| IED ID | IndEnz0002002381 |
| Enzyme Type ID | protease002381 |
| Protein Name |
E3 ubiquitin-protein ligase MARCHF6 EC 2.3.2.27 Membrane-associated RING finger protein 6 Membrane-associated RING-CH protein VI MARCH-VI RING-type E3 ubiquitin transferase MARCHF6 |
| Gene Name | Marchf6 Kiaa0597 March6 |
| 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 | MDTAEEDICRVCRSEGTPEKPLYHPCVCTGSIKFIHQECLVQWLKHSRKEYCELCKHRFAFTPIYSPDMPSRLPIQDIFAGLVTSIGTAIRYWFHYTLVAFAWLGVVPLTACRIYKCLFTGSVSSLLTLPLDMLSTENLLADCLQGCFVVTCTLCAFISLVWLREQIVHGGAPIWLEHAAPPFNAAGHHQNEAPVGGNGAENPAADQPANPAGENAVLGENPDAQDGQAEEEEEDNEEEDDAGVEDAADANNGAQDDMNWNALEWDRAAEELTWERMLGLDGSLVFLEHVFWVVSLNTLFILVFAFCPYHIGHFSLVGLGFEEHVQASHFEGLITTIVGYILLAITLIICHALATLVKFHRSRRLLGVCYIVVKVSLLVVVEIGVFPLICGWWLDICSLEMFDATLKDRELSFQSAPGTTMFLHWLVGMVYVFYFASFILLLREVLRPGVLWFLRNLNDPDFNPVQEMIHLPIYRHLRRFILSVIVFGSIVLLMLWLPIRIIKSLLPNFLPYNVMLYSDAPVSELSLELLLLQVVLPALLEQGHTRQWLKGLVRAWTVTAGYLLDLHSYLLGDQEENENSANQQVNNNQPARNNNAVPAGEGLHAAHQAILQQGGPVGFQPYRRPLNFPLRIFLLIVFMCITLLIASLICLTLPVFAGRWLMSFWTGTAKIHELYTAACGLYVCWLTIRAVTVLVAWMPQGRRVIFQKVKEWSLMIMKTLIVAVLLAGVVPLLLGLLFELVIVAPLRVPLDQTPLFYPWQDWALGVLHAKIIAAITLMGPQWWLKTVIEQVYANGIRNIDLHYIIRKLAAPVISVLLLSLCVPYVIASGAVPLLGVTAEMQNLVHRRIYPFLLMVVVLMGILSFQVRQFKRLYEHIKNDKYLVGQRLVNYERKSGKQGPSTPPPVSSQE |
| Enzyme Length | 909 |
| Uniprot Accession Number | Q6ZQ89 |
| 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:O60337}; |
| DNA Binding | |
| EC Number | 2.3.2.27 |
| Enzyme Function | FUNCTION: E3 ubiquitin-protein ligase that promotes 'Lys-48'-linked ubiquitination of target proteins, leading to their proteasomal degradation. Promotes ubiquitination of DIO2, leading to its degradation. Promotes ubiquitination of SQLE, leading to its degradation. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. May cooperate with UBE2G1. {ECO:0000250|UniProtKB:O60337}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:O60337}. |
| nucleotide Binding | |
| Features | Alternative sequence (3); Chain (1); Compositional bias (1); Erroneous initiation (1); Metal binding (8); Modified residue (1); Region (1); Sequence conflict (1); Topological domain (15); Transmembrane (14); Zinc finger (1) |
| Keywords | Acetylation;Alternative splicing;Endoplasmic reticulum;Membrane;Metal-binding;Reference proteome;Transferase;Transmembrane;Transmembrane helix;Ubl conjugation;Ubl conjugation pathway;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60337}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60337}. |
| Modified Residue | MOD_RES 1; /note=N-acetylmethionine; /evidence=ECO:0000250|UniProtKB:O60337 |
| Post Translational Modification | PTM: Auto-ubiquitinated, which results in proteasomal degradation. {ECO:0000250|UniProtKB:O60337}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 12466851; 12520002; 15741177; 16602821; 17967808; 18799693; |
| Motif | |
| Gene Encoded By | |
| Mass | 102,273 |
| Kinetics | |
| Metal Binding | METAL 9; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00623; METAL 12; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00623; METAL 26; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00623; METAL 28; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00623; METAL 36; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00623; METAL 39; /note=Zinc 1; /evidence=ECO:0000255|PROSITE-ProRule:PRU00623; METAL 52; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00623; METAL 55; /note=Zinc 2; /evidence=ECO:0000255|PROSITE-ProRule:PRU00623 |
| Rhea ID | |
| Cross Reference Brenda |