EC                Enzyme                                 

FLICE2, Mch4;
ICE-like apoptotic protease 4;
apoptotic protease Mch-4;
FAS-associated death domain protein interleukin-1beta-converting enzyme 2
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
BRITE hierarchy
Strict requirement for Asp at position P1 and has a preferred cleavage sequence of Leu-Gln-Thr-Asp!Gly
Caspase-10 is an initiator caspase, as are caspase-2 (EC, caspase-8 (EC and caspase-9 (EC [1]. Like caspase-8, caspase-10 contains two tandem death effector domains (DEDs) in its N-terminal prodomain, and these play a role in procaspase activation [1]. The enzyme has many overlapping substrates in common with caspase-8, such as RIP (the cleavage of which impairs NF-kappaB survival signalling and starts the cell-death process) and PAK2 (associated with some of the morphological features of apoptosis, such as cell rounding and apoptotic body formation) [2]. Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC, caspase-8 and caspase-10 at Lys-Gln-Thr-Asp! to yield the pro-apoptotic p15 fragment. The p15 fragment is N-myristoylated and enhances the release of cytochrome c from mitochondria (which, in turn, initiatiates the intrinsic apoptosis pathway). Bid can be further cleaved by caspase-10 and granzyme B but not by caspase-3 or caspase-8 at Ile-Glu-Thr-Asp! to yield a p13 fragment that is not N-myristoylated [2]. Belongs in peptidase family C14.
EC created 2007
K04400  caspase 10
HSA: 843(CASP10)
PTR: 459873(CASP10)
PPS: 100972863(CASP10)
GGO: 101131419(CASP10)
PON: 100174433(CASP10)
NLE: 100585413(CASP10)
MCC: 701295(CASP10)
MCF: 102144792(CASP10)
CSAB: 103217635(CASP10)
RRO: 104671862(CASP10)
RBB: 108532107(CASP10)
CJC: 100394139(CASP10)
SBQ: 101028043(CASP10)
HGL: 101712620(Casp10)
CCAN: 109688485(Casp10)
OCU: 100101580(CASP10)
TUP: 102496563(CASP10)
CFA: 488472(CASP10)
VVP: 112922875(CASP10)
AML: 100475128(CASP10)
UMR: 103659739(CASP10)
UAH: 113250594(CASP10)
ORO: 101366538(CASP10)
FCA: 101085995(CASP10)
PTG: 102962753(CASP10)
PPAD: 109260756(CASP10)
AJU: 106987987(CASP10)
BTA: 100848685
BOM: 102284480(CASP10)
BIU: 109575574
BBUB: 102394793
CHX: 102172107(CASP10)
OAS: 101103049(CASP10)
SSC: 100154896(CASP10)
CFR: 102514092(CASP10)
CDK: 105099180(CASP10)
BACU: 103001347(CASP10)
LVE: 103076785(CASP10)
OOR: 101282021(CASP10)
DLE: 111171725(CASP10)
PCAD: 102989304(CASP10)
ECB: 100068201(CASP10)
EPZ: 103566002(CASP10)
EAI: 106823486(CASP10)
MYB: 102249546 102253536(CASP10)
MYD: 102763065(CASP10)
MNA: 107533942(CASP10)
HAI: 109379185(CASP10)
DRO: 112308028(CASP10)
PALE: 102877929(CASP10)
RAY: 107503159(CASP10)
MJV: 108404750(CASP10)
LAV: 100663859
TMU: 101341837
MDO: 100016987(CASP10)
SHR: 100930260(CASP10)
PCW: 110197140(CASP10)
OAA: 100092695
GGA: 424081(CASP10)
MGP: 100550034(CASP10)
CJO: 107316521(CASP10)
NMEL: 110400691
APLA: 101799731
ACYG: 106040000(CASP10)
TGU: 100220453
LSR: 110484588
SCAN: 103814509(CASP10)
GFR: 102044879(CASP10)
FAB: 101815409(CASP10)
PHI: 102103849(CASP10)
PMAJ: 107207334(CASP10)
CCAE: 111931987(CASP10)
CCW: 104693775(CASP10)
FPG: 101918719(CASP10)
FCH: 102057122(CASP10)
CLV: 102085114(CASP10)
EGZ: 104130512(CASP10)
NNI: 104010195(CASP10)
ACUN: 113482525
PADL: 103923449(CASP10)
AAM: 106492410
ASN: 102380890(CASP10)
AMJ: 102573990(CASP10)
PSS: 102463731
CMY: 102931579(CASP10)
CPIC: 101941379(CASP10)
ACS: 100564281(casp10)
PVT: 110089021
PMUR: 107296977(CASP10) 107300634
TSR: 106547531(CASP10)
PMUA: 114584652
GJA: 107122423
XLA: 397820(casp10.S) 398762(casp10.L)
XTR: 548432(casp10)
SGH: 107560797
IPU: 108266930
PHYP: 113525919
AMEX: 103037118
TRU: 101061322
LCO: 104924422
ONL: 109194206
XCO: 114147142
PRET: 103459939
CVG: 107082055
NFU: 107389982
KMR: 108239714
ALIM: 106512902
POV: 109631024
LCF: 108881527
SDU: 111218362
SLAL: 111648895
BPEC: 110166585
ELS: 105024762
SFM: 108920617
PKI: 111859671
LCM: 102349989
RTP: 109929744
CRG: 105346084
ADF: 107335801
AMIL: 114951335
 » show all
1  [PMID:11104820]
Chang HY, Yang X.
Proteases for cell suicide: functions and regulation of caspases.
Microbiol Mol Biol Rev 64:821-46 (2000)
2  [PMID:16186808]
Fischer U, Stroh C, Schulze-Osthoff K.
Unique and overlapping substrate specificities of caspase-8 and caspase-10.
Oncogene 25:152-9 (2006)
3  [PMID:12884866]
Shikama Y, Yamada M, Miyashita T.
Caspase-8 and caspase-10 activate NF-kappaB through RIP, NIK and IKKalpha kinases.
Eur J Immunol 33:1998-2006 (2003)
4  [PMID:15209560]
Boatright KM, Deis C, Denault JB, Sutherlin DP, Salvesen GS.
Activation of caspases-8 and -10 by FLIP(L).
Biochem J 382:651-7 (2004)
Other DBs
ExplorEnz - The Enzyme Database:
IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 189088-85-5

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