Alanine aminopeptidase

Alanyl (membrane) aminopeptidase
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 4FYQ, 4FYR, 4FYS, 4FYT
Identifiers
Symbols	ANPEP ; APN; CD13; GP150; LAP1; P150; PEPN
External IDs	OMIM: 151530 MGI: 96749 HomoloGene: 68163 ChEMBL: 1907 GeneCards: ANPEP Gene
EC number	3.4.11.2
Gene ontology Molecular function • virus receptor activity • aminopeptidase activity • receptor activity • metallopeptidase activity • zinc ion binding • peptide binding • metalloaminopeptidase activity Cellular component • extracellular space • lysosomal membrane • endoplasmic reticulum-Golgi intermediate compartment • cytosol • integral component of plasma membrane • external side of plasma membrane • extracellular exosome Biological process • angiogenesis • angiotensin maturation • proteolysis • cell differentiation • peptide catabolic process • cellular protein metabolic process • viral entry into host cell Sources: Amigo / QuickGO
RNA expression pattern
File:PBB GE ANPEP 202888 s at tn.png
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	290	16790
Ensembl	ENSG00000166825	ENSMUSG00000039062
UniProt	P15144	P97449
RefSeq (mRNA)	NM_001150	NM_008486
RefSeq (protein)	NP_001141	NP_032512
Location (UCSC)	Chr 15: 89.78 – 89.82 Mb	Chr 7: 79.82 – 79.85 Mb
PubMed search	[1]	[2]

Alanine aminopeptidase (EC 3.4.11.2) is an enzyme that is used as a biomarker to detect damage to the kidneys, and that may be used to help diagnose certain kidney disorders. It is found at high levels in the urine when there are kidney problems.

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. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. Defects in this gene appear to be a cause of various types of leukemia or lymphoma.

External links

• The MEROPS online database for peptidases and their inhibitors: M01.001
• CD13 Antigens at the US National Library of Medicine Medical Subject Headings (MeSH)