| Finding | Quantitative value(s) | Experimental basis | Source (include DOI URL if available) |
|---|---:|---|---|
| Glycan specificity | Prefers high-mannose **Man7–9GlcNAc2** glycans; strongest recognition of **D1/A-arm Manα1-2Manα1-2Man** motif; trimming or glucosylation of the terminal α1,2-mannose abolishes/reduces binding; one FAC-derived affinity value is reported in review text as **“7.1 × 10^8 M^-1”** for immobilized VIP36 with Man7–9 glycans | Frontal affinity chromatography, competition with Man7–9 glycopeptides, glycan trimming/glucosylation perturbation, and co-crystal structural analysis of the VIP36 CRD | Gupta 2012, https://doi.org/10.1007/978-3-7091-1065-2_7; Reiterer 2010, https://doi.org/10.5451/unibas-005405317; Yamamoto 2014, https://doi.org/10.2183/pjab.90.67 (pqac-00000020, pqac-00000021, pqac-00000022, pqac-00000024) |
| pH optimum for sugar binding | Optimal binding reported at **~pH 6.5**; other assays reported **~pH 6.0**; binding increases under mildly acidic conditions consistent with Golgi localization | Recombinant CRD binding assays and FAC; review synthesis of primary studies | Reiterer 2010, https://doi.org/10.5451/unibas-005405317; Gupta 2012, https://doi.org/10.1007/978-3-7091-1065-2_7; Yamamoto 2014, https://doi.org/10.2183/pjab.90.67 (pqac-00000014, pqac-00000015, pqac-00000021, pqac-00000022, pqac-00000023) |
| Ca2+ dependence evidence | Structural evidence supports **1 Ca2+** bound adjacent to the carbohydrate-binding site; key residues **Asp131, Asn166, His190** directly contact ligand; however, some biochemical studies reported binding at pH 6.0 without strict Ca2+ dependence, so evidence is mixed | X-ray crystallography of VIP36 CRD with mannosyl ligands plus biochemical glycan-binding assays | Gupta 2012, https://doi.org/10.1007/978-3-7091-1065-2_7; Reiterer 2010, https://doi.org/10.5451/unibas-005405317 (pqac-00000020, pqac-00000021, pqac-00000023) |
| Cycling kinetics | **ER→Golgi t1/2 = 105 ± 39 min**; **Golgi→ER t1/2 = 1.67 ± 0.45 min** | FRAP analysis of cycling in the early secretory pathway | Reiterer 2010, https://doi.org/10.5451/unibas-005405317 (pqac-00000001, pqac-00000015) |
| Localization polarity | **Apical/basolateral ratio ≈ 7** in polarized cells | Cell biological localization studies in polarized epithelial cells summarized in review literature | Gupta 2012, https://doi.org/10.1007/978-3-7091-1065-2_7 (pqac-00000000, pqac-00000013) |
| Ectodomain shedding site | Cleavage at **F298↓L299**; local sequence reported as **SVNF↓LKSP**; detected across all analyzed cell lines and scored as a high-confidence metalloprotease-sensitive shedding site | Quantitative protein terminomics with metalloprotease inhibitor BB-94; cleavage-site mapping and PWM-based sheddase analysis | Tsumagari et al. 2021, https://doi.org/10.1101/2020.09.23.310102 (pqac-00000009, pqac-00000010, pqac-00000011, pqac-00000028) |
| Recent proteomics association: granulosa cells | **Log2FC = 1.23**, **q = 0.04**, **n = 5** biological replicates | Mass-spectrometry proteomics of cultured human granulosa cells treated 24 h with **30 µM CBD** versus ethanol control | Eubler et al. 2023, https://doi.org/10.1093/molehr/gaad029 (pqac-00000027) |
| Recent CKD genetics/proteomics association | PWAS identified LMAN2 among **22** CKD-associated plasma proteins; ARIC proteomics **n = 7,213** European-ancestry participants; MR for **BUN OR = 1.032, FDR = 5.85 × 10^-3**; MR for **CKD OR = 1.283, FDR = 5.63 × 10^-2**; MR for **eGFR OR = 0.989, FDR = 0.141**; colocalization **PP4 < 0.01** for CKD/eGFR/BUN | Proteome-wide association study integrating cis-pQTLs with CKD/eGFR/BUN GWAS, followed by Mendelian randomization and Bayesian colocalization | Xiong et al. 2024, https://doi.org/10.1016/j.heliyon.2024.e31704 (pqac-00000006, pqac-00000007, pqac-00000008) |


*Table: This table compiles the main experimentally supported functional parameters and the most relevant recent quantitative disease/proteomics associations for human LMAN2/VIP36. It is useful as a compact evidence summary for annotation, emphasizing what is measured directly versus what remains inferential or mixed.*