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Database: UniProt
Entry: A0A3B4TKF3_SERDU
LinkDB: A0A3B4TKF3_SERDU
Original site: A0A3B4TKF3_SERDU 
ID   A0A3B4TKF3_SERDU        Unreviewed;       448 AA.
AC   A0A3B4TKF3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Caspase 8 {ECO:0000313|Ensembl:ENSSDUP00000006711.1};
OS   Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000006711.1, ECO:0000313|Proteomes:UP000261420};
RN   [1] {ECO:0000313|Ensembl:ENSSDUP00000006711.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
CC       {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR   AlphaFoldDB; A0A3B4TKF3; -.
DR   Ensembl; ENSSDUT00000006842.1; ENSSDUP00000006711.1; ENSSDUG00000004716.1.
DR   GeneTree; ENSGT00940000166591; -.
DR   Proteomes; UP000261420; Unplaced.
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   3: Inferred from homology;
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..77
FT                   /note="DED"
FT                   /evidence="ECO:0000259|PROSITE:PS50168"
FT   DOMAIN          93..170
FT                   /note="DED"
FT                   /evidence="ECO:0000259|PROSITE:PS50168"
FT   DOMAIN          204..328
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   DOMAIN          365..447
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
SQ   SEQUENCE   448 AA;  50910 MW;  884E507D3A5231D2 CRC64;
     MDRLKLSHID EELDSSEVAA LRFLCLGIVN RKRMEGIKDA KQLFLRLEEN GLLDNGVFLA
     ELLHTIRRAD LLSLLEADSR RPEETDARPT LSPYRVMLYG IYEDMTTENF EKMKFLLSSK
     LGRRQIEASN TALDLFVEME KADLLSPTKL NDMHAVLKEF DQQLALTVKR YMDEVRQQNP
     TRVPPPPHVS MVFQLCYYDL NHNPRGLCVV INNEKFLGEE LKDRGGTQED ANVLKSVFSR
     LGFTVVVHNN LTASRIRSEL RELSKNDFLA HDALVICVLS HGEKGCVFGT DEKKVGLREL
     TLPFTSKNAP TLARKPKLFF IQACQGDGYQ EGSVPCPPRP GEEEVRHSRL QEDAGPVRGE
     TVAWDADFLM GMATVPECKS FRNTSTGSIY IQELCRQLIR SADSVEMDDI LSVLTRVNRE
     VGKGEYLTHK QMPEPKYTLT KKLVLKYV
//
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