FGA supplies structural alpha-chain material to fibrinogen and fibrin. Its assembled alpha-C material also binds tPA and plasminogen and supports plasmin generation. These distinct contributions support the structural and enzyme-substrate adaptor core functions. Thrombin, Factor XIIIa and tPA perform their respective catalytic steps.
The literature journal, direct source guide and database source guide give the relevant experiments and access limits. The review contains 131 decisions and 90 complete reference assessments. The two natural splice records are preserved, while two separate cleavage-product classes retain official coordinates and their limits. No quote or NEW annotation is introduced.
The direct source records, database source evidence, product map, raw processed-product joins, ontology evidence and phylogeny evidence provide source identity and interpretation. The review YAML is the authority for final decisions; these records preserve provenance rather than duplicate decisions.
The decisions comprise 76 ACCEPT, 36 KEEP_AS_NON_CORE, three MODIFY, six TOO_GENERAL and 10 UNDECIDED. Mixed free-peptide/mature-chain rows and unresolved specific proteomics joins retain their uncertainty. Generic K18 and kinase-substrate interactions remain non-core under the explicit campaign curation instructions, which override the generic validator’s REMOVE preference for these supported interactions. Their evidence does not justify inventing a more specific molecular function. Related BioPlex maps are not counted as independent replication.
The final source set contains 87 genuine normal files: 37 publications, 47 Reactome entries and three PANTHER/PAINT files. The 42 additional discovery caches remain private and unchanged. Primary read scopes are explicit; source records do not imply that every figure, supplement or pathway branch was independently examined.
The same-term HDA source limits and the two mixed free-FPA/mature-chain rows remain explicit. Heterotypic adhesion is retained as a non-core contribution within intact fibrinogen by curator deference to the positive original abstract; the full chain-resolved assay remains inaccessible. BioPlex refinement identifies a measured partner class in tagged-ORF detergent-lysate AP-MS, not direct affinity, endogenous colocalization or a regulatory activity. A secretory/intracellular compartment mismatch remains an unresolved physiological limitation.
The feedback assessment uses the original BioPlex 2.0 Methods, “Generation of Stable Cell Lines,” “Affinity-Purification Mass Spectrometry” and “Identification of Interacting Proteins” (PMID:28514442(https://pubmed.ncbi.nlm.nih.gov/28514442/)); BioPlex 3.0 STAR Methods, “Creation of Stable Cell Lines,” “Affinity Purification of Protein Complexes” and “Identification of High Confidence Interacting Proteins” (PMID:33961781(https://pubmed.ncbi.nlm.nih.gov/33961781/)); and its 293T network row containing FGA/2243 and YWHAQ/10971. These methods describe tagged constructs, NP40 lysates, gene-level protein grouping and background-aware scoring. They do not establish direct binary binding or endogenous colocalization. The original abstract of PMID:8100742(https://pubmed.ncbi.nlm.nih.gov/8100742/) directly reports intact-fibrinogen-dependent leukocyte/endothelial adhesion; accepting that bounded complex contribution does not claim recovery of its full text or an alpha-chain receptor interface.
Official strict is_a/part_of ancestry distinguishes plasminogen activation and fibrinolysis: neither is an ancestor of the other. Both describe supported aspects of the existing alpha-C cofactor core. The broader structural molecular function additionally covers soluble fibrinogen assembly, so the synthesis avoids a duplicate parent/child molecular-function core.