ID F7I563_CALJA Unreviewed; 204 AA.
AC F7I563;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Caspase-6 {ECO:0000256|ARBA:ARBA00029534};
DE EC=3.4.22.59 {ECO:0000256|ARBA:ARBA00029486};
GN Name=CASP6 {ECO:0000313|Ensembl:ENSCJAP00000029764.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000029764.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000029764.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000029764.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for Asp at position P1 and has a preferred
CC cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59;
CC Evidence={ECO:0000256|ARBA:ARBA00029356};
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 18 kDa (Caspase-6 subunit p18) and a
CC 11 kDa (Caspase-6 subunit p11) subunit.
CC {ECO:0000256|ARBA:ARBA00029473}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family.
CC {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR AlphaFoldDB; F7I563; -.
DR STRING; 9483.ENSCJAP00000029764; -.
DR Ensembl; ENSCJAT00000031452.4; ENSCJAP00000029764.4; ENSCJAG00000016170.5.
DR GeneTree; ENSGT00940000155140; -.
DR InParanoid; F7I563; -.
DR Proteomes; UP000008225; Chromosome 3.
DR Bgee; ENSCJAG00000016170; Expressed in ovary and 6 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProt.
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:SF206; CASPASE-6; 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 Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 3..78
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 107..201
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
SQ SEQUENCE 204 AA; 22678 MW; 78F0B7A3066EFEAC CRC64;
MSTASGLREV RPAVSTSSHT DADCFMCVFL SHGEGNHIYA YDAKIEIQTL TGLFKGDKCR
SLVGKPKIFI IQACRGNQHD VPVIPLDVVD NQTDKLDTNV TEVDAASVYT LPAGADFLMC
YSVAEGYYSH RETINGSWYI QDLCEMLGKY GSSLEFTELL TLVNRKVSQR RVDFCKDPSA
IGKKQVPCFA SMLTKKLHFF PKSD
//