polymeric immunoglobulin receptor; poly-Ig receptor; PIGR; hepatocellular carcinoma-associated protein TB6 (PIGR)

Function: - binds polymeric IgA & IgM at the basolateral surface of epithelial cells - the receptor complex is then transported across the cell to be secreted at the apical surface - during this process a cleavage occurs that separates the extracellular (known as the secretory component) from the transmembrane segment Structure: - N-glycosylation is not necessary for Ig binding - contains 5 Ig-like V-type domains (immunoglobulin-like) Compartment: - cell membrane - secretory component: secreted

General

cell surface receptor glycoprotein phosphoprotein

Properties

SIZE: entity length = 764 aa MW = 83 kD COMPARTMENT: cellular membrane MOTIF: signal sequence {1-18} immunoglobulin superfamily domain {19-120} MOTIF: cysteine residue {C40} MODIFICATION: cysteine residue {C110} cysteine residue {C56} MODIFICATION: cysteine residue {C64} cysteine residue {C64} MODIFICATION: cysteine residue {C56} N-glycosylation site {N83} N-glycosylation site {N90} cysteine residue {C110} MODIFICATION: cysteine residue {C40} N-glycosylation site {N135} immunoglobulin superfamily domain {145-237} MOTIF: cysteine residue {C152} MODIFICATION: cysteine residue {C220} N-glycosylation site {N186} cysteine residue {C220} MODIFICATION: cysteine residue {C152} immunoglobulin superfamily domain {250-352} MOTIF: cysteine residue {C257} MODIFICATION: cysteine residue {C325} cysteine residue {C271} MODIFICATION: cysteine residue {C279} cysteine residue {C279} MODIFICATION: cysteine residue {C271} cysteine residue {C325} MODIFICATION: cysteine residue {C257} immunoglobulin superfamily domain {364-458} MOTIF: cysteine residue {C371} MODIFICATION: cysteine residue {C441} cysteine residue {C385} MODIFICATION: cysteine residue {C395} cysteine residue {C395} MODIFICATION: cysteine residue {C385} N-glycosylation site {N421} cysteine residue {C441} MODIFICATION: cysteine residue {C371} immunoglobulin superfamily domain {462-561} MOTIF: N-glycosylation site {N469} cysteine residue {C482} MODIFICATION: cysteine residue {C544} cysteine residue {C486} MODIFICATION: cysteine residue {C520} cysteine residue {C496} MODIFICATION: cysteine residue {C503} N-glycosylation site {N499} cysteine residue {C503} MODIFICATION: cysteine residue {C496} cysteine residue {C520} MODIFICATION: cysteine residue {C486} cysteine residue {C544} MODIFICATION: cysteine residue {C482} transmembrane domain {639-661} Ser phosphorylation site {S682} Ser phosphorylation site {S734}

Database Correlations

OMIM 173880 UniProt P01833 Pfam PF07686 Kegg hsa:5284

References

UniProt :accession P01833