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Literature summary for 3.4.23.5 extracted from

  • Li, C.; Zhang, H.; Li, L.; Song, L.
    Identification of a cathepsin D potentially involved in H2A cleavage from scallop Chlamys farreri (2010), Mol. Biol. Rep., 37, 1451-1460.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Azumapecten farreri
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the peptide has two potential glycosylation sites Azumapecten farreri

Source Tissue

Source Tissue Comment Organism Textmining
adductor muscle
-
Azumapecten farreri
-
gill
-
Azumapecten farreri
-
gonad
-
Azumapecten farreri
-
hemocyte
-
Azumapecten farreri
-
hepatopancreas highest expression Azumapecten farreri
-
mantle
-
Azumapecten farreri
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
histone H2A + H2O
-
Azumapecten farreri ?
-
?

Synonyms

Synonyms Comment Organism
CatD
-
Azumapecten farreri
CTSD
-
Azumapecten farreri

Expression

Organism Comment Expression
Azumapecten farreri after 8 h Vibrio anguillarum challenge, the expression level of cathepsin D changes significantly in all examined tissues except mantle and hemocytes up