CPD (gene): Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Carboxypeptidase D''' is an [[enzyme]] that in humans is encoded by the ''CPD'' [[gene]].<ref name="pmid9628828">{{cite journal | vauthors = Riley DA, Tan F, Miletich DJ, Skidgel RA | title = Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1) | journal = Genomics | volume = 50 | issue = 1 | pages = 105–8 | date = May 1998 | pmid = 9628828 | pmc =  | doi = 10.1006/geno.1998.5295 }}</ref><ref name="pmid9355738">{{cite journal | vauthors = Tan F, Rehli M, Krause SW, Skidgel RA | title = Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains | journal = The Biochemical Journal | volume = 327 ( Pt 1) | issue = Pt 1 | pages = 81–7 | date = Oct 1997 | pmid = 9355738 | pmc = 1218766 | doi = }}</ref><ref name="entrez"/>
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Carboxypeptidase D
| HGNCid = 2301
| Symbol = CPD
| AltSymbols =;
| OMIM = 603102
| ECnumber = 
| Homologene = 999
| MGIid = 107265
| GeneAtlas_image1 = PBB_GE_CPD_201941_at_tn.png
| GeneAtlas_image2 = PBB_GE_CPD_201940_at_tn.png
| GeneAtlas_image3 = PBB_GE_CPD_201942_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004180 |text = carboxypeptidase activity}} {{GNF_GO|id=GO:0004182 |text = carboxypeptidase A activity}} {{GNF_GO|id=GO:0004187 |text = carboxypeptidase D activity}} {{GNF_GO|id=GO:0008237 |text = metallopeptidase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008472 |text = metallocarboxypeptidase D activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1362
    | Hs_Ensembl = ENSG00000108582
    | Hs_RefseqProtein = NP_001295
    | Hs_RefseqmRNA = NM_001304
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 25730110
    | Hs_GenLoc_end = 25819825
    | Hs_Uniprot = O75976
    | Mm_EntrezGene = 12874
    | Mm_Ensembl = ENSMUSG00000020841
    | Mm_RefseqmRNA = XM_001001063
    | Mm_RefseqProtein = XP_001001063
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 76598184
    | Mm_GenLoc_end = 76663191
    | Mm_Uniprot = Q5SVH8
  }}
}}
'''Carboxypeptidase D''', also known as '''CPD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CPD carboxypeptidase D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1362| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
The [[metallocarboxypeptidase]] family of enzymes is divided into 2 subfamilies based on sequence similarities: the pancreatic [[carboxypeptidase]]-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a [[hepatitis B]] virus binding protein. [[Transcript variant]]s utilizing alternative [[polyadenylation]] signals exist for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CPD carboxypeptidase D| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1362| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = The metallocarboxypeptidase family of enzymes is divided into 2 subfamilies based on sequence similarities. The pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a hepatitis B virus-binding protein. Transcript variants utilizing alternative polyadenylation signals exist for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: CPD carboxypeptidase D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1362| accessdate = }}</ref>
}}


