EC                Enzyme                                 

cathepsin E;
slow-moving proteinase;
erythrocyte membrane aspartic proteinase;
erythrocyte membrane aspartic proteinase;
non-pepsin proteinase;
cathepsin D-like acid proteinase;
cathepsin E-like acid proteinase;
cathepsin D-type proteinase
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Similar to cathepsin D, but slightly broader specificity
Found in stomach, spleen, erythrocyte membrane; not lysosomal. Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomer. In peptidase family A1 (pepsin A family)
EC created 1992
K01382  cathepsin E
HSA: 1510(CTSE)
PTR: 457677(CTSE)
PPS: 100996015(CTSE)
GGO: 101124402(CTSE)
PON: 100452388(CTSE)
NLE: 100603573(CTSE)
MCC: 696202(CTSE)
MCF: 102122689(CTSE)
CSAB: 103230206(CTSE)
RRO: 104661729(CTSE)
RBB: 108535115(CTSE)
CJC: 100413525(CTSE)
SBQ: 101046996(CTSE)
MMU: 13034(Ctse)
MCAL: 110297944(Ctse)
MPAH: 110322114(Ctse)
RNO: 25424(Ctse)
MUN: 110541651(Ctse)
CGE: 100757212(Ctse)
NGI: 103725942(Ctse)
HGL: 101699894(Ctse)
CCAN: 109697219(Ctse)
OCU: 100009063(CTSE)
TUP: 102483572(CTSE)
CFA: 488577(CTSE)
VVP: 112914539(CTSE)
AML: 100475014(CTSE)
UMR: 103671000(CTSE)
UAH: 113242470(CTSE)
ORO: 101364641(CTSE)
FCA: 101088455(CTSE)
PTG: 102960694(CTSE)
PPAD: 109257566(CTSE)
AJU: 106972890(CTSE)
BOM: 106701532(CTSE)
OOR: 105748678(CTSE)
DLE: 111184605(CTSE)
PCAD: 112067583(CTSE)
ECB: 100055161(CTSE)
EPZ: 103553838(CTSE)
EAI: 106823465(CTSE)
MYB: 102250825(CTSE)
MYD: 102753719(CTSE)
MNA: 107539403(CTSE)
HAI: 109386433(CTSE)
DRO: 112315908(CTSE)
PALE: 102890366(CTSE)
RAY: 107508871(CTSE)
MJV: 108390208(CTSE)
LAV: 100663037(CTSE)
TMU: 101345963
MDO: 100019361(CTSE)
SHR: 100934264(CTSE)
PCW: 110219635(CTSE)
OAA: 100081153
GGA: 417848(CTSEAL) 771791(CTSE)
MGP: 100548063(CTSE) 100548118
CJO: 107310248 107324888(CTSE)
NMEL: 110388319(CTSE) 110392329
APLA: 101789387(CTSE) 101804173
ACYG: 106041279(CTSE) 106045567
TGU: 100228499(CTSE)
LSR: 110473079(CTSE) 110477989
SCAN: 103813448 103822388(CTSE)
GFR: 102041269 102043260(CTSE)
FAB: 101814202 101815239(CTSE)
PHI: 102101700 102104842(CTSE)
PMAJ: 107205210 107214812(CTSE)
CCAE: 111932764 111939682(CTSE)
CCW: 104692361(CTSE) 104698380
ETL: 114062146 114066524(CTSE)
FPG: 101920453(CTSE) 101923255
FCH: 102049037 102051110(CTSE)
CLV: 102089416(CTSE) 102097331
EGZ: 104132915 104134468(CTSE)
NNI: 104010999 104013197(CTSE)
ACUN: 113488852(CTSE) 113491191
PADL: 103919789(CTSE) 103919953
AAM: 106484553(CTSE) 106488475
ASN: 102380654 102384944(CTSE)
AMJ: 102566566(NOTS) 102567770(CTSE)
PSS: 102461548 102463529(CTSE)
CMY: 102931323(CTSE) 102933016
CPIC: 101933009(CTSE) 101941871
ACS: 100561705(ctse) 100561900
PVT: 110081416(CTSE)
PBI: 103067272(CTSE)
PMUR: 107283823 107292374(CTSE)
TSR: 106539374(CTSE)
GJA: 107105702 107115330(CTSE)
XLA: 373572(ctse.L) 373573(ctse.S)
XTR: 100145572(ctse)
NPR: 108787647(CTSE) 108804543
DRE: 114367(nots)
SRX: 107725781
SANH: 107677818
SGH: 107569115
CCAR: 109062605
IPU: 108279983
PHYP: 113531975
AMEX: 103036771
EEE: 113573545
TRU: 777958(nts)
LCO: 104935800
NCC: 104947164
MZE: 101475107
ONL: 100700379
OLA: 101159061
XMA: 102238257
XCO: 114160681
PRET: 103459337
CVG: 107089060
NFU: 107387581
KMR: 108250475
ALIM: 106532841
AOCE: 111569281
LCF: 108901352
SDU: 111224749
SLAL: 111664974
HCQ: 109532693
BPEC: 110161516
MALB: 109967703
ELS: 105023104
SFM: 108936584
LCM: 102345230(CTSE) 102354975
CMK: 103185314(ctse)
DER: 6555650
DSI: Dsimw501_GD29212(Dsim_GD29212)
CLEC: 106672750
BRP: 103841663
BNA: 106364978
RCN: 112165553
PEQ: 110035315
CMT: CCM_00473
SMIN: v1.2.003841.t1(symbB.v1.2.003841.t1) v1.2.015387.t1(symbB.v1.2.015387.t1) v1.2.018093.t1(symbB.v1.2.018093.t1) v1.2.018143.t1(symbB.v1.2.018143.t1) v1.2.018682.t1(symbB.v1.2.018682.t1) v1.2.018682.t2(symbB.v1.2.018682.t2) v1.2.022081.t1(symbB.v1.2.022081.t1) v1.2.024260.t1(symbB.v1.2.024260.t1) v1.2.037886.t1(symbB.v1.2.037886.t1)
 » show all
1  [PMID:3741628]
Lapresle C, Puizdar V, Porchon-Bertolotto C, Joukoff E, Turk V.
Structural differences between rabbit cathepsin E and cathepsin D.
Biol Chem Hoppe Seyler 367:523-6 (1986)
2  [PMID:3058036]
Yonezawa S, Fujii K, Maejima Y, Tamoto K, Mori Y, Muto N.
Further studies on rat cathepsin E: subcellular localization and existence of the active subunit form.
Arch Biochem Biophys 267:176-83 (1988)
3  [PMID:3058118]
Jupp RA, Richards AD, Kay J, Dunn BM, Wyckoff JB, Samloff IM, Yamamoto K.
Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E.
Biochem J 254:895-8 (1988)
4  [PMID:2674141]
Azuma T, Pals G, Mohandas TK, Couvreur JM, Taggart RT.
Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases.
J Biol Chem 264:16748-53 (1989)
Other DBs
ExplorEnz - The Enzyme Database:
IUBMB Enzyme Nomenclature:
ExPASy - ENZYME nomenclature database:
BRENDA, the Enzyme Database:
CAS: 110910-42-4

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