Mannose 6-phosphate receptor

The mannose 6-phosphate receptors (MPRs) are transmembrane glycoproteins that target enzymes to lysosomes in vertebrates.

Cation-independent mannose-6-phosphate receptor repeat
Identifiers
SymbolCIMR
PfamPF00878
InterProIPR000479
SCOP21e6f / SCOPe / SUPFAM
Membranome30
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cation-dependent mannose-6-phosphate receptor
Identifiers
SymbolM6PR
NCBI gene4074
HGNC6752
OMIM154540
RefSeqNM_002355
UniProtP20645
Other data
LocusChr. 12 p13
Search for
StructuresSwiss-model
DomainsInterPro
Cation-independent mannose-6 phosphate receptor
Identifiers
SymbolIGF2R
NCBI gene3482
HGNC5467
OMIM147280
RefSeqNM_000876
UniProtP11717
Other data
LocusChr. 6 q25q27
Search for
StructuresSwiss-model
DomainsInterPro

Mannose 6-phosphate receptors bind newly synthesized lysosomal hydrolases in the trans-Golgi network (TGN) and deliver them to pre-lysosomal compartments. There are two different MPRs, one of ~300kDa and a smaller, dimeric receptor of ~46kDa. The larger receptor is known as the cation-independent mannose 6-phosphate receptor (CI-MPR), while the smaller receptor (CD-MPR) requires divalent cations to efficiently recognize lysosomal hydrolases. While divalent cations are not essential for ligand binding by the human CD-MPR, the nomenclature has been retained.

Both of these receptors bind terminal mannose 6-phosphate with similar affinity (CI-MPR = 7 μM, CD-MPR = 8 μM) and have similar signals in their cytoplasmic domains for intracellular trafficking.

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