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ER membrane protein complex subunit 4 (EMC4)

Target
EMC4
Molecular classification
Other (multi-pass transmembrane protein; subunit of a larger membrane insertase/chaperone complex)
01

Overview

ER membrane protein complex subunit 4 (EMC4) is a conserved, multi-pass transmembrane protein that forms part of the endoplasmic reticulum (ER) membrane protein complex (EMC), which consists of 9–10 subunits in mammals[1][2][4]. EMC4 is one of the key transmembrane constituents involved in forming the core insertase cavity and structure of the complex, along with EMC3 and EMC6[1][4]. The EMC plays essential roles in the co- and post-translational insertion of transmembrane helices from a wide range of tail-anchored and multipass membrane proteins into the ER, thus facilitating correct membrane protein topology, folding, assembly, and quality control[1][4]. Loss of EMC function (including by dysfunctional EMC4) is associated with ER stress, disruption of membrane protein biosynthesis, and has been implicated in a variety of diseases such as cancer and metabolic or neurological disorders, but EMC4 itself is not directly a therapeutic target or drug receptor[4].\n\nClarifications\n- EMC4 is a structural component and not currently considered a direct drug target or receptor. Its primary biological function is in supporting the insertase and chaperone activity of the EMC[1][4].\n- No known drugs directly interact with EMC4, nor is EMC4 used as a direct biomarker or therapeutic target. Disruption mostly produces cellular pathology through loss of complex function.\n- The alternative names (aliases) stem from prior gene/protein annotation and predicted proliferative effects, but the canonical name in human gene nomenclature is ER membrane protein complex subunit 4 (EMC4)[2][4].

Other names
EMC4TMEM85HSPC184PIG17FLJ90746MGC24415Cell proliferation-inducing gene 17 proteinTransmembrane protein 85
02

Biological functions

Membrane protein biogenesis (as part of the ER membrane protein complex)Co- and post-translational insertion of transmembrane helicesMembrane protein quality controlProtein folding and assembly in the ERPossibly involved in cell proliferation
03

Disease associations

Cancer (implicated via the EMC complex in some pathological phenotypes)Neurological disorders (via complex dysfunction)Metabolic disease, including type 2 diabetes (via broader EMC roles)Virus replication (as part of the EMC complex)
04

Safety considerations

Not a direct therapeutic target; disruption may cause global defects in membrane protein biogenesis and ER stressPossible implications in diseases due to broader EMC dysfunction, not EMC4 itself

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