[1]
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NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 538-564; 886-908; 922-942 AND 961-965, AND TISSUE SPECIFICITY.
PubMed=8805662 [NCBI, ExPASy, EBI, Israel, Japan]
Chen H.,
Kinzer C.A.,
Paul W.E.;
"p161, a murine membrane protein expressed on mast cells and some macrophages, is mouse CD13/aminopeptidase N.";
J. Immunol. 157:2593-2600(1996).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II, and FVB/N;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[3]
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FUNCTION, AND ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
PubMed=8103749 [NCBI, ExPASy, EBI, Israel, Japan]
Hansen A.S.,
Noren O.,
Sjostrom H.,
Werdelin O.;
"A mouse aminopeptidase N is a marker for antigen-presenting cells and appears to be co-expressed with major histocompatibility complex class II molecules.";
Eur. J. Immunol. 23:2358-2364(1993).
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[4]
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ENZYMATIC CLEAVAGE OF ANTIGEN PEPTIDES BOUND TO CLASS II MHC.
DOI=10.1084/jem.184.1.183; PubMed=8691132 [NCBI, ExPASy, EBI, Israel, Japan]
Larsen S.L.,
Pedersen L.O.,
Buus S.,
Stryhn A.;
"T cell responses affected by aminopeptidase N (CD13)-mediated trimming of major histocompatibility complex class II-bound peptides.";
J. Exp. Med. 184:183-189(1996).
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[5]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-852, AND MASS SPECTROMETRY.
TISSUE=Mast cell;
PubMed=17947660 [NCBI, ExPASy, EBI, Israel, Japan]
Cao L.,
Yu K.,
Banh C.,
Nguyen V.,
Ritz A.,
Raphael B.J.,
Kawakami Y.,
Kawakami T.,
Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell signaling.";
J. Immunol. 179:5864-5876(2007).
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- FUNCTION: Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May be involved in the metabolism of regulatory peptides of diverse cell types. May have a role in angiogenesis (By similarity). Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells.
- CATALYTIC ACTIVITY: Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
- SUBUNIT: Homodimer.
- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein.
- TISSUE SPECIFICITY: Highly expressed in intestinal tract and kidney, present in liver, lymph node, spleen, and brain. Found as well in monocytes, macrophages, dendritic cells, veiled cells and B-cells but not on T-cells and thymocytes.
- PTM: Sulfated (By similarity).
- SIMILARITY: Belongs to the peptidase M1 family [view classification].
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