EC Number | Cloned (Comment) | Organism |
---|---|---|
3.4.17.22 | expressed by transient expression in a human kidney cell line and primary duck hepatocytes | Anas platyrhynchos |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
3.4.17.22 | R166A/R169A | enzyme is cleaved by furin. Proteins sequence reveals a consensus sequence for furin cleavage (RXXR) at positions 166 to 169. Cleavage at this site removes the N-terminal 169 residues to generate a truncated protein of approximately 151 kDa. Substitution of the two arginines with alanine completely abolishes cleavage of DCPD | Anas platyrhynchos |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.4.17.22 | dynorphin A | - |
Anas platyrhynchos | |
3.4.17.22 | Met-enkephalin-KK | - |
Anas platyrhynchos | |
3.4.21.75 | decanoyl-RVKR-chloromethylketone | the furin inhibitor reduces DHBV infection of primary duck hepatocytes | Anas platyrhynchos |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
3.4.17.22 | endosome | DCPD, glycine decarboxylase and duck Hepatitis B virus large enveloppe protein are colocalized in the endosomal fraction of duck hepatocytes | Anas platyrhynchos | 5768 | - |
3.4.21.75 | endosome | - |
Anas platyrhynchos | 5768 | - |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
3.4.17.22 | 170000 | - |
SDS-PAGE | Anas platyrhynchos |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.4.17.22 | Anas platyrhynchos | Q90240 | - |
- |
3.4.21.75 | Anas platyrhynchos | - |
- |
- |
EC Number | Posttranslational Modification | Comment | Organism |
---|---|---|---|
3.4.17.22 | proteolytic modification | enzyme is cleaved by furin. Proteins sequence reveals a consensus sequence for furin cleavage (RXXR) at positions 166 to 169. Cleavage at this site removes the N-terminal 169 residues to generate a truncated protein of approximately 151 kDa. Substitution of the two arginines with alanine completely abolishes cleavage of DCPD | Anas platyrhynchos |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
3.4.21.75 | hepatocyte | - |
Anas platyrhynchos | - |
3.4.21.75 | liver | - |
Anas platyrhynchos | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.4.21.75 | duck carboxypeptidase D + H2O | i.e. DCPD, duck carboxypeptidase D acts as species-specific docking receptor for the duck hepatitis B virus. No cleavage of recombinant DCPD expressed in LMH cells | Anas platyrhynchos | ? | - |
? | |
3.4.21.75 | duck hepatitis B virus large envelope pre-S protein + H2O | the protein needs to be cleaved by duck endosomal furin or furin-like proprotein convertase for duck hepatocyte infection by duck hepatitis B virus | Anas platyrhynchos | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.4.17.22 | DCPD | - |
Anas platyrhynchos |
3.4.17.22 | duck carboxypeptidase D | - |
Anas platyrhynchos |
3.4.21.75 | furin-like proprotein convertase | - |
Anas platyrhynchos |
3.4.21.75 | furin-like protease | - |
Anas platyrhynchos |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.4.17.22 | physiological function | transfected DCPD could confer duck hepatitis B virus binding to non-duck cell lines which is followed by rapid virus release from cells. Coexpression of furin leads to DCPD cleavage and increases virus retention | Anas platyrhynchos |
3.4.21.75 | malfunction | furin or a furin-like proprotein convertase facilitates duck hepatitis B virus, DHBV, infection by cleaving both the docking receptor and the viral large envelope protein | Anas platyrhynchos |