Target intelligence / Profile preview

Ribophorin I (RPN1)

Target
RPN1
Molecular classification
Transmembrane glycoprotein, Endoplasmic reticulum membrane protein, Component of oligosaccharyltransferase complex
01

Overview

Ribophorin I is a highly conserved, dome-shaped transmembrane glycoprotein found exclusively in the membrane of the rough endoplasmic reticulum (ER), where it is a key subunit of the oligosaccharyltransferase (OST) complex[1][2][3][4][5]. Its primary roles include binding the large (60S) ribosomal subunit, facilitating protein translocation into the ER lumen, and selectively presenting substrate proteins for N-linked glycosylation via the OST catalytic core[1][2][3]. Ribophorin I operates as a type I membrane protein, with a significant portion of its structure facing the ER lumen[3][1]. It does not occur in the smooth ER and is only present in eukaryotic cells[1]. The protein is encoded in humans by the RPN1 gene located at chromosome 3q21.3[1]. While essential for correct protein folding and modification, ribophorin I is mainly considered a structural and functional component of cellular machinery rather than a direct therapeutic target. No approved drugs act directly on ribophorin I, and there are no established uses of ribophorin I as a clinical biomarker or pharmacological intervention point. Defects in RPN1 may, however, impact protein quality control and ER homeostasis, potentially contributing to rare congenital disorders[1][2].

Other names
RPN1OST subunit ribophorin IRibophorin-1Ribophorin I subunit of oligosaccharyltransferase
02

Biological functions

Binding of ribosomes to the rough endoplasmic reticulumRegulation of co-translational translocation of proteins into the ERSubstrate recognition and delivery for N-linked glycosylation (N-glycosylation) by oligosaccharyltransferase complexChaperone-like function, preferentially interacting with misfolded proteins to facilitate their glycosylation
03

Disease associations

Potential roles in congenital disorders of glycosylation (when mutated)Other (no major direct implication in common diseases established)
04

Safety considerations

Broadly considered an essential housekeeping component, so loss of function may cause general ER stress or failure in protein N-glycosylationNo direct safety or therapeutic concerns as a pharmacological target reported

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