CASP8_DROPS
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 03-AUG-2022, entry version 88.
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 {ECO:0000250|UniProtKB:Q8IRY7}; ORFNames=GA20387;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL32626.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
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., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., 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: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Effector of the programmed cell death (PCD) activators rpr,
CC grim and W. May play an apoptotic role in the germline as well as soma.
CC Role in immune response, required to resist Gram-negative bacterial
CC infections by regulating DptA. Fadd interacts with Dredd, Fadd promotes
CC cleavage of Dredd and is necessary and sufficient for enhancing Dredd-
CC induced apoptosis. {ECO:0000250|UniProtKB:Q8IRY7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for Asp at position P1 and has a preferred
CC cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala).;
CC EC=3.4.22.61;
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 15 kDa (caspase-8 subunit p15) and a
CC 10 kDa (caspase-8 subunit p10) subunit. Interacts with the N-terminus
CC of Fadd (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14790}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL32626.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH379063; EAL32626.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001355567.1; XM_001355531.2.
DR AlphaFoldDB; Q29IM7; -.
DR SMR; Q29IM7; -.
DR STRING; 7237.FBpp0273519; -.
DR MEROPS; C14.040; -.
DR EnsemblMetazoa; FBtr0275081; FBpp0273519; FBgn0080382.
DR GeneID; 4816060; -.
DR KEGG; dpo:Dpse_GA20387; -.
DR eggNOG; KOG3573; Eukaryota.
DR HOGENOM; CLU_036904_4_2_1; -.
DR InParanoid; Q29IM7; -.
DR OMA; HGFEGAV; -.
DR PhylomeDB; Q29IM7; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0080382; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0043067; P:regulation of programmed cell death; IEA:UniProt.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 3: Inferred from homology;
KW Apoptosis; Cytoplasm; Hydrolase; Immunity; Innate immunity; Protease;
KW Reference proteome; Thiol protease; Zymogen.
FT PROPEP 1..242
FT /evidence="ECO:0000250|UniProtKB:Q8IRY7"
FT /id="PRO_0000271414"
FT CHAIN 243..405
FT /note="Caspase-8 subunit p15"
FT /evidence="ECO:0000255"
FT /id="PRO_0000271415"
FT PROPEP 406..415
FT /evidence="ECO:0000250|UniProtKB:Q8IRY7"
FT /id="PRO_0000271416"
FT CHAIN 416..511
FT /note="Caspase-8 subunit p10"
FT /evidence="ECO:0000255"
FT /id="PRO_0000271417"
FT ACT_SITE 352
FT /evidence="ECO:0000250|UniProtKB:Q14790"
FT ACT_SITE 393
FT /evidence="ECO:0000250|UniProtKB:Q14790"
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
