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The inhibitor of apoptosis (IAP) proteins maintain a balance between cell proliferation and cell death by inhibiting caspase activity and facilitating immune responses. In this study, phylogenetic analysis revealed lineage-specific expansion and tandem duplication of IAPs in the Pacific oyster Crassostrea gigas. We then investigated a representative oyster-specific XIAP-like gene (CgIAP2) to understand how it regulates initiator caspase. Cloning of full-length CgIAP2 from oyster cDNA uncovered a deduced protein containing two BIR domains and a RING domain. Homolog comparison demonstrated that CgIAP2 clustered into the invertebrate branch. We found that CgIAP2 was likely involved in apoptosis inhibition and immune defense, based on high mRNA expression in the gills and labial palps, as well as increased mRNA expression after bacterial challenge. A yeast two-hybrid assay revealed that the BIR2 domain was necessary and sufficient to mediate interaction between CgIAP2 and Cgcaspase-2, providing direct evidence that CgIAP2 participates in apoptosis inhibition.
Pubmed ID: 25720977
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THIS RESOURCE IS NO LONGER IN SERVICE, documented on January 19, 2022. Command line version of multiple sequence alignment program Clustal for DNA or proteins. Alignment is progressive and considers sequence redundancy. No longer being maintained. Please consider using Clustal Omega instead which accepts nucleic acid or protein sequences in multiple sequence formats NBRF/PIR, EMBL/UniProt, Pearson (FASTA), GDE, ALN/ClustalW, GCG/MSF, RSF.
View all literature mentionsDatabase of protein families and domains that is based on the observation that, while there is a huge number of different proteins, most of them can be grouped, on the basis of similarities in their sequences, into a limited number of families. Proteins or protein domains belonging to a particular family generally share functional attributes and are derived from a common ancestor. It is complemented by ProRule, a collection of rules based on profiles and patterns, which increases the discriminatory power of profiles and patterns by providing additional information about functionally and/or structurally critical amino acids. ScanProsite finds matches of your protein sequences to PROSITE signatures. PROSITE currently contains patterns and profiles specific for more than a thousand protein families or domains. Each of these signatures comes with documentation providing background information on the structure and function of these proteins. The database is available via FTP.
View all literature mentionsWeb sevice of ClustalW provided by DNA data bank of Japan.
View all literature mentions