Protein: XIAP_MOUSE
Sequence: MTFNSFEGTRTFVLADTNKDEEFVEEFNRLKTFANFPSSSPVSASTLARAGFLYTGEGDTVQCFSCHAAIDRWQYGDSAVGRHRRISPNCRFINGFYFENGAAQSTNPGIQNGQYKSENCVGNRNPFAPDRPPETHADYLLRTGQVVDISDTIYPRNPAMCSEEARLKSFQNWPDYAHLTPRELASAGLYYTGADDQVQCFCCGGKLKNWEPCDRAWSEHRRHFPNCFFVLGRNVNVRSESGVSSDRNFPNSTNSPRNPAMAEYEARIVTFGTWTSSVNKEQLARAGFYALGEGDKVKCFHCGGGLTDWKPSEDPWEQHAKWYPGCKYLLDEKGQEYINNIHLTHSLEESLGRTAEKTPSLTKKIDDTIFQNPMVQEAIRMGFSFKDIKKTMEEKIQTSGSSYLSLEVLIADLVSAQKDNTEDESSQTSLQKDISTEEQLRRLQEEKLCKICMDRNIAIVFVPCGHLVTCKQCAEAVDKCPMCYTVITFKQKIFMS
What is the function of this protein?
Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, copper homeostasis, mitogenic kinase signaling, cell proliferation, as well as cell invasion and metastasis.  Acts as a direct caspase inhibitor.  Directly bind to the active site pocket of CASP3 and CASP7 and obstructs substrate entry.  Inactivates CASP9 by keeping it in s a monomeric, inactive state.  Inhibits apoptosis in intestinal crypt cells, its activity is mitigated via its interaction with SEPTIN4 isoform ARTS (PubMed:30389919).  Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and the target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin.  Ubiquitination of CCS leads to enhancement of its chaperone activity toward its physiologic target, SOD1, rather than proteasomal degradation.  Ubiquitination of MAP3K2/MEKK2 and AIFM1 does not lead to proteasomal degradation.  Plays a role in copper homeostasis by ubiquitinating COMMD1 and promoting its proteasomal degradation.  Can also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation.  Ubiquitinates and therefore mediates the proteosomal degradation of BCL2 in response to apoptosis (By similarity).  Regulates the BMP signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways leading to NF-kappa-B and JNK activation.  Acts as an important regulator of innate immune signaling via regulation of Nod-like receptors (NLRs).  Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner.  Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8.  Acts as a positive regulator of Wnt signaling and ubiquitinates TLE1, TLE2, TLE3, TLE4 and AES.  Ubiquitination of TLE3 results in inhibition of its interaction with TCF7L2/TCF4 thereby allowing efficient recruitment and binding of the transcriptional coactivator beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific transcriptional program.  Positive regulator of dermal wound repair, potentially via its interaction with SEPTIN4 (PubMed:23788729).
What are the official names of this protein?
E3 ubiquitin-protein ligase XIAP, Baculoviral IAP repeat-containing protein 4, IAP homolog A, Inhibitor of apoptosis protein 3, IAP-3, mIAP-3, mIAP3, RING-type E3 ubiquitin transferase XIAP, X-linked inhibitor of apoptosis protein, X-linked IAP.
What is the protein family that this protein belongs to?
Belongs to the IAP family.
What are the subcellular locations of this protein?
Cytoplasm. Nucleus. Note=TLE3 promotes its nuclear localization.