Q8BHG1 (NRDC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1161 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the peptidase M16 family.

Ontologies

Keywords
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 1161	1143	Nardilysin		PRO_0000026756
Regions
	Compositional bias	139 – 209	71	Asp/Glu-rich (highly acidic)
	Compositional bias	140 – 151	12	Poly-Glu
	Compositional bias	152 – 165	14	Poly-Asp
	Compositional bias	185 – 190	6	Poly-Asp
	Compositional bias	193 – 196	4	Poly-Asp
Sites
	Active site	247	1	Proton acceptor By similarity
	Metal binding	244	1	Zinc By similarity
	Metal binding	248	1	Zinc By similarity
	Metal binding	325	1	Zinc By similarity
Amino acid modifications
	Modified residue	85	1	Phosphoserine Ref.3
	Modified residue	91	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BHG1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 21334221632A5122	FASTA	1,161	132,891
	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

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. , 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. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK031548 mRNA. Translation: BAC27445.1. BC036128 mRNA. Translation: AAH36128.1.
IPI	IPI00408822.
RefSeq	NP_666262.2. NM_146150.2.
UniGene	Mm.274950. Mm.442231.
3D structure databases
ProteinModelPortal	Q8BHG1.
SMR	Q8BHG1. Positions 79-134.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BHG1.
PTM databases
PhosphoSite	Q8BHG1.
Proteomic databases
PRIDE	Q8BHG1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000065977; ENSMUSP00000068328; ENSMUSG00000053510.
GeneID	230598.
KEGG	mmu:230598.
Organism-specific databases
CTD	4898.
MGI	MGI:1201386. Nrd1.
Phylogenomic databases
HOVERGEN	HBG006530.
OrthoDB	EOG4PC9R9.
PhylomeDB	Q8BHG1.
Gene expression databases
ArrayExpress	Q8BHG1.
Bgee	Q8BHG1.
Genevestigator	Q8BHG1.
GermOnline	ENSMUSG00000053510. Mus musculus.
Family and domain databases
InterPro	IPR011249. Metalloenz_metal-bd. IPR011237. Pept_M16_core. IPR011765. Pept_M16_N. IPR001431. Pept_M16_Zn_BS. IPR007863. Peptidase_M16_C. [Graphical view]
Gene3D	G3DSA:3.30.830.10. Pept_M16_core. 3 hits.
KO	K01411.
Pfam	PF00675. Peptidase_M16. 1 hit. PF05193. Peptidase_M16_C. 2 hits. [Graphical view]
SUPFAM	SSF63411. Metalloenz_metal-bd. 4 hits.
PROSITE	PS00143. INSULINASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	379973.
SOURCE	Search...

Entry information

Entry name

NRDC_MOUSE

Accession

Primary (citable) accession number: Q8BHG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 11, 2003
Last sequence update:	March 1, 2003
Last modified:	November 16, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program