| IED ID | IndEnz0002013034 |
| Enzyme Type ID | protease013034 |
| 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 |
| Gene Name | xiap birc4 |
| Organism | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| 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 Silurana Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) |
| Enzyme Sequence | MEPQLAEFVLKEEMTCQCPKMSDGAYDMDVDQNYFEEEVRLASFANFPSSYPVSAPALARAGFYYTGDGDRVKCFSCLAMVEGWQHGDTAIGKHRKISPNCKFINGFNNLRSDCILTQVPVMQNGFQNSAEDLAERSSSEIMADYLLRTGRVVDMSTPKYPRHMEMCSEEARLQTFQNWPAYSPLTPKELANAGLFYTGINDQVKCFCCGGKLMNWEPSDKAWTEHKKHFPECYFVLGRDVGNVATEANTHGGRRRGSELACPAMNDYNARLETFSSWSFPIDKETLAKAGFYSIGDGDATKCFHCGGVLNCWSATDDPWEEHAKAYPGCKFLIDEKGQHFINHAQLKRPILHKANSADASPALPKDSNLLKSPLVTDAQQMGFPLEEIKKVMGQKLKTTGKNYTCVEEFVSDLCAQKETVLEKPKEIEISLEEKLRQLEEEKICKVCMDRRISIVFIPCGHLVACAVCADVLDKCPICCTIVERRQKIFMS |
| Enzyme Length | 492 |
| Uniprot Accession Number | Q5BKL8 |
| 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:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Metal binding (4); Repeat (3); Zinc finger (1) |
| Keywords | Apoptosis;Cytoplasm;Developmental protein;Metal-binding;Protease inhibitor;Reference proteome;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. Stabilized indirectly by MAPK, which acts to delay caspase activation, rather than directly phosphorylating xiap. {ECO:0000250|UniProtKB:A5D8Q0}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 55,292 |
| Kinetics | |
| Metal Binding | METAL 303; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 306; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 323; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029"; METAL 330; /note="Zinc"; /evidence="ECO:0000250|UniProtKB:O15392, ECO:0000255|PROSITE-ProRule:PRU00029" |
| Rhea ID | |
| Cross Reference Brenda |