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The MPT complex takes over after the SEC61 complex: following membrane insertion of the first few transmembrane segments of proteins by the SEC61 complex, the MPT complex occludes the lateral gate of the SEC61 complex to promote insertion of subsequent transmembrane regions (PubMed:36261528). Within the MPT complex, the PAT subcomplex sequesters any highly polar regions in the transmembrane domains away from the non-polar membrane environment until they can be buried in the interior of the fully assembled protein (PubMed:36261528). Within the PAT subcomplex, WDR83OS/Asterix binds to and redirects the substrate to a location behind the SEC61 complex (PubMed:36261528)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"}],"value":"Component of the PAT complex, composed of WDR83OS/Asterix and CCDC47 (PubMed:36261528). The PAT complex is part of the multi-pass translocon (MPT) complex, composed of three subcomplexes, the GEL complex (composed of RAB5IF/OPTI and TMCO1), the BOS complex (composed of NCLN/Nicalin, NOMO1 and TMEM147) and the PAT complex (composed of WDR83OS/Asterix and CCDC47) (PubMed:36261528). The MPT complex associates with the SEC61 complex (PubMed:36261528)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the Asterix family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y284"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"PAT complex subunit Asterix","featureId":"PRO_0000457555"},{"type":"Topological domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TM3"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TUT"}]},{"type":"Transmembrane","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TM3"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TUT"}]},{"type":"Topological domain","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TM3"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TUT"}]},{"type":"Transmembrane","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TM3"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TUT"}]},{"type":"Topological domain","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TM3"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TUT"}]},{"type":"Transmembrane","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TM3"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TUT"}]},{"type":"Topological domain","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36261528"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TM3"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"7TUT"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"N-acetylserine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y284"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0007","category":"PTM","name":"Acetylation"},{"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"16341006","citationType":"journal article","authors":["Lindblad-Toh K.","Wade C.M.","Mikkelsen T.S.","Karlsson E.K.","Jaffe D.B.","Kamal M.","Clamp M.","Chang J.L.","Kulbokas E.J. 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