ERGIC membranes purified from brefeldin A-treated HepG2 cells (enriched ~110-fold over ERGIC-53) contain established and putative cargo receptors of the early secretory pathway, including VIP36, identified by mass spectrometry.

Large-scale LC-MS/MS profiling of human urinary exosomes catalogued >1100 proteins; VIP36 is one such proteomics hit (HDA), reflecting presence in secreted vesicles rather than a functional localization.

VIP36 is an L-type lectin that localizes to the Golgi and cycles early in the secretory pathway, binding high-mannose glycans in vitro with a pH optimum of 6.5.

VIP36 binds exclusively the high-mannose form of alpha1-antitrypsin; the complex localizes to Golgi and ER and recycles from the Golgi back to the ER, and silencing VIP36 accelerates alpha1-AT transport, consistent with a post-ER quality-control rather than anterograde role.

VIP36 (a lectin-domain transmembrane protein postulated as a cargo receptor for Golgi-to-ER transport) is subject to ectodomain shedding mainly on the cell surface, and the amount of VIP36 regulates phagocytosis in macrophages in a shedding-dependent manner.

VIP36 localizes mainly to the ER and Golgi; only the Endo-H-resistant cell-surface glycoform is shed, and lectin activity is dispensable for the enhancement of phagocytosis.

Shotgun proteomics of prostatic-secretion-derived urinary exosomes detected ~900 proteins; VIP36 is one such HDA proteomics hit, reflecting presence in secreted vesicles.

Using an ultrafiltration assay with fluorescently labeled high-mannose-type glycans, VIP36 carbohydrate-binding affinity constants were measured and agreed with values from ITC and frontal affinity chromatography.

Intracellular L-type lectin of the early secretory pathway that interacts with high-mannose-type glycans and is involved in the transport and sorting of high-mannose glycoproteins; single-pass type I membrane protein of the ERGIC, Golgi and ER membranes; binds 2 calcium ions per subunit as a structural cofactor.