EMC1

Chr 1p36.13

ER membrane protein complex subunit 1

MANE:: ENST00000477853.6

OMIM: 616846 ↗NCBI: 23065 ↗Ensembl ↗

Annotations refreshed 9 hours ago.

Predicted protein structure

AlphaFold predicted structure

EMC1 · Q8N766

v62025-08-01

Predicted Aligned Error matrix for EMC1 — diagonal shows residue index, colour shows pairwise prediction confidence (lower is better) — Predicted Aligned Error

Mean pLDDT

87.4/ 100

Confident

993 residues

Confidence breakdown

Very high(≥ 90)67%
Confident(70–90)22%
Low(50–70)8%
Very low(< 50)3%

Open interactive 3D viewer

AlphaFold (Jumper et al., 2021) · CC BY 4.0

Clinical relevance (Genomics England PanelApp)

Diagnostic Grade (Green)

DDG2P
BIALLELIC, autosomal or pseudoautosomal
Intellectual disability
BOTH monoallelic and biallelic, autosomal or pseudoautosomal
Fetal anomalies
BIALLELIC, autosomal or pseudoautosomal
Retinal disorders

Disease associations (Open Targets)

cerebellar atrophy, visual impairment, and psychomotor retardation;
0.76
hereditary disease
0.50
Retinal dystrophy
0.49
Global developmental delay
0.41
Cerebellar atrophy
0.41
global developmental delay-visual anomalies-progressive cerebellar atrophy-truncal hypotonia syndrome
0.37
autosomal recessive retinitis pigmentosa
0.33
congenital anomaly of kidney and urinary tract
0.27
Obesity
0.26
complex neurodevelopmental disorder with motor features
0.23

Score is the Open Targets composite evidence score (0-1). Higher = stronger gene-disease association.

Protein function (UniProt)

ER membrane protein complex subunit 1

Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins (PubMed:29242231, PubMed:29809151, PubMed:30415835, PubMed:32439656, PubMed:32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:29242231, PubMed:29809151, PubMed:30415835). Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:29809151, PubMed:30415835). It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29242231, PubMed:29809151). By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins like the G protein-coupled receptors (PubMed:30415835). By regulating the insertion of various proteins in membranes, it is indirectly involved in many cellular processes (Probable)