UniProt ID | ATG4_YEAST | |
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UniProt AC | P53867 | |
Protein Name | Cysteine protease ATG4 | |
Gene Name | ATG4 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 494 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | Cysteine protease required for the cytoplasm to vacuole transport (Cvt) and autophagy. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Cleaves the C-terminal amino acid of ATG8 to reveal a C-terminal glycine. ATG8 ubiquitin-like activity requires the exposure of the glycine at the C-terminus for its conjugation to phosphatidylethanolamine (PE) and its insertion to membranes, which is necessary for autophagy. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy. Moreover not only conjugation, but also subsequent ATG8-PE deconjugation performed also by ATG4 is an important step required to delipidate ATG8 to release the protein from membranes, which facilitates multiple events during macroautophagy, and especially for efficient autophagosome biogenesis, the assembly of ATG9-containing tubulovesicular clusters into phagophores/autophagosomes, and for the disassembly of PAS-associated ATG components. ATG8 delipidation by ATG4 also recycles ATG8-PE generated on inappropriate membranes to maintain a reservoir of unlipidated ATG8 that is required for autophagosome formation at the PAS.. | |
Protein Sequence | MQRWLQLWKMDLVQKVSHGVFEGSSEEPAALMNHDYIVLGEVYPERDEESGAEQCEQDCRYRGEAVSDGFLSSLFGREISSYTKEFLLDVQSRVNFTYRTRFVPIARAPDGPSPLSLNLLVRTNPISTIEDYIANPDCFNTDIGWGCMIRTGQSLLGNALQILHLGRDFRVNGNESLERESKFVNWFNDTPEAPFSLHNFVSAGTELSDKRPGEWFGPAATARSIQSLIYGFPECGIDDCIVSVSSGDIYENEVEKVFAENPNSRILFLLGVKLGINAVNESYRESICGILSSTQSVGIAGGRPSSSLYFFGYQGNEFLHFDPHIPQPAVEDSFVESCHTSKFGKLQLSEMDPSMLIGILIKGEKDWQQWKLEVAESAIINVLAKRMDDFDVSCSMDDVESVSSNSMKKDASNNENLGVLEGDYVDIGAIFPHTTNTEDVDEYDCFQDIHCKKQKIVVMGNTHTVNANLTDYEVEGVLVEKETVGIHSPIDEKC | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
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17 | Phosphorylation | MDLVQKVSHGVFEGS HHHHHHHHCCCCCCC | 22.89 | 19779198 | |
36 | Phosphorylation | AALMNHDYIVLGEVY HHHCCCCEEEEEEEC | 5.84 | 19779198 | |
43 | Phosphorylation | YIVLGEVYPERDEES EEEEEEECCCCCCCC | 8.62 | 19779198 | |
393 | Phosphorylation | RMDDFDVSCSMDDVE CCCCCCCCCCHHHHH | 11.43 | 27017623 | |
395 | Phosphorylation | DDFDVSCSMDDVESV CCCCCCCCHHHHHHH | 20.10 | 30377154 | |
401 | Phosphorylation | CSMDDVESVSSNSMK CCHHHHHHHCCCCCC | 27.44 | 21440633 | |
403 | Phosphorylation | MDDVESVSSNSMKKD HHHHHHHCCCCCCCC | 32.83 | 20377248 | |
404 | Phosphorylation | DDVESVSSNSMKKDA HHHHHHCCCCCCCCC | 30.67 | 21440633 | |
406 | Phosphorylation | VESVSSNSMKKDASN HHHHCCCCCCCCCCC | 33.65 | 20377248 | |
483 | Phosphorylation | GVLVEKETVGIHSPI EEEEEEEECCCCCCC | 34.79 | 22369663 | |
488 | Phosphorylation | KETVGIHSPIDEKC- EEECCCCCCCCCCC- | 22.94 | 22369663 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of ATG4_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of ATG4_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of ATG4_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASSSPECTROMETRY. |