| IED ID | IndEnz0002010109 |
| Enzyme Type ID | protease010109 |
| Protein Name |
E3 ubiquitin-protein ligase XIAP EC 2.3.2.27 Baculoviral IAP repeat-containing protein 4 RING-type E3 ubiquitin transferase XIAP X-linked inhibitor of apoptosis protein X-linked IAP xXIAP |
| Gene Name | xiap birc4 |
| Organism | Xenopus laevis (African clawed frog) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amphibia Batrachia Anura Pipoidea Pipidae Xenopodinae Xenopus Xenopus Xenopus laevis (African clawed frog) |
| Enzyme Sequence | MEPQIVKFVFKEEMTCQCPKMSDSACDVDTDQNYFEEEVRLASFANFSSSYPVSAPALARAGFYYTGDGDRVKCFSCMAMVEDWQHGDTAIGKHRKISPNCKFINGFNNFRSDCIQTQAPVMQNSHANGFPNSAEDPGEKSSSEIMADYMLRTGRVVDMSKPKYPRHMAMCSEEARLQTFQNWPGYSPLMPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDRAWTEHKKHFPECYFVLGRDVGNVTRDASVQGSTYMNSYNARLETFSSWPFPIDKETLAKAGFYRIGDEDATKCFSCGGMLNCWAANDDPWEEHAKAYPGCQFLIEEKGQQFINNAQLQRPILHKANSGEASPALPKDTSFLKNPLVIYAQQMGFPLEEIKKVMGQKLKTTGNNYTCVEEFVSDLLCAQSETIADKPMKREISIEEKLRQLEEEKVCKVCMDRRITIVFIPCGHLVACAVCADVLDKCPICCTIIERRQKIFMS |
| Enzyme Length | 488 |
| Uniprot Accession Number | A5D8Q0 |
| 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; |
| DNA Binding | |
| EC Number | 2.3.2.27 |
| Enzyme Function | FUNCTION: Multi-functional protein which regulates not only caspases and apoptosis, but also acts as an E3 ubiquitin-protein ligase mediating ubiquitination and subsequent proteasomal degradation of its target proteins. Acts as a direct caspase inhibitor. A key apoptotic suppressor in eggs. Acts as a positive regulator of Wnt signaling. {ECO:0000269|PubMed:15853809, ECO:0000269|PubMed:22304967}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Chain (1); Erroneous initiation (1); Metal binding (4); Repeat (3); Sequence conflict (1); Zinc finger (1) |
| Keywords | Alternative splicing;Apoptosis;Cytoplasm;Developmental protein;Metal-binding;Protease inhibitor;Repeat;Thiol protease inhibitor;Transferase;Ubl conjugation pathway;Wnt signaling pathway;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P98170}. |
| Modified Residue | |
| Post Translational Modification | PTM: Degraded in a 2-step mechanism; a caspase-independent first step and a caspase-dependent second step (PubMed:15853809). Stabilized indirectly by MAPK, which acts to delay caspase activation, rather than directly phosphorylating xiap (PubMed:15853809). {ECO:0000269|PubMed:15853809}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,129 |
| Kinetics | |
| Metal Binding | METAL 298; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 301; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 318; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 325; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029" |
| Rhea ID | |
| Cross Reference Brenda |