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MGP001934

UniProt Annotations

Entry Information
Gene Namemembrane metallo-endopeptidase
Protein EntryNEP_HUMAN
UniProt IDP08473
SpeciesHuman
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=55.1 uM for angiotensin-1 {ECO:0000269|PubMed:15283675}; KM=179 uM for angiotensin-2 {ECO:0000269|PubMed:15283675}; KM=111.4 uM for angiotensin 1-9 {ECO:0000269|PubMed:15283675};
Catalytic ActivityPreferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'. {ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:8168535}.
CofactorName=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566};
Enzyme RegulationInhibited in a dose dependent manner by opiorphin. {ECO:0000269|PubMed:17101991}.
FunctionThermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids (PubMed:15283675, PubMed:8168535). Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond (PubMed:17101991). Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9 (PubMed:15283675). Involved in the degradation of atrial natriuretic factor (ANF) (PubMed:2531377, PubMed:2972276). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers (PubMed:20876573). {ECO:0000269|PubMed:15283675, ECO:0000269|PubMed:17101991, ECO:0000269|PubMed:20876573, ECO:0000269|PubMed:2531377, ECO:0000269|PubMed:2972276}.
InteractionP21926:CD9; NbExp=6; IntAct=EBI-353759, EBI-4280101; P08107:HSPA1B; NbExp=3; IntAct=EBI-353759, EBI-629985; P04792:HSPB1; NbExp=4; IntAct=EBI-353759, EBI-352682;
MiscellaneousImportant cell surface marker in the diagnostic of human acute lymphocytic leukemia.
PtmGlycosylation at Asn-628 is necessary both for surface expression and neutral endopeptidase activity. {ECO:0000269|PubMed:10669592, ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:14747736, ECO:0000269|PubMed:17704566, ECO:0000269|PubMed:22766194}.
PtmMyristoylation is a determinant of membrane targeting. {ECO:0000269|PubMed:19756956}.
Sequence CautionSequence=CAA30157.1; Type=Erroneous initiation; Evidence={ECO:0000305};
SimilarityBelongs to the peptidase M13 family. {ECO:0000305}.
Subcellular LocationCell membrane; Single-pass type II membrane protein.
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/MMEID41386ch3q25.html";
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