LMAN2 (VIP36) — Gene Review Notes
UniProt: Q12907 (LMAN2_HUMAN). Gene symbol: LMAN2 (HGNC:16986), synonym C5orf8.
Protein name: Vesicular integral-membrane protein VIP36 (also Glycoprotein GP36b, Lectin
mannose-binding 2). 356 aa precursor; signal peptide 1-44; mature chain 45-356; single-pass
type I membrane protein (lumenal 45-322, TM 323-345, cytoplasmic 346-356).
What VIP36 is
VIP36/LMAN2 is a type I transmembrane leguminous-type (L-type) lectin of the early
secretory pathway. Its lumenal L-type lectin-like domain (52-276) binds carbohydrate in a
Ca2+-dependent manner [file:human/LMAN2/LMAN2-uniprot.txt "L-type lectin-like"; UniProt COFACTOR
"Binds 2 calcium ions per subunit"]. UniProt FUNCTION: "Plays a role as an intracellular lectin
in the early secretory pathway. Interacts with N-acetyl-D-galactosamine and high-mannose type
glycans and may also bind to O-linked glycans. Involved in the transport and sorting of
glycoproteins carrying high mannose-type glycans" [file:human/LMAN2/LMAN2-uniprot.txt].
It is a member of the same L-type lectin family as LMAN1/ERGIC-53 (P49257; PANTHER
PTN000259611). It is NOT a glycosidase / mannosidase — it has no catalytic activity; it is a
carbohydrate-binding cargo/sorting receptor. The CDD/InterPro signatures are lectin signatures
(cd06901 lectin_VIP36_VIPL; IPR035664 VIP36_lectin; PF03388 Lectin_leg-like).
Localization (core CC = ERGIC/Golgi/ER membrane of the early secretory pathway)
UniProt SUBCELLULAR LOCATION (from PubMed:10444376, Fullekrug et al. "VIP36 localisation to the
early secretory pathway"): "Endoplasmic reticulum-Golgi intermediate compartment membrane ...
Golgi apparatus membrane ... Endoplasmic reticulum membrane" [file:human/LMAN2/LMAN2-uniprot.txt].
It cycles early in the secretory pathway between ER/ERGIC and Golgi.
- ERGIC IDA: PMID:20477988 and the localization of VIP36 to Golgi/ER cycling.
- ERGIC IDA: PMID:15308636 ERGIC membrane proteomics from BFA-treated HepG2 cells —
"purification of ERGIC membranes ... enriched 110-fold over the homogenate for ERGIC-53";
VIP36 was among the cycling/cargo-receptor proteins in this ERGIC-enriched fraction.
- Golgi apparatus IDA: HPA immunofluorescence (GO_REF:0000052) and PMID:20477988.
Carbohydrate / D-mannose binding (core MF)
- In vitro VIP36 binds high-mannose glycans with a pH optimum ~6.5: PMID:20477988.
- In the living cell VIP36 bound exclusively the high-mannose form of its cargo: PMID:20477988. This is the basis for the
D-mannose binding IMP.
- Quantitative lectin-glycan binding (carbohydrate binding IDA): PMID:23701871 using "fluorescently labeled high-mannose-type glycans and recombinant intracellular
lectins."
Transport / sorting / quality control (core BP)
VIP36 functions in post-ER quality control and ER<->Golgi cycling of high-mannose glycoproteins:
- Silencing VIP36 accelerated cargo transport, arguing against a pure anterograde role and
consistent with a quality-control / retrograde recycling role: PMID:20477988.
- Retrograde Golgi-to-ER recycling (basis for GO:0006890 IMP): PMID:20477988.
- VIP36 is "postulated as a cargo receptor for Golgi-to-endoplasmic reticulum transport"
PMID:22016386.
- Reactome: COPII-mediated vesicle transport (R-HSA-204005); Cargo concentration in the ER
(R-HSA-5694530); consistent with COPII vesicle (GO:0030134) and ER-to-Golgi transport
(GO:0006888) IBA annotations.
Interactions
- alpha1-antitrypsin (SERPINA1, P01009) is a glycoprotein cargo identified by YFP-fragment
complementation: source of the protein binding IPI (WITH P01009). PMID:20477988. This is a lectin-cargo
(sugar-dependent) interaction; the bare "protein binding" GO term is uninformative and the real
informative MF is the mannose/carbohydrate binding.
- heat shock protein binding IPI (GO:0031072), WITH UniProtKB:P11021 (BiP / HSPA5 / GRP78):
recorded by UniProt from PMID:20477988. P11021 is the ER chaperone BiP. This is a specific,
more-informative interaction than bare protein binding but is not the defining sorting
mechanism; kept non-core. (The cached PMID:20477988 entry is abstract-only — full_text_available:
false — so the BiP interaction detail is in the full text seen by the curator, not the abstract.)
