Carboxypeptidase A6

CPA6
Identifiers
AliasesCPA6, CPAH, ETL5, FEB11, carboxypeptidase A6
External IDsMGI: 3045348 HomoloGene: 75130 GeneCards: CPA6
Orthologs
SpeciesHumanMouse
Entrez

57094

329093

Ensembl

ENSG00000165078

ENSMUSG00000042501

UniProt

Q8N4T0

Q5U901

RefSeq (mRNA)

NM_001127445
NM_020361

NM_001289497
NM_177834

RefSeq (protein)

NP_065094

NP_001276426
NP_808502

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

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. 1 2 "Entrez Gene: Carboxypeptidase A6". Retrieved 2011-11-25.
  4. 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. PMID 18178555. doi:10.1074/jbc.M707680200.

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. 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 2992257 Freely accessible. PMID 20855895. doi:10.1074/jbc.M110.158626. 


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