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Database: UniProt
Entry: A0A1S2ZDG7_ERIEU
LinkDB: A0A1S2ZDG7_ERIEU
Original site: A0A1S2ZDG7_ERIEU 
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
//
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