CLV_NDR_NDR_1
ELM server details
ELM
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Functional site class:
NDR cleavage site
Functional site description:
N-arginine dibasic convertase (NRD convertase) is a endopeptidase in dibasic sites processing secreted proteins.
ELM(s): CLV_NDR_NDR_1
CLV_NDR_NDR_1 description: N-Arg dibasic convertase (nardilysine) cleavage site (Xaa-|-Arg-Lys or Arg-|-Arg-Xaa)
Pattern: .RK|RR[^KR]
Present in taxon(s): Metazoa  
Not represented in taxon(s):

o Abstract

N-Arg dibasic convertase is a metalloendopeptidase primarily cloned
from rat brain cortex and testis that cleaves peptide substrates on
the N terminus of Arg residues in dibasic stretches. It hydrolyses polypeptides, preferably at -Xaa-+-Arg-Lys-, and less commonly at -Arg-+-Arg-Xaa-, in which Xaa is not Arg or Lys. It is proved that it can cleave alpha-neoendorphin, ANF, dynorphin, preproneurotensin and somatostatin. Also there is an evidence for extracellular localization of active NDR.

o Selected references

Chow KM, Csuhai E, Juliano MA, St Pyrek J, Juliano L, Hersh LB
Studies on the subsite specificity of rat nardilysin (N-arginine dibasic convertase).
J Biol Chem 2000 Jun 30;275(26) : 19545-51.
PMID: 10764809

Hospital V, Chesneau V, Balogh A, Joulie C, Seidah NG, Cohen P, Prat A
N-arginine dibasic convertase (nardilysin) isoforms are soluble dibasic-specific metalloendopeptidases that localize in the cytoplasm and at the cell surface.
Biochem J 2000 Jul 15;349() : 587-97.
PMID: 10880358

Pierotti AR, Prat A, Chesneau V, Gaudoux F, Leseney AM, Foulon T, Cohen P
N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a class of processing enzymes.
Proc Natl Acad Sci U S A 1994 Jun 21;91(13) : 6078-82.
PMID: 8016118

o This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.

Biological Process
  proteolysis and peptidolysis
Cellular Component
  extracellular
  Golgi apparatus
  cell surface
Molecular Function
  metalloendopeptidase
  nardilysin

 

o Instances for CLV_NDR_NDR_1

No instances annotated