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Information on EC 3.4.17.22 - metallocarboxypeptidase D
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
silver, gp180, cpd-n, metallocarboxypeptidase d, duck carboxypeptidase d, carboxypeptidase-d, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Carboxypeptidase D
carboxypeptidase-D
CPD
gp180
additional information
Drosophila sp. (in: flies)
-
Silver encodes the homolog of human carboxypeptidase D
Carboxypeptidase D
-
-
-
-
CPD
-
-
-
-
gp180
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
releases C-terminal Arg and Lys from polypeptides
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
153967-26-1
not distinguished from EC 3.4.16.6 in Chemical Abstracts
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys + H2O
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly + Lys
adipokinetic hormone intermediates containing C-terminal basic residues is processed by CPD
-
-
?
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys-Arg + H2O
pGlu-Leu-Thr-Phe-Ser-Pro-Asp-Trp-Gly-Lys + Arg
adipokinetic hormone intermediates containing C-terminal basic residues is processed by CPD
-
-
?
additional information
?
-
-
enzyme is involved in targeting duck hepatitis B virus particles to the secretary pathway for proteolytic cleavage of the viral envelope protein
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
the enzyme removes only the C-terminal Lys or Arg from peptides, with the first domain more efficient towards Arg and the second domain more efficient towards Lys. Peptides containing Pro in the penultimate position are poorly cleaved. Cleavage of a peptide with Ala in the penultimate position is most efficient, with the order of decreasing efficiency Ala, Met, Ser, Phe, tyr, Trp, Thr, Gln, Asp, Leu, Gly, Pro. There are only minor differences between the first and the second domains regarding the influence of the penultimate amino acid
-
-
?
additional information
?
-
-
the enzyme plays a role in processing of many proteins that transit the secretory pathway
-
-
?
additional information
?
-
-
production of growth factors and/or growth factor receptors, processing of peptide hormones
-
-
?
additional information
?
-
-
displays only a very weak binding with duck hepatitis B virus preS
-
-
?
additional information
?
-
-
does not interact with duck hepatitis B virus preS
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine from polypeptides
-
-
?
additional information
?
-
CPD cleaves C-terminal Lys or Arg from a subset of the peptides. Most of the identified substrates of domain I contain C-terminal Arg, whereas comparable numbers of Lys- and Arg-containing peptides are substrates of domain II. Some peptides with C-terminal basic residues are not cleaved by either domain I or II
-
-
?
additional information
?
-
-
CPD cleaves C-terminal Lys or Arg from a subset of the peptides. Most of the identified substrates of domain I contain C-terminal Arg, whereas comparable numbers of Lys- and Arg-containing peptides are substrates of domain II. Some peptides with C-terminal basic residues are not cleaved by either domain I or II
-
-
?
additional information
?
-
multicatalytic enzyme with three carboxypeptidase-like domains, although only the first two domains are predicted to be enzymatically active. The enzyme cleaves exclusively C-terminal basic residues. A quantitative peptidomics approach is used to compare the activities of CPD domains I and II towards a large number of peptides. the enzyme cleaves C-terminal Lys or Arg from a subset of the peptides. Most of the identified substrates of domain I contain C-terminal Arg, whereas comparable numbers of Lys- and Arg-containing peptides are substrates of domain II. Some peptides with C-terminal basic residues are not cleaved by either domain I or II, showing the importance of the P1 position for CPD activity. The preference of domain I for C-terminal Arg is validated through molecular docking experiments
-
-
?
additional information
?
-
-
multicatalytic enzyme with three carboxypeptidase-like domains, although only the first two domains are predicted to be enzymatically active. The enzyme cleaves exclusively C-terminal basic residues. A quantitative peptidomics approach is used to compare the activities of CPD domains I and II towards a large number of peptides. the enzyme cleaves C-terminal Lys or Arg from a subset of the peptides. Most of the identified substrates of domain I contain C-terminal Arg, whereas comparable numbers of Lys- and Arg-containing peptides are substrates of domain II. Some peptides with C-terminal basic residues are not cleaved by either domain I or II, showing the importance of the P1 position for CPD activity. The preference of domain I for C-terminal Arg is validated through molecular docking experiments
-
-
?
additional information
?
