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CD13; aminopeptidase-N; aminopeptidase-M; gp150; microsomal aminopeptidase; alanine aminopeptidase (ANPEP, PEPN)
Function:
- broad specificity aminopeptidase
- role in final digestion of peptides generated from hydrolysis of proteins by gastric & pancreatic proteases
- may be involved in metabolism of regulatory peptides of diverse cell types (see expression)
- found to cleave antigen peptides bound to MHC class II molecules of presenting cells
- degrades neurotransmitters at synaptic junctions
- implicated as a regulator of IL-8 bioavailability in the endometrium
- may contribute to the regulation of angiogenesis
- may undergo proteolysis & give rise to a soluble form
- 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 Pro, the two may be released as an intact Xaa-Pro dipeptide
Cofactor: binds 1 Zn+2 per subunit (putative)
Structure:
- homodimer
- N- & O-glycosylated
- amino acids 260-353 are essential to mediate susceptibility to infection with HCoV-229E
- belongs to the peptidase M1 family
Compartment:
- cell membrane, cytoplasm
- plasma membrane, exoplasmic face
- bile, concentration in human hepatic bile 17.3- 57.6 ug/mL
Expression:
- brush border membranes of small intestine
- renal proximal tubules
- placenta
- CNS synaptic membranes
- granulocytes
- macrophages
- endothelial cells
- bile duct canaliculi
- fibroblasts
- osteoclasts
- perineurium of peripheral nerves
- some large granular lymphocytes
- estradiol & IL-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% & 30%, respectively
Pathology:
- defects associated with various leukemias/lymphomas
a) AML M1-M5 ~75-95% M6 usually
- marker for acute myeloid leukemia CML ~90% pre-B ALL ~7-10% pre-T ALL rare
- plays a role in tumor invasion
- found to serve as a receptor for tumor-homing peptides, more specifically NGR peptides, thus could serve as a target for delivering drugs into tumors
- human coronavirus 229E (HCoV-229E) infection
a) serves as receptor for HCoV-229E spike glycoprotein
b) interacts with the S1 domain of HCoV-229E spike protein
- mediates as human cytomegalovirus (HCMV) infection sulfated (putative)
- autoantibodies associated with chronic graft versus host disease
- may play role in pathogenesis of cholesterol gallstone disease
Related
CD13 Ag in tissue
CD13 cells in body fluid
CD13 cells in specimen
Specific
muscle aminopeptidase-N
General
aminopeptidase
cluster-of-differentiation antigen; cluster designation antigen; CD antigen
phosphoprotein
zinc metalloprotease
Properties
SIZE: entity length = 967 aa
MW = 110 kD
COMPARTMENT: cytoplasm
cellular membrane
plasma membrane
CELL: monocyte
granulocyte
epithelial cell
hepatocyte
MOTIF: transmembrane domain {9-32}
Cytosolic Ser/Thr-rich junction {33-68}
Metalloprotease {69-967}
MOTIF: N-glycosylation site {N128}
N-glycosylation site {N234}
HCoV-229E interaction {260-353}
N-glycosylation site {N265}
N-glycosylation site {N319}
Zn+2-binding site
SITE: 388-388
glutamate residue {E389}
Zn+2-binding site
SITE: 392-392
Zn+2-binding site
SITE: 411-411
tyrosine residue {Y477}
N-glycosylation site {N527}
N-glycosylation site {N573}
N-glycosylation site {N625}
N-glycosylation site {N681}
N-glycosylation site {N735}
N-glycosylation site {N818}
Thr phosphorylation site {T928}
Database Correlations
OMIM 151530
UniProt P15144
Pfam PF01433
KEGG correlations
ENZYME 3.4.11.2
References
- Taylor A.
Aminopeptidases: structure and function.
FASEB J. 1993 Feb 1;7(2):290-8. Review.
PMID: 8440407
- PROSITE :accession PS00142
- Cotran et al Robbins Pathologic Basis of Disease,
W.B. Saunders Co, Philadelphia, PA 1989 pg 165
- http://www.pathologyoutlines.com/cdmarkers.html
15 October 2002
- UniProt :accession P15144