| IED ID | IndEnz0002010421 |
| Enzyme Type ID | protease010421 |
| Protein Name |
E3 ubiquitin-protein ligase rififylin EC 2.3.2.27 FYVE-RING finger protein Sakura RING finger and FYVE-like domain-containing protein 1 RING-type E3 ubiquitin transferase rififylin |
| Gene Name | Rffl |
| Organism | Rattus norvegicus (Rat) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Rattus Rattus norvegicus (Rat) |
| Enzyme Sequence | MWASCCNWFCLDGQPEETPPPQGARTQAYSNPGYSSFPSPTGSEPSCKACGVHFASTTRKQTCLDCKKNFCMTCSSQEGNGPRLCLLCLRFRATAFQREELMKMKVKDLRDYLSLHDISTEMCREKEELVFLVLGQQPVISEADRTRAPTLPQAFPEQQAFLTQPQSSTVPPTSPGLPSSPAQVTSVLAQDQETQQAIGHVSQDHEEPIFLESTARVPPEDETQSVDSEDSFVPGRRASLSDLTHLEDIEGLTVRQLKEILARNFVNYKGCCEKWELMERVTRLYKDQKGLQHLVSGNEDQNGGAVPSGLEENLCKICMDSPIDCVLLECGHMVTCTKCGKRMNECPICRQYVIRAVHVFRS |
| Enzyme Length | 362 |
| Uniprot Accession Number | Q8CIN9 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8WZ73}; |
| DNA Binding | |
| EC Number | 2.3.2.27 |
| Enzyme Function | FUNCTION: E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Also ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate apoptosis downstream of death domain receptors. Also negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling. {ECO:0000269|PubMed:12859687}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q8WZ73}. |
| nucleotide Binding | |
| Features | Alternative sequence (1); Chain (1); Compositional bias (1); Domain (2); Modified residue (4); Region (2); Zinc finger (2) |
| Keywords | Alternative splicing;Apoptosis;Cell membrane;Cytoplasm;Endosome;Lipoprotein;Membrane;Metal-binding;Palmitate;Phosphoprotein;Reference proteome;Repeat;Transferase;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12859687}. Cell membrane {ECO:0000269|PubMed:12859687}; Peripheral membrane protein {ECO:0000269|PubMed:12859687}. Recycling endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=The FYVE-type zinc finger may mediate phosphatidylinositol phosphate-binding and control subcellular localization. |
| Modified Residue | MOD_RES 225; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 228; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903; MOD_RES 231; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q6ZQM0; MOD_RES 239; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:22673903 |
| Post Translational Modification | PTM: Autoubiquitinated. {ECO:0000305|PubMed:12859687}.; PTM: Palmitoylated. {ECO:0000269|PubMed:12859687}.; PTM: Undergoes caspase-mediated cleavage upon death-receptor activation, by TNFSF10 for instance. May be mediated by the caspases CASP8 and CASP10 in a negative feedback loop (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 21357277; 28827789; |
| Motif | |
| Gene Encoded By | |
| Mass | 40,409 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |