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Overview

Uniprot IDQ8N766
Protein NameER membrane protein complex subunit 1
Gene NameEMC1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
52 LEFSPGSKKLVVATE
53 EFSPGSKKLVVATEK
620 QVAPPVLKRPILQSL

Function

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)

Protein Sequence

10 MAAEWASRFW 20 LWATLLIPAA 30 AVYEDQVGKF 40 DWRQQYVGKV 50 KFASLEFSPG 60 SKKLVVATEK 70 NVIAALNSRT 80 GEILWRHVDK 90 GTAEGAVDAM 100 LLHGQDVITV 110 SNGGRIMRSW 120 ETNIGGLNWE 130 ITLDSGSFQA 140 LGLVGLQESV 150 RYIAVLKKTT 160 LALHHLSSGH 170 LKWVEHLPES 180 DSIHYQMVYS 190 YGSGVVWALG 200 VVPFSHVNIV 210 KFNVEDGEIV 220 QQVRVSTPWL 230 QHLSGACGVV 240 DEAVLVCPDP 250 SSRSLQTLAL 260 ETEWELRQIP 270 LQSLDLEFGS 280 GFQPRVLPTQ 290 PNPVDASRAQ 300 FFLHLSPSHY 310 ALLQYHYGTL 320 SLLKNFPQTA 330 LVSFATTGEK 340 TVAAVMACRN 350 EVQKSSSSED 360 GSMGSFSEKS 370 SSKDSLACFN 380 QTYTINLYLV 390 ETGRRLLDTT 400 ITFSLEQSGT 410 RPERLYIQVF 420 LKKDDSVGYR 430 ALVQTEDHLL 440 LFLQQLAGKV 450 VLWSREESLA 460 EVVCLEMVDL 470 PLTGAQAELE 480 GEFGKKADGL 490 LGMFLKRLSS 500 QLILLQAWTS 510 HLWKMFYDAR 520 KPRSQIKNEI 530 NIDTLARDEF 540 NLQKMMVMVT 550 ASGKLFGIES 560 SSGTILWKQY 570 LPNVKPDSSF 580 KLMVQRTTAH 590 FPHPPQCTLL 600 VKDKESGMSS 610 LYVFNPIFGK 620 WSQVAPPVLK 630 RPILQSLLLP 640 VMDQDYAKVL 650 LLIDDEYKVT 660 AFPATRNVLR 670 QLHELAPSIF 680 FYLVDAEQGR 690 LCGYRLRKDL 700 TTELSWELTI 710 PPEVQRIVKV 720 KGKRSSEHVH 730 SQGRVMGDRS 740 VLYKSLNPNL 750 LAVVTESTDA 760 HHERTFIGIF 770 LIDGVTGRII 780 HSSVQKKAKG 790 PVHIVHSENW 800 VVYQYWNTKA 810 RRNEFTVLEL 820 YEGTEQYNAT 830 AFSSLDRPQL 840 PQVLQQSYIF 850 PSSISAMEAT 860 ITERGITSRH 870 LLIGLPSGAI 880 LSLPKALLDP 890 RRPEIPTEQS 900 REENLIPYSP 910 DVQIHAERFI 920 NYNQTVSRMR 930 GIYTAPSGLE 940 STCLVVAYGL 950 DIYQTRVYPS 960 KQFDVLKDDY 970 DYVLISSVLF 980 GLVFATMITK 990 RLAQVKLLNR AWR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0072546 EMC complex
Cellular Component GO:0005789 endoplasmic reticulum membrane
Cellular Component GO:0016020 membrane
Cellular Component GO:0032991 protein-containing complex
Biological Process GO:0045050 protein insertion into ER membrane by stop-transfer membrane-anchor sequence
Biological Process GO:0071816 tail-anchored membrane protein insertion into ER membrane

Reference

[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.