ID G3FGP3_BRALA Unreviewed; 544 AA.
AC G3FGP3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Caspase 1/2 {ECO:0000313|EMBL:AEO22139.1};
OS Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7740 {ECO:0000313|EMBL:AEO22139.1};
RN [1] {ECO:0000313|EMBL:AEO22139.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21933445; DOI=10.1186/1741-7007-9-60;
RA Xu L.Q.;
RT "The conservation and uniqueness of the caspase family in the basal
RT chordate, amphioxus.";
RL BMC Biol. 9:60-60(2011).
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR EMBL; JF717868; AEO22139.1; -; mRNA.
DR AlphaFoldDB; G3FGP3; -.
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 GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00032; CASc; 1.
DR CDD; cd01670; Death; 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; IPR000488; Death_domain.
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; PTHR10454; CASPASE; 1.
DR PANTHER; PTHR10454:SF220; DED DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SMART; SM00005; DEATH; 1.
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; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50168; DED; 1.
PE 2: Evidence at transcript level;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
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..84
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT DOMAIN 150..221
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT DOMAIN 291..414
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 452..541
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 90..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 544 AA; 61561 MW; 9FC00B54FFB01545 CRC64;
MAEKSRYDLY LEISQNLEDH ESKDLRTYVS SNKLLPARDL QRMNPQQIFV KLEQKGKLQT
GDLSLLVDLM TKINRDDFVK EAEKVAARER EALKRENKSD RGSDFSDETL AVPPAKRPRF
QQPPGQSAKQ TTTVDVSKHF DTVIKGVSHN WDGLAEELGF SDNDIKGLRH NQYLPDPDRK
CREVLHRWKN KHASKATLQV LQNALININE GETAEKLEGG AGSSSSGLGK DLVGDQKQIT
GNHVTGRELL ILKAGGDEGD GKIDVKVEKC DVGFWEKIMD EENPYKMGSK PRGYALVLNN
RNFTNLRDRK GAAVDLDNIN ALLEGLSFKT HVLPDKTAEE IKEEVRAFSQ RKDHRQMDCC
FVVLMSHGDE GVIYGTDDKT VKLDDIFAMF DDNKCPRLKG KPKLFFIQAC RGRNIYKGED
ETDSSAPDVQ VDLKSEMRRL LYPPKDEADG PAAGETSTRT DMFCGYATQL GYQAIRNTEH
GSWFIQAITK VFMKHAKNTR LVRMMEMVKR DVSKREASFG GKQEVDFLST LQKQKPLYFF
PGED
//
