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Literature summary for 3.4.17.22 extracted from
- Viral and cellular determinants involved in hepadnaviral entry (2007), World J. Gastroenterol., 13, 22-38.
Application
| Application | Comment | Organism |
|---|---|---|
| medicine | for duck hepatitis B virus and probably all other avian hepadnaviruses, carboxypeptidase D (CPD) is shown to be indispensable for infection. The striking correlation of the infection competition activity of duck hepatitis B virus-preS polypeptides with their ability to bind duck carboxypeptidase D suggests that it is this molecule which is addressed and inactivated at the surface of hepatocytes | Anas platyrhynchos |
| medicine | essential for duck hepatitis B virus infection. PreS-induced CPD conformational changes may play an important role in the fusion of the viral and cellular membrane | Anas platyrhynchos |
| medicine | is not involved in hepatitis B virus infection | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | duck CPD (dCPD) like all other CPDs identified, consists of three luminal/extracellular carboxypeptidase E like domains of about 50 kDa each, one transmembrane domain and a highly conserved cytoplasmic tail required for accurate retrieval to the trans-Golgi network. While two of the three luminal/extracellular domains bind Zn2+-ions and exhibit enzymatic carboxypeptidase activity towards yet unidentified cellular proteins that cross the secretory pathway, the membrane proximal C-domain of dCPD is enzymatically inactive and binds duck hepatitis B virus-preS polypeptide with very high affinity | Anas platyrhynchos |
| additional information | CPD mutant lacking the cytoplasmic trans-Golgi network-retrieval signal into primary duck hepatocytes, abolishes duck hepatitis B virus infection of transduced cells | Anas platyrhynchos |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | CPD contains a highly conserved cytoplasmic tail required for accurate retrieval to the trans-Golgi network | Anas platyrhynchos | 5829 | - |
| membrane | CPD contains one transmembrane domain | Anas platyrhynchos | 16020 | - |
| additional information | CPD contains three luminal/extracellular carboxypeptidase E like domains of about 50 kDa each | Anas platyrhynchos | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | - |
Anas platyrhynchos |  |
| Zn2+ | two of the three luminal/extracellular domains bind Zn2+-ions | Anas platyrhynchos | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 120000 | - |
- |
Anas platyrhynchos |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Anas platyrhynchos | - |
- |
- |
| Anas platyrhynchos | Q90240 | - |
- |
| Gallus gallus | - |
- |
- |
| Homo sapiens | - |
- |
- |
| Mus musculus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Anas platyrhynchos |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| hepatocyte | CPD is greatly and selectively down regulated in duck hepatitis B virus infected primary hepatocytes | Anas platyrhynchos | - |
| kidney | - |
Anas platyrhynchos | - |
| liver | CPD is greatly and selectively down regulated in duck hepatitis B virus infected livers | Anas platyrhynchos | - |
| pancreas | - |
Anas platyrhynchos | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | displays only a very weak binding with duck hepatitis B virus preS | Gallus gallus | ? | - |
? | |
| additional information | does not interact with duck hepatitis B virus preS | Mus musculus | ? | - |
? | |
| additional information | does not interact with duck hepatitis B virus preS | Homo sapiens | ? | - |
? | |
| additional information | two of the three luminal/extracellular domains exhibit enzymatic carboxypeptidase activity towards unidentified cellular proteins that cross the secretory pathway. The membrane proximal C-domain of CPD is enzymatically inactive and binds duck hepatitis B virus preS with very high affinity | Anas platyrhynchos | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Carboxypeptidase D | - |
Gallus gallus |
| Carboxypeptidase D | - |
Mus musculus |
| Carboxypeptidase D | - |
Homo sapiens |
| Carboxypeptidase D | - |
Anas platyrhynchos |
| CPD | - |
Gallus gallus |
| CPD | - |
Mus musculus |
| CPD | - |
Homo sapiens |
| CPD | - |
Anas platyrhynchos |
| gp180 | - |
Anas platyrhynchos |
| p170 | - |
Anas platyrhynchos |
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