ID   CASP8_DROPS             Reviewed;         511 AA.
AC   Q29IM7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   05-MAY-2009, entry version 24.
DE   RecName: Full=Caspase-8;
DE            EC=3.4.22.61;
DE   AltName: Full=Death-related Ced-3/NEDD2-like protein;
DE   Contains:
DE     RecName: Full=Caspase-8 subunit p15;
DE   Contains:
DE     RecName: Full=Caspase-8 subunit p10;
DE   Flags: Precursor;
GN   Name=Dredd; ORFNames=GA20387;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P.,
RA   Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J.,
RA   van Batenburg M.F., Howells S.L., Scherer S.E., Sodergren E.,
RA   Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D.,
RA   Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D.,
RA   Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R.,
RA   Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L.,
RA   Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura:
RT   chromosomal, gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Effector of the programmed cell death (PCD) activators
CC       rpr, grim and W. May play an apoptotic role in the germline as
CC       well as soma. Role in immune response, required to resist Gram-
CC       negative bacterial infections by regulating Dpt. BG4 interacts
CC       with Dredd, BG4 promotes cleavage of Dredd and is necessary and
CC       sufficient for enhancing Dredd-induced apoptosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: Strict requirement for Asp at position P1 and
CC       has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-
CC       (Gly/Ser/Ala).
CC   -!- SUBUNIT: Heterotetramer that consists of two anti-parallel
CC       arranged heterodimers, each one formed by a 15 kDa (caspase-8
CC       subunit p15) and a 10 kDa (caspase-8 subunit p10) subunit.
CC       Interacts with the N-terminus of Dredd (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL32626.1; Type=Erroneous gene model prediction;
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DR   EMBL; CH379063; EAL32626.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001355567.1; -.
DR   GeneID; 4816060; -.
DR   KEGG; dpo:Dpse_GA20387; -.
DR   FlyBase; FBgn0080382; Dpse\GA20387.
DR   OMA; Q29IM7; HIADILT.
DR   BRENDA; 3.4.22.61; 190795.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016505; F:apoptotic protease activator activity; ISS:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; ISS:UniProtKB.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR   GO; GO:0006955; P:immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR011600; Pept_C14_cat.
DR   InterPro; IPR001309; Pept_C14_ICE_p20.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR002398; Pept_C14_p45.
DR   InterPro; IPR015917; Pept_C14_p45_core.
DR   PANTHER; PTHR10454; Pept_C14_p45; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   3: Inferred from homology;
KW   Apoptosis; Complete proteome; Cytoplasm; Hydrolase; Immune response;
KW   Protease; Thiol protease; Zymogen.
FT   PROPEP        1    242       By similarity.
FT                                /FTId=PRO_0000271414.
FT   CHAIN       243    405       Caspase-8 subunit p15.
FT                                /FTId=PRO_0000271415.
FT   PROPEP      406    415       By similarity.
FT                                /FTId=PRO_0000271416.
FT   CHAIN       416    511       Caspase-8 subunit p10.
FT                                /FTId=PRO_0000271417.
FT   ACT_SITE    352    352       By similarity.
FT   ACT_SITE    393    393       By similarity.
SQ   SEQUENCE   511 AA;  57576 MW;  5DA4C77BB7E2C11C CRC64;
     MSGHNILTQL ESIDVLDLPY VERDLNFAQL VSLSFLLYGD EHSTATYILQ KLLVLARATA
     SDWPHSDILS QYAKSKPQTW RKYLVEALCI IGARQVLRKL GLCWQELRMH YLPHVGSIRV
     HIHPLLKSLY TICEELTLAQ RGRMVLDIKE KNSVGDPLRF YDAEYLEIFL LDWLTRRLIR
     LGDFNANGSD VQLLIEYFKF NDLHAQATLL VDTVNAYATS SCSPATPNVL LPMDGNGIAN
     ESSSPTAAAS RPRAKNALQL SRENAGIALI INQQEFYRDA NDDYKVYLPP IELPLRNGTD
     MDKQRLTNVF SMLGYKVEAH DNLDHLSMLH HIRQACKRSL LHESLVVCIL SHGFEDAVYG
     ANSVALRISD IENVLCSYEN LYEKPKLVVI QACQQEDKEN NALPYKINAS TKSPCQYLNM
     LRAMSTVPGF PALRHTQTGS WFIQSLCDAI VEHSNSDHIA DILTIVINNV ANKRGNKNET
     MVPWTGGALR QHVYFPRTSA TDKVVPDSPG L
//