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    LGALS3

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    For Research Use Only. Not For Clinical Use.


    Background

    LGALS3 encodes a member of the galectin family of carbohydrate binding proteins. Members of this protein family have an affinity for beta-galactosides. The encoded protein is characterized by an N-terminal proline-rich tandem repeat domain and a single C-terminal carbohydrate recognition domain. This protein can self-associate through the N-terminal domain allowing it to bind to multivalent saccharide ligands. This protein localizes to the extracellular matrix, the cytoplasm and the nucleus. This protein plays a role in numerous cellular functions including apoptosis, innate immunity, cell adhesion and T-cell regulation. The protein exhibits antimicrobial activity against bacteria and fungi.
    Protein class

    Cancer-related genes, Plasma proteins

    Predicted location

    Intracellular, Secreted (different isoforms)

    Single cell type specificity

    Cell type enhanced (Proximal enterocytes, Distal enterocytes, Paneth cells)

    Immune cell specificity

    Group enriched (classical monocyte, intermediate monocyte, non-classical monocyte, myeloid DC, T-reg)

    Cell line specificity

    Cell line enhanced (ASC TERT1, CAPAN-2, OE19, SK-MEL-30)

    Interaction

    Probably forms homo- or heterodimers. Interacts with DMBT1 (By similarity). Interacts with CD6 and ALCAM (PubMed:24945728). Forms a complex with the ITGA3, ITGB1 and CSPG4. Interacts with LGALS3BP, LYPD3, CYHR1 and UACA. Interacts with TRIM16; this interaction mediates autophagy of damage endomembranes. Interacts with cargo receptor TMED10; the interaction mediates the translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and thereby secretion (PubMed:32272059).

    Molecular function

    IgE-binding protein

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