Version 5.4
Mus musculus Protein: Nrd1
Summary
InnateDB Protein IDBP-173853.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Nrd1
Protein Name nardilysin, N-arginine dibasic convertase, NRD convertase 1
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000068328
InnateDB Gene IDBG-173849 (Nrd1)
Protein Structure
UniProt Annotation
Function Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs.
Subcellular Localization
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 19 interaction(s) predicted by orthology.
Predicted by orthology
Total 19 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0004222 metalloendopeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005739 mitochondrion
Protein Structure and Domains
PDB ID MGI:1201386
InterPro IPR007863 Peptidase M16, C-terminal domain
IPR011249 Metalloenzyme, LuxS/M16 peptidase-like
IPR011765 Peptidase M16, N-terminal
PFAM PF05193
PF00675
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q8BHG1
PhosphoSite PhosphoSite-Q8BHG1
TrEMBL Q8R1H1
UniProt Splice Variant
Entrez Gene 230598
UniGene Mm.274950
RefSeq NP_666262
MGI ID
MGI Symbol Nrd1
OMIM
CCDS CCDS18460
HPRD
IMGT
EMBL AK031548 AK040377 AL627406 BC024544 BC036128
GenPept AAH24544 AAH36128 BAC27445 BAE20579

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca