ID CASP6_BOVIN Reviewed; 293 AA. AC Q3T0P5; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2005, sequence version 1. DT 16-JUN-2009, entry version 35. DE RecName: Full=Caspase-6; DE Short=CASP-6; DE EC=3.4.22.59; DE Contains: DE RecName: Full=Caspase-6 subunit p18; DE Contains: DE RecName: Full=Caspase-6 subunit p11; DE Flags: Precursor; GN Name=CASP6; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the activation cascade of caspases CC responsible for apoptosis execution. Cleaves poly(ADP-ribose) CC polymerase in vitro, as well as lamins. Overexpression promotes CC programmed cell death (By similarity). CC -!- CATALYTIC ACTIVITY: Strict requirement for Asp at position P1 and CC has a preferred cleavage sequence of Val-Glu-His-Asp-|-. CC -!- ENZYME REGULATION: Activation is suppressed by phosphorylation at CC Ser-257 (By similarity). CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel CC arranged heterodimers, each one formed by a 18 kDa (p18) and a 11 CC kDa (p11) subunit (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- PTM: Cleavages by caspase-3, caspase-8 or -10 generate the two CC active subunits (By similarity). CC -!- SIMILARITY: Belongs to the peptidase C14A family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC102309; AAI02310.1; -; mRNA. DR IPI; IPI00699138; -. DR RefSeq; NP_001030496.1; -. DR UniGene; Bt.48879; -. DR MEROPS; C14.005; -. DR Ensembl; ENSBTAG00000012537; Bos taurus. DR GeneID; 538409; -. DR KEGG; bta:538409; -. DR HOVERGEN; Q3T0P5; -. DR OMA; Q3T0P5; HERFFWH. DR BRENDA; 3.4.22.59; 251. 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:apoptosis; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR InterPro; IPR015469; Caspase_6. DR InterPro; IPR011600; Pept_C14_cat. DR InterPro; IPR001309; Pept_C14_ICE_p20. DR InterPro; IPR016129; Pept_C14_ICE_p20_AS. DR InterPro; IPR002138; Pept_C14_p10. DR InterPro; IPR002398; Pept_C14_p45. DR InterPro; IPR015917; Pept_C14_p45_core. DR PANTHER; PTHR10454:SF29; Casp6; 1. DR PANTHER; PTHR10454; Pept_C14_p45; 1. DR Pfam; PF00656; Peptidase_C14; 1. DR PRINTS; PR00376; IL1BCENZYME. DR SMART; SM00115; CASc; 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; Cytoplasm; Hydrolase; Phosphoprotein; Protease; KW Thiol protease; Zymogen. FT PROPEP 1 23 By similarity. FT /FTId=PRO_0000282876. FT CHAIN 24 179 Caspase-6 subunit p18. FT /FTId=PRO_0000282877. FT PROPEP 180 193 By similarity. FT /FTId=PRO_0000282878. FT CHAIN 194 293 Caspase-6 subunit p11. FT /FTId=PRO_0000282879. FT ACT_SITE 121 121 By similarity. FT ACT_SITE 163 163 By similarity. FT MOD_RES 257 257 Phosphoserine (By similarity). SQ SEQUENCE 293 AA; 33350 MW; AC47609E52B0F00F CRC64; MSSEPPPRRA RGPGEEQNMT EIDAFPRREI FDPTEKYKMD HKRRGIALIF NHERFFWHLT LPNRPGTSAD RDNLRRRFSD LGFEVKCFDD LRAEELLLKI HEASTASHVD ADCFLCVFLS HGEGNHIYAY DAKIEIQTLT GLFKGDKCQS LVGKPKIFII QACRGSQHDV PVIPLDVVDH RTDTPDANLT QVDAASVYTL PAGADFLMCY SVAEGYYSHR ETVNGSWYIQ DLCEMLGKFG SSLEFTELLT LVNRKVSQRR VDFCRDPNAI GKKQVPCFAS MLTKKLHFSP KSK //