Literature summary extracted from

Tong, Y.; Tong, S.; Zhao, X.; Wang, J.; Jun, J.; Park, J.; Wands, J.; Li, J.
Initiation of duck hepatitis B virus infection requires cleavage by a furin-like protease (2010), J. Virol., 84, 4569-4578.

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

Localization

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	-

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
3.4.17.22	170000	-	SDS-PAGE	Anas platyrhynchos

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.17.22	Anas platyrhynchos	Q90240	-	-
3.4.21.75	Anas platyrhynchos	-	-	-

Posttranslational Modification

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

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
3.4.21.75	hepatocyte	-	Anas platyrhynchos	-
3.4.21.75	liver	-	Anas platyrhynchos	-

Substrates and Products (Substrate)

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	?	-	?

Synonyms

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

General Information

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

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Release 2023.1 (January 2023)