ID A0A1S2ZDG7_ERIEU Unreviewed; 277 AA.
AC A0A1S2ZDG7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Caspase-3 {ECO:0000256|ARBA:ARBA00039708};
DE EC=3.4.22.56 {ECO:0000256|ARBA:ARBA00038900};
GN Name=LOC103108693 {ECO:0000313|RefSeq:XP_007517715.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007517715.1};
RN [1] {ECO:0000313|RefSeq:XP_007517715.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12)
CC subunit. Interacts with BIRC6/bruce. {ECO:0000256|ARBA:ARBA00038525}.
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 RefSeq; XP_007517715.1; XM_007517653.2.
DR AlphaFoldDB; A0A1S2ZDG7; -.
DR STRING; 9365.ENSEEUP00000008378; -.
DR GeneID; 103108693; -.
DR CTD; 836; -.
DR eggNOG; KOG3573; Eukaryota.
DR InParanoid; A0A1S2ZDG7; -.
DR OrthoDB; 2873736at2759; -.
DR Proteomes; UP000079721; Unplaced.
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 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 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000079721};
KW S-nitrosylation {ECO:0000256|ARBA:ARBA00022799};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 43..167
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 183..277
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 277 AA; 31493 MW; E9070C1B71D47BBC CRC64;
MENSENSVDS KSIKNSEMKN LHGSKSVDSG ISLDNSYKMD YPEMGLCIII NNKNFHKSTG
MSFRSGTDVD AASLRETFLN LNYEVRNKND LTREEIVELL YNVSKEDHSK RSSFVCILLS
HGEEGIIFGT NGPIDLKKLT GFFRGDYCRS LTGKPKLFII QACRGTELDS GIETDSSTED
DMACQKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC AMLKQYAHKL ELMHILTRVN
QKVATEFESY SLDCTFHAKK QIPCIVSMLT KELYFYH
//