Carboxypeptidase A6

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]

CPA6
Identifiers
AliasesCPA6, CPAH, ETL5, FEB11, carboxypeptidase A6
External IDsOMIM: 609562 MGI: 3045348 HomoloGene: 75130 GeneCards: CPA6
Gene location (Human)
Chr.Chromosome 8 (human)[1]
Band8q13.2Start67,422,038 bp[1]
End67,746,378 bp[1]
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[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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


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