ID   S5CK83_CYPCA            Unreviewed;       475 AA.
AC   S5CK83;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Caspase-8 {ECO:0000313|EMBL:AGQ03809.1};
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962 {ECO:0000313|EMBL:AGQ03809.1};
RN   [1] {ECO:0000313|EMBL:AGQ03809.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23954723; DOI=10.1016/j.dci.2013.08.004;
RA   Gao D., Xu Z., Zhang X., Zhu C., Wang Y., Min W.;
RT   "Cadmium triggers kidney cell apoptosis of purse red common carp (Cyprinus
RT   carpio) without caspase-8 activation.";
RL   Dev. Comp. Immunol. 41:728-737(2013).
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
CC       {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR   EMBL; KC822471; AGQ03809.1; -; mRNA.
DR   AlphaFoldDB; S5CK83; -.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR   CDD; cd00032; CASc; 1.
DR   CDD; cd08792; DED_Caspase_8_10_r1; 1.
DR   CDD; cd08334; DED_Caspase_8_10_r2; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   Gene3D; 1.10.533.10; Death Domain, Fas; 2.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR033139; Caspase_cys_AS.
DR   InterPro; IPR011029; DEATH-like_dom_sf.
DR   InterPro; IPR001875; DED_dom.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   InterPro; IPR015917; Pept_C14A.
DR   PANTHER; PTHR48169:SF5; CASPASE 10; 1.
DR   PANTHER; PTHR48169; DED DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01335; DED; 2.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   SMART; SM00031; DED; 2.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   SUPFAM; SSF47986; DEATH domain; 2.
DR   PROSITE; PS01122; CASPASE_CYS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
DR   PROSITE; PS50168; DED; 2.
PE   2: Evidence at transcript level;
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          6..77
FT                   /note="DED"
FT                   /evidence="ECO:0000259|PROSITE:PS50168"
FT   DOMAIN          98..173
FT                   /note="DED"
FT                   /evidence="ECO:0000259|PROSITE:PS50168"
FT   DOMAIN          237..360
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   DOMAIN          387..474
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
SQ   SEQUENCE   475 AA;  54658 MW;  5B9F585FBC76CEA7 CRC64;
     MDLKKLHEID EDLTSSEVAQ LKFLCMDIIP KKRLETVTDA KELFLRLEEQ ALLDDGLLVP
     ELLITIGRLN LLGILNMSKE DVERKLLQRD MSSMGISAYR KMLFRISEDM TEENLRAVKF
     LVELPRSKLG PSATFLDVMI EMEKLQKLGE DNLDELYNVL DKCDKRLACR IEEYRAREQG
     GRLPLREVFG SAQVSLPAES VQRYQMETGN GWRRDSLITD SDTEPRPEEY YNMTQRPLGY
     CLIVNNYNFK ESSSLKNRTG THKDRDDLSR VFRRMHFEVV VQDDLTASDM KEMIKEFAKK
     DHTRMGAFVC CVLSHGEKGT VLGVDGKGVE IRELTMPIAE CQTLASKPKL FFIQACQGSV
     GQNGVWTADS PENATEEEYE ADAYNPAYRF IPIEADMLIG MATVEHYQSF RHTREGSIYI
     QELCNQLENL CPRREDILSI LTKVNHEVSL KWLMGHKQMP EPRYTLTKKL VLPMD
//