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Reviewed, UniProtKB/Swiss-Prot Q8BHG1 (NRDC_MOUSE)

Last modified June 16, 2009. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length1161 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

Sequence similarities

Belongs to the peptidase M16 family.

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Ontologies

Keywords
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: MGI

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 11611143Nardilysin
PRO_0000026756

Regions

Compositional bias139 – 20971Asp/Glu-rich (highly acidic)
Compositional bias140 – 15112Poly-Glu
Compositional bias152 – 16514Poly-Asp
Compositional bias185 – 1906Poly-Asp
Compositional bias193 – 1964Poly-Asp

Sites

Active site2471Proton acceptor By similarity
Metal binding2441Zinc By similarity
Metal binding2481Zinc By similarity
Metal binding3251Zinc By similarity

Amino acid modifications

Modified residue851Phosphoserine
Modified residue911Phosphoserine By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q8BHG1-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 21334221632A5122

FASTA1,161132,891
        10         20         30         40         50         60 
MLRRVAVAAV CVTGRKLRCE AGRELTALGR IEARGLCEES SKPFPTLTMP GRNKAKSTCS 

        70         80         90        100        110        120 
CPDLQPNGQD LGESGRLARL GADESEEEGR SFSNVGDPEI IKSPSDPKQY RYIKLQNGLQ 

       130        140        150        160        170        180 
ALLISDLSNV EGKTGNATDE EEEEEEEEEE EDDDDDDDDD DDDEDSGAEI QDDDEEGFDD 

       190        200        210        220        230        240 
EEEFDDDDDD EHDDDDLENE ENELEELEER VEARKKTTEK QSAAALCVGV GSFADPDDLP 

       250        260        270        280        290        300 
GLAHFLEHMV FMGSLKYPDE NGFDAFLKKH GGSDNASTDC ERTVFQFDVQ RKYFKEALDR 

       310        320        330        340        350        360 
WAQFFIHPLM IRDAIDREVE AVDSEYQLAR PSDANRKEML FGSLARPGHP MGKFFWGNAE 

       370        380        390        400        410        420 
TLKHEPKKNN IDTHARLREF WMRYYSAHYM TLVVQSKETL DTLEKWVTEI FSQIPNNGLP 

       430        440        450        460        470        480 
KPNFSHLTDP FDTPAFNKLY RVVPIRKIHA LTITWALPPQ QQHYRVKPLH YISWLVGHEG 

       490        500        510        520        530        540 
KGSILSYLRK KCWALALFGG NGETGFEQNS TYSVFSISIT LTDEGYEHFY EVAHTVFQYL 

       550        560        570        580        590        600 
KMLQKLGPEK RVFEEIQKIE DNEFHYQEQT DPVEYVENMC ENMQLYPRQD FLTGDQLLFE 

       610        620        630        640        650        660 
YKPEVIAEAL NQLVPQKANL VLLSGANEGR CDLKEKWFGT QYSIEDIENS WTELWKSNFD 

       670        680        690        700        710        720 
LNPDLHLPAE NKYIATDFTL KAFDCPETEY PAKIVNTAQG CLWYKKDNKF KIPKAYIRFH 

       730        740        750        760        770        780 
LISPLIQKSA ANVVLFDIFV NILTHNLAEP AYEADVAQLE YKLVAGEHGL IIRVKGFNHK 

       790        800        810        820        830        840 
LPLLFQLIID YLTEFSSTPA VFTMITEQLK KTYFNILIKP ETLAKDVRLL ILEYSRWSMI 

       850        860        870        880        890        900 
DKYQALMDGL SLDSLLNFVK DFKSQLFVEG LVQGNVTSTE SMDFLKYVVD KLNFAPLERE 

       910        920        930        940        950        960 
MPVQFQVVEL PSGHHLCKVR ALNKGDANSE VTVYYQSGTR SLREYTLMEL LVMHMEEPCF 

       970        980        990       1000       1010       1020 
DFLRTKQTLG YHVYPTCRNT SGILGFSVTV GTQATKYNSE TVDKKIEEFL SSFEEKIENL 

      1030       1040       1050       1060       1070       1080 
TEDAFNTQVT ALIKLKECED THLGEEVDRN WNEVVTQQYL FDRLAHEIEA LKSFSKSDLV 

      1090       1100       1110       1120       1130       1140 
SWFKAHRGPG SKMLSVHVVG YGKYELEEDG APFGEDSNSR EGMQLTYLPP SPVLAESTTP 

      1150       1160 
ITDIRAFTAT LSLFPYHKIV K

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References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Testis.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
[3]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK031548 mRNA. Translation: BAC27445.1.
BC036128 mRNA. Translation: AAH36128.1.
IPIIPI00408822.
RefSeqNP_666262.2.
UniGeneMm.274950
Mm.442231

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ8BHG1.

Genome annotation databases

EnsemblENSMUSG00000053510. Mus musculus. [Contig view]
GeneID230598.
KEGGmmu:230598.

Organism-specific databases

MGIMGI:1201386. Nrd1.

Phylogenomic databases

HOGENOMQ8BHG1.
HOVERGENQ8BHG1.

Enzyme and pathway databases

BRENDA3.4.24.61. 244.

Gene expression databases

ArrayExpressQ8BHG1.
BgeeQ8BHG1.
GermOnlineENSMUSG00000053510. Mus musculus.

Family and domain databases

InterProIPR011237. Pept_M16_core.
IPR011765. Pept_M16_N.
IPR001431. Pept_M16_Zn_BS.
IPR007863. Peptidase_M16_C.
[Graphical view]
Gene3DG3DSA:3.30.830.10. Pept_M16_core. 1 hit.
PfamPF00675. Peptidase_M16. 1 hit.
PF05193. Peptidase_M16_C. 2 hits.
[Graphical view]
PROSITEPS00143. INSULINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio379973.
SOURCESearch...

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Entry information

Entry nameNRDC_MOUSE
AccessionPrimary (citable) accession number: Q8BHG1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 11, 2003
Last sequence update: March 1, 2003
Last modified: June 16, 2009
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents