Alanine aminopeptidase

This article is about the cell membrane alanyl aminopeptidase. For the cytosolic alanine aminopeptidase, see NPEPPS.

Membrane alanyl aminopeptidase (EC 3.4.11.2) also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme that in humans is encoded by the ANPEP gene.

ANPEP
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4FYQ, 4FYR, 4FYS, 4FYT
Identifiers
Aliases	ANPEP, APN, CD13, GP150, LAP1, P150, PEPN, alanyl aminopeptidase, membrane, AP-M, hAPN, AP-N
External IDs	OMIM: 151530; MGI: 5000466; HomoloGene: 68163; GeneCards: ANPEP; OMA:ANPEP - orthologs
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q26.1 Start 89,784,895 bp[1] End 89,815,401 bp[1]
Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 D2 Start 79,471,551 bp[2] End 79,510,807 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa duodenum body of pancreas mucosa of ileum mucosa of transverse colon right lobe of liver stromal cell of endometrium gallbladder human kidney blood Top expressed in jejunum duodenum ileum crypt of lieberkuhn of small intestine lactiferous gland lip right lobe of liver epithelium of stomach lacrimal gland aortic valve More reference expression data BioGPS More reference expression data
Gene ontology Molecular function virus receptor activity zinc ion binding metalloaminopeptidase activity hydrolase activity metal ion binding peptidase activity aminopeptidase activity metallopeptidase activity peptide binding signaling receptor activity Cellular component lysosomal membrane integral component of membrane membrane endoplasmic reticulum-Golgi intermediate compartment external side of plasma membrane extracellular exosome extracellular space nucleus plasma membrane secretory granule membrane cytoplasm Biological process viral process peptide catabolic process proteolysis viral entry into host cell multicellular organism development cell differentiation angiogenesis neutrophil degranulation signal transduction cell-cell signaling regulation of blood pressure Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 290 16790 Ensembl ENSG00000166825 ENSMUSG00000039062 UniProt P15144 P97449 RefSeq (mRNA) NM_001150 NM_001381923 NM_001381924 NM_008486 RefSeq (protein) NP_001141 NP_001368852 NP_001368853 NP_032512 Location (UCSC) Chr 15: 89.78 – 89.82 Mb Chr 7: 79.47 – 79.51 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Function

Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. In the small intestine aminopeptidase N plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Its function in proximal tubular epithelial cells and other cell types is less clear. The large extracellular carboxyterminal domain contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloproteinase superfamily. Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. The latter enzyme was thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, granulocytes, and synaptic membranes from the CNS. Defects in this gene appear to be a cause of various types of leukemia or lymphoma.^[5]

AAP is also used by some viruses as a receptor to which these viruses bind to and then enter cells. It is a receptor for human coronavirus 229E, feline coronavirus serotype II (FCoV-II), TGEV, PEDV,^[6] canine coronavirus genotype II (CCoV-II)^[7] as well as several Deltacoronaviruses.^[8]