ID I6XSF1_9SALA Unreviewed; 295 AA.
AC I6XSF1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Caspase-3 {ECO:0000256|ARBA:ARBA00039708};
DE EC=3.4.22.56 {ECO:0000256|ARBA:ARBA00038900};
OS Cynops orientalis (oriental fire-bellied newt).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Caudata; Salamandroidea; Salamandridae; Pleurodelinae; Cynops.
OX NCBI_TaxID=137245 {ECO:0000313|EMBL:AFN55260.1};
RN [1] {ECO:0000313|EMBL:AFN55260.1}
RP NUCLEOTIDE SEQUENCE.
RA Wang D.-H., Yang W.-X.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFN55260.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=22768170; DOI=10.1371/journal.pone.0039920;
RA Wang D.H., Hu J.R., Wang L.Y., Hu Y.J., Tan F.Q., Zhou H., Shao J.Z.,
RA Yang W.X.;
RT "The Apoptotic Function Analysis of p53, Apaf1, Caspase3 and Caspase7
RT during the Spermatogenesis of the Chinese Fire-Bellied Newt Cynops
RT orientalis.";
RL PLoS ONE 7:E39920-E39920(2012).
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; JQ320088; AFN55260.1; -; mRNA.
DR AlphaFoldDB; I6XSF1; -.
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 56..180
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 196..290
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 295 AA; 32817 MW; 0EA254C5CFE7EB04 CRC64;
MADTTDYVHS GGDAPDARVS SSKANTGKCS QSGQSMEVDA KPGEIHSFQY NMDFPEKSLC
YIINNKNFHP STGMGLRSGT DVDAANLRKC FLTLGFEVKV FNDQACKGIV DILKNVSQQD
HSKRSCFVCI LLSHGEDGTI FGTDDFIPLK NLTTLFRGDK CRTLVGKPKL FFIQACRGTE
LDGGIEADSG GDSSDDQQRI PVEADFLYAY STVPGYYSWR NTMNGSWFIQ SLCEMLKQYG
DTLEIMNLLT RVNRKVAYEF ESSSNIPNFD GKKQIPCIVS MLTKELYFSP KNHSL
//
