3.4.22.27: cathepsin S
This is an abbreviated version!
For detailed information about cathepsin S, go to the full flat file.
Word Map on EC 3.4.22.27
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3.4.22.27
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cathepsins
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lysosomal
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point-of-care
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cystatins
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dendritic
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atherosclerosis
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proteinases
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elastin
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papain
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antigen-presenting
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histocompatibility
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autoimmune
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drug development
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lacrimal
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papain-like
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diagnostics
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ii-associated
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elastolytic
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resource-limited
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s-deficient
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procathepsins
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l-like
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pharmacology
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endostatin
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microglial
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fractalkine
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medicine
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par2
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collagenolytic
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syphilis
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ii-restricted
- 3.4.22.27
- cathepsins
- lysosomal
-
point-of-care
- cystatins
- dendritic
- atherosclerosis
- proteinases
- elastin
- papain
-
antigen-presenting
-
histocompatibility
- autoimmune
- drug development
-
lacrimal
-
papain-like
- diagnostics
-
ii-associated
-
elastolytic
-
resource-limited
-
s-deficient
-
procathepsins
-
l-like
- pharmacology
- endostatin
- microglial
- fractalkine
- medicine
- par2
-
collagenolytic
- syphilis
-
ii-restricted
Reaction
similar to cathepsin L, but with much less activity on Z-Phe-Arg-/-NHMec, and additional information activity on the Z-Val-Val-Arg-/- compound =
Synonyms
C01.034, Cat S, Cat-S, cath S, cathepsin S, cathepsin S-like cysteine proteinase, cathepsin Sa, CatS, CatSPP, CTSS, Hacp-s, PfCTSSa, PoCtS, rs1136774, rs16827671, rs34495036, rs35989725, rs3754212, rs7534124, SoCatS
ECTree
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Subunits
Subunits on EC 3.4.22.27 - cathepsin S
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monomer
additional information
monomer
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enzyme has 217 amino acids, the structure of CatS is composed of 2 domains
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most of the loss of procathepsin S occurs during folding, probably because of aggregation. Concentrations lower than 0.02 mg/ml of procathepsin S are necessary to minimise such aggregation
additional information
enzyme SoCatS possesses the typical cathepsin S domain architecture, i.e. a signal peptide (residues 1-21), an N-terminal proregion known as protease inhibitor I-29 (residues 34-94), and a C-terminal C1-peptidase domain (residues 122-337)
additional information
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enzyme SoCatS possesses the typical cathepsin S domain architecture, i.e. a signal peptide (residues 1-21), an N-terminal proregion known as protease inhibitor I-29 (residues 34-94), and a C-terminal C1-peptidase domain (residues 122-337)
additional information
the enzyme contains a signal peptide (1-17 aa), a propeptide inhibitor domain (18-113 aa), and a mature peptide (114-326 aa). The mature peptide consists of four catalytic residues (Gln132, Cys138, His274, and Asn294), four N-glycosylation sites, eight conserved cysteine sites, and six dominant subsites for the binding of specific substrates