LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Homologous_superfamily |
| Description | 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 [ ]. 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) [ ] reveals structural similarity to the fifteen homologous, repeating domains comprising the extracellular region of human CI-MPR []. The structure consists of a partly opened, nine-stranded, β-barrel [, ]. |
| Short Name | Man6P_isomerase_rcpt-bd_dom_sf |