-
-
does not interact with duck hepatitis B virus preS
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme is involved in targeting duck hepatitis B virus particles to the secretary pathway for proteolytic cleavage of the viral envelope protein
-
-
?
additional information
?
-
-
the enzyme plays a role in processing of many proteins that transit the secretory pathway
-
-
?
additional information
?
-
-
production of growth factors and/or growth factor receptors, processing of peptide hormones
-
-
?
additional information
?
-
-
releases C-terminal arginine or lysine from polypeptides
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-[[(3,4-dinitrophenyl)carbonyl]amino]-2-(6-hydroxy-3-oxo-3H-xanthen-9-yl)benzoic acid
-
-
additional information
-
not inhibitory: iodoacetate, phenylmethylsulfonylfluoride, benzamidine, N-tosyl-L-Phe chloromethyl ketone, N- tosyl-L-Lys chloromethyl ketone
-
siRNA
downregulation of CpD by siRNA leads to downregulation of transforming growth factor-beta
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
transforming growth factor-beta
leads to upregulation of CpD in primary human blood monocytes. Does not upregulate CpD in HepG2 cells
-
transforming growth factor-beta
-
upregulates CpD in ANA-1 cells and RAW 264.7 cells
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
turnover numbers of domain 1 and 2
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.5
6.5
7
domain I is most active at pH 7 whereas domain II is most active at pH 5.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7
5 - 7.5
5.3 - 7.5
-
pH 5.3: about 45% of maximal activity, pH 7.5: about 35% of maximal activity
6.5 - 7.5
mutant enzyme E762Q displays more than 50% activity from pH 6.5 to 7.5
5 - 7
enzyme with all three domains intact and enzyme with mutation of domain I display more than 50% activity from pH 5.0 to 7.5
5 - 7.5
mutant enzyme E350Q displays more than 50% activity from pH 5.0 to 7.5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
two different C-terminal tail sequences that result from alternative splicing determine the intracellular distribution of both CPD variants
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
it is demonstrated that CpD is up-regulated by TGF-beta in murine macrophage cell lines ANA-1 and RAW 264.7 but HepG2 cells - cells not primarily associated with innate immune responses- show only minimal regulation of CpD by TGF-beta
brenda
additional information
-
ACTH-immunreactive cells outside clustered small cell island (CSCI) show a strong carboxypeptidase D immunoreactivity, whereas ACTH-immunreactive cells in clustered small cell island show uniformly weak reactivity
brenda
-
following prolonged culture of primary hepatocytes, duck carboxypeptidase D expression but not enzyme expression is diminished, which impairs effective duck hepatitis B virus infection
brenda
CPD is greatly and selectively down regulated in duck hepatitis B virus infected primary hepatocytes
brenda
CPD is greatly and selectively down regulated in duck hepatitis B virus infected livers
brenda
it is demonstrated that CpD is up-regulated by TGF-beta in CD14 + human blood monocytes
brenda
Cpd and CPE are strictly co-localized in the mouse placenta from late mid-gestation to term. While there is no strict overlap between Cpe and Cpd transcripts at the early developmental stages, E8 and E10, from E12 onwards there is no obvious difference in the expression patterns of the two genes. Just like Cpe, Cpd is expressed primarily in decidua and in chorionic plate and yolk sac, with weak expression in the labyrinth. At E18, Cpd is expressed at a level higher than Cpe. In interspecies hybrid placental dysplasia placentas, the expression of Cpd overlapps with that of Cpe. There is no difference in the pattern of expression of Cpd in wild-type and fat placentas at E18. Strong expression in decidua and yolk sac, but weak and diffuse expression in the labyrinth
brenda
additional information
-
CpD is significantly downregulated in CD14 positive cells isolated from patients with rheumatoid arthritis, Takayasus arteritis, multiple sclerosis, systemic lupus erythematosus as compared to healthy controls
brenda
additional information
CpD is significantly downregulated in CD14 positive cells isolated from patients with rheumatoid arthritis, Takayasus arteritis, multiple sclerosis, systemic lupus erythematosus as compared to healthy controls
brenda
additional information
-
in ACTH-immunoreactive cells outside clustered small cell islands, intermediate/strong carboxypeptidase D immunoreactivity. Within clustered small cell islands and basophil invasion uniformly weak reactivity and common patterns for carboxypeptidase D
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
DCPD, glycine decarboxylase and duck Hepatitis B virus large enveloppe protein are colocalized in the endosomal fraction of duck hepatocytes
brenda
