ID   NRDC_RAT                Reviewed;        1161 AA.
AC   P47245; O35836;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 149.
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   AltName: Full=Nardilysin convertase {ECO:0000250|UniProtKB:O43847};
DE   Flags: Precursor;
GN   Name=Nrdc {ECO:0000250|UniProtKB:O43847}; Synonyms=Nrd1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=8016118; DOI=10.1073/pnas.91.13.6078;
RA   Pierotti A.R., Prat A., Chesneau V., Gaudoux F., Leseney A.-M., Foulon T.,
RA   Cohen P.;
RT   "N-arginine dibasic convertase, a metalloendopeptidase as a prototype of a
RT   class of processing enzymes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:6078-6082(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=9581555; DOI=10.1042/bj3270773;
RA   Hospital V., Prat A., Joulie C., Cherif D., Day R., Cohen P.;
RT   "Human and rat testis express two mRNA species encoding variants of NRD
RT   convertase, a metalloendopeptidase of the insulinase family.";
RL   Biochem. J. 327:773-779(1997).
RN   [3]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=7819328; DOI=10.1016/0300-9084(94)90151-1;
RA   Chesneau V., Pierotti A.R., Prat A., Gaudoux F., Foulon T., Cohen P.;
RT   "N-arginine dibasic convertase (NRD convertase): a newcomer to the family
RT   of processing endopeptidases. An overview.";
RL   Biochimie 76:234-240(1994).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-91, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Cleaves peptide substrates on the N-terminus of arginine
CC       residues in dibasic pairs.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and
CC         less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.;
CC         EC=3.4.24.61;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=NRD1;
CC         IsoId=P47245-1; Sequence=Displayed;
CC       Name=2; Synonyms=NRD2;
CC         IsoId=P47245-2; Sequence=VSP_007115;
CC   -!- TISSUE SPECIFICITY: Testis, and in a lower level in brain, heart and
CC       adrenal glands.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; L27124; AAA21818.1; -; mRNA.
DR   EMBL; X93208; CAA63696.1; -; mRNA.
DR   PIR; I59311; I59311.
DR   RefSeq; NP_037125.1; NM_012993.2. [P47245-1]
DR   AlphaFoldDB; P47245; -.
DR   SMR; P47245; -.
DR   BioGRID; 247532; 3.
DR   STRING; 10116.ENSRNOP00000010462; -.
DR   MEROPS; M16.005; -.
DR   iPTMnet; P47245; -.
DR   PhosphoSitePlus; P47245; -.
DR   jPOST; P47245; -.
DR   PaxDb; P47245; -.
DR   PRIDE; P47245; -.
DR   GeneID; 25499; -.
DR   KEGG; rno:25499; -.
DR   UCSC; RGD:3210; rat. [P47245-1]
DR   CTD; 4898; -.
DR   RGD; 3210; Nrdc.
DR   eggNOG; KOG0959; Eukaryota.
DR   InParanoid; P47245; -.
DR   PhylomeDB; P47245; -.
DR   PRO; PR:P47245; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR   GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:RGD.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0052548; P:regulation of endopeptidase activity; ISO:RGD.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; SSF63411; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Metal-binding; Metalloprotease;
KW   Phosphoprotein; Protease; Reference proteome; Signal; Zinc.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..1161
FT                   /note="Nardilysin"
FT                   /id="PRO_0000026757"
FT   REGION          42..105
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        77..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..207
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        247
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         244
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         248
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         325
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         91
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43847"
FT   VAR_SEQ         221
FT                   /note="Q -> QQSQNLFLLWSKLTDRLWFKSSYSKMSSTLLVETRNLYGVVGAESRS
FT                   APVEHLAGWQVEEQQGETDTVL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9581555"
FT                   /id="VSP_007115"
SQ   SEQUENCE   1161 AA;  132976 MW;  64A0CCEFB29386BB CRC64;
     MLRRVAVAAV FATGRKLRCE AGRDVTAVGR IEARGLCEES AKPFPTLTMP GRNKAKSTCS
     CPDLQPNGQD LGESGRVARL GADESEEEGR SLSNVGDPEI IKSPSDPKQY RYIKLQNGLQ
     ALLISDLSNV EGKTGNATDE EEEEEEEEEE GEEEEEEEED DDDDDDEDSