Carboxypeptidase A6
Template:PBB/57094
| Carboxypeptidase A6 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | CPA6; CBPA6; CPAH | ||||||||||||
| External IDs | OMIM: 609562 HomoloGene: 75130 GeneCards: Gene | ||||||||||||
| EC number | 3.4.17.1 | ||||||||||||
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| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 57094 | 329093 | |||||||||||
| Ensembl | ENSG00000165078 | ENSMUSG00000042501 | |||||||||||
| UniProt | Q8N4T0 | Q5U901 | |||||||||||
| RefSeq (mRNA) | n/a | NM_177834.3 | |||||||||||
| RefSeq (protein) | NP_065094.3 | NP_808502.2 | |||||||||||
| Location (UCSC) |
Chr 8: 68.33 – 68.66 Mb |
Chr 1: 10.31 – 10.71 Mb | |||||||||||
| PubMed search | |||||||||||||
Carboxypeptidase A6 (CPA6) is an metallocarboxypeptidase enzyme that in humans is encoded by the CPA6 gene.[1] It is highly expressed in the adult mouse olfactory bulb and is broadly expressed in the embryonic brain and other tissues.[2]
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.[1]
CPA6 processes several neuropeptides, including [Met]- and [Leu]enkephalin, angiotensin I, and neurotensin in vitro.[2] 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.[2] 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
References
- 1 2 "Entrez Gene: Carboxypeptidase A6". Retrieved 2011-11-25.
- 1 2 3 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. doi:10.1074/jbc.M707680200. PMID 18178555.
Further reading
- 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. doi:10.1074/jbc.M112254200. PMID 11836249.
- 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. doi:10.1074/jbc.M707680200. PMID 18178555.
- 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. doi:10.1002/art.24814. PMID 19790060.
- Lyons, P. J.; Fricker, L. D. (2010). "Substrate Specificity of Human Carboxypeptidase A6". Journal of Biological Chemistry 285 (49): 38234–38242. doi:10.1074/jbc.M110.158626. PMC 2992257. PMID 20855895.
External links
- CPA6 at the US National Library of Medicine Medical Subject Headings (MeSH)
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