also detectable in the cytosol after 24 h treatment with interleukin-2
brenda
additional information
CPD contains a highly conserved cytoplasmic tail required for accurate retrieval to the trans-Golgi network
brenda
metallocarboxypeptidase D is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways
brenda
metallocarboxypeptidase D is a membrane-bound component of the trans-Golgi network that cycles to the cell surface through exocytic and endocytic pathways
brenda
additional information
-
CPD contains three luminal/extracellular carboxypeptidase E like domains of about 50 kDa each
-
brenda
additional information
CPD contains three luminal/extracellular carboxypeptidase E like domains of about 50 kDa each
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
-
carboxypeptidase D is a host specific binding partner for full-length large envelope protein of duck hepatitis B virus. Carboxypeptidase D is important in productive DHBV infection, although it can not confer susceptibility to duck hepatitis B virus infection in any cell line
malfunction
to investigate the function of the various carboxypeptidase domains (1-3 active or inactive domains), transgenic flies are created expressing specific forms of CPD in the embryonic-lethal svrPG33 mutant. All constructs containing an active carboxypeptidase domain rescue the lethality with varying degrees, and full viability require inactive carboxypeptidase domain-3
malfunction
-
knockdown of endogenous CPD expression in Huh7 HCC cells by RNA interference reduces cell proliferation, blocks the cell cycle at G1 phase, and increases apoptosis
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
physiological function
transgenic flies overexpressing active carboxypeptidase domain-1 or -2 are similar to each other and to the viable svr mutants Overexpression of carboxypeptidase domain-1 or -2 reduce the levels of Lys/Arg-extended adipokinetic hormone intermediates. CPD domains-1 and -2 have largely redundant functions in the processing of growth factors, hormones, and neuropeptides
physiological function
carboxypeptidase D is the only enzyme responsible for antibody C-terminal lysine cleavage in Chinese Hamster Ovary (CHO) cells
physiological function
Svr regulates the memory formation via insulin pathway in neurosecretory cells outside the mushroom body of brain
physiological function
Drosophila sp. (in: flies)
-
the carboxypeptidase D homolog silver regulates memory formation via insulin pathway in Drosophila
physiological function
together with the differences in pH optima, the different substrate specificities of CPD domains I and II allow the enzyme to perform distinct functions in the various locations within the cell
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
antisera raised against the N-terminal region of the 1A form and the C-terminal region of the tail-2 form of CPD
170000
180000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
hydrophobic regions at N-terminus and C- terminus, the latter being the transmembrane anchor
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of carboxypeptidase D domain II, sitting drop vapour diffusion method
-
crystal structure of duck carboxypeptidase D domain II in a complex with the peptidomimetic inhibitor guanidinoethylmercaptosuccinic acid, occupying the specificity pocket
-
three-dimensional-structure of carboxypeptidase D domain II in a complex with the peptidomimetic inhibitor, guanidinoethylmercaptosuccinic acid,occupying the specificity pocket
-
comparative modeling of the active sites of CPD domains I, II and III and molecular docking of peptide substrates
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
E350Q
E350Q/E762Q
E762Q
additional information
E350Q
critical active site residue in domain I, displays more than 50% activity from pH 5.0-7.5, similar to wild-type
E350Q
pH optimum of mutant enzyme is identical to wild-type enzyme, pH-range with 50% of maximal activity is pH 5.0-7.5 compared to pH 5.0-7.0 for wild-type enzyme
E350Q/E762Q
completely inactive towards all substrates and at all pH values tested
E350Q/E762Q
no detectable enzyme activity at any of the pH values examined
E762Q
critical active site residue in domain II, displays more than 50% activity from pH 6.5 to 7.5
E762Q
pH optimum of mutant enzyme is pH 7.0, compared to pH 6.5 for wild-type enzyme. pH-range with 50% of maximal activity is pH 6.5-7.5 compared to pH 5.0-7.0 for wild-type enzyme
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
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
additional information
-
a noninfectious pre-S deletion mutant devoid of the binding region for carboxypeptidase D can be rendered infectious for primary duck hepatocytes by treatment with chymotrypsin
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
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
additional information