==References==
== References ==
{{reflist|2}}
{{reflist}}
==Further reading==
 
==External links==
* {{UCSC gene info|CPD}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA | title = A "double adaptor" method for improved shotgun library construction | journal = Analytical Biochemistry | volume = 236 | issue = 1 | pages = 107–13 | date = Apr 1996 | pmid = 8619474 | doi = 10.1006/abio.1996.0138 }}
| citations =
* {{cite journal | vauthors = McGwire GB, Tan F, Michel B, Rehli M, Skidgel RA | title = Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein | journal = Life Sciences | volume = 60 | issue = 10 | pages = 715–24 | year = 1997 | pmid = 9064476 | doi = 10.1016/S0024-3205(96)00642-X }}
*{{cite journal | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
* {{cite journal | vauthors = Varlamov O, Fricker LD | title = Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: localization to the trans-Golgi network and recycling from the cell surface | journal = Journal of Cell Science | volume = 111 ( Pt 7) | issue = 7 | pages = 877–85 | date = Apr 1998 | pmid = 9490632 | doi =  }}
*{{cite journal | author=McGwire GB, Tan F, Michel B, ''et al.'' |title=Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein. |journal=Life Sci. |volume=60 |issue= 10 |pages= 715-24 |year= 1997 |pmid= 9064476 |doi= }}
* {{cite journal | vauthors = Ishikawa T, Murakami K, Kido Y, Ohnishi S, Yazaki Y, Harada F, Kuroki K | title = Cloning, functional expression, and chromosomal localization of the human and mouse gp180-carboxypeptidase D-like enzyme | journal = Gene | volume = 215 | issue = 2 | pages = 361–70 | date = Jul 1998 | pmid = 9714835 | doi = 10.1016/S0378-1119(98)00270-4 }}
*{{cite journal  | author=Tan F, Rehli M, Krause SW, Skidgel RA |title=Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains. |journal=Biochem. J. |volume=327 ( Pt 1) |issue=  |pages= 81-7 |year= 1997 |pmid= 9355738 |doi=  }}
* {{cite journal | vauthors = Reznik SE, Salafia CM, Lage JM, Fricker LD | title = Immunohistochemical localization of carboxypeptidases E and D in the human placenta and umbilical cord | journal = The Journal of Histochemistry and Cytochemistry | volume = 46 | issue = 12 | pages = 1359–68 | date = Dec 1998 | pmid = 9815277 | doi = 10.1177/002215549804601204 }}
*{{cite journal | author=Varlamov O, Fricker LD |title=Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: localization to the trans-Golgi network and recycling from the cell surface. |journal=J. Cell. Sci. |volume=111 ( Pt 7) |issue= |pages= 877-85 |year= 1998 |pmid= 9490632 |doi=  }}
* {{cite journal | vauthors = Hadkar V, Skidgel RA | title = Carboxypeptidase D is up-regulated in raw 264.7 macrophages and stimulates nitric oxide synthesis by cells in arginine-free medium | journal = Molecular Pharmacology | volume = 59 | issue = 5 | pages = 1324–32 | date = May 2001 | pmid = 11306718 | doi =  }}
*{{cite journal | author=Riley DA, Tan F, Miletich DJ, Skidgel RA |title=Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1). |journal=Genomics |volume=50 |issue= 1 |pages= 105-8 |year= 1999 |pmid= 9628828 |doi= 10.1006/geno.1998.5295 }}
* {{cite journal | vauthors = Fan X, Olson SJ, Blevins LS, Allen GS, Johnson MD | title = Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary | journal = The Journal of Histochemistry and Cytochemistry | volume = 50 | issue = 11 | pages = 1509–16 | date = Nov 2002 | pmid = 12417617 | doi = 10.1177/002215540205001111 }}
*{{cite journal  | author=Ishikawa T, Murakami K, Kido Y, ''et al.'' |title=Cloning, functional expression, and chromosomal localization of the human and mouse gp180-carboxypeptidase D-like enzyme. |journal=Gene |volume=215 |issue= 2 |pages= 361-70 |year= 1998 |pmid= 9714835 |doi= }}
* {{cite journal | vauthors = Kalinina EV, Fricker LD | title = Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking | journal = The Journal of Biological Chemistry | volume = 278 | issue = 11 | pages = 9244–9 | date = Mar 2003 | pmid = 12643288 | doi = 10.1074/jbc.M209379200 }}
*{{cite journal | author=Reznik SE, Salafia CM, Lage JM, Fricker LD |title=Immunohistochemical localization of carboxypeptidases E and D in the human placenta and umbilical cord. |journal=J. Histochem. Cytochem. |volume=46 |issue= 12 |pages= 1359-68 |year= 1999 |pmid= 9815277 |doi= }}
* {{cite journal | vauthors = Zhang H, Li XJ, Martin DB, Aebersold R | title = Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry | journal = Nature Biotechnology | volume = 21 | issue = 6 | pages = 660–6 | date = Jun 2003 | pmid = 12754519 | doi = 10.1038/nbt827 }}
*{{cite journal | author=Hadkar V, Skidgel RA |title=Carboxypeptidase D is up-regulated in raw 264.7 macrophages and stimulates nitric oxide synthesis by cells in arginine-free medium. |journal=Mol. Pharmacol. |volume=59 |issue= 5 |pages= 1324-32 |year= 2001 |pmid= 11306718 |doi=  }}
* {{cite journal | vauthors = O'Malley PG, Sangster SM, Abdelmagid SA, Bearne SL, Too CK | title = Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells | journal = The Biochemical Journal | volume = 390 | issue = Pt 3 | pages = 665–73 | date = Sep 2005 | pmid = 15918796 | pmc = 1199659 | doi = 10.1042/BJ20050025 }}
*{{cite journal | author=Fan X, Olson SJ, Blevins LS, ''et al.'' |title=Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary. |journal=J. Histochem. Cytochem. |volume=50 |issue= 11 |pages= 1509-16 |year= 2003 |pmid= 12417617 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Kalinina EV, Fricker LD |title=Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking. |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9244-9 |year= 2003 |pmid= 12643288 |doi= }}
*{{cite journal | author=Zhang H, Li XJ, Martin DB, Aebersold R |title=Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. |journal=Nat. Biotechnol. |volume=21 |issue= 6 |pages= 660-6 |year= 2003 |pmid= 12754519 |doi= 10.1038/nbt827 }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=O'Malley PG, Sangster SM, Abdelmagid SA, ''et al.'' |title=Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells. |journal=Biochem. J. |volume=390 |issue= Pt 3 |pages= 665-73 |year= 2006 |pmid= 15918796 |doi= 10.1042/BJ20050025 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{gene-17-stub}}
{{WikiDoc Sources}}

