FAM158A (Vector Vector will be determined during the manufacturing process, either pENTR223.1 or pUC

Length: 627 Sequence: atgggggagg tggagatctc ggccctggcc tacgtgaaga tgtgcctgca tgctgcccgg tacccacacg ccgcagtcaa cgggctgttt ttggcgccag cgccgcggtc tggagaatgc ctgtgcctca ccgactgtgt gcccctcttc cacagccacc tggccctgtc cgtcatgttg gaggtcgccc tcaaccaggt ggatgtgtgg ggagcacagg ccggtctggt ggtggctggt tactaccatg ccaatgcagc tgtgaacgat cagagccctg ggcccctggc cttgaaaatt gctgggcgaa ttgcagaatt cttccctgat gcagtactta ttatgttgga taatcagaaa ctggtgcctc agcctcgtgt gcccccggtc atcgtcctgg agaaccaagg tctccgctgg gtccctaagg ataagaactt agtgatgtgg agggactggg aagagtcacg gcagatggtg ggagctctac tggaagatcg ggcccaccag caccttgtgg actttgactg ccaccttgat gacatccggc aggactggac caaccagcgg ctcaacactc aaatcaccca gtgggttggt cccactaatg gaaatggaaa Protein 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:30415835, PubMed:29809151, PubMed:29242231, PubMed:32459176). Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues (PubMed:30415835, PubMed:29809151, PubMed:29242231). Involved in the cotranslational insertion of multi- pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices (PubMed:30415835, PubMed:29809151). It is also required for the post-translational insertion of tail- anchored/TA proteins in endoplasmic reticulum membranes (PubMed:29809151, PubMed:29242231). 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). [The UniProt Consortium]