic tail provides a coherent molecular scope; this does not relocate the extracellular alpha chain to the cytosol or resolve the defective-POMT alpha-chain assignments. |
| GO:1904395 positive regulation of skeletal muscle acetylcholine-gated channel clustering | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The mouse ortholog supports acetylcholine-receptor clustering at muscle synapses. Reason: The exact mouse IMP donor PMID:9454835 supports positive regulation of receptor clustering. DAG1 contributes a matrix-linked organizing surface, not the acetylcholine-gated channel activity itself. |
| GO:1904862 inhibitory synapse assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Mouse evidence supports a contribution to inhibitory-synapse assembly. Reason: Both the automatic and manual ortholog transfers retain the literal mouse donor supported by IMP evidence from PMID:40473926. This is a contextual developmental function rather than an additional core biochemical activity; the duplicate term reflects distinct source assertions, not two independent human experiments. |
| GO:1904862 inhibitory synapse assembly | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Mouse evidence supports a contribution to inhibitory-synapse assembly. Reason: Both the automatic and manual ortholog transfers retain the literal mouse donor supported by IMP evidence from PMID:40473926. This is a contextual developmental function rather than an additional core biochemical activity; the duplicate term reflects distinct source assertions, not two independent human experiments. |
Loading supporting content…
Download this section (compressed HTML)Q: How do calcium occupancy and local glycosylation alter the conformation and ligand competence of full-length dystroglycan under physiological extracellular conditions?
Q: Which processed DAG1 species occupy nuclear, extracellular-vesicle and defective-glycosylation compartments, and what functions do those species perform there?
Q: Which platelet cytoskeletal associations are direct interfaces, and which require intermediate proteins or specific phosphorylation states?
Experiment: Measure calcium affinity and occupancy of full-length, glycosylated dystroglycan and the isolated IGL–SEA fragment at matched physiological ionic conditions. Compare native coordinating-residue substitutions with folding, ligand binding and processing controls.
Experiment: Resolve alpha-, beta- and released N-terminal species with chain-specific quantitative proteomics and orthogonal imaging in nuclear, extracellular-vesicle and defective-glycosylation samples, including fraction-purity controls.
Experiment: Test purified beta-tail and the relevant platelet cytoskeletal partners alongside endogenous complex perturbation, retaining phosphorylation state and topology controls to distinguish direct binding from bridged association.
Loading supporting content…
Download this section (compressed HTML)Loading supporting content…
Download this section (compressed HTML)