Revision as of 09:59, 30 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Carboxypeptidase D is an enzyme that in humans is encoded by the CPD gene.[1][2][3]

Function

The metallocarboxypeptidase family of enzymes is divided into 2 subfamilies based on sequence similarities: the pancreatic carboxypeptidase-like and the regulatory B-type carboxypeptidase subfamilies. Carboxypeptidase D has been identified as a regulatory B-type carboxypeptidase. CPD is a homolog of duck gp180, a hepatitis B virus binding protein. Transcript variants utilizing alternative polyadenylation signals exist for this gene.[3]

References

  1. ↑ Riley DA, Tan F, Miletich DJ, Skidgel RA (May 1998). "Chromosomal localization of the genes for human carboxypeptidase D (CPD) and the active 50-kilodalton subunit of human carboxypeptidase N (CPN1)". Genomics. 50 (1): 105–8. doi:10.1006/geno.1998.5295. PMID 9628828.
  2. ↑ Tan F, Rehli M, Krause SW, Skidgel RA (Oct 1997). "Sequence of human carboxypeptidase D reveals it to be a member of the regulatory carboxypeptidase family with three tandem active site domains". The Biochemical Journal. 327 ( Pt 1) (Pt 1): 81–7. PMC 1218766. PMID 9355738.
  3. ↑ 3.0 3.1 "Entrez Gene: CPD carboxypeptidase D".

External links

Further reading

  • Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (Apr 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
  • McGwire GB, Tan F, Michel B, Rehli M, Skidgel RA (1997). "Identification of a membrane-bound carboxypeptidase as the mammalian homolog of duck gp180, a hepatitis B virus-binding protein". Life Sciences. 60 (10): 715–24. doi:10.1016/S0024-3205(96)00642-X. PMID 9064476.
  • Varlamov O, Fricker LD (Apr 1998). "Intracellular trafficking of metallocarboxypeptidase D in AtT-20 cells: localization to the trans-Golgi network and recycling from the cell surface". Journal of Cell Science. 111 ( Pt 7) (7): 877–85. PMID 9490632.
  • Ishikawa T, Murakami K, Kido Y, Ohnishi S, Yazaki Y, Harada F, Kuroki K (Jul 1998). "Cloning, functional expression, and chromosomal localization of the human and mouse gp180-carboxypeptidase D-like enzyme". Gene. 215 (2): 361–70. doi:10.1016/S0378-1119(98)00270-4. PMID 9714835.
  • Reznik SE, Salafia CM, Lage JM, Fricker LD (Dec 1998). "Immunohistochemical localization of carboxypeptidases E and D in the human placenta and umbilical cord". The Journal of Histochemistry and Cytochemistry. 46 (12): 1359–68. doi:10.1177/002215549804601204. PMID 9815277.
  • Hadkar V, Skidgel RA (May 2001). "Carboxypeptidase D is up-regulated in raw 264.7 macrophages and stimulates nitric oxide synthesis by cells in arginine-free medium". Molecular Pharmacology. 59 (5): 1324–32. PMID 11306718.
  • Fan X, Olson SJ, Blevins LS, Allen GS, Johnson MD (Nov 2002). "Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary". The Journal of Histochemistry and Cytochemistry. 50 (11): 1509–16. doi:10.1177/002215540205001111. PMID 12417617.
  • Kalinina EV, Fricker LD (Mar 2003). "Palmitoylation of carboxypeptidase D. Implications for intracellular trafficking". The Journal of Biological Chemistry. 278 (11): 9244–9. doi:10.1074/jbc.M209379200. PMID 12643288.
  • Zhang H, Li XJ, Martin DB, Aebersold R (Jun 2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nature Biotechnology. 21 (6): 660–6. doi:10.1038/nbt827. PMID 12754519.
  • O'Malley PG, Sangster SM, Abdelmagid SA, Bearne SL, Too CK (Sep 2005). "Characterization of a novel, cytokine-inducible carboxypeptidase D isoform in haematopoietic tumour cells". The Biochemical Journal. 390 (Pt 3): 665–73. doi:10.1042/BJ20050025. PMC 1199659. PMID 15918796.
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