ER membrane protein complex subunit 3 (Transmembrane protein 111)
1_MAGPE 6_ LLLDS 11_ NIRLW 16_ VVLPI 21_ VIITF 26_ FVGMI 31_ RHYVS 36_ ILLQS 41_ DKKLT 46_ QEQVS 51_ DSQVL 56_ IRSRV 61_ LRENG 66_ KYIPK 71_ QSFLT 76_ RKYYF 81_ NNPED 86_ GFFKK 91_ TKRKV 96_ VPPSP 101_ MTDPT 106_ MLTDM 111_ MKGNV 116_ TNVLP 121_ MILIG 126_ GWINM 131_ TFSGF 136_ VTTKV 141_ PFPLT 146_ LRFKP 151_ MLQQG 156_ IELLT 161_ LDASW 166_ VSSAS 171_ WYFLN 176_ VFGLR 181_ SIYSL 186_ ILGQD 191_ NAADQ 196_ SRMMQ 201_ EQMTG 206_ AAMAM 211_ PADTN 216_ KAFKT 221_ EWEAL 226_ ELTDH 231_ QWALD 236_ DVEEE 241_ LMAKD 246_ LHFEG 251_ MFKKE 256_LQTSI
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)