ER membrane protein complex subunit 7
1_MAAAL 6_ WGFFP 11_ VLLLL 16_ LLSGD 21_ VQSSE 26_ VPGAA 31_ AEGSG 36_ GSGVG 41_ IGDRF 46_ KIEGR 51_ AVVPG 56_ VKPQD 61_ WISAA 66_ RVLVD 71_ GEEHV 76_ GFLKT 81_ DGSFV 86_ VHDIP 91_ SGSYV 96_ VEVVS 101_ PAYRF 106_ DPVRV 111_ DITSK 116_ GKMRA 121_ RYVNY 126_ IKTSE 131_ VVRLP 136_ YPLQM 141_ KSSGP 146_ PSYFI 151_ KRESW 156_ GWTDF 161_ LMNPM 166_ VMMMV 171_ LPLLI 176_ FVLLP 181_ KVVNT 186_ SDPDM 191_ RREME 196_ QSMNM 201_ LNSNH 206_ ELPDV 211_ SEFMT 216_ RLFSS 221_ KSSGK 226_ SSSGS 231_ SKTGK 236_SGAGK
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)