Target intelligence / Profile preview

ER membrane protein complex subunit 2 (EMC2)

Target
EMC2
Molecular classification
Other (subunit of ER membrane protein complex), Tetratricopeptide repeat (TPR)-containing protein, Protein complex subunit
01

Overview

ER membrane protein complex subunit 2 (EMC2) is a conserved, cytosolic subunit of the ER membrane protein complex (EMC), which is essential for the insertion of specific transmembrane helices from newly synthesized membrane proteins into the endoplasmic reticulum (ER) membrane. EMC2 helps form the cytosolic disc region of the EMC through a series of tetratricopeptide repeats (TPRs) that serve as a scaffold for protein-protein interactions between other core EMC subunits. By aiding both cotranslational insertion of multi-pass membrane proteins and post-translational insertion of tail-anchored proteins, EMC2 is indirectly involved in the biogenesis of various membrane proteins including G protein-coupled receptors. As part of the broader EMC, EMC2 does not itself possess enzymatic or receptor activity, nor is it presently a direct drug target; rather, its proper function is necessary for the accurate assembly and maturation of many membrane proteins critical to cell and organelle physiology. No drugs currently target EMC2 specifically, and the gene is not commonly associated with direct disease mutations, though EMC dysfunction can have broad bioenergetic and signaling consequences.

Other names
EMC2KIAA0103TTC35Tetratricopeptide repeat protein 35TPR repeat protein 35
02

Biological functions

Membrane protein biogenesis (insertase function for transmembrane helices)Cotranslational insertion of multi-pass membrane proteinsPosttranslational insertion of tail-anchored proteinsProtein-protein interaction scaffold within the ER membrane complexRegulation of membrane protein topology, including G protein-coupled receptors
03

Disease associations

Other (not directly implicated in major disease classes, but alterations may affect membrane protein biogenesis and cell physiology)
04

Safety considerations

No direct safety concerns or therapeutic challenges reported; disruption may broadly affect membrane protein insertion and ER function, potentially leading to cell stress or dysfunction in protein biogenesis

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