svrPG33 mutants, do not survive past the early larval stage. These mutants have a P-element insertion within exon 1B upstream of the initiation ATG, which greatly reduces mRNA levels of all forms of CPD. Both svr1 and svrpoi mutants are viable, both deletions eliminate enzyme activity of the second CP-like domain and appear to cause the misfolding of the protein. This greatly reduces the levels of the long forms of CPD protein but do not affect the levels of the short forms
additional information
enzyme with mutations in both domains I and II is completely inactive towards all substrates and at all pH values
additional information
-
enzyme with mutations in both domains I and II is completely inactive towards all substrates and at all pH values
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
wild-type enzyme and various point mutants expressed in a baculovirus expression system
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
baculovirus expression of constructs containing either the 1A or the 1B form and one of three different sequences of domain 2 of CPD (wild type, mutants svr1, or svrpoi) in Sf9 cells
expressed by transient expression in a human kidney cell line and primary duck hepatocytes
human carboxypeptidase D (residues 32-1298) is cloned into the pTriExTM-7 expression vector that encodes an IgM secretion signal sequence and an N-terminal Strep-Tag II fusion protein. The CPD-pTrieX-7 construct ias transfected into mammalian HEK293F cells for transient expression, using polyethylenimine as transfection reagent
wild-type enzyme and point mutants are expressed at high levels in Sf9 cells using the baculovirus expression system
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
Drosophila CPD is encoded by the silver gene svr, which is differentially spliced to produce long transmembrane protein forms with three metallocarboxypeptidase-like domains and short soluble forms with a single metallocarboxypeptidase domain. Flies that retain the short form are viable, whereas flies that are missing all forms of CPD do not survive past the early larval stages
medicine
CpD is significantly downregulated in CD14 positive cells isolated from patients with lupus erythematosus. Moreover, it is shown that downregulation of CpD leads to downmodulation of TGF-beta itself, suggesting a role for CpD in a positive feedback loop, providing further evidence for a role of this enzyme in lupus erythematosus
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
medicine
-
CpD is part of an autoregulatory feedback loop in which it is both upstream and downstream of transforming growth factor-beta signaling
medicine
CpD is part of the transforming growth factor-beta pathway and is dysregulated in patients with Lupus erythematosus and other autoimmune diseases
medicine
CPE, probably in combination with CPD, has a functional role in normal placental development, specifically in control of giant cell and glycogen cell growth. In addition, Cpe together with Cpd is an upstream determinant of interspecies hybrid placental dysplasia, whose lack produces placental phenotypes reminiscent of interspecies hybrid placental dysplasia. Pathways regulated by these enzymes are not only important in placentation, but potentially also for speciation in the genus Mus
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
medicine
-
for infection of primary duck hepatocytes with duck hepatitis B virus, binding of the pre-S domain of the large surface protein to the cellular glycoprotein gp180 as a ubiquitous carboxypeptidase is required
medicine
CPD, nitrotyrosine, and proliferation marker Ki67 levels are higher in prostate cancer than in benign tissue and tend to colocalize, along with phospho-Stat5. The CPD-Arg-NO pathway may be involved in the regulation of prostate cancer cell proliferation
medicine
knocking out CpD gene expression provides one solution to eliminating C-terminal lysine heterogeneity for therapeutic antibody production
medicine
The CPD-Arg-nitric oxide pathway contributes to breast cancer progression in vitro and in vivo. There are progressive increases in CPD, nitrotyrosine, Ki67, and Cullin-3 from low levels in benign tissues to high levels in ductal carcinoma in situ, low-grade, high-grade, and triple-negative breast cancer. CPD and nitrotyrosine staining are closely associated, implicating CPD in nitric oxide production
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Song, L.; Fricker, L.D.
Tissue distribution and characterization of soluble and membrane-bound forms of metallocarboxypeptidase D
J. Biol. Chem.
271
28884-28889
1996
Bos taurus, Rattus norvegicus
brenda
Kuroki, K.; Eng, F.; Ishikawa, T.; Turck, C.; Harada, F.; Ganem, D.
Gp180, a host cell glycoprotein that binds duck hepatitis B virus particles, is encoded by a member of the carboxypeptidase gene family
J. Biol. Chem.
270
15022-15028
1995
Anas platyrhynchos
brenda
Song, L.; Fricker, L.D.
Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme from bovine pituitary
J. Biol. Chem.
270
25007-25013
1995
Bos taurus
brenda
Eng, F.J.; Novikova, E.G.; Kuroki, K.; Ganem, D.; Fricker, L.D.
gp180, A protein that binds duck hepatitis B virus particles, has metallocarboxypeptidase D-like enzymatic activities
J. Biol. Chem.
273
8382-8388
1998
Anas platyrhynchos
brenda
Xin, X.; Varlamov, O.; Day, R.; Bridgett, M.M.; Leiter, E.H.; Fricker, L.D.
Cloning and sequence analysis of cDNA encoding rat carboxypeptidase D
DNA Cell Biol.
16
897-909
1997
Rattus norvegicus
brenda
Tan, F.; Rehli, M.; Krause, S.W.; Skidgel, R.A.
Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains
Biochem. J.
327
81-87
1997
Homo sapiens
brenda
McGwire, G.B.; Tan, F.; Michael, B.; Rehli, M.; Skidgel, R.A.
Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein
Life Sci.
60
715-724
1997
Homo sapiens, Mus musculus
brenda
Kuroki, K.; Cheung, M.; Marion, P.L.; Ganem, D.
A cell surface protein that binds avian hepatitis B virus particles
J. Virol.
68
2091-2096
1994
Anas platyrhynchos
brenda
Gomis-Rth, F.X.; Companys, V.; Qian, Y.; Fricker, L.D.; Vendrell, J.; Aviles, F.X.; Coll, M.
Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily
EMBO J.
18
5817-5826
1999
Anas sp.
brenda
Aloy, P.; Companys, V.; Vendrell, J.; Aviles, F.X.; Fricker, L.D.; Coll, M.; Gomis-Ruth, F.X.
The crystal structure of the inhibitor-complexed carboxypeptidase D domain II and the modeling of regulatory carboxypeptidases
J. Biol. Chem.
276
16177-16184
2001
Anas sp.
brenda
Novikova, E.G.; Eng, F.J.; Yan, L.; Qian, Y.; Fricker, L.D.
Characterization of the enzymatic properties of the first and second domains of metallocarboxypeptidase D
J. Biol. Chem.
274
28887-28892
1999
Anas sp.
brenda
Spangenberg, H.C.; Lee, H.B.; Li, J.; Tan, F.; Skidgel, R.; Wands, J.R.; Tong, S.
A short sequence within domain C of duck carboxypeptidase D is critical for duck hepatitis B virus binding and determines host specificity
J. Virol.
75
10630-10642
2001
Anas sp.
brenda
O'Malley, P.G.; Sangster, S.M.; Abdelmagid, S.A.; Bearne, S.L.; Too, C.K.
Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells
Biochem. J.
390
665-673
2005
Rattus norvegicus, Rattus norvegicus (Q9JHW1)
brenda
Sidyelyeva, G.; Baker, N.E.; Fricker, L.D.
Characterization of the molecular basis of the Drosophila mutations in carboxypeptidase D. Effect on enzyme activity and expression
J. Biol. Chem.
281
13844-13852
2006
Drosophila melanogaster (P42787)
brenda
Kalinina, E.; Fontenele-Neto, J.D.; Fricker, L.D.
Drosophila S2 cells produce multiple forms of carboxypeptidase D with different intracellular distributions
J. Cell. Biochem.
3
770-783
2006
Drosophila melanogaster
brenda
Li, J.; Tong, S.; Lee, H.B.; Perdigoto, A.L.; Spangenberg, H.C.; Wands, J.R.
Glycine decarboxylase mediates a postbinding step in duck hepatitis B virus infection
J. Virol.
78
1873-1881
2004
Anas platyrhynchos
brenda
Singh, U.; Yu, Y.; Kalinina, E.; Konno, T.; Sun, T.; Ohta, H.; Wakayama, T.; Soares, M.J.; Hemberger, M.; Fundele, R.H.
Carboxypeptidase E in the mouse placenta
Differentiation
74
648-660
2006
Mus musculus (O89001)
brenda
Yamashita, M.; Sano, T.; Qian, Z.R.; Kovacs, K.; Horvath, E.
Diversity of ACTH- immunoreactive cells in the human adenohypophysis: an immunohistochemical study with special reference to cluster formation and follicular cell association
Endocr. Pathol.
