Contents

Search


leucyl-cystinyl aminopeptidase (LNPEP, cystinyl aminopeptidase, oxytocinase, OTase, insulin-regulated membrane aminopeptidase, insulin-responsive aminopeptidase, IRAP, placental leucine aminopeptidase, P-LAP)

Function: - cleaves N-terminal amino acid, before Cys, Leu & other amino acid residues - degrades peptide hormones - oxytocin - vasopressin - angiotensin 3 - neuronal peptides in brain? - met-enkephalin - dynorphin - binds angiotensin IV; may be angiotensin IV receptor brain - binds tankyrases 1 & 2 Cofactor: binds 1 Zn+2 ion per subunit Structure: - N-glycosylated - homodimer Compartment: - cell membrane - resides in intracellular vesicles together with GLUT4 - may translocate to the cell surface in response to insulin &/or oxytocin - pregnancy serum form: secreted - pregnancy serum form is derived from the membrane-bound form by proteolytic processing - in brain only the membrane-bound form is found Alternative splicing: named isoforms=3 Expression: - expressed in placenta, heart, kidney & small intestine > neuronal cells in the brain, in skeletal muscle, spleen, liver, testes & colon

General

aminopeptidase cell surface receptor glycoprotein metalloprotein oligomerizing protein

Properties

CONFIGURATION: dimer SIZE: MW = 117 kD entity length = 1025 aa COMPARTMENT: plasma membrane MOTIF: Dileucine internalization motif {53-54} Dileucine internalization motif {76-77} Tankyrase binding {96-101} transmembrane domain {111-131} N-glycosylation site {N145} proteolytic site {154-155} N-glycosylation site {N184} N-glycosylation site {N215} N-glycosylation site {N256} N-glycosylation site {N266} N-glycosylation site {N368} N-glycosylation site {N374} N-glycosylation site {N448} Zn+2-binding site SITE: 464-464 glutamate residue {E465} Zn+2-binding site SITE: 468-468 Zn+2-binding site SITE: 487-487 N-glycosylation site {N525} N-glycosylation site {N578} N-glycosylation site {N598} N-glycosylation site {N664} N-glycosylation site {N682} N-glycosylation site {N760} N-glycosylation site {N834} N-glycosylation site {N850} N-glycosylation site {N989}

Database Correlations

OMIM 151300 UniProt Q9UIQ6 Pfam PF01433 ENZYME 3.4.11.3

References

  1. UniProt :accession Q9UIQ6
  2. Taylor A. Aminopeptidases: structure and function. FASEB J. 1993 Feb 1;7(2):290-8. Review. PMID: 8440407