Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663  62 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 141
Cdd:cd08333    1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLTSHLGVS 80

                 ..
gi 119590663 142 KE 143
Cdd:cd08333   81 RE 82

Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663   303 YQMKSKPRGYCLIINNHNFakarekvpklHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCT-VEQIYEILKIYQLMDH 381
Cdd:smart00115   1 YKMNSKPRGLALIINNENF----------HSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTaEEMLEELKEFAAMPEH 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663   382 SNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPyLEMD 461
Cdd:smart00115  71 SDSDSFVCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPE-SEGE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663   462 LSSPQTryIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERcPRGDDILTILTEVNYEVSNKDDKKNMGKQMP 541
Cdd:smart00115 150 DDAIYK--IPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEY-ARSLDLLDILTEVNRKVADKFESVNAKKQMP 226

                          250
                   ....*....|....
gi 119590663   542 QPTF-TLRKKLVFP 554
Cdd:smart00115 227 TIESmTLTKKLYFF 240

Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663  62 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 141
Cdd:cd08333    1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLTSHLGVS 80

                 ..
gi 119590663 142 KE 143
Cdd:cd08333   81 RE 82

Death effector domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663   62 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 141
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80

                  ..
gi 119590663  142 KE 143
Cdd:pfam01335  81 RE 82

Death effector domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663  193 RQVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKS-LLKIINDYE 271
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQdLLKKIEKYE 80

                  .
gi 119590663  272 E 272
Cdd:pfam01335  81 R 81

Caspase, interleukin-1 beta converting enzyme (ICE) homologues; Cysteine aspartases that mediate programmed cell death (apoptosis). Caspases are synthesised as zymogens and activated by proteolysis of the peptide backbone adjacent to an aspartate. The resulting two subunits associate to form an (alpha)2(beta)2-tetramer which is the active enzyme. Activation of caspases can be mediated by other caspase homologues.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663   303 YQMKSKPRGYCLIINNHNFakarekvpklHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCT-VEQIYEILKIYQLMDH 381
Cdd:smart00115   1 YKMNSKPRGLALIINNENF----------HSLPRRNGTDVDAENLTELFQSLGYEVQVKNNLTaEEMLEELKEFAAMPEH 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663   382 SNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPyLEMD 461
Cdd:smart00115  71 SDSDSFVCVLLSHGEEGGIYGTDGDPLPLDEIFSLFNGDNCPSLAGKPKLFFIQACRGDELDGGVPVEDSVADPE-SEGE 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663   462 LSSPQTryIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERcPRGDDILTILTEVNYEVSNKDDKKNMGKQMP 541
Cdd:smart00115 150 DDAIYK--IPVEADFLAAYSTTPGYVSWRNPTRGSWFIQSLCQVLKEY-ARSLDLLDILTEVNRKVADKFESVNAKKQMP 226

                          250
                   ....*....|....
gi 119590663   542 QPTF-TLRKKLVFP 554
Cdd:smart00115 227 TIESmTLTKKLYFF 240

Death effector domain, repeat 1, of Caspase-8; Death effector domain (DED) found in caspase-8 (CASP8, FLICE), repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-10, and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 also plays many important non-apoptotic functions including roles in embryonic development, cell adhesion and motility, immune cell proliferation and differentiation, T-cell activation, and NFkappaB signaling. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663  62 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 141
Cdd:cd08333    1 FRKLLFAISEELDREDLAALKFLSLDHIPRRKQENIKDALALFLALQEKGMLEEGNLSFLKELLFRIGRIDLLTSHLGVS 80

                 ..
gi 119590663 142 KE 143
Cdd:cd08333   81 RE 82

Death effector domain, repeat 2, of initator caspase-like proteins; Death Effector Domain (DED), second repeat, found in initator caspase-like proteins like caspase-8, -10 and c-FLIP. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of DISC. All members contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119590663 194 QVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQI-NKSLLKIINDY 270
Cdd:cd08775    4 RVMLYQVSEELSRSELRSLKFLLQEEISSCKLDDDMNFLDIVIEMENRVLLGPGKVDILKRMLRQLrRKDLLKQINDY 81

Death effector domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663   62 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTR 141
Cdd:pfam01335   1 FRKLLLEISEELTEEELESLKFLCKDHIPKRKLEKIKSALDLFIELEKQGLLSEDNLDLLEELLRRIGRQDLLKKIEKYE 80

                  ..
gi 119590663  142 KE 143
Cdd:pfam01335  81 RE 82

Death effector domain, repeat 1, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119590663  62 FSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLL 134
Cdd:cd08792    1 FRKLLLDIDEELDSDDLDALKFLCTDVLPRNKLEKVESGLDLFSRLEEQGLLSEEDPFLLAELLYRIGRKDLL 73

Death effector domain;

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119590663   194 QVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDdMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDY 270
Cdd:smart00031   4 RVLLLLISEELDSEELEVLLFLCKDLIPKRKLEI-KTFLDLFSALEEQGLLSEDNLSLLAELLYRLRRLDLLRRLFG 79

Death Effector Domain: a protein-protein interaction domain; Death Effector Domains comprise a subfamily of the Death Domain (DD) superfamily. DED-containing proteins include Fas-Associated via Death Domain (FADD), Astrocyte phosphoprotein PEA-15, the initiator caspases (caspase-8 and -10), and FLICE-inhibitory protein (FLIP), among others. These proteins are prominent components of the programmed cell death (apoptosis) pathway. Some members also have non-apoptotic functions such as regulation of insulin signaling (DEDD and PEA15) and cell cycle progression (DEDD). DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119590663  66 LYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLIT 136
Cdd:cd00045    5 LLKISDELTSEELRSLKFLCKDVIPAGKLERISRGRDLFTELEKQGKISPGNLSLLEELLRSIGRRDLLEK 75

