CPD (gene)

CPD
Identifiers
Aliases	CPD , GP180, carboxypeptidase D
External IDs	OMIM: 603102; MGI: 107265; HomoloGene: 999; GeneCards: CPD; OMA:CPD - orthologs
Gene location (Human) Chr. Chromosome 17 (human) [1] Band 17q11.2 Start 30,378,927 bp [1] End 30,469,989 bp [1]
Gene location (Mouse) Chr. Chromosome 11 (mouse) [2] Band 11 B5|11 46.05 cM Start 76,669,250 bp [2] End 76,737,844 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in parotid gland islet of Langerhans bronchial epithelial cell nasal epithelium Achilles tendon pancreatic ductal cell sperm epithelium of colon gallbladder stromal cell of endometrium Top expressed in submandibular gland parotid gland lacrimal gland epithelium of stomach mucous cell of stomach left colon decidua stria vascularis corneal stroma seminal vesicula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function carboxypeptidase activity zinc ion binding peptidase activity hydrolase activity metallopeptidase activity metal ion binding metallocarboxypeptidase activity serine-type carboxypeptidase activity Cellular component integral component of membrane plasma membrane extracellular exosome membrane extracellular space Biological process protein processing peptide metabolic process proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1362 12874 Ensembl ENSG00000108582 ENSMUSG00000020841 UniProt O75976 O89001 RefSeq (mRNA) NM_001199775 NM_001304 NM_007754 RefSeq (protein) NP_001186704 NP_001295 NP_031780 Location (UCSC) Chr 17: 30.38 – 30.47 Mb Chr 11: 76.67 – 76.74 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Carboxypeptidase D is an enzyme that in humans is encoded by the CPD gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000108582 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020841 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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. doi:10.1042/bj3270081. PMC   1218766 . PMID   9355738.
7. "Entrez Gene: CPD carboxypeptidase D".

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. doi:10.1242/jcs.111.7.877. 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. doi:10.1124/mol.59.5.1324. PMID   11306718. S2CID   10456432.
• 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. S2CID   581283.
• 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.

External links

• Human CPD genome location and CPD gene details page in the UCSC Genome Browser .