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Information on EC 3.4.21.B6 - prostasin

for references in articles please use BRENDA:EC3.4.21.B6
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.B6 prostasin
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This record set is specific for:
UNIPROT: Q99L44
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
endoprotease activity. Trypsin-like enzymatic activity
Synonyms
prostasin, cap-1, prss8, cap1/prss8, channel-activating protease 1, channel activating protease 1, tracheal-prostasin, channel-activating protease-1, channel activating protease-1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
channel-activating protease 1
-
CAS REGISTRY NUMBER
COMMENTARY hide
157857-10-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene PRSS8
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
prostasin is glycosylphosphatidylinositol-anchored to the cell surface
Manually annotated by BRENDA team
a membrane-anchored protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
prostasin null mice lack barrier formation and display fatal postnatal dehydration. But mice homozygous for a point mutation in the Prss8 gene, which causes the substitution of the active site serine within the catalytic histidine-aspartate-serine triad with alanine and renders prostasin catalytically inactive, develop barrier function and are healthy when followed for up to 20 weeks. Phenotypes, overview
physiological function
prostasin supports epidermal development and postnatal homeostasis independent of its enzymatic activity
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q99L44_MOUSE
339
0
36216
TrEMBL
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S238A
inactive
S313N/S314L
lacks the preferred GPI attachment sites and shows decreased activity
S313N/S314L/R322A
mutant alters both the preferred GPI attachment sites and the potential COOH-terminal tryptic cleavage site, activity is not different from wild type prostasin
additional information
construction of Prss8 knockout mutant mice. A T to G substitution, leading to substitution of the active site serine within the catalytic histidine-aspartate-serine triad with alanine, is introduced into exon 6 by site-directed mutagenesis, the clone is injected into strain C57BL/6J blastocysts
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in M-1 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Verghese, G.M.; Gutknecht, M.F.; Caughey, G.H.
Prostasin regulates epithelial monolayer function: cell-specific Gpld1-mediated secretion and functional role for GPI anchor
Am. J. Physiol.
291
C1258-C1270
2006
Mus musculus (Q99L44), Mus musculus
Manually annotated by BRENDA team
Peters, D.E.; Szabo, R.; Friis, S.; Shylo, N.A.; Uzzun Sales, K.; Holmbeck, K.; Bugge, T.H.
The membrane-anchored serine protease prostasin (CAP1/PRSS8) supports epidermal development and postnatal homeostasis independent of its enzymatic activity
J. Biol. Chem.
289
14740-14749
2014
Mus musculus (Q99L44), Mus musculus C57BL/6N (Q99L44)
Manually annotated by BRENDA team