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Literature summary for 3.4.21.B6 extracted from

  • 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 (2014), J. Biol. Chem., 289, 14740-14749.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.B6

Cloned(Commentary)

Cloned (Comment) Organism
gene Prss8 Mus musculus

Protein Variants

Protein Variants Comment Organism
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 Mus musculus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane a membrane-anchored protein Mus musculus 16020
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Organism

Organism UniProt Comment Textmining
Mus musculus Q99L44 gene PRSS8
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Mus musculus C57BL/6N Q99L44 gene PRSS8
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Source Tissue

Source Tissue Comment Organism Textmining
epithelial cell
-
 Mus musculus
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Synonyms

Synonyms Comment Organism
CAP1
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 Mus musculus
channel-activating protease 1
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 Mus musculus
PRSS8
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 Mus musculus

General Information

General Information Comment Organism
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 Mus musculus
physiological function prostasin supports epidermal development and postnatal homeostasis independent of its enzymatic activity Mus musculus