Carboxypeptidase A6

Details

Name
Carboxypeptidase A6
Synonyms
  • 3.4.17.-
  • CPAH
Gene Name
CPA6
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052489|Carboxypeptidase A6
MKCLGKRRGQAAAFLPLCWLFLKILQPGHSHLYNNRYAGDKVIRFIPKTEEEAYALKKIS
YQLKVDLWQPSSISYVSEGTVTDVHIPQNGSRALLAFLQEANIQYKVLIEDLQKTLEKGS
SLHTQRNRRSLSGYNYEVYHSLEEIQNWMHHLNKTHSGLIHMFSIGRSYEGRSLFILKLG
RRSRLKRAVWIDCGIHAREWIGPAFCQWFVKEALLTYKSDPAMRKMLNHLYFYIMPVFNV
DGYHFSWTNDRFWRKTRSRNSRFRCRGVDANRNWKVKWCDEGASMHPCDDTYCGPFPESE
PEVKAVANFLRKHRKHIRAYLSFHAYAQMLLYPYSYKYATIPNFRCVESAAYKAVNALQS
VYGVRYRYGPASTTLYVSSGSSMDWAYKNGIPYAFAFELRDTGYFGFLLPEMLIKPTCTE
TMLAVKNITMHLLKKCP
Number of residues
437
Molecular Weight
51007.48
Theoretical pI
Not Available
GO Classification
Functions
metallocarboxypeptidase activity / zinc ion binding
Processes
proteolysis
Components
extracellular space
General Function
May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II (PubMed:18178555). Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine (PubMed:20855895).
Specific Function
Metallocarboxypeptidase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0052490|Carboxypeptidase A6 (CPA6)
ATGAAGTGTCTCGGGAAGCGCAGGGGCCAGGCAGCTGCTTTCCTGCCTCTTTGCTGGCTC
TTTTTGAAGATTCTGCAACCGGGGCACAGCCACCTTTATAACAACCGCTATGCTGGTGAT
AAAGTGATAAGATTTATTCCCAAAACAGAAGAGGAAGCATATGCACTGAAGAAAATATCC
TATCAACTTAAGGTGGACCTGTGGCAGCCCAGCAGTATCTCCTATGTATCAGAGGGAACA
GTTACTGATGTCCATATCCCCCAAAATGGTTCCCGAGCCCTGTTAGCCTTCTTACAGGAA
GCCAACATCCAGTACAAGGTCCTCATAGAAGATCTTCAGAAAACACTGGAGAAGGGAAGC
AGCTTGCACACCCAGAGAAACCGAAGATCCCTCTCTGGATATAATTATGAAGTTTATCAC
TCCTTAGAAGAAATTCAAAATTGGATGCATCATCTGAATAAAACTCACTCAGGCCTCATT
CACATGTTCTCTATTGGAAGATCATATGAGGGAAGATCTCTTTTTATTTTAAAGCTGGGC
AGACGATCACGACTCAAAAGAGCTGTTTGGATAGACTGTGGTATTCATGCAAGAGAATGG
ATTGGTCCTGCCTTTTGTCAGTGGTTTGTAAAAGAAGCTCTTCTAACATATAAGAGTGAC
CCAGCCATGAGAAAAATGTTGAATCATCTATATTTCTATATCATGCCTGTGTTTAACGTC
GATGGATACCATTTTAGTTGGACCAATGATCGATTTTGGAGAAAAACAAGGTCAAGGAAC
TCAAGGTTTCGCTGCCGTGGAGTGGATGCCAATAGAAACTGGAAAGTGAAGTGGTGTGAT
GAAGGAGCTTCTATGCACCCTTGTGATGACACATACTGTGGCCCTTTTCCAGAATCTGAG
CCGGAAGTGAAGGCTGTAGCTAACTTCCTTCGAAAACACAGAAAGCACATTAGGGCTTAT
CTCTCCTTTCATGCATATGCTCAGATGTTACTGTATCCCTATTCTTACAAATATGCAACA
ATTCCCAATTTTAGATGTGTGGAATCTGCAGCTTATAAAGCTGTGAATGCACTTCAGTCA
GTATACGGGGTACGATACAGATATGGACCAGCCTCCACAACGTTGTATGTGAGCTCTGGT
AGCTCAATGGATTGGGCCTACAAAAATGGAATACCTTATGCATTTGCTTTCGAACTACGT
GACACTGGATATTTTGGATTTTTACTCCCAGAGATGCTCATCAAACCCACCTGTACAGAA
ACTATGCTGGCTGTGAAAAATATCACAATGCACCTGCTAAAGAAATGTCCCTGA
Chromosome Location
8
Locus
8q13.2
External Identifiers
ResourceLink
UniProtKB IDQ8N4T0
UniProtKB Entry NameCBPA6_HUMAN
HGNC IDHGNC:17245
General References
  1. Wei S, Segura S, Vendrell J, Aviles FX, Lanoue E, Day R, Feng Y, Fricker LD: Identification and characterization of three members of the human metallocarboxypeptidase gene family. J Biol Chem. 2002 Apr 26;277(17):14954-64. doi: 10.1074/jbc.M112254200. Epub 2002 Feb 8. [Article]
  2. Pizzuti A, Calabrese G, Bozzali M, Telvi L, Morizio E, Guida V, Gatta V, Stuppia L, Ion A, Palka G, Dallapiccola B: A peptidase gene in chromosome 8q is disrupted by a balanced translocation in a duane syndrome patient. Invest Ophthalmol Vis Sci. 2002 Dec;43(12):3609-12. [Article]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [Article]
  4. Lyons PJ, Callaway MB, Fricker LD: Characterization of carboxypeptidase A6, an extracellular matrix peptidase. J Biol Chem. 2008 Mar 14;283(11):7054-63. doi: 10.1074/jbc.M707680200. Epub 2008 Jan 4. [Article]
  5. Lyons PJ, Fricker LD: Substrate specificity of human carboxypeptidase A6. J Biol Chem. 2010 Dec 3;285(49):38234-42. doi: 10.1074/jbc.M110.158626. Epub 2010 Sep 20. [Article]
  6. Salzmann A, Guipponi M, Lyons PJ, Fricker LD, Sapio M, Lambercy C, Buresi C, Ouled Amar Bencheikh B, Lahjouji F, Ouazzani R, Crespel A, Chaigne D, Malafosse A: Carboxypeptidase A6 gene (CPA6) mutations in a recessive familial form of febrile seizures and temporal lobe epilepsy and in sporadic temporal lobe epilepsy. Hum Mutat. 2012 Jan;33(1):124-35. doi: 10.1002/humu.21613. Epub 2011 Oct 31. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB12668MetenkefalininvestigationalunknownsubstrateDetails