GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms.

GO_REF:0000043

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

PMID:10318872

A novel and highly divergent homolog of human eosinophil granule major basic protein.

PMID:25037231

Extracellular matrix signatures of human primary metastatic colon cancers and their metastases to liver.

PMID:28344315

Proteomic characterization of human multiple myeloma bone marrow extracellular matrix.

Reactome:R-HSA-6798745

Exocytosis of tertiary granule lumen proteins

Reactome:R-HSA-6798749

Exocytosis of specific granule lumen proteins

file:human/PRG3/PRG3-deep-research-perplexity.md

Deep research on PRG3 function

file:human/PRG3/PRG3-deep-research-falcon.md

Falcon deep research on PRG3 (Edison Scientific Literature)

PRG3 encodes major basic protein 2 (MBP2), a C-type lectin-like fold cationic granule effector with no enzymatic activity, classifying it as a non-enzymatic effector protein.

"PRG3 encodes major basic protein 2 (MBP2), a member of the MBP family of eosinophil granule proteins that adopt a C-type lectin-like fold (lectin-like structural homology rather than canonical Ca2+-dependent lectin activity). The MBP family is best understood as cationic secretory/granule effector proteins that can damage membranes and stimulate immune and stromal cells; no enzymatic reaction has been assigned to MBP family proteins (including MBP1 and MBP2)."
PRG3/MBP2 is localized to the eosinophil secondary (specific) granule, not tertiary granules.

"PRG3/MBP2 is localized to the eosinophil secondary (specific) granule, supported by biochemical identification in granule lysates and immunologic localization assays discussed in the foundational characterization/review."
PRG3/MBP2 has lower predicted pI (~8.7) than MBP1 (~11.4) and is generally less potent biologically, consistent with reduced cationicity as a determinant of effector strength.

"Foundational synthesis reports MBP2 has lower predicted pI (~8.7) than MBP1 (~11.4) and is generally less potent in biological activities, consistent with reduced cationicity as a determinant of effector strength."
MBPH/PRG3 grouped with MBP family proteins capable of membrane disintegration and antimicrobial activity; depletion linked to impaired Candida albicans killing.

"MBPH/PRG3 is grouped with MBP family proteins described as capable of membrane disintegration and antimicrobial activity, and changes in phagosomal granule content (including MBPH/PRG3 and MBP) are linked to impaired Candida albicans yeast killing in mobilized granulocytes."
PRG3 ranks among the top 15 most abundant proteins in human peripheral blood eosinophils, supporting it as a prominent eosinophil granule constituent.

"Deep proteomics placed PRG3 (bone marrow proteoglycan 3 / MBP2) among the major eosinophil granule proteins and among the top 15 most abundant eosinophil proteins, supporting its status as a prominent eosinophil granule constituent and useful marker of eosinophil content/degranulation."