SCARB2 / LIMP-2 (human, Q14108) curation notes

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UniProt.

Localization (benchmark-relevant)

• Principal location is the lysosomal / late endosomal limiting membrane, not the cell surface:
  UniProt SUBCELLULAR LOCATION: Lysosome membrane ...; Multi-pass membrane protein;
  PMID:12356916
• The large glycosylated domain faces the lumen (topologically equivalent to extracellular).
• A minor plasma-membrane pool exists and is the entry receptor for enterovirus 71 (UniProt,
  microbial infection FUNCTION), so the protein is partially surface-accessible; the many Reactome
  plasma-membrane rows were kept as non-core on that basis rather than accepted as the main site.
• Focal adhesion (single HDA hit) marked over-annotated; lysosome marked TOO_GENERAL beside
  lysosomal membrane; generic membrane modified to lysosomal + late endosome membrane.

Function

• Cargo receptor for GBA1: PMID:18022370 and "beta-glucocerebrosidase activity and protein levels were
  severely decreased in LIMP-2-deficient mouse tissues."
• Lipid binding/transport: [PMID:29199275 crystal structure of luminal-domain dimer with bound
  cholesterol and phosphatidylcholine; dimer prefers phosphatidylserine; "LIMP-2 facilitates
  transport of phospholipids into murine fibroblasts"]. Kept as non-core secondary activity.
• Organelle morphology: overexpression enlarges early and late endosomes/lysosomes PMID:12356916.

Review decisions

• GO:0005044 scavenger receptor activity (IBA/ISS/IEA/TAS) MODIFYed to GO:0038024 cargo receptor activity: the CD36/SR-BI family node is sound but SCARB2 has diverged to an intralumenal cargo
  receptor; a propagation_review records this against PANTHER:PTN000230217.
• GO:0004888 transmembrane signaling receptor activity likewise modified to cargo receptor
  activity.
• Nine generic GO:0005515 rows removed per policy; enzyme binding (GBA1) accepted.