Summary for peptidase A01.010: cathepsin E

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Human EST Mouse EST Substrates Inhibitors Pharma

 

Names
MEROPS Namecathepsin E
Other nameserythrocyte membrane aspartic proteinase, gastric cathepsin, slow-moving proteinase
Name and HistoryCathepsin E is a secreted aspartic endopeptidase. It is synthesized as an inactive precursor and when activated forms a disulfide-linked homodimer (Tsukuba et al., 1996). Cathepsin E is present in antigen-presenting cells of the immune system (Muto et al., 1988), osteoclasts (Yoshimine et al., 1995) and gastric cells (Saku et al., 1991), and it may be associated with the plasma membrane.
Domain architecture
MEROPS Classification
Classification Clan AA >> Subclan (none) >> Family A1 >> Subfamily A >> A01.010
Holotypecathepsin E (Homo sapiens), Uniprot accession P14091 (peptidase unit: 61-396), MERNUM MER0000944
History Identifier created: Handbook of Proteolytic Enzymes (1998) Academic Press, London.
Activity
Catalytic typeAspartic
PeplistIncluded in the Peplist with identifier PL00008
NC-IUBMBSubclass 3.4 (Peptidases) >> Sub-subclass 3.4.23 (Aspartic endopeptidases) >> Peptidase 3.4.23.34
EnzymologyBRENDA database
Proteolytic eventsCutDB database (31 cleavages)
Activity statushuman: active (Kay & Tatnell, 2004)
mouse: active (Tatnell et al., 1997)
SpecificityQuantitative N-terminal proteomics has been used to study substrate specificity (Impens et al., 2010).
PhysiologyCathepsin E is an endosomal peptidase and has proposed roles in antigen presentation by the MHC class II system, through processing of both invariant chain and protein antigens (Maric et al., 1994; Chain et al., 2005).
KnockoutMice lacking cathepsin E spontaneously develop skin lesions similar to those of humans with atopic dermatitis (Tsukuba et al., 2003).
Pharmaceutical relevanceActivity of cathepsin E seems to contribute to excitotoxin-induced neuronal cell death (Tominaga et al., 1998).
Pathways KEGGLysosome
Other databases WIKIPEDIAhttp://en.wikipedia.org/wiki/Cathepsin_E
Cleavage site specificity Explanations of how to interpret the following cleavage site sequence logo and specificity matrix can be found here.
Cleavage pattern-/-/-/lfScissile bondv/-/-/- (based on 1596 cleavages)
weblogo
Specificity matrix
 
Amino acid P4 P3 P2 P1 P1' P2' P3' P4'
Gly 135 71 49 24 19 79 91 181
Pro 127 47 1 0 6 0 21 76
Ala 130 74 172 67 201 244 116 199
Val 89 167 189 14 326 211 140 102
Leu 120 161 77 646 235 140 210 131
Ile 68 108 100 14 222 103 110 74
Met 25 59 36 99 53 25 48 42
Phe 49 77 19 339 108 19 37 28
Tyr 42 49 37 81 78 24 15 36
Trp 7 15 3 13 1 0 1 1
Ser 95 89 147 24 67 132 103 96
Thr 79 101 80 23 51 127 115 107
Cys 24 24 36 32 10 34 17 21
Asn 55 49 101 14 38 34 80 72
Gln 65 68 92 22 30 92 78 87
Asp 100 123 159 39 47 83 109 78
Glu 139 153 182 134 74 143 173 119
Lys 107 86 53 3 25 96 127 131
Arg 87 52 35 7 3 9 3 2
His 44 18 26 1 0 0 0 6
Human genetics
Gene symbol Locus Megabases Ensembl Entrez gene Gene Cards OMIM
CTSE 1q31 ENSG00000196188 1510 CTSE 116890
Mouse genetics
Gene symbol Position Megabases Ensembl Entrez gene MGI
Ctse 1:E4 ENSMUSG00000004552 13034 MGI:107361