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; OMA:CPA6 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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: 10.39 – 10.79 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

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000165078Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000042501Ensembl, 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. ^ a b "Entrez Gene: Carboxypeptidase A6". Retrieved 2011-11-25.
  6. ^ 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. doi:10.1074/jbc.M707680200. PMID 18178555.

Further reading

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