DNPEP

Aspartyl aminopeptidase
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4DYO​
Identifiers
Symbols	DNPEP ; ASPEP; DAP
External IDs	OMIM: 611367 MGI: 1278328 HomoloGene: 6110 ChEMBL: 2761 GeneCards: DNPEP Gene
EC number	3.4.11.21
Gene ontology Molecular function • aminopeptidase activity • protein binding • metallopeptidase activity • zinc ion binding Cellular component • nucleus • nucleoplasm • cytoplasm • blood microparticle Biological process • proteolysis • peptide metabolic process Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23549	13437
Ensembl	ENSG00000123992	ENSMUSG00000026209
UniProt	Q9ULA0	Q9Z2W0
RefSeq (mRNA)	NM_012100	NM_001110831
RefSeq (protein)	NP_036232	NP_001104301
Location (UCSC)	Chr 2: 219.37 – 219.4 Mb	Chr 1: 75.31 – 75.32 Mb
PubMed search

Aspartyl aminopeptidase is an enzyme that in humans is encoded by the DNPEP gene.^[1][2]

Function

The protein encoded by this gene is an aminopeptidase which prefers acidic amino acids, and specifically favors aspartic acid over glutamic acid. It is thought to be a cytosolic protein involved in general metabolism of intracellular proteins.^[2]

Model organisms

Model organisms have been used in the study of DNPEP function. A conditional knockout mouse line called Dnpep^{tm1e(EUCOMM)Wtsi} was generated at the Wellcome Trust Sanger Institute.^[3] Male and female animals underwent a standardized phenotypic screen^[4] to determine the effects of deletion.^[5][6][7][8] Additional screens performed: - In-depth immunological phenotyping^[9]

Dnpep knockout mouse phenotype

Characteristic	Phenotype
All data available at.[4][9]
Peripheral blood leukocytes 6 Weeks	Normal
Insulin	Normal
Haematology 6 Weeks	Normal
Homozygous viability at P14	Normal
Homozygous Fertility	Normal
Body weight	Normal
Neurological assessment	Normal
Grip strength	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Haematology 16 Weeks	Normal
Peripheral blood leukocytes 16 Weeks	Normal
Heart weight	Normal
Salmonella infection	Normal
Cytotoxic T Cell Function	Normal
Spleen Immunophenotyping	Normal
Mesenteric Lymph Node Immunophenotyping	Normal
Bone Marrow Immunophenotyping	Normal
Epidermal Immune Composition	Normal
Trichuris Challenge	Normal

References

1. Wilk S, Wilk E, Magnusson RP (Jun 1998). "Purification, characterization, and cloning of a cytosolic aspartyl aminopeptidase". The Journal of Biological Chemistry 273 (26): 15961–70. doi:10.1074/jbc.273.26.15961. PMID 9632644.
2. "Entrez Gene: DNPEP aspartyl aminopeptidase".
3. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
4. "International Mouse Phenotyping Consortium".
5. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (Jun 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
6. Dolgin E (Jun 2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
7. Collins FS, Rossant J, Wurst W (Jan 2007). "A mouse for all reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
8. White JK, Gerdin AK, Karp NA, Ryder E, Buljan M, Bussell JN, Salisbury J, Clare S, Ingham NJ, Podrini C, Houghton R, Estabel J, Bottomley JR, Melvin DG, Sunter D, Adams NC, Tannahill D, Logan DW, Macarthur DG, Flint J, Mahajan VB, Tsang SH, Smyth I, Watt FM, Skarnes WC, Dougan G, Adams DJ, Ramirez-Solis R, Bradley A, Steel KP (Jul 2013). "Genome-wide generation and systematic phenotyping of knockout mice reveals new roles for many genes". Cell 154 (2): 452–64. doi:10.1016/j.cell.2013.06.022. PMC 3717207. PMID 23870131.
9. "Infection and Immunity Immunophenotyping (3i) Consortium".

Further reading

• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Prieto I, Hermoso F, de Gasparo M, Vargas F, Alba F, Segarra AB, Banegas I, Ramírez M (May 2003). "Angiotensinase activities in the kidney of renovascular hypertensive rats". Peptides 24 (5): 755–60. doi:10.1016/S0196-9781(03)00121-9. PMID 12895663.
• Wilk S, Wilk E, Magnusson RP (Nov 2002). "Identification of histidine residues important in the catalysis and structure of aspartyl aminopeptidase". Archives of Biochemistry and Biophysics 407 (2): 176–83. doi:10.1016/S0003-9861(02)00494-0. PMID 12413488.

External links

• The MEROPS online database for peptidases and their inhibitors: M18.002