This domain is predicted to contain 6 alpha helices and to have the same fold as the Death domain SM00005. This similarity may mean that this is a protein-protein interaction domain.
The DAPIN (Domain in Apoptosis and INterferon response) domain is an 80-100- residue domain which is found in the N terminus of diverse vertebrate and vertebrate-specific viral proteins involved in apoptosis, cancer, inflammation, and immune response. The DAPIN domain can be found alone or in association with other domains [ (PUBMED:1166557) (PUBMED:11166558) (PUBMED:11250163) ] like CARD, LRR, SPRY, Caspase or Zinc finger B-box. It has been proposed that the DAPIN domain might have an adaptor function, coupling apoptosis and immune disorders [ (PUBMED:11166557) (PUBMED:11166558) (PUBMED:11250163) ]. It has been shown that the DAPIN domain is a protein-protein interaction domain capable of binding to other DAPIN domains [ (PUBMED:11166557) ].
Secondary structure predictions have identified the DAPIN domain as mostly alpha-helical and it has been suggested that it could belong to the DEATH- domain-fold superfamily, which includes the CARD, the DEATH domain (DD) and the DEATH effector domain (DED) [ (PUBMED:11166557) (PUBMED:11166558) (PUBMED:11250163) ].
The DAPIN domain has also been called pyrin domain, pyrin N-terminal homology domain (PYD) or PAAD (after the protein families pyrin, AIM, ASC death-domain- like) [ (PUBMED:11166558) (PUBMED:11250163) ].
Family alignment:
There are 4728 PYRIN domains in 4335 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing PYRIN domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with PYRIN domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing PYRIN domain in the selected taxonomic class.
Apoptotic molecular machinery: vastly increased complexity in vertebratesrevealed by genome comparisons.
Science. 2001; 291: 1279-84
Display abstract
A comparison of the proteins encoded in the recently (nearly) completed humangenome to those from the fly and nematode genomes reveals a major increase in thecomplexity of the apoptotic molecular machinery in vertebrates, in terms of both the number of proteins involved and their domain architecture. Several componentsof the apoptotic system are shared by humans and flies, to the exclusion ofnematodes, which seems to support the existence of a coelomate clade in animalevolution. A considerable repertoire of apoptotic protein domains was detected inActinomycetes and Cyanobacteria, which suggests a major contribution ofhorizontal gene transfer to the early evolution of apoptosis.
PAAD - a new protein domain associated with apoptosis, cancer and autoimmunediseases.
Trends Biochem Sci. 2001; 26: 85-7
Display abstract
A new protein domain was found in several proteins involved in apoptosis,inflammation, cancer and immune responses. Its location within these proteins andpredicted fold suggests that it functions as a protein-protein interactiondomain, possibly uniting different signaling pathways.
The DAPIN family: a novel domain links apoptotic and interferon responseproteins.
Trends Biochem Sci. 2001; 26: 83-5
Display abstract
We report the discovery of a protein domain, hereafter referred to as DAPIN, indiverse vertebrate and viral proteins that is associated with tumor biology,apoptosis and inflammation. Based on a secondary structure prediction, we suggestan all-alpha fold for DAPIN, which is also adopted by apoptotic protein domainsof the CARD, death domain and death effector domain type.
