ID A0A3B3U508_9TELE Unreviewed; 331 AA.
AC A0A3B3U508;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Caspase-6 {ECO:0000256|ARBA:ARBA00029534};
DE EC=3.4.22.59 {ECO:0000256|ARBA:ARBA00029486};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000008490.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000008490.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A3B3U508; -.
DR Ensembl; ENSPLAT00000002804.1; ENSPLAP00000008490.1; ENSPLAG00000011197.1.
DR GeneTree; ENSGT00940000155140; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
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 Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 97..211
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 235..329
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
SQ SEQUENCE 331 AA; 37855 MW; F437AF82B27B69A6 CRC64;
MYNELNTPRD RLKPRRLAAD LQWFCSTDWE ASQQGVTGAE ACRLFFLFLF CIWSVINLEM
SFHSAATTEN LAETDGFYRS SPVVLDPAEE YTMTRKRRGV ALIFNQESFF WRLGLNPRSG
TNADRHNLER RFVFLKQEEP VAQVQQLYLN DHSDADCFLL AFLSHGENDH VYAYDGKINI
QDITAMFRGN KCRSLIGKPK IFIVQACRGE QHDDPVTPCD AVDNVTNETV VDACAIHTLP
AGADFIMCYS VAEGFYSHRE TINGSWYIQD LCELLRKYGS SLEFTELLTL VNRKVSMREV
GNCKDLSAIG KKQVPCFASM LTKKLYFRPK K
//
