Alanine aminopeptidase

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
External IDs	OMIM: 151530 MGI: 5000466 HomoloGene: 68163 GeneCards: ANPEP
Gene ontology Molecular function • virus receptor activity • zinc ion binding • receptor activity • metalloaminopeptidase activity • hydrolase activity • metal ion binding • peptide binding • peptidase activity • aminopeptidase activity • metallopeptidase activity Cellular component • vesicle lumen • integral component of plasma membrane • lysosomal membrane • extracellular space • cytoplasm • vesicle membrane • integral component of membrane • membrane • cytosol • endoplasmic reticulum-Golgi intermediate compartment • external side of plasma membrane • extracellular exosome • plasma membrane Biological process • negative regulation of renal sodium excretion • viral process • peptide catabolic process • proteolysis • viral entry into host cell • multicellular organism development • cell differentiation • angiogenesis • cellular aromatic compound metabolic process Sources:Amigo / QuickGO
RNA expression pattern
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_001141.2	NP_032512.2
Location (UCSC)	Chr 15: 89.78 – 89.82 Mb	Chr 7: 79.82 – 79.86 Mb
PubMed search	[1]	[2]
Wikidata

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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.^[3]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. "Entrez Gene: ANPEP alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)".

Further reading

• Yeager CL, Ashmun RA, Williams RK, et al. (1992). "Human aminopeptidase N is a receptor for human coronavirus 229E". Nature. 357 (6377): 420–2. doi:10.1038/357420a0. PMID 1350662.
• Shapiro LH, Ashmun RA, Roberts WM, Look AT (1991). "Separate promoters control transcription of the human aminopeptidase N gene in myeloid and intestinal epithelial cells". J. Biol. Chem. 266 (18): 11999–2007. PMID 1675638.
• O'Connell PJ, Gerkis V, d'Apice AJ (1991). "Variable O-glycosylation of CD13 (aminopeptidase N)". J. Biol. Chem. 266 (7): 4593–7. PMID 1705556.
• Watt VM, Willard HF (1990). "The human aminopeptidase N gene: isolation, chromosome localization, and DNA polymorphism analysis". Hum. Genet. 85 (6): 651–4. doi:10.1007/BF00193592. PMID 1977688.
• Look AT, Peiper SC, Rebentisch MB, et al. (1986). "Molecular cloning, expression, and chromosomal localization of the gene encoding a human myeloid membrane antigen (gp150)". J. Clin. Invest. 78 (4): 914–21. doi:10.1172/JCI112680. PMC 423717. PMID 2428842.
• Look AT, Ashmun RA, Shapiro LH, Peiper SC (1989). "Human myeloid plasma membrane glycoprotein CD13 (gp150) is identical to aminopeptidase N". J. Clin. Invest. 83 (4): 1299–307. doi:10.1172/JCI114015. PMC 303821. PMID 2564851.
• Olsen J, Cowell GM, Kønigshøfer E, et al. (1988). "Complete amino acid sequence of human intestinal aminopeptidase N as deduced from cloned cDNA". FEBS Lett. 238 (2): 307–14. doi:10.1016/0014-5793(88)80502-7. PMID 2901990.
• Kruse TA, Bolund L, Grzeschik KH, et al. (1988). "Assignment of the human aminopeptidase N (peptidase E) gene to chromosome 15q13-qter". FEBS Lett. 239 (2): 305–8. doi:10.1016/0014-5793(88)80940-2. PMID 2903074.
• Tokioka-Terao M, Hiwada K, Kokubu T (1985). "Purification and characterization of aminopeptidase N from human plasma". Enzyme. 32 (2): 65–75. PMID 6149934.
• Watanabe Y, Iwaki-Egawa S, Mizukoshi H, Fujimoto Y (1995). "Identification of an alanine aminopeptidase in human maternal serum as a membrane-bound aminopeptidase N". Biol. Chem. Hoppe-Seyler. 376 (7): 397–400. doi:10.1515/bchm3.1995.376.7.397. PMID 7576235.
• Favaloro EJ, Browning T, Facey D (1993). "CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated". Exp. Hematol. 21 (13): 1695–701. PMID 7902291.
• Núñez L, Amigo L, Rigotti A, et al. (1993). "Cholesterol crystallization-promoting activity of aminopeptidase-N isolated from the vesicular carrier of biliary lipids". FEBS Lett. 329 (1-2): 84–8. doi:10.1016/0014-5793(93)80199-5. PMID 8102610.
• Söderberg C, Giugni TD, Zaia JA, et al. (1993). "CD13 (human aminopeptidase N) mediates human cytomegalovirus infection". J. Virol. 67 (11): 6576–85. PMC 238095. PMID 8105105.
• Kolb AF, Maile J, Heister A, Siddell SG (1996). "Characterization of functional domains in the human coronavirus HCV 229E receptor". J. Gen. Virol. 77. ( Pt 10): 2515–21. PMID 8887485.
• Norén K, Hansen GH, Clausen H, et al. (1997). "Defectively N-glycosylated and non-O-glycosylated aminopeptidase N (CD13) is normally expressed at the cell surface and has full enzymatic activity". Exp. Cell Res. 231 (1): 112–8. doi:10.1006/excr.1996.3455. PMID 9056417.
• Kolb AF, Hegyi A, Siddell SG (1997). "Identification of residues critical for the human coronavirus 229E receptor function of human aminopeptidase N". J. Gen. Virol. 78. ( Pt 11): 2795–802. PMID 9367365.
• Hegyi A, Kolb AF (1998). "Characterization of determinants involved in the feline infectious peritonitis virus receptor function of feline aminopeptidase N". J. Gen. Virol. 79. ( Pt 6): 1387–91. PMID 9634079.
• Dong X, An B, Salvucci Kierstead L, et al. (2000). "Modification of the amino terminus of a class II epitope confers resistance to degradation by CD13 on dendritic cells and enhances presentation to T cells". J. Immunol. 164 (1): 129–35. doi:10.4049/jimmunol.164.1.129. PMID 10605003.
• Pasqualini R, Koivunen E, Kain R, et al. (2000). "Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis". Cancer Res. 60 (3): 722–7. PMID 10676659.
• Renold A, Cescato R, Beuret N, et al. (2000). "Basolateral sorting signals differ in their ability to redirect apical proteins to the basolateral cell surface". J. Biol. Chem. 275 (13): 9290–5. doi:10.1074/jbc.275.13.9290. PMID 10734069.

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)