KEGG   ENZYME: 3.4.23.34Help
Entry
EC 3.4.23.34                Enzyme                                 

Name
cathepsin E;
slow-moving proteinase;
erythrocyte membrane aspartic proteinase;
SMP;
erythrocyte membrane aspartic proteinase;
EMAP;
non-pepsin proteinase;
cathepsin D-like acid proteinase;
cathepsin E-like acid proteinase;
cathepsin D-type proteinase
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
BRITE hierarchy
Reaction(IUBMB)
Similar to cathepsin D, but slightly broader specificity
Comment
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)
History
EC 3.4.23.34 created 1992
Orthology
K01382  
cathepsin E
Genes
HSA: 
1510(CTSE)
PTR: 
457677(CTSE)
PPS: 
100996015(CTSE)
GGO: 
101124402(CTSE)
PON: 
100452388(CTSE)
MCC: 
696202(CTSE)
MCF: 
102122689(CTSE)
MMU: 
13034(Ctse)
RNO: 
25424(Ctse)
CGE: 
100757212(Ctse)
HGL: 
101699894(Ctse)
TUP: 
102483572(CTSE)
CFA: 
488577(CTSE)
AML: 
100475014(CTSE)
FCA: 
101088455(CTSE)
PTG: 
102960694(CTSE)
SSC: 
102160195(CTSE)
ECB: 
100055161(CTSE)
MYB: 
102250825(CTSE)
MYD: 
102753719(CTSE)
PALE: 
102890366(CTSE)
MDO: 
100019361(CTSE)
SHR: 
100934264(CTSE)
GGA: 
771791(CTSE)
MGP: 
TGU: 
100228499(CTSE)
FAB: 
101815239(CTSE)
PHI: 
102104842(CTSE)
APLA: 
101789387(CTSE)
FPG: 
101920453(CTSE)
FCH: 
102051110(CTSE)
CLV: 
102089416(CTSE)
ASN: 
102384944(CTSE)
AMJ: 
102567770(CTSE)
PSS: 
102463529(CTSE)
CMY: 
102931323(CTSE)
ACS: 
PBI: 
103067272(CTSE)
XLA: 
373572(ctse-a) 373573(ctse-b)
XTR: 
100145572(ctse)
LCM: 
102345230(CTSE)
CMK: 
103185314(ctse)
CSL: 
PCO: 
PSQ: 
ADL: 
FME: 
ABV: 
AGABI2DRAFT211096(AGABI2DRAFT_211096)
MLR: 
TAN: 
TET: 
PIF: 
 » show all
Taxonomy
Reference
1  [PMID:3741628]
  Authors
Lapresle C, Puizdar V, Porchon-Bertolotto C, Joukoff E, Turk V.
  Title
Structural differences between rabbit cathepsin E and cathepsin D.
  Journal
Biol. Chem. Hoppe. Seyler. 367 (1986) 523-6.
  Organism
Oryctolagus cuniculus
Reference
2  [PMID:3058036]
  Authors
Yonezawa S, Fujii K, Maejima Y, Tamoto K, Mori Y, Muto N.
  Title
Further studies on rat cathepsin E: subcellular localization and existence of the active subunit form.
  Journal
Arch. Biochem. Biophys. 267 (1988) 176-83.
  Organism
Rattus norvegicus
Reference
3  [PMID:3058118]
  Authors
Jupp RA, Richards AD, Kay J, Dunn BM, Wyckoff JB, Samloff IM, Yamamoto K.
  Title
Identification of the aspartic proteinases from human erythrocyte membranes and gastric mucosa (slow-moving proteinase) as catalytically equivalent to cathepsin E.
  Journal
Biochem. J. 254 (1988) 895-8.
  Organism
Homo sapiens
Reference
4  [PMID:2674141]
  Authors
Azuma T, Pals G, Mohandas TK, Couvreur JM, Taggart RT.
  Title
Human gastric cathepsin E. Predicted sequence, localization to chromosome 1, and sequence homology with other aspartic proteinases.
  Journal
J. Biol. Chem. 264 (1989) 16748-53.
  Organism
Homo sapiens
  Sequence
[hsa:1510]
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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