Annotation inferences using phylogenetic trees
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan.
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AGR3 was reported to bind C4.4a/LYPD3 and alpha-dystroglycan in yeast two-hybrid screens.
"Yeast two-hybrid cloning identified metastasis-associated GPI-anchored C4.4a protein and extracellular alpha-dystroglycan (DAG-1) as binding partners for both hAG-2 and hAG-3"
A molecular specificity code for the three mammalian KDEL receptors.
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AGR3/hAG-3 is ER localized and loses ER localization when its C-terminal retrieval motif is removed.
"Three of the 16 constructs, ERp18, Hag3, and GP7R, changed their localization from the ER to the Golgi when the putative ER-retention motif was not present"
Next-generation sequencing to generate interactome datasets.
A proteome-scale map of the human interactome network.
The Endoplasmic Reticulum Resident Protein AGR3. Required for Regulation of Ciliary Beat Frequency in the Airway.
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AGR3 is required for calcium-mediated ciliary beat regulation and mucociliary clearance in airway epithelium.
"AGR3 deficiency had no detectable effects on ciliary beat frequency (CBF) when airways were perfused with a calcium-free solution, suggesting that AGR3 is required for calcium-mediated regulation of ciliary function. Decreased CBF was associated with impaired mucociliary clearance in AGR3-deficient airways."
Anterior gradient protein 3 is associated with less aggressive tumors and better outcome of breast cancer patients.
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AGR3 is expressed in ciliated cells of the oviduct and in several cancer contexts.
"AGR3 expression was demonstrated in various cancers, including breast,7 prostate,21 ovary,19,20 and liver.18"
A reference map of the human binary protein interactome.
Falcon deep research report for human AGR3.
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AGR3 is not currently supported as a canonical protein disulfide isomerase despite its PDI-family/thioredoxin-like fold.
"Although structurally in the PDI/thioredoxin family, AGR3's **DCYQS** motif (lacking the second cysteine) supports the view that AGR3 is **not a canonical disulfide isomerase**; it likely mediates **selective protein interactions** or specialized redox behavior rather than generalized thiol-disulfide exchange"