ID W5UT65_ICTPU Unreviewed; 525 AA.
AC W5UT65;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Caspase-8 {ECO:0000313|EMBL:AHH42833.1};
GN Name=Casp8 {ECO:0000313|EMBL:AHH42833.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:AHH42833.1};
RN [1] {ECO:0000313|EMBL:AHH42833.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mixed {ECO:0000313|EMBL:AHH42833.1};
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR EMBL; JT418755; AHH42833.1; -; mRNA.
DR AlphaFoldDB; W5UT65; -.
DR MEROPS; C14.009; -.
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; 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 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 5..82
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT DOMAIN 93..156
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT DOMAIN 277..402
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 429..516
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 174..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 525 AA; 59597 MW; 55E3C25EA5D15C9A CRC64;
MEDQEFRKLL VQVHNSLSQN EMLELVFLCS DILKKDLSDV VTARDLFSLL QKRDLLSSDD
SSLLVELLKI IKRDQLIRDL QLNPQLSRSR VSPFRRMLFE LSENISDDDL RNIKFLLNNT
LPRRKLQQNV TVLQLFLEME KRGYMSANNL GTLESITEPV CPSLKKIISL YQKENGSSVP
EEMKGRDKSD SQDTSVTTRP DPPEDTAAYH QEEPPSYLSH PLCTEEHSSG NAVQEQVAHL
RLSETRNLAE GDRNLSFPEP NQNNTPKLEQ YDMSGDWRGF ALIINNYDFS NCQELKNREG
TDIDEKSLVA VLRWLGFEIV KRQDCNRESM LEALDELRRR DHTQADCVVC CVLTHGCEGG
VQGVDGKTVL LRELMELLDG IHCPSLQQKP KLFFIQACQG VHEQQVVFLQ SDGPNNTSDV
EFFCDAEVPR ESIPAGADYL VAMATVSGCV SFREKSKGSW FIQSLCKNLE QLVPSGIDLL
SILTKVNNDM SKKADRTGTR KQMSKPEFTL TKRIVFPIPK TPMPP
//
