PROSITE logo

PROSITE documentation PDOC50209

View entry in NiceDoc format
View entry in raw text format (no links)
{PDOC50209}
{PS50209; CARD}
{BEGIN}
*******************************************
* CARD caspase recruitment domain profile *
*******************************************

The apoptotic  signal  coming  from  ligand-induced  oligomerization  of death
receptors is  mediated  by a number of adaptor proteins containing specialized
interaction domains. Besides the caspase recruitment domain (CARD), this group
is formed  by  the  death domain (DD) (see <PDOC50017>) and the death effector
domain (DED) (see <PDOC50168>).

The CARD  domain was first described as a homology region in the N-terminus of
the death  adaptor  protein  RAIDD  and  the  caspases  ced-3  and  CASP2 [1].
Recently, it  was  shown  that  this  domain  is  widespread  among  apoptotic
signaling molecules  and  a  function in caspase-recruitment has been proposed
[2]. The CARD domain typically associates with other CARD-containing proteins,
forming either dimers or trimers [1,2,3,4]. It has been predicted that CARD is
related in  structure  and  sequence to both DD and DED domains, which work in
similar pathways and show similar interaction properties [2].

Important members of the CARD family occur in the following proteins:

 - RAIDD death adaptor protein [1].
 - Caspases: Ced-3, CASP1, CASP2, CASP4, CASP5, CASP9 and CASP12.
 - Inhibitor of apoptosis (IAP) proteins c-IAP1 and c-IAP2.
 - Caenorhabditis elegans cell death protein ced-4 and its mammalian homologue
   Apaf-1.
 - Equine herpes virus protein E10.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Hofmann K.; 
Kay.Hofmann@memorec.com -Last update: December 2001 / First entry. [ 1] Duan H., Dixit V.M. "RAIDD is a new 'death' adaptor molecule." Nature 385:86-89(1997). PubMed=8985253 [ 2] Hofmann K., Bucher P., Tschopp J. "The CARD domain: a new apoptotic signalling motif." Trends Biochem. Sci. 22:155-156(1997). PubMed=9175472 [ 3] Chinnaiyan A.M., Chaudhary D., O'Rourke K., Koonin E.V., Dixit V.M. "Role of CED-4 in the activation of CED-3." Nature 388:728-729(1997). PubMed=9285582; DOI=10.1038/41913 [ 4] Irmler M., Hofmann K., Vaux D., Tschopp J. "Direct physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4." FEBS Lett. 406:189-190(1997). PubMed=9109415 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}