17
155-164
2006
Homo sapiens
brenda
Hoff, N.P.; Degrandi, D.; Hengge, U.; Pfeffer, K.; Wurthner, J.U.
Carboxypeptidase D: a novel TGF-beta target gene dysregulated in patients with lupus erythematosus
J. Clin. Immunol.
27
568-579
2007
Homo sapiens, Homo sapiens (O75976), Mus musculus
brenda
Glebe, D.; Urban, S.
Viral and cellular determinants involved in hepadnaviral entry
World J. Gastroenterol.
13
22-38
2007
Anas platyrhynchos, Anas platyrhynchos (Q90240), Gallus gallus, Homo sapiens, Mus musculus
brenda
Maenz, C.; Chang, S.F.; Iwanski, A.; Bruns, M.
Entry of duck hepatitis B virus into primary duck liver and kidney cells after discovery of a fusogenic region within the large surface protein
J. Virol.
81
5014-5023
2007
Anas platyrhynchos
brenda
Abdelmagid, S.A.; Too, C.K.
Prolactin and estrogen up-regulate carboxypeptidase-D to promote nitric oxide production and survival of MCF-7 breast cancer cells
Endocrinology
149
4821-4828
2008
Homo sapiens
brenda
Sidyelyeva, G.; Wegener, C.; Schoenfeld, B.P.; Bell, A.J.; Baker, N.E.; McBride, S.M.; Fricker, L.D.
Individual carboxypeptidase D domains have both redundant and unique functions in Drosophila development and behavior
Cell. Mol. Life Sci.
67
2991-3004
2010
Drosophila melanogaster (P42787)
brenda
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
J. Virol.
84
4569-4578
2010
Anas platyrhynchos (Q90240), Anas platyrhynchos
brenda
Jin, T.; Fu, J.; Feng, X.J.; Wang, S.M.; Huang, X.; Zhu, M.H.; Zhang, S.H.
SiRNA-targeted carboxypeptidase D inhibits hepatocellular carcinoma growth
Cell Biol. Int.
37
929-939
2013
Homo sapiens
brenda
Hu, Z.; Zhang, H.; Haley, B.; Macchi, F.; Yang, F.; Misaghi, S.; Elich, J.; Yang, R.; Tang, Y.; Joly, J.C.; Snedecor, B.R.; Shen, A.
Carboxypeptidase D is the only enzyme responsible for antibody C-terminal lysine cleavage in Chinese hamster ovary (CHO) cells
Biotechnol. Bioeng.
113
2100-2106
2016
Cricetulus griseus (G3HR95)
brenda
Thomas, L.N.; Chedrawe, E.R.; Barnes, P.J.; Too, C.K.L.
Prolactin/androgen-inducible carboxypeptidase-D increases with nitrotyrosine and Ki67 for breast cancer progression in vivo, and upregulates progression markers VEGF-C and Runx2 in vitro
Breast Cancer Res. Treat.
164
27-40
2017
Homo sapiens (O75976), Homo sapiens
brenda
Li, J.; Tong, S.
From DCPD to NTCP the long journey towards identifying a functional hepatitis B virus receptor
Clin. Mol. Hepatol.
21
193-199
2015
Anas sp.
brenda
Garcia-Pardo, J.; Tanco, S.; Diaz, L.; Dasgupta, S.; Fernandez-Recio, J.; Lorenzo, J.; Aviles, F.X.; Fricker, L.D.
Substrate specificity of human metallocarboxypeptidase D Comparison of the two active carboxypeptidase domains
PLoS ONE
12
e0187778
2017
Homo sapiens (O75976), Homo sapiens
brenda
Thomas, L.N.; Merrimen, J.; Bell, D.G.; Rendon, R.; Too, C.K.
Prolactin- and testosterone-induced carboxypeptidase-D correlates with increased nitrotyrosines and Ki67 in prostate cancer
Prostate
75
1726-1736
2015
Homo sapiens (O75976)
brenda
Lu, B.; Zhao, Y.; Zhao, J.; Yao, X.; Shuai, Y.; Ma, W.; Zhong, Y.
The carboxypeptidase D homolog silver regulates memory formation via insulin pathway in Drosophila
Protein Cell
7
606-610
2016
Drosophila melanogaster (P42787), Drosophila sp. (in: flies)
brenda
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