| IED ID | IndEnz0002003005 |
| Enzyme Type ID | protease003005 |
| Protein Name |
DNA damage-inducible protein 1 EC 3.4.23.- v-SNARE-master 1 |
| Gene Name | DDI1 VSM1 YER143W |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MDLTISNELTGEIYGPIEVSEDMALTDLIALLQADCGFDKTKHDLYYNMDILDSNRTQSLKELGLKTDDLLLIRGKISNSIQTDAATLSDEAFIEQFRQELLNNQMLRSQLILQIPGLNDLVNDPLLFRERLGPLILQRRYGGYNTAMNPFGIPQDEYTRLMANPDDPDNKKRIAELLDQQAIDEQLRNAIEYTPEMFTQVPMLYINIEINNYPVKAFVDTGAQTTIMSTRLAKKTGLSRMIDKRFIGEARGVGTGKIIGRIHQAQVKIETQYIPCSFTVLDTDIDVLIGLDMLKRHLACVDLKENVLRIAEVETSFLSEAEIPKSFQEGLPAPTSVTTSSDKPLTPTKTSSTLPPQPGAVPALAPRTGMGPTPTGRSTAGATTATGRTFPEQTIKQLMDLGFPRDAVVKALKQTNGNAEFAASLLFQ |
| Enzyme Length | 428 |
| Uniprot Accession Number | P40087 |
| Absorption | |
| Active Site | ACT_SITE 220; /evidence=ECO:0000305 |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by the proteinase inhibitors indinavir, lopinavir, nelfinavir, isovaleryl pepstatin, ritonavir, saquinavir and tipranavir. {ECO:0000269|PubMed:21266539}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.23.- |
| Enzyme Function | FUNCTION: Aspartic protease (PubMed:21266539). Appears to act as negative regulator of constitutive exocytosis (PubMed:10330187, PubMed:12051757). May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly (PubMed:12925750). Acts as a linker between the 19S proteasome and polyubiquitinated proteins like the HO endonuclease and UFO1 via UBA domain interactions with ubiquitin for their subsequent degradation (PubMed:17144915, PubMed:16478980). Required for S-phase checkpoint control (PubMed:11238935, PubMed:17144915). {ECO:0000269|PubMed:10330187, ECO:0000269|PubMed:11238935, ECO:0000269|PubMed:12051757, ECO:0000269|PubMed:12925750, ECO:0000269|PubMed:15964793, ECO:0000269|PubMed:16478980, ECO:0000269|PubMed:17144915, ECO:0000305|PubMed:21266539}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (14); Chain (1); Compositional bias (2); Cross-link (2); Domain (2); Helix (17); Mutagenesis (1); Region (1); Turn (4) |
| Keywords | 3D-structure;Aspartyl protease;Cell membrane;Cytoplasm;Hydrolase;Isopeptide bond;Membrane;Protease;Protein transport;Reference proteome;Transport;Ubl conjugation |
| Interact With | P0CG63; P0CG48 |
| Induction | INDUCTION: By DNA damage via PDR3. {ECO:0000269|PubMed:11713673, ECO:0000269|PubMed:15452273, ECO:0000269|PubMed:9157248, ECO:0000269|PubMed:9826765}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10330187}. Cell membrane {ECO:0000269|PubMed:10330187}; Peripheral membrane protein {ECO:0000269|PubMed:10330187}; Cytoplasmic side {ECO:0000269|PubMed:10330187}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (6); X-ray crystallography (2) |
| Cross Reference PDB | 2I1A; 2MR9; 2MRO; 2MRP; 2MWS; 2N7E; 4Z2Z; 5KES; |
| Mapped Pubmed ID | 10379359; 10688190; 11283351; 11323716; 11516960; 14690591; 15121879; 15571806; 16056265; 16405905; 16429126; 16554755; 16671359; 17082762; 18035052; 18485869; 18562697; 18616603; 18719252; 19536198; 20059542; 21094643; 21278740; 21327160; 21380517; 21427232; 21627799; 22318722; 22933181; 23105008; 23545414; 23874186; 24359926; 24722989; 25703377; 27170182; 27378755; 27646017; 29363267; 31276951; 31902667; 32193351; 32330640; 9294038; |
| Motif | |
| Gene Encoded By | |
| Mass | 47,354 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |