ID A0A337S6U2_FELCA Unreviewed; 276 AA.
AC A0A337S6U2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Caspase-3 {ECO:0000256|ARBA:ARBA00039708};
DE EC=3.4.22.56 {ECO:0000256|ARBA:ARBA00038900};
GN Name=CASP3 {ECO:0000313|Ensembl:ENSFCAP00000042583.1,
GN ECO:0000313|VGNC:VGNC:60382};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000042583.1, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000042583.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000042583.1,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000042583.1, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000042583.1,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000042583.1}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000042583.1};
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AANG04002583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A337S6U2; -.
DR Ensembl; ENSFCAT00000062987.2; ENSFCAP00000042583.1; ENSFCAG00000025408.4.
DR VGNC; VGNC:60382; CASP3.
DR GeneTree; ENSGT00940000153232; -.
DR Proteomes; UP000011712; Chromosome B1.
DR Bgee; ENSFCAG00000025408; Expressed in embryonic head and 10 other cell types or tissues.
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:UP000011712};
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..243
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
SQ SEQUENCE 276 AA; 31143 MW; FE0A9463ED851522 CRC64;
MENSENSVDA KSIKNSETKI FHGSKSMDSG IYMDNSYKMD YPEMGLCIII NNKNFHESTG
MPSRSGTDVD AANLRETFTN LKYEVRNKND LTREQIVALL DSVSREDHSK RSSFICVLLS
HGDEGIIYGT NGPVDLKKLT GFFRGDYCRS LTGKPKLFII QACRGTELDC GIETDSGTED
DIACQKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC SMLRLYAHKL EFMHILTRVN
RKMRRQWRET GSEVRSAREG SSTSIAVLMS APGPIR
//