Death effector domain, repeat 2, of initator caspases 8 and 10; Death Effector Domain (DED) found in caspase-8 and caspase-10, repeat 2. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-8 and -10 are the initiators of death receptor mediated apoptosis, and they play partially redundant roles. Together with FADD and the pseudo-caspase c-FLIP, they form the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. Caspase-8 and -10 also play important functions in cell adhesion and motility. They contain two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663  56 PFKKMdfsrnLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELL 125
Cdd:cd08334    3 PYRVL-----LYEISEDLTSEDLKSLKFLLSSKLPRRKLEKNKSALDVFVEMEKRGLLSEDNLDELKKIL 67

Death effector domain, repeat 1, of Caspase-10; Death effector domain (DED) found in caspase-10, repeat 1. Caspases are aspartate-specific cysteine proteases with functions in apoptosis and immune signaling. Initiator caspases are the first to be activated following death- or inflammation-inducing signals. Caspase-10 is an initiator of death receptor mediated apoptosis. Together with FADD, caspase-8 and the pseudo-caspase c-FLIP, it forms the death-inducing signaling complex (DISC), whose formation is triggered by the activation of type 1 tumor necrosis factor (TNF) receptors such as Fas, TNF receptor 1, and TRAIL receptor. It contains two N-terminal DED domains and a C-terminal caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119590663  60 MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLL 134
Cdd:cd08341    1 IKFNQQLLIIDENLGVEDIEALKFLCSDLLSNKKLEKVESGHDLFQHLMAEDLLNEEDYFLLAELLYIIRHHKLL 75

Death Effector Domain of Astrocyte phosphoprotein PEA-15; Death Effector Domain (DED) similar to that found in PEA-15 (Astrocyte phosphoprotein PEA-15). PEA-15 is a multifunctional phosphoprotein that modulates signaling pathways, like the ERK MAP kinase cascade by binding to ERK and changing its subcellular localization. It has been implicated in apoptosis, cell proliferation, and glucose metabolism. It does not possess enzymatic activity and mainly acts as an adaptor protein. PEA-15 contains an N-terminal DED domain and a C-terminal disordered region. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663  61 DFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNT 140
Cdd:cd08338    2 EYGSLLQDLTENITSEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLEKHNKLDQDNLSYIEHVFEISRRPDLLTMVVDY 81

                 ...
gi 119590663 141 RKE 143
Cdd:cd08338   82 RTK 84

Death Effector Domain, repeat 1, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 1, similar to that found in FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590663  66 LYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALmlfqrlqeKRMLEESNLSF--LKELLFRINRLDLLITYLNTRKE 143
Cdd:cd08337    6 LHQVEEELDTDEDEMLLFLCRDAAPDCTTAQLRDAL--------CALNERGKLTLagLAELLYRVKRFDLLKRILHLSKE 77

                 ...
gi 119590663 144 EME 146
Cdd:cd08337   78 TVE 80

Death Effector Domain of DEDD; Death Effector Domain (DED) found in DEDD. DEDD has been shown to block mitotic progression by inhibiting Cdk1 and to be involved in regulating the insulin signaling cascade. DEDD can bind to itself, to DEDD2, and to the two tandem DED-containing caspases, caspase-8 and -10. In general, DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119590663  69 IGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLL 134
Cdd:cd08790   12 VGDQLTHRDVRVLSFLFVDVIDEYERGRIRDGRDFLLALEKQGRCDETNFRQVLQLLRIITRHDLL 77

Death Effector Domain found in Fas-Associated via Death Domain; Death Effector Domain (DED) found in Fas-Associated via Death Domain (FADD). DEDs comprise a subfamily of the Death Domain (DD) superfamily. FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor and its DED recruits the initiator caspases 8 and 10 to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119590663 194 QVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKS-LLKIINDYE 271
Cdd:cd08336    4 KVLLLEISKSLSDEELESLKFLCKDHIGKRKLEEVQSGLDLFEALEERDKLSPENTAFLRELLKSIGREdLIRKLEEFE 82

Death Effector Domain, repeat 2, of cellular FLICE-Inhibitory Protein; Death Effector Domain (DED), repeat 2, similar to that found in cellular FLICE-inhibitory protein (c-FLIP/CASH, also known as Casper/iFLICE/FLAME-1/CLARP/MRIT/usurpin). c-FLIP is a catalytically inactive homolog of the initator procaspases-8 and -10. It negatively influences apoptotic signaling by interfering with the efficient formation of the Death Inducing Signalling Complex (DISC). At low levels, c-FLIP has been shown to enhance apoptotic signaling by allosterically activating caspase-8. As a modulator of the initiator caspases, c-FLIP regulates life and death in various types of cells and tissues. All members contain two N-terminal DEDs and a C-terminal pseudo-caspase domain. DEDs comprise a subfamily of the Death Domain (DD) superfamily. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and CARD (Caspase activation and recruitment domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119590663 194 QVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDIL 252
Cdd:cd08340    4 RVLMVCVSEELDKSDLRSLIFLLKDLNPSGSTAKSKSFLDLVVELEKLNLVSPSSVDLL 62