3.4.23.5: cathepsin D
This is an abbreviated version!
For detailed information about cathepsin D, go to the full flat file.
Word Map on EC 3.4.23.5
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3.4.23.5
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lysosomal
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pepstatin
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estrogen
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metastasis
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alzheimer
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proteinases
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aspartyl
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node
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vacuole
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lymph
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renin
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pepsin
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endosomes
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progesterone
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hydrolases
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endocytic
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phagosomes
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amyloid
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beta-glucuronidase
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plasminogen
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mannose
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6-phosphate
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axillary
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autophagosomes
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saposins
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lysosomal-associated
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leupeptin
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plasmepsins
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beta-hexosaminidase
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missorting
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mannose-6-phosphate
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chymosin
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lysotracker
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lipofuscinosis
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lc3-ii
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autophagy-lysosomal
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rab7
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ceroid
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estrogen-regulated
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immunoradiometric
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medicine
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lc3
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lamp-1
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node-negative
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trans-golgi
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upa
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endocytosed
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node-positive
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c-erbb-2
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autolysosomes
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cation-independent
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molecular biology
- 3.4.23.5
- lysosomal
- pepstatin
- estrogen
- metastasis
- alzheimer
- proteinases
-
aspartyl
- node
- vacuole
- lymph
- renin
- pepsin
- endosomes
- progesterone
- hydrolases
-
endocytic
-
phagosomes
-
amyloid
- beta-glucuronidase
- plasminogen
- mannose
- 6-phosphate
-
axillary
-
autophagosomes
-
saposins
-
lysosomal-associated
- leupeptin
-
plasmepsins
- beta-hexosaminidase
-
missorting
- mannose-6-phosphate
- chymosin
-
lysotracker
- lipofuscinosis
-
lc3-ii
-
autophagy-lysosomal
- rab7
-
ceroid
-
estrogen-regulated
-
immunoradiometric
- medicine
- lc3
- lamp-1
-
node-negative
-
trans-golgi
- upa
-
endocytosed
-
node-positive
-
c-erbb-2
-
autolysosomes
-
cation-independent
- molecular biology
Reaction
Specificity similar to, but narrower than, that of pepsin A. Does not cleave the Gln4-His bond in B chain of insulin =
Synonyms
BmCatD, CAD 1, CAD 2, CAD 3, CapD, Cat D, CAT-D, CatD, Cath D, cath-D, cathD, cathepsin D, cathepsin D-like proteinase, cathepsin D1, cathepsin D2, CD1, CTSD, EC 3.4.4.23, matCTSD, PCD, Pep4p, preproCatD, pro-cathepsin, pro-cathepsin D, pro-CD, pro-CtsD, proCat, proCDrec, proCTSD, Proteinase A
ECTree
3.4.23.5 cathepsin DAdvanced search results
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results (Posttranslational Modification
Posttranslational Modification on EC 3.4.23.5 - cathepsin D
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POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glycoprotein
proteolytic modification
side-chain modification
additional information
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human cathepsin D is synthesized as a di-glycosylated precursor of approximately 53 kDa that is processed by proteolysis first into an intermediate single-chain of 48 kDa and eventually into the mature double-chain form
glycoprotein
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contains one N-linked carbohydrate moiety of high-mannose type
glycoprotein
the enzyme has one N-glycosylation site located at Asn131
glycoprotein
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proCDrec is largely secreted into the culture medium, although it contains high-mannose oligosaccharides with uncovered mannose-6-phosphate residues
glycoprotein
the enzyme is glycosylated at two N-linked glycosylation sites (Asn residues 134 and 263)
proteolytic modification
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intracellular proCDrec is processed into the 48 kDa intermediate single-chain and the 31 plus 13 kDa double-chain form. Processing is slower than in normal cells
proteolytic modification
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synthesized as a 53000 Da precursor protein and converted to the active 46000 da protease following transport through golgi compartments
proteolytic modification
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synthesized as a 53000 Da precursor protein and converted to the active 46000 da protease following transport through golgi compartments
proteolytic modification
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induced on injury, a metalloprotease cleaves the inactive proenzyme of 40000 Da to generate active enzyme of 37000 Da
proteolytic modification
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procathepsin D, cleavage to single-chain cathepsin D may occur via a unimolecular mechanism
side-chain modification
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the only glycosylation is a cluster of mannose 6-sulfate residues on N-linked oligosaccharide chains
side-chain modification
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presence of mannose residues, but no lectin-available sialic acid, fucose, N-acetylglucosamine and galactose residues
side-chain modification
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N-linked oligosaccharide extends from Asn70 towards Lys-203
side-chain modification
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cathepsin D-I: neutral sugar content 6%, contains mannose, glucose, galactose, fucose and glucosamine in a ratio of 8:2:1:1:5
side-chain modification
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four attachment sites, one attachment site this in the light chain and three in the heavy chain. Each carbohydrate unit contains 2 residues of mannose and 1 residue of glucosamine
side-chain modification
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each isoenzyme contains 8 mannose and 4 glucosamine residues per mol
