ID A0A091QJI4_HALAL Unreviewed; 294 AA.
AC A0A091QJI4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Caspase-6 {ECO:0000256|ARBA:ARBA00029534};
DE EC=3.4.22.59 {ECO:0000256|ARBA:ARBA00029486};
DE Flags: Fragment;
GN ORFNames=N329_12885 {ECO:0000313|EMBL:KFQ09639.1};
OS Haliaeetus albicilla (White-tailed sea-eagle) (Falco albicilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Accipitridae;
OC Accipitrinae; Haliaeetus.
OX NCBI_TaxID=8969 {ECO:0000313|EMBL:KFQ09639.1, ECO:0000313|Proteomes:UP000054379};
RN [1] {ECO:0000313|EMBL:KFQ09639.1, ECO:0000313|Proteomes:UP000054379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N329 {ECO:0000313|EMBL:KFQ09639.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KK663404; KFQ09639.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QJI4; -.
DR MEROPS; C14.005; -.
DR Proteomes; UP000054379; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000054379};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT DOMAIN 45..169
FT /note="Caspase family p20"
FT /evidence="ECO:0000259|PROSITE:PS50208"
FT DOMAIN 197..291
FT /note="Caspase family p10"
FT /evidence="ECO:0000259|PROSITE:PS50207"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ09639.1"
FT NON_TER 294
FT /evidence="ECO:0000313|EMBL:KFQ09639.1"
SQ SEQUENCE 294 AA; 33444 MW; A89C4A4914506870 CRC64;
AGHIQLDSRP TLTTTDGNQN ITEVDALDTR QTLDPAVQYK MNHQRRGIAL IFNHEHFFWH
LRLPDRRGTL ADRNNLKCTL TDLGFEVRHF DDLKAEDVLR KIYEASQDDH SNADCFLCVF
LSHGENDHVY AYDAQIKIET ITDMFRGDKC QSLVGKPKIF IIQACRGDKH DDPVIARDST
DGSDESIVND TEVDAAGVYT LPAGADFIMC YSVAQGYFSH RETVNGSWYI QDLCEALKKH
GSSLEFTELL TVVNRKVSHR RVDMCRDINA IGKKQIPCFA SMLTKKLYFH PKSK
//
