MGP Database

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MGP000151

UniProt Annotations

Entry Information
Gene Namealanyl (membrane) aminopeptidase
Protein EntryAMPN_HUMAN
UniProt IDP15144
SpeciesHuman
Comments
Comment typeDescription
Catalytic ActivityRelease 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. {ECO:0000269|PubMed:22932899}.
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:22932899}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:22932899};
DomainAmino acids 260-353 are essential to mediate susceptibility to infection with HCoV-229E (in porcine/human chimeric studies) and more specifically amino acids 288-295 (mutagenesis studies).
FunctionBroad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. Is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. Is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. In case of human coronavirus 229E (HCoV-229E) infection, serves as receptor for HCoV-229E spike glycoprotein. Mediates as well human cytomegalovirus (HCMV) infection. {ECO:0000269|PubMed:10605003, ECO:0000269|PubMed:10676659, ECO:0000269|PubMed:11384645, ECO:0000269|PubMed:12473585, ECO:0000269|PubMed:9056417}.
InductionEstradiol and IL8/interleukin-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% and 30%, respectively. {ECO:0000269|PubMed:11384645}.
MiscellaneousFound to serve as a receptor for tumor-homing peptides, more specifically NGR peptides. It could serve thus as a target for delivering drugs into tumors. Concentration in human hepatic bile, varies from 17.3 to 57.6 micrograms/ml.
PtmMay undergo proteolysis and give rise to a soluble form.
PtmN- and O-glycosylated. {ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:1705556, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:9056417}.
PtmSulfated. {ECO:0000250}.
SimilarityBelongs to the peptidase M1 family. {ECO:0000305}.
Subcellular LocationCell membrane; Single-pass type II membrane protein. Cytoplasm, cytosol {ECO:0000305}. Note=A soluble form has also been detected.
SubunitHomodimer. Interacts with the S1 domain of HCoV-229E spike protein. {ECO:0000269|PubMed:12551991, ECO:0000269|PubMed:1350662, ECO:0000269|PubMed:22932899, ECO:0000269|PubMed:6149934}.
Tissue SpecificityExpressed in epithelial cells of the kidney, intestine, and respiratory tract; granulocytes, monocytes, fibroblasts, endothelial cells, cerebral pericytes at the blood- brain barrier, synaptic membranes of cells in the CNS. Also expressed in endometrial stromal cells, but not in the endometrial glandular cells. Found in the vasculature of tissues that undergo angiogenesis and in malignant gliomas and lymph node metastases from multiple tumor types but not in blood vessels of normal tissues. A soluble form has been found in plasma. It is found to be elevated in plasma and effusions of cancer patients.
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