ID I6UVT8_CIOSA Unreviewed; 678 AA.
AC I6UVT8;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Caspase-8 {ECO:0000313|EMBL:AFN02465.1};
GN Name=casp8 {ECO:0000313|EMBL:AFN02465.1};
OS Ciona savignyi (Pacific transparent sea squirt).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=51511 {ECO:0000313|EMBL:AFN02465.1};
RN [1] {ECO:0000313|EMBL:AFN02465.1}
RP NUCLEOTIDE SEQUENCE.
RA Sakamaki K., Satou Y., Nozaki M.;
RT "Identification of caspase-8 in the ascidian, Ciona savignyi.";
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ920435; AFN02465.1; -; mRNA.
DR AlphaFoldDB; I6UVT8; -.
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; cd00045; DED; 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:SF3; CASP8 AND FADD-LIKE APOPTOSIS REGULATOR A-RELATED; 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 6..82
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT DOMAIN 102..183
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT DOMAIN 415..562
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 581..664
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 281..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 77196 MW; B038A01E2898D3A2 CRC64;
MDSEHDFRLL LHELCEGLTD EHVAMVRYLC KDAIPQGKDL PTAIDFISYF ESKGWIQSGD
LGFLAEVLYR INRHDLLKKL PGVKNRRDYE DSYLEQGQNF TAFRVTCFML ADELTLSDLK
ILKNLCCAKM SQRNLRMSED VLTWLTCMEQ EDLVSPDDLE FIIKILQRLD NQKPYKLFQK
LRDGDNSIML PKHKQKALMS SLHSHVAGSS NLYMNNNFYQ SSSSKLEPQH HNNGNSRVFS
NETLHYNASS LYRNPSYTTA PKSYDTHHVA NERVFNVDDT TESFKEHQRN VPQNTSPVES
SGMSISTSQS RDTMRPNSLL PASENNVVNA QQQHMTHYTP TSMACSTEYS NTENTCSNPI
TEQTVEATME PTNAVYTDAC VRNDVKYELG QNKKNTISKD GNIEKITLDK YPMERRGYCL
VINNENFENN VNEDEVRRRL TMSTSSDYPV PNVGLKNRVG SRSDAESLKR LFISFGFTVD
VKYDLDQRQI EKVIQEYTKK DHSSKDCFVC VVMSHGLAGC VYGVDGLSVS TSKISKSFRP
DNCPSLIGKP KIFFFQACQG DRTMDGHSAP VDDVESDGLP GRQIVPSEAD FLIGHSTVPG
YLSYRSRTDG SWFISTLVES LDKYHKHEDL LSIMINVNQE MATKPFKQMP MPIATLRKKV
FFEKCLPQPI VSTEENEE
//