ID   NRDC_MOUSE              Reviewed;        1161 AA.
AC   Q8BHG1;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Nardilysin;
DE            EC=3.4.24.61;
DE   AltName: Full=N-arginine dibasic convertase;
DE            Short=NRD convertase;
DE            Short=NRD-C;
DE   Flags: Precursor;
GN   Name=Nrd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Cleaves peptide substrates on the N-terminus of arginine
CC       residues in dibasic pairs.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of polypeptides, preferably at
CC       -Xaa-|-Arg-Lys-, and less commonly at -Arg-|-Arg-Xaa-, in which
CC       Xaa is not Arg or Lys.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031548; BAC27445.1; -; mRNA.
DR   EMBL; BC036128; AAH36128.1; -; mRNA.
DR   IPI; IPI00408822; -.
DR   RefSeq; NP_666262.2; -.
DR   UniGene; Mm.274950; -.
DR   UniGene; Mm.442231; -.
DR   PhosphoSite; Q8BHG1; -.
DR   Ensembl; ENSMUSG00000053510; Mus musculus.
DR   GeneID; 230598; -.
DR   KEGG; mmu:230598; -.
DR   MGI; MGI:1201386; Nrd1.
DR   HOGENOM; Q8BHG1; -.
DR   HOVERGEN; Q8BHG1; -.
DR   BRENDA; 3.4.24.61; 244.
DR   NextBio; 379973; -.
DR   ArrayExpress; Q8BHG1; -.
DR   Bgee; Q8BHG1; -.
DR   GermOnline; ENSMUSG00000053510; Mus musculus.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR011237; Pept_M16_core.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Gene3D; G3DSA:3.30.830.10; Pept_M16_core; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW   Signal; Zinc.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19   1161       Nardilysin.
FT                                /FTId=PRO_0000026756.
FT   COMPBIAS    139    209       Asp/Glu-rich (highly acidic).
FT   COMPBIAS    140    151       Poly-Glu.
FT   COMPBIAS    152    165       Poly-Asp.
FT   COMPBIAS    185    190       Poly-Asp.
FT   COMPBIAS    193    196       Poly-Asp.
FT   ACT_SITE    247    247       Proton acceptor (By similarity).
FT   METAL       244    244       Zinc (By similarity).
FT   METAL       248    248       Zinc (By similarity).
FT   METAL       325    325       Zinc (By similarity).
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES      91     91       Phosphoserine (By similarity).
SQ   SEQUENCE   1161 AA;  132891 MW;  21334221632A5122 CRC64;
     MLRRVAVAAV CVTGRKLRCE AGRELTALGR IEARGLCEES SKPFPTLTMP GRNKAKSTCS
     CPDLQPNGQD LGESGRLARL GADESEEEGR SFSNVGDPEI IKSPSDPKQY RYIKLQNGLQ
     ALLISDLSNV EGKTGNATDE EEEEEEEEEE EDDDDDDDDD DDDEDSGAEI QDDDEEGFDD
     EEEFDDDDDD EHDDDDLENE ENELEELEER VEARKKTTEK QSAAALCVGV GSFADPDDLP
     GLAHFLEHMV FMGSLKYPDE NGFDAFLKKH GGSDNASTDC ERTVFQFDVQ RKYFKEALDR
     WAQFFIHPLM IRDAIDREVE AVDSEYQLAR PSDANRKEML FGSLARPGHP MGKFFWGNAE
     TLKHEPKKNN IDTHARLREF WMRYYSAHYM TLVVQSKETL DTLEKWVTEI FSQIPNNGLP
     KPNFSHLTDP FDTPAFNKLY RVVPIRKIHA LTITWALPPQ QQHYRVKPLH YISWLVGHEG
     KGSILSYLRK KCWALALFGG NGETGFEQNS TYSVFSISIT LTDEGYEHFY EVAHTVFQYL
     KMLQKLGPEK RVFEEIQKIE DNEFHYQEQT DPVEYVENMC ENMQLYPRQD FLTGDQLLFE
     YKPEVIAEAL NQLVPQKANL VLLSGANEGR CDLKEKWFGT QYSIEDIENS WTELWKSNFD
     LNPDLHLPAE NKYIATDFTL KAFDCPETEY PAKIVNTAQG CLWYKKDNKF KIPKAYIRFH
     LISPLIQKSA ANVVLFDIFV NILTHNLAEP AYEADVAQLE YKLVAGEHGL IIRVKGFNHK
     LPLLFQLIID YLTEFSSTPA VFTMITEQLK KTYFNILIKP ETLAKDVRLL ILEYSRWSMI
     DKYQALMDGL SLDSLLNFVK DFKSQLFVEG LVQGNVTSTE SMDFLKYVVD KLNFAPLERE
     MPVQFQVVEL PSGHHLCKVR ALNKGDANSE VTVYYQSGTR SLREYTLMEL LVMHMEEPCF
     DFLRTKQTLG YHVYPTCRNT SGILGFSVTV GTQATKYNSE TVDKKIEEFL SSFEEKIENL
     TEDAFNTQVT ALIKLKECED THLGEEVDRN WNEVVTQQYL FDRLAHEIEA LKSFSKSDLV
     SWFKAHRGPG SKMLSVHVVG YGKYELEEDG APFGEDSNSR EGMQLTYLPP SPVLAESTTP
     ITDIRAFTAT LSLFPYHKIV K
//