Carboxypeptidase A6

CPA6
Identifiers
Aliases	CPA6 , CPAH, ETL5, FEB11, carboxypeptidase A6
External IDs	OMIM: 609562; MGI: 3045348; HomoloGene: 75130; GeneCards: CPA6; OMA:CPA6 - orthologs
Gene location (Human) Chr. Chromosome 8 (human) [1] Band 8q13.2 Start 67,422,038 bp [1] End 67,746,378 bp [1]
Gene location (Mouse) Chr. Chromosome 1 (mouse) [2] Band 1|1 A2 Start 10,394,945 bp [2] End 10,790,170 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell mucosa of transverse colon urethra rectum epithelium of colon prostate vagina tibia mucosa of sigmoid colon smooth muscle tissue Top expressed in otolith organ utricle calvaria lumbar subsegment of spinal cord tail of embryo spermatid inferior olivary nucleus umbilical cord seminiferous tubule stroma of bone marrow More reference expression data BioGPS n/a
Gene ontology Molecular function carboxypeptidase activity zinc ion binding peptidase activity hydrolase activity metallopeptidase activity metal ion binding metallocarboxypeptidase activity Cellular component extracellular region extracellular space Biological process proteolysis Sources:Amigo / QuickGO
Orthologs Species Human Mouse 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 Mb Chr 1: 10.39 – 10.79 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Carboxypeptidase A6 (CPA6) is a metallocarboxypeptidase enzyme that in humans is encoded by the CPA6 gene. ^[5] It is highly expressed in the adult mouse olfactory bulb and is broadly expressed in the embryonic brain and other tissues. ^[6]

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. ^[5]

CPA6 processes several neuropeptides, including [Met]- and [Leu]-enkephalin, angiotensin I, and neurotensin in vitro. ^[6] 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. ^[6] 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

• Carboxypeptidase A inhibitor
• Carboxypeptidase

References

1. GRCh38: Ensembl release 89: ENSG00000165078 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000042501 – 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. "Entrez Gene: Carboxypeptidase A6" . Retrieved 2011-11-25.
6. 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. PMC   3757557 . 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 U.S. National Library of Medicine Medical Subject Headings (MeSH)