Carboxypeptidase A6

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Aliases CPA6, CPAH, ETL5, FEB11, carboxypeptidase A6
External IDs MGI: 3045348 HomoloGene: 75130 GeneCards: CPA6
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 8: 67.42 – 67.75 Mb Chr 1: 10.32 – 10.72 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Carboxypeptidase A6 (CPA6) is an metallocarboxypeptidase enzyme that in humans is encoded by the CPA6 gene.[3] It is highly expressed in the adult mouse olfactory bulb and is broadly expressed in the embryonic brain and other tissues.[4]

The protein encoded by this gene belongs to the family of carboxypeptidases, which catalyze the release of C-terminal amino acid, and have functions ranging from digestion of food to selective biosynthesis of neuroendocrine peptides. Polymorphic variants and a reciprocal translocation t(6;8)(q26;q13) involving this gene, have been associated with Duane retraction syndrome.[3]

CPA6 processes several neuropeptides, including [Met]- and [Leu]enkephalin, angiotensin I, and neurotensin in vitro.[4] Whereas CPA6 is capable of converting the enkephalins and neurotensin into inactive forms, it can convert the inactive angiotensin I into the active angiotensin II.[4] CPA6 may have additional roles in processing peptides and proteins in vivo, but the nature of these substrates and the effects of these cleavages are currently unknown.

See also[edit]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b "Entrez Gene: Carboxypeptidase A6". Retrieved 2011-11-25. 
  4. ^ a b c Lyons PJ, Callaway MB, Fricker LD (March 2008). "Characterization of carboxypeptidase A6, an extracellular matrix peptidase". The Journal of Biological Chemistry. 283 (11): 7054–63. PMID 18178555. doi:10.1074/jbc.M707680200. 

Further reading[edit]

  • Wei, S.; Segura, S.; Vendrell, J.; Aviles, F. X.; Lanoue, E.; Day, R.; Feng, Y.; Fricker, L. D. (2002). "Identification and characterization of three members of the human metallocarboxypeptidase gene family". The Journal of Biological Chemistry. 277 (17): 14954–14964. PMID 11836249. doi:10.1074/jbc.M112254200. 
  • Pizzuti, A.; Calabrese, G.; Bozzali, M.; Telvi, L.; Morizio, E.; Guida, V.; Gatta, V.; Stuppia, L.; Ion, A.; Palka, G.; Dallapiccola, B. (2002). "A peptidase gene in chromosome 8q is disrupted by a balanced translocation in a duane syndrome patient". Investigative Ophthalmology & Visual Science. 43 (12): 3609–3612. PMID 12454025. 
  • Lyons, P. J.; Callaway, M. B.; Fricker, L. D. (2008). "Characterization of Carboxypeptidase A6, an Extracellular Matrix Peptidase". Journal of Biological Chemistry. 283 (11): 7054–7063. PMID 18178555. doi:10.1074/jbc.M707680200. 
  • Sharif, S. A.; Du, X.; Myles, T.; Song, J. J.; Price, E.; Lee, D. M.; Goodman, S. B.; Nagashima, M.; Morser, J.; Robinson, W. H.; Leung, L. L. K. (2009). "Thrombin-activatable carboxypeptidase B cleavage of osteopontin regulates neutrophil survival and synoviocyte binding in rheumatoid arthritis". Arthritis & Rheumatism. 60 (10): 2902–2912. PMID 19790060. doi:10.1002/art.24814. 
  • Lyons, P. J.; Fricker, L. D. (2010). "Substrate Specificity of Human Carboxypeptidase A6". Journal of Biological Chemistry. 285 (49): 38234–38242. PMC 2992257Freely accessible. PMID 20855895. doi:10.1074/jbc.M110.158626. 

External links[edit]