Secondary / cell-surface role (ectodomain shedding, macrophages)
A minor pool of Endo-H-resistant (late-Golgi / cell-surface) VIP36 reaches the plasma membrane
and is shed; the shed/cell-surface VIP36 regulates phagocytosis in macrophages:
- PMID:22016386
- PMID:22016386
- PMID:22016386
This is the basis for the extracellular region / plasma membrane / cell surface IDA and the
positive regulation of phagocytosis IMP/IEA. These are genuine but secondary to the core
ER-Golgi lectin/sorting function, which dominates the protein's biology. Notably the lectin
activity is dispensable for phagocytosis enhancement PMID:22016386, underscoring that this is a separate moonlighting
role rather than the core function.
Proteomics-only localizations (non-core / over-annotation)
- extracellular exosome (GO:0070062) HDA from urinary/prostatic exosome shotgun proteomics
[PMID:23533145; PMID:19056867] — large-scale proteomic catalogs (~900-1132 proteins), no
VIP36-specific functional claim; reflects presence in secreted vesicles, not core residence.
- membrane (GO:0016020) IEA (InterPro IPR005052) — bare "membrane" is uninformative; the protein
is specifically an ER/ERGIC/Golgi single-pass membrane protein.
Lectin domain binds 2 Ca2+ per subunit as a structural cofactor required for carbohydrate
binding [file:human/LMAN2/LMAN2-uniprot.txt COFACTOR "Binds 2 calcium ions per subunit"]; multiple
Ca2+-binding residues (162, 164, 166, 193). UniProt keyword "Metal-binding" / GO:0046872 metal ion
binding (IEA) is a structural attribute, not the core function. (No metal/calcium binding row is
present in the GOA TSV stub, so no annotation is reviewed for it.)
Summary of review decisions
- Core MF: D-mannose binding (GO:0005537), carbohydrate binding (GO:0030246) — ACCEPT.
- Core CC: ERGIC (GO:0005793), ERGIC membrane (GO:0033116), Golgi membrane (GO:0000139),
Golgi apparatus (GO:0005794), ER membrane (GO:0005789), COPII vesicle (GO:0030134) — ACCEPT.
- Core BP: ER-to-Golgi vesicle-mediated transport (GO:0006888), retrograde Golgi-to-ER transport
(GO:0006890) — ACCEPT.
- heat shock protein binding (GO:0031072), protein binding (GO:0005515) — KEEP_AS_NON_CORE.
- positive regulation of phagocytosis (GO:0050766, IMP + IEA) — KEEP_AS_NON_CORE (secondary
macrophage role); IEA ortholog one MARK_AS_OVER_ANNOTATED.
- extracellular region/plasma membrane/cell surface (22016386 IDA) — KEEP_AS_NON_CORE (shedding).
- extracellular exosome (HDA), membrane (IEA) — MARK_AS_OVER_ANNOTATED.
Falcon deep-research findings (incorporated 2026-06)
- Specific ectodomain-shedding cleavage site (mechanism for the existing cell-surface/shedding role):
quantitative protein terminomics maps VIP36/LMAN2 as a metalloprotease-regulated shedding substrate
cleaved at F298 down-arrow L299 (SVNF/LKSP), reproducible across multiple cell lines and
suppressed by the broad-spectrum metalloprotease inhibitor BB-94 [PMID:33796845 (Tsumagari et al.,
iScience 2021) "Exploring the landscape of ectodomain shedding by quantitative protein terminomics";
DOI 10.1016/j.isci.2021.102476]. This refines the mechanistic basis of the previously curated
cell-surface/plasma-membrane/extracellular-region IDA and the shedding-dependent phagocytosis role
(PMID:22016386). Added as MEDIUM-relevance reference; no annotation change (shedding already
KEEP_AS_NON_CORE).
- Glycan-binding specificity detail (Falcon synthesis of prior reviews; consistent with existing
D-mannose/carbohydrate binding annotations): VIP36 prefers high-mannose Man7-9GlcNAc2 with strongest
recognition of the D1/A-arm Man-alpha-1,2-Man-alpha-1,2-Man motif; binding is pH-sensitive (optimum
~pH 6.0-6.5, matching early-Golgi/ERGIC lumen) and structurally Ca2+-assisted (residues Asp131,
Asn166, His190 contact ligand). Reinforces the existing core MF; reviews (Gupta 2012, Yamamoto 2014,
Reiterer 2010 thesis) are not PubMed-cached primary sources — notes-only, not added to YAML.
- Disease/association context (Falcon; non-causal, not gene function): 2024 plasma-proteome PWAS
(Xiong et al., Heliyon) associates LMAN2 with CKD-related traits (BUN/eGFR), but colocalization
PP4 < 0.01 does NOT support a shared causal cis-variant, so LMAN2 is at best an associated marker;
2023 granulosa-cell proteomics (Eubler et al.) reports LMAN2 as differentially abundant under
cannabidiol. Both are association/proteomics only and do not inform VIP36 molecular function;
notes-only, not added to YAML.