The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
Accession:
Functional site class:
NRD cleavage site
Functional site description:
N-arginine dibasic convertase (NRD convertase) is a endopeptidase in dibasic sites processing secreted proteins.
ELM Description:
N-Arg dibasic convertase (nardilysin) cleavage site (X-|-R-K or R-|-R-X).
Pattern: (.RK)|(RR[^KR])
Pattern Probability: 0.0074647
Present in taxon: Metazoa
Interaction Domain:
Peptidase_M16 (PF00675) Insulinase (Peptidase family M16) (Stochiometry: 1 : 1)
o See 2 Instances for CLV_NRD_NRD_1
o Abstract
N-arginine dibasic (NRD) 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 has been shown to cleave alpha-neoendorphin, ANF, dynorphin, preproneurotensin and somatostatin. Also there is an evidence for extracellular localization of active NRD.
o 3 selected references:

o 6 GO-Terms:

o 2 Instances for CLV_NRD_NRD_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
P06300 Pdyn
PDYN_RAT
207 209 YKRYGGFLRRIRPKLKWDNQ TP 1 Rattus norvegicus (Norway rat)
P60042 Sst
SMS_RAT
100 102 SNPAMAPRERKAGCKNFFWK TP 1 Rattus norvegicus (Norway rat)
Please cite: ELM 2016-data update and new functionality of the eukaryotic linear motif resource. (PMID:26615199)

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