ID A0A3B4YPT4_SERLL Unreviewed; 437 AA.
AC A0A3B4YPT4;
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 2 {ECO:0000313|Ensembl:ENSSLDP00000030281.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000030281.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000030281.1}
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; A0A3B4YPT4; -.
DR STRING; 1841481.ENSSLDP00000030281; -.
DR Ensembl; ENSSLDT00000031157.1; ENSSLDP00000030281.1; ENSSLDG00000023329.1.
DR GeneTree; ENSGT00940000156657; -.
DR Proteomes; UP000261360; Unplaced.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00032; CASc; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR Gene3D; 3.30.70.1470; Caspase-like; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR InterPro; IPR001315; CARD.
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; IPR011600; Pept_C14_caspase.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR47901:SF7; CASPASE 2; 1.
DR PANTHER; PTHR47901; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 18; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PIRSF; PIRSF038001; Caspase_ICE; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00114; CARD; 1.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 6..96
FT /note="CARD"
FT /evidence="ECO:0000259|PROSITE:PS50209"
FT DOMAIN 166..295
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 338..431
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 311..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 437 AA; 49317 MW; BAB7824C87B52D81 CRC64;
MLECGMLDRD RQTLRRRSAV LCKQLVVDEM LIQSLQADDI LTESMAETIM AEQTSQKRSW
RLLLLLPKRG PRAFSSFCAA LQETEQQHLC DLLTQSLQKD DKETHVERSP LPLPTQEGIA
AKRARTHESM EFSLDADSPI NTPVLPCTPD FYLSHCQQSY RMNSSPRGFA LVISNVTFDT
CAAAADLDPR KGGEVDDEVL RKVFTELDYM VAVHRDLTAQ GMRSCIENFC RRQDHRTVDS
CVVCLLSHGV EGAVYGTDGE LLQLDWVFEA FDNAHCPLLQ NKPKMFFIQA CRGDEMDCGV
EQIDGPARTC SPSCEQRDAG REGQGDADSR QRGDLGRPRI KLPQRSDMIC GFASLKGTAA
MRNTKRGSWF IQELNTALRL HARDTHLADI LVQVNGRIKE REGYAPGTAH HRCKEMSEFT
SSLCKDLYLF PKYQPQY
//