ID Q1KZF6_DICLA Unreviewed; 281 AA.
AC Q1KZF6;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 80.
DE RecName: Full=Caspase-3 {ECO:0000256|ARBA:ARBA00039708};
DE EC=3.4.22.56 {ECO:0000256|ARBA:ARBA00038900};
GN Name=CASP3 {ECO:0000313|EMBL:ABC70997.1};
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489 {ECO:0000313|EMBL:ABC70997.1};
RN [1] {ECO:0000313|EMBL:ABC70997.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=16780952; DOI=10.1016/j.molimm.2006.04.028;
RA Reis M.I., Nascimento D.S., do Vale A., Silva M.T., dos Santos N.M.;
RT "Molecular cloning and characterisation of sea bass (Dicentrarchus labrax
RT L.) caspase-3 gene.";
RL Mol. Immunol. 44:774-783(2007).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for an Asp residue at positions P1 and P4.
CC It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a
CC hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid
CC residue at P3, although Val or Ala are also accepted at this
CC position.; EC=3.4.22.56; Evidence={ECO:0000256|ARBA:ARBA00036189};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR EMBL; DQ345773; ABC70996.1; -; mRNA.
DR EMBL; DQ345774; ABC70997.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1KZF6; -.
DR MEROPS; C14.003; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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 InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
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:SF198; CASPASE-3; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; Caspase-like; 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 2: Evidence at transcript level;
KW Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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 50..174
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 187..281
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 31147 MW; 4AF5A597F4C0F79A CRC64;
MSLNGPGEDS TDARRGDGQE SEASFSASGP MDVDAKPNSR SFRYSLNYPS MGQCIIINNK
NFDRRTGMNQ RNGTDVDAGN AMKVFTKLGY KTKIYNDQTV EQMKQVLISV SKEDHSCNAS
FICVLLSHGD EGVFFGTDGS VELKYLTSLF RGNHCISLVG KPKLFFIQAC RGTDLDPGIE
TDSGEDGTTK IPVEADFLYA FSTAPGYYSW RNTTTGSWFI QSLCDLISKY GKELELQHIM
TRVNHKVAVE FESISNSPGF NAKKQIPCIV SMLTKEMYFS P
//
