ID A0A3Q3FRI0_9LABR Unreviewed; 540 AA.
AC A0A3Q3FRI0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Caspase-8-like {ECO:0000313|Ensembl:ENSLBEP00000022442.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000022442.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000022442.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; A0A3Q3FRI0; -.
DR STRING; 56723.ENSLBEP00000022442; -.
DR Ensembl; ENSLBET00000023622.1; ENSLBEP00000022442.1; ENSLBEG00000017240.1.
DR GeneTree; ENSGT00940000160994; -.
DR InParanoid; A0A3Q3FRI0; -.
DR OrthoDB; 2873736at2759; -.
DR Proteomes; UP000261660; Unplaced.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR016129; Caspase_his_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; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
DR PROSITE; PS50168; DED; 2.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 2..79
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT DOMAIN 90..156
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT DOMAIN 297..423
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 434..521
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 176..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 540 AA; 60552 MW; 05EB786751714A90 CRC64;
MDFQKLQLDV GKALSQEEVK ALAFLCTDLL GLKVTSVGSA SDLFSRMVEQ DLLSAEKPHL
LTELLLIIQR TRLIRDLRLT ESTTKNLISS YRKLLYNLSE DITDANLKDI KFLLKGQLSR
RQLEDNVTTL EVFLEMEHKD LINDTNLNLL EKLLQTCCPV LTEEINRYKE QQASLHSSHI
AQETGRPRSI SCPPEPNQNQ CLPFSHPERC RSTDFSDPPP LPESTMSPSN TSVDEYLSLS
LSRLSTTRSS SPSSNVGSDA SVISPSQLNE NSSQQQTAQT TNTNTEDLGS YPMTAAKRGL
CLIINNNNFS ESKQRLQMRE GTMVDEERLT KVFEWLAFHV VIERDCDRKK MLCLVQNLGK
EDHHDVDCLV CCVLSHGEQD GVYGVDGLTV TLNELKEPFN GSKCPSLTEK PKLFFIQACQ
GVSRQEPVYI ESDGHDSIPS EADFLLAMAT VPSYVSFRER SNGTWFIQAL CQNLIQMVPK
GLDLMSILTK VNADVSRKTD NTGQKKQMPQ PAFTLRKKVV FPIPKAPPPS LKSLINSHNK
//