| IED ID | IndEnz0002016416 |
| Enzyme Type ID | protease016416 |
| Protein Name |
Protein DOA1 Degradation of alpha protein 1 Ubiquitin fusion degradation protein 3 |
| Gene Name | DOA1 UFD3 ZZZ4 YKL213C |
| 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 | MGYQLSATLKGHDQDVRDVVAVDDSKVASVSRDGTVRLWSKDDQWLGTVVYTGQGFLNSVCYDSEKELLLFGGKDTMINGVPLFATSGEDPLYTLIGHQGNVCSLSFQDGVVISGSWDKTAKVWKEGSLVYNLQAHNASVWDAKVVSFSENKFLTASADKTIKLWQNDKVIKTFSGIHNDVVRHLAVVDDGHFISCSNDGLIKLVDMHTGDVLRTYEGHESFVYCIKLLPNGDIVSCGEDRTVRIWSKENGSLKQVITLPAISIWSVDCMSNGDIIVGSSDNLVRIFSQEKSRWASEDEINELSTQVEKSTISSKTIEFDESKLSPYEILQSPGRKEGQIVVVKSPQGTIEAHQFSNSSWKKVGDVVGAGATGNDKKIEFEGKTYDYVFDVDIEDGKPPLKLPINVSDNPYTAADNFLARYELPMSYRDQVVQFILKNTNGISLDQPNDNASSSAVSPSKTSVMKVLPVKQYLIMENYNPDTIFNGIVKINSNEKTFDDEILAQIGGALHDIDESWELLLSFANTIRSNWEIKTPAYDIVRLIVKKLPYSSDIKDYIEEGLGNKNITLTMLTVRILVNCFNNENWGVKLLESNQVYKSIFETIDTEFSQASAKQSQNLAIAVSTLIFNYSALVTKGNSDLELLPIVADAINTKYGPLEEYQECEEAAYRLTVAYGNLATVEPTLRQFANSVTWLANIKRSYGNVPRFKDIFDDLS |
| Enzyme Length | 715 |
| Uniprot Accession Number | P36037 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: Ubiquitin-binding protein involved in protein ubiquitination, sorting and degradation (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:18508771, PubMed:20508643, PubMed:27044889). Acts as a ubiquitinated substrate-recruiting adapter for chaperone ATPase CDC48 by binding mono- or polyubiquitin chains (PubMed:15096053, PubMed:16427015, PubMed:16428438, PubMed:27044889). Depending on the context, promotes or prevents proteasomal degradation of ubiquitinated proteins (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:27044889). Involved in the ubiquitin fusion degradation (UFD) pathway by promoting the degradation of ubiquitinated proteins (PubMed:2111732, PubMed:8890162, PubMed:19805280, PubMed:27044889). Involved in the mitochondria-associated degradation pathway (MAD) by promoting the degradation of several ubiquitinated membrane proteins (PubMed:27044889). By competing with UFD2 to bind CDC48, prevents the multi-ubiquitination and subsequent degradation of UFD2-dependent substrates (PubMed:16427015). Required for ribophagy, a process which relocalizes ribosomal particles into the vacuole for degradation in response to starvation (PubMed:20508643). Involved in the ubiquitin-mediated sorting of membrane proteins into multivesicular bodies (MVBs) (PubMed:18508771). In addition, plays an essential role in maintaining cellular ubiquitin levels (PubMed:7615550, PubMed:16427015, PubMed:16428438, PubMed:18508771, PubMed:19805280). May affect indirectly the degradation of ubiquitinylated proteins by regulating cellular ubiquitin levels (PubMed:7615550, PubMed:23525333). {ECO:0000269|PubMed:15096053, ECO:0000269|PubMed:16427015, ECO:0000269|PubMed:16428438, ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:19805280, ECO:0000269|PubMed:20508643, ECO:0000269|PubMed:2111732, ECO:0000269|PubMed:23525333, ECO:0000269|PubMed:27044889, ECO:0000269|PubMed:7615550, ECO:0000269|PubMed:8890162}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (31); Chain (1); Domain (2); Helix (22); Modified residue (1); Mutagenesis (22); Region (1); Repeat (13); Sequence conflict (1); Turn (7) |
| Keywords | 3D-structure;Cytoplasm;Direct protein sequencing;Endosome;Membrane;Mitochondrion;Mitochondrion outer membrane;Nucleus;Phosphoprotein;Reference proteome;Repeat;Ubl conjugation pathway;WD repeat |
| Interact With | P25694; P38753; Q01477; Q01853 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}. Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}. Mitochondrion outer membrane {ECO:0000269|PubMed:27044889}; Peripheral membrane protein {ECO:0000269|PubMed:27044889}; Cytoplasmic side {ECO:0000269|PubMed:27044889}. Endosome membrane {ECO:0000269|PubMed:18508771}; Peripheral membrane protein {ECO:0000269|PubMed:18508771}; Cytoplasmic side {ECO:0000269|PubMed:18508771}. Note=Predominantly localizes to the cytoplasm. Probably localizes to endosomes and mitochondria in a transient manner. {ECO:0000269|PubMed:18508771, ECO:0000269|PubMed:27044889}. |
| Modified Residue | MOD_RES 332; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (5) |
| Cross Reference PDB | 3GAE; 3L3F; 3ODT; 3PSP; 3PST; |
| Mapped Pubmed ID | 10567550; 11056159; 11743162; 11805826; 12149442; 12399380; 14755638; 16429126; 16507144; 16554755; 16705165; 17142044; 17707817; 19067491; 19286982; 19423704; 19536198; 19841731; 19887378; 20675578; 21148305; 21282470; 21427232; 21526151; 21548784; 21741246; 22042866; 22214660; 22660740; 22729030; 22842922; 22964839; 23645753; 24607902; 24845679; 26349035; 26585826; 26670610; 26945625; 26975376; 27693354; 27715443; 8668160; |
| Motif | |
| Gene Encoded By | |
| Mass | 79,506 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |