The following text describes a protein:
Function:
Lipid transfer protein required for autophagosome completion and peroxisome degradation. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. ATG2 binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, using basic residues in its N-terminal region (NR) and to the expanding edge of the IM through its C-terminal region. The latter binding is assisted by an ATG18-PtdIns3P interaction. ATG2 then extracts phospholipids from the membrane source using its NR and transfers them to ATG9 to the IM through its predicted beta-sheet-rich structure for membrane expansion. ATG2 is also involved in the recruitment of lipids to a restricted region close to the vacuole, termed the vacuole-isolation membrane contact site (VICS), which is also essential for autophagosome formation. Necessary for the localization of ATG18 to the preautophagosomal structure (PAS) and the binding of ATG18 to ATG9. ATG2 is the most downstream ATG protein in the preautophagosomal structure organization process. Involved in correct ATG9 trafficking through the preautophagosomal structure and in peroxisome degradation. Plays a significant role in life span extension.
Miscellaneous:
MISCELLANEOUS: Present with 876 molecules/cell in log phase SD medium.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Localizes to the IM-ERES contact site.
Domain:
The N-terminal region (NR) associates with the endoplasmic reticulum (ER) and is responsible for the formation of the isolation membrane at the PAS; The amphipathic helix in the C-terminal region binds to membranes and facilitates ATG18 binding to PtdIns3P to target the ATG2-ATG18 complex to the PAS.
Sequence:
MAFWLPQNIQKRLLLYVLQQISLFSNIDLSNLDVSIGSKSHFSFHDVNLSLDDLNIPNVQINEGIVDELVLKLTVSGGVEIDGSGLRFIMTPLYSSGSQELHSDFLVKSIQDLTNSMLQFSDPLTTYNRYKEDDISSSDSSSDLNSNIEASKPAANGSYTLQNMRNKALNVALAKLKIALKDVTIRFIVNDRDPSDNIVEVHLESIQLITTDANLRHINIENITISSIQKQAVPDSPVHPFNNDDLSQSVYLSKMEATSLYMSAMEEQSNEDPSEPQVTQEEQENDKCKESLMEINNLNIAFKGLSSVNDLRMSNIVIDIQDVHLAIHKIVEIKNSTLKNIIDIIVTHLDANESFSCQDSQSPSPDKQEPSALSSVDIKCIYLNLGQDITVILKSFKLEQKENNSLAFSLGSFYSNSSPLTISHKTKPLLTGEQTPQSIALNMGDELDIIISHDGIAHFFKIFQFVSKCMSFYQNKSKGMMPQIASDTKRTVQLTSKAVKLSLKFPYFLLCFQVSPFIYDSNRELYIELVDVFKKLPSRCTKILTMSSITISNLQSPLQLGSYDDTLKEALIYSSVHAIIKEVIFNEEYSGIVQLVEDISAFGKLFTDSKNSECTGKSKSKRGSFLQRSVRVLNSSRFVYKQSLSANFSLKIDSMKLKVSEIIGPQFGSVEALLSNNFFAITDDSQIVYFTKNLKVERKTPSLLEPQEIMSVVLNKAVNEPVLYVHRRANGKLKVIFNNIRIHYYARWLEILKKNIGPDNASSKDEPVSQKLSKKQPTSGFPWELKCLDCSLILHPFRLKSVMVIVLDNLTTGGSSFIPQAKLLSKANTLFLIDDYQNFKIQKDKNWPSLINFYAGQGFSAIGKIDTLNFLINKSDGALLLDCKIEQVGLSLCADSFQTFCQLCIDLKYPQTFPDEEKFRTQLKNPIDVFKDIDCDLFNSAFIRENNHQNDYDSVHLVDSFLDKTHEFNNGARSKLSSQGSYEMDSSSGTATGGILLPHESYLDSAQPKEEDTPPIASKEQERDVDIRGSIDVEKVVIKLFDGYDWKYTRKFIANTVEKLDKELSKAEASSSKSNVPQSEANIFDSIYISANKNNVTDLRRNLDGEIQGVQNSFSDVSKVNLRPSKHYKALIQLNKVHVNLKNYRVDEPDESNSDNSTDVLNRCVVSIYEFEIIDNVPTSTWNKFVTLLKHEPWPHSSPMFLLDLEFIRPIDFLQAVELVMQLNVAPLRLHVDQDTLEFLIRFLGFKDKRFELIDEYPDIVFIQKFSTNSIKLRLDYKPKKVDYAGLRSGQTSELMNFFTLDGSKIILKSVVLYGLNGFDELNNKLKAIWTPDITKKQLPGVLEGLAPVRSFMAIGSGVKTLVTVLMSEYRQEGHLGRSLKKGGNVFLKTTTGDFVKLGVKLTSGTQAILENTEELFGGVGSNGRVYDASKFGSADGADSDTAAVLDLDTLFEEDQLVGSKYSRIRDHEPTAVVIDMSSPGDHNEPTIVSLYADQPLDLPTGLKEAYSSLEKHMHIAYDAVWRAKGQMKDDKRGGPSAAAVYVARAAPVAIIRPLIGATEAVSKTLQGIANQVDKTHNEQINDKYKSNRTDS