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O43847 (NRDC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nardilysin

EC=3.4.24.61
Alternative name(s):
N-arginine dibasic convertase
Short name=NRD convertase
Short name=NRD-C
Gene names
Name:NRD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1150 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs.

Catalytic activity

Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Tissue specificity

Primarily in adult heart, skeletal muscle, and testis and at much lower levels in other tissues.

Sequence similarities

Belongs to the peptidase M16 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TP53P046376EBI-2371631,EBI-366083

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43847-1)

Also known as: NRD1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O43847-2)

Also known as: NRD2;

The sequence of this isoform differs from the canonical sequence as follows:
     209-209: Q → QQLQSLFLLWSKLTDRLWFKSTYSKMSSTLLVETRNLYGVVGAESRSAPVQHLAGWQAEEQQGETDTVL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 11501130Nardilysin
PRO_0000026755

Regions

Compositional bias142 – 20059Asp/Glu-rich (highly acidic)
Compositional bias144 – 15310Poly-Glu

Sites

Active site2351Proton acceptor By similarity
Metal binding2321Zinc By similarity
Metal binding2361Zinc By similarity
Metal binding3131Zinc By similarity

Amino acid modifications

Modified residue861Phosphoserine By similarity
Modified residue941Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11

Natural variations

Alternative sequence2091Q → QQLQSLFLLWSKLTDRLWFK STYSKMSSTLLVETRNLYGV VGAESRSAPVQHLAGWQAEE QQGETDTVL in isoform 2.
VSP_007114
Natural variant1531E → EE. Ref.2 Ref.3 Ref.4
VAR_021221
Natural variant8311Y → S.
Corresponds to variant rs34957144 [ dbSNP | Ensembl ].
VAR_057058

Experimental info

Sequence conflict23 – 242EL → DV in CAA63698. Ref.2
Sequence conflict23 – 242EL → DV in CAA63694. Ref.2
Sequence conflict5261Q → L in CAA63698. Ref.2
Sequence conflict5261Q → L in CAA63694. Ref.2
Sequence conflict6401A → G in AAC39597. Ref.1
Sequence conflict7521V → A in CAA63698. Ref.2
Sequence conflict7521V → A in CAA63694. Ref.2
Sequence conflict10861V → A in AAC39597. Ref.1
Sequence conflict10991T → S in CAA63698. Ref.2
Sequence conflict10991T → S in CAA63694. Ref.2
Sequence conflict1125 – 115026DCIIP…HKIVK → SVSSPLLISGLSQQHSTFSP TIK Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NRD1) [UniParc].

Last modified April 11, 2003. Version 2.
Checksum: 3B46DADB898E038B

FASTA1,150131,572
        10         20         30         40         50         60 
MLRRVTVAAV CATRRKLCEA GRELAALWGI ETRGRCEDSA AARPFPILAM PGRNKAKSTC 

        70         80         90        100        110        120 
SCPDLQPNGQ DLGENSRVAR LGADESEEEG RRGSLSNAGD PEIVKSPSDP KQYRYIKLQN 

       130        140        150        160        170        180 
GLQALLISDL SNMEGKTGNT TDDEEEEEVE EEEDDDEDSG AEIEDDDEEG FDDEDEFDDE 

       190        200        210        220        230        240 
HDDDLDTEDN ELEELEERAE ARKKTTEKQS AAALCVGVGS FADPDDLPGL AHFLEHMVFM 

       250        260        270        280        290        300 
GSLKYPDENG FDAFLKKHGG SDNASTDCER TVFQFDVQRK YFKEALDRWA QFFIHPLMIR 

       310        320        330        340        350        360 
DAIDREVEAV DSEYQLARPS DANRKEMLFG SLARPGHPMG KFFWGNAETL KHEPRKNNID 

       370        380        390        400        410        420 
THARLREFWM RYYSSHYMTL VVQSKETLDT LEKWVTEIFS QIPNNGLPRP NFGHLTDPFD 

       430        440        450        460        470        480 
TPAFNKLYRV VPIRKIHALT ITWALPPQQQ HYRVKPLHYI SWLVGHEGKG SILSFLRKKC 

       490        500        510        520        530        540 
WALALFGGNG ETGFEQNSTY SVFSISITLT DEGYEHFYEV AYTVFQYLKM LQKLGPEKRI 

       550        560        570        580        590        600 
FEEIRKIEDN EFHYQEQTDP VEYVENMCEN MQLYPLQDIL TGDQLLFEYK PEVIGEALNQ 

       610        620        630        640        650        660 
LVPQKANLVL LSGANEGKCD LKEKWFGTQY SIEDIENSWA ELWNSNFELN PDLHLPAENK 

       670        680        690        700        710        720 
YIATDFTLKA FDCPETEYPV KIVNTPQGCL WYKKDNKFKI PKAYIRFHLI SPLIQKSAAN 

       730        740        750        760        770        780 
VVLFDIFVNI LTHNLAEPAY EADVAQLEYK LVAGEHGLII RVKGFNHKLP LLFQLIIDYL 

       790        800        810        820        830        840 
AEFNSTPAVF TMITEQLKKT YFNILIKPET LAKDVRLLIL EYARWSMIDK YQALMDGLSL 

       850        860        870        880        890        900 
ESLLSFVKEF KSQLFVEGLV QGNVTSTESM DFLKYVVDKL NFKPLEQEMP VQFQVVELPS 

       910        920        930        940        950        960 
GHHLCKVKAL NKGDANSEVT VYYQSGTRSL REYTLMELLV MHMEEPCFDF LRTKQTLGYH 

       970        980        990       1000       1010       1020 
VYPTCRNTSG ILGFSVTVGT QATKYNSEVV DKKIEEFLSS FEEKIENLTE EAFNTQVTAL 

      1030       1040       1050       1060       1070       1080 
IKLKECEDTH LGEEVDRNWN EVVTQQYLFD RLAHEIEALK SFSKSDLVNW FKAHRGPGSK 

      1090       1100       1110       1120       1130       1140 
MLSVHVVGYG KYELEEDGTP SSEDSNSSCE VMQLTYLPTS PLLADCIIPI TDIRAFTTTL 

      1150 
NLLPYHKIVK 

« Hide

Isoform 2 (NRD2) [UniParc].

Checksum: 071971B4E83016AF
Show »

FASTA1,218139,284

References

« Hide 'large scale' references
[1]"Human NRD convertase: a highly conserved metalloendopeptidase expressed at specific sites during development and in adult tissues."
Fumagalli P., Accarino M., Egeo A., Scartezzini P., Rappazzo G., Pizzuti A., Avvantaggiato V., Simeone A., Arrigo G., Zuffardi O., Ottolenghi S., Taramelli R.
Genomics 47:238-245(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Heart.
[2]"Human and rat testis express two mRNA species encoding variants of NRD convertase, a metalloendopeptidase of the insulinase family."
Hospital V., Prat A., Joulie C., Cherif D., Day R., Cohen P.
Biochem. J. 327:773-779(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT GLU-153 INS.
Tissue: Testis.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-153 INS.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLU-153 INS.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[6]"Gene expression of the dibasic-pair cleaving enzyme NRD convertase (N-arginine dibasic convertase) is differentially regulated in the GH3 pituitary and Mat-Lu prostate cell lines."
Winter A.G., Pierotti A.R.
Biochem. J. 351:755-764(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-107.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U64898 mRNA. Translation: AAC39597.1.
X93209 mRNA. Translation: CAA63698.1.
X93207 mRNA. Translation: CAA63694.1.
AL589663, AL050343 Genomic DNA. Translation: CAH74100.1.
AL050343, AL589663 Genomic DNA. Translation: CAI22216.1.
CH471059 Genomic DNA. Translation: EAX06809.1.
BC008775 mRNA. Translation: AAH08775.1.
AJ000350 Genomic DNA. Translation: CAA04025.1.
RefSeqNP_001095132.1. NM_001101662.1.
NP_001229290.1. NM_001242361.1.
NP_002516.2. NM_002525.2.
UniGeneHs.584782.

3D structure databases

ProteinModelPortalO43847.
SMRO43847. Positions 206-1088.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110954. 38 interactions.
IntActO43847. 7 interactions.
STRING9606.ENSP00000346890.

Protein family/group databases

MEROPSM16.005.

PTM databases

PhosphoSiteO43847.

Proteomic databases

MaxQBO43847.
PaxDbO43847.
PRIDEO43847.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000352171; ENSP00000262679; ENSG00000078618.
GeneID4898.
KEGGhsa:4898.
UCSCuc009vzb.3. human. [O43847-1]

Organism-specific databases

CTD4898.
GeneCardsGC01M052254.
H-InvDBHIX0000576.
HGNCHGNC:7995. NRD1.
HPAHPA023679.
HPA053661.
MIM602651. gene.
neXtProtNX_O43847.
PharmGKBPA31774.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1025.
HOVERGENHBG006530.
KOK01411.
OrthoDBEOG7HHWRD.
PhylomeDBO43847.

Enzyme and pathway databases

BRENDA3.4.24.61. 2681.
SignaLinkO43847.

Gene expression databases

ArrayExpressO43847.
BgeeO43847.
CleanExHS_NRD1.
GenevestigatorO43847.

Family and domain databases

Gene3D3.30.830.10. 5 hits.
InterProIPR011249. Metalloenz_LuxS/M16.
IPR011237. Pept_M16_dom.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]
SUPFAMSSF63411. SSF63411. 5 hits.
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNRD1. human.
GeneWikiNRD1.
GenomeRNAi4898.
NextBio18847.
PROO43847.
SOURCESearch...

Entry information

Entry nameNRDC_HUMAN
AccessionPrimary (citable) accession number: O43847
Secondary accession number(s): A6NI41 expand/collapse secondary AC list , O15241, O15242, Q5VUL0, Q96HB2, Q9NU57
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 11, 2003
Last modified: June 11, 2014
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM