CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000789
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nardilysin 
Protein Synonyms/Alias
 N-arginine dibasic convertase; NRD convertase; NRD-C 
Gene Name
 NRD1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
283DVQRKYFKEALDRWAubiquitination[1]
325RPSDANRKEMLFGSLubiquitination[1]
341RPGHPMGKFFWGNAEubiquitination[1]
351WGNAETLKHEPRKNNubiquitination[1]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
 Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. 
Sequence Annotation
 ACT_SITE 235 235 Proton acceptor (By similarity).
 METAL 232 232 Zinc (By similarity).
 METAL 236 236 Zinc (By similarity).
 METAL 313 313 Zinc (By similarity).
 MOD_RES 86 86 Phosphoserine (By similarity).
 MOD_RES 94 94 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism; Protease; Reference proteome; Signal; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1150 AA 
Protein Sequence
MLRRVTVAAV CATRRKLCEA GRELAALWGI ETRGRCEDSA AARPFPILAM PGRNKAKSTC 60
SCPDLQPNGQ DLGENSRVAR LGADESEEEG RRGSLSNAGD PEIVKSPSDP KQYRYIKLQN 120
GLQALLISDL SNMEGKTGNT TDDEEEEEVE EEEDDDEDSG AEIEDDDEEG FDDEDEFDDE 180
HDDDLDTEDN ELEELEERAE ARKKTTEKQS AAALCVGVGS FADPDDLPGL AHFLEHMVFM 240
GSLKYPDENG FDAFLKKHGG SDNASTDCER TVFQFDVQRK YFKEALDRWA QFFIHPLMIR 300
DAIDREVEAV DSEYQLARPS DANRKEMLFG SLARPGHPMG KFFWGNAETL KHEPRKNNID 360
THARLREFWM RYYSSHYMTL VVQSKETLDT LEKWVTEIFS QIPNNGLPRP NFGHLTDPFD 420
TPAFNKLYRV VPIRKIHALT ITWALPPQQQ HYRVKPLHYI SWLVGHEGKG SILSFLRKKC 480
WALALFGGNG ETGFEQNSTY SVFSISITLT DEGYEHFYEV AYTVFQYLKM LQKLGPEKRI 540
FEEIRKIEDN EFHYQEQTDP VEYVENMCEN MQLYPLQDIL TGDQLLFEYK PEVIGEALNQ 600
LVPQKANLVL LSGANEGKCD LKEKWFGTQY SIEDIENSWA ELWNSNFELN PDLHLPAENK 660
YIATDFTLKA FDCPETEYPV KIVNTPQGCL WYKKDNKFKI PKAYIRFHLI SPLIQKSAAN 720
VVLFDIFVNI LTHNLAEPAY EADVAQLEYK LVAGEHGLII RVKGFNHKLP LLFQLIIDYL 780
AEFNSTPAVF TMITEQLKKT YFNILIKPET LAKDVRLLIL EYARWSMIDK YQALMDGLSL 840
ESLLSFVKEF KSQLFVEGLV QGNVTSTESM DFLKYVVDKL NFKPLEQEMP VQFQVVELPS 900
GHHLCKVKAL NKGDANSEVT VYYQSGTRSL REYTLMELLV MHMEEPCFDF LRTKQTLGYH 960
VYPTCRNTSG ILGFSVTVGT QATKYNSEVV DKKIEEFLSS FEEKIENLTE EAFNTQVTAL 1020
IKLKECEDTH LGEEVDRNWN EVVTQQYLFD RLAHEIEALK SFSKSDLVNW FKAHRGPGSK 1080
MLSVHVVGYG KYELEEDGTP SSEDSNSSCE VMQLTYLPTS PLLADCIIPI TDIRAFTTTL 1140
NLLPYHKIVK 1150 
Gene Ontology
 GO:0009986; C:cell surface; TAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:UniProtKB.
 GO:0048408; F:epidermal growth factor binding; TAS:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004222; F:metalloendopeptidase activity; NAS:UniProtKB.
 GO:0016477; P:cell migration; TAS:UniProtKB.
 GO:0008283; P:cell proliferation; TAS:UniProtKB.
 GO:0007528; P:neuromuscular junction development; TAS:ProtInc.
 GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
 GO:0006508; P:proteolysis; NAS:UniProtKB.
 GO:0052548; P:regulation of endopeptidase activity; IDA:BHF-UCL. 
Interpro
 IPR011249; Metalloenz_LuxS/M16.
 IPR011237; Pept_M16_dom.
 IPR011765; Pept_M16_N.
 IPR001431; Pept_M16_Zn_BS.
 IPR007863; Peptidase_M16_C. 
Pfam
 PF00675; Peptidase_M16
 PF05193; Peptidase_M16_C 
SMART
  
PROSITE
 PS00143; INSULINASE 
PRINTS