Annotation inferences using phylogenetic trees
Combined Automated Annotation using Multiple IEA Methods.
An ELISA for SGP28/CRISP-3, a cysteine-rich secretory protein in human neutrophils, plasma, and exocrine secretions.
Identification of human cysteine-rich secretory protein 3 (CRISP-3) as a matrix protein in a subset of peroxidase-negative granules of neutrophils and in the granules of eosinophils.
Cysteine-rich secretory protein-3: a potential biomarker for prostate cancer.
Preferential expression of cystein-rich secretory protein-3 (CRISP-3) in chronic pancreatitis.
Human colostrum: identification of minor proteins in the aqueous phase by proteomics.
SGP28, a novel matrix glycoprotein in specific granules of human neutrophils with similarity to a human testis-specific gene product and a rodent sperm-coating glycoprotein.
Exocytosis of tertiary granule lumen proteins
Exocytosis of specific granule lumen proteins
Deep research report on CRISP3
Falcon deep research report on CRISP3 (Edison Scientific Literature, 2026-05)
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Human CRISP3 binds the plasma membrane Ca2+ exporter PMCA4b via its N-terminal CAP domain but, unlike hCRISP1 and rat CRISP4, does not inhibit PMCA4b-mediated Ca2+ extrusion, suggesting paralog-specific functional divergence (Miya 2024).
"human CRISP3 interacts with PMCA4b via the N-terminal CAP domain. Unlike hCRISP1 and rat CRISP4, **hCRISP3 did not inhibit PMCA4b-mediated Ca2+ extrusion** in their assay system, implying functional divergence among paralogs."
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CRISP3 is bound by alpha-1-B glycoprotein (A1BG) with nanomolar affinity; A1BG coexpression with CRISP-family proteins reduces sterol secretion/export by more than 50%, supporting a CAP-domain ligand/sterol-binding function (El Atab 2024).
"CRISP3 is an abundant seminal plasma protein that can bind **alpha-1-B glycoprotein (A1BG)** with **nanomolar affinity**, and showed that coexpression of A1BG with **CRISP3** (and other CAP/CRISP proteins) can reduce sterol secretion/export by **>50%** in cellular systems"
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CRISP3 localizes to secretory epithelium throughout the male genital tract, with strongest staining in the cauda epididymis and ampulla/vas deferens; seminal plasma CRISP3 is free in solution and not prostasome-associated (Udby 2005).
"CRISP3 localizes to **secretory epithelium throughout the male genital tract**, with **particularly strong staining in the cauda epididymis and ampulla/vas deferens**, and that seminal plasma CRISP3 is **free in solution (not prostasome-associated)**."
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CRISP3 binds beta-microseminoprotein (MSMB/PSP94) in human seminal plasma, indicating participation in seminal plasma protein complexes.
"CRISP3 binds **beta-microseminoprotein (MSMB; also called PSP94)** in human seminal plasma, a reproducible interaction that suggests CRISP3 participates in seminal plasma protein complexes."
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Plasma CRISP3 is upregulated in adult sepsis and shows biomarker performance in two trauma cohorts (AUC 0.811 and 0.772), consistent with secreted/extracellular CRISP3 acting as an inflammation-associated systemic marker (Zhang 2024).
"Trauma cohort 1 (n=54): admission CRISP3 associated with sepsis incidence (**OR 1.004 [1.002–1.006], p < 0.001**) and ROC performance **AUC 0.811 (0.681–0.905)**."
Mammalian cysteine-rich secretory proteins interact with plasma membrane Ca(2+) exporter PMCA4b.
Alpha-1-B glycoprotein (A1BG) inhibits sterol-binding and export by CRISP2.
Upregulation of CRISP3 and its clinical values in adult sepsis: a comprehensive analysis based on microarrays and a two-retrospective-cohort study.
Cysteine-rich secretory protein-3 (CRISP3) is strongly up-regulated in prostate carcinomas with the TMPRSS2-ERG fusion gene.
Association of cysteine-rich secretory protein 3 and beta-microseminoprotein with outcome after radical prostatectomy.
Characterization and localization of cysteine-rich secretory protein 3 (CRISP-3) in the human male reproductive tract.
Cysteine-rich secretory protein 3: inflammation role in adult varicocoele.