Homologous Superfamily

Mannose-6-phosphate receptor binding domain superfamily (IPR009011)

Short name: Man6P_isomerase_rcpt-bd_dom_sf

Overlapping entries


Mannose-6-phosphate receptors (MPRs) are transmembrane proteins involved in the transport of lysosomal enzymes from the Golgi complex and the cell surface to lysosomes [PMID: 1376319]. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to MPRs in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelysosomal compartment, where the low pH mediates dissociation of the complex. There are two distinct MPRs that function in the recognition of mannose-6-phosphate-containing proteins: the cation-dependent MPR (CD-MPR) and the cation-independent MPR (CI-MPR). The CI-MPR is also known as the insulin-like growth factor II receptor, a multi-functional protein implicated in tumour suppression.

The crystal structure of the N-terminal, extracytoplasmic, receptor-binding domain of bovine CD-MPR (excluding the signal sequence) [PMID: 11786557] reveals structural similarity to the fifteen homologous, repeating domains comprising the extracellular region of human CI-MPR [PMID: 11867533]. The structure consists of a partly opened, nine-stranded, beta-barrel.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.