| IED ID | IndEnz0002012810 |
| Enzyme Type ID | protease012810 |
| Protein Name |
E3 ubiquitin-protein ligase rififylin EC 2.3.2.27 RING finger and FYVE-like domain-containing protein 1 Fring RING-type E3 ubiquitin transferase rififylin |
| Gene Name | Rffl |
| Organism | Mus musculus (Mouse) |
| 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 Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MSQPSLWKDSHYFIMWASCCNWFCLDGQPEEAPPPQGARTQAYSNPGYSSFPSPTGSEPSCKACGVHFASTTRKQTCLDCKKNFCMTCSSQEGNGPRLCLLCLRFRATAFQREELMKMKVKDLRDYLSLHDISTEMCREKEELVFLVLGQQPVISEADRTRVPHLPQAFPEQQAFLTQPQTSTVPPTSPGLPSSPAQVTSVPLAQDQETQQAVGHVSQDHEEPIFPESTARVPTEDETQSVDSEDSFVPGRRASLSDLTHLEDIEGLTVRQLKEILARNFVNYKGCCEKWELMERVTRLYKDQKGLQHLVSGNEDQNGGAVPSGLEENLCKICMDSPIDCVLLECGHMVTCTKCGKRMNECPICRQYVIRAVHVFRS |
| Enzyme Length | 377 |
| Uniprot Accession Number | Q6ZQM0 |
| 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:15229288, ECO:0000269|PubMed:22609986}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q8WZ73}. |
| nucleotide Binding | |
| Features | Alternative sequence (4); Chain (1); Compositional bias (1); Domain (2); Modified residue (4); Region (1); Sequence conflict (1); 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 | INDUCTION: Up-regulation by LPA/lysophosphatidic acid is dependent on GNA12. {ECO:0000269|PubMed:22609986}. |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15229288}. Cell membrane {ECO:0000269|PubMed:15229288}; Peripheral membrane protein {ECO:0000269|PubMed:15229288}. Recycling endosome membrane {ECO:0000305|PubMed:15229288}; Peripheral membrane protein {ECO:0000305|PubMed:15229288}. Note=The FYVE-type zinc finger may mediate phosphatidylinositol phosphate-binding and control subcellular localization. |
| Modified Residue | MOD_RES 240; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 243; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 246; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079; MOD_RES 254; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:21183079 |
| Post Translational Modification | PTM: Autoubiquitinated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; 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 | 11217851; 12383505; 12466851; 14610273; 15226823; 15618518; 17967808; 18450452; 18799693; 24114843; |
| Motif | |
| Gene Encoded By | |
| Mass | 42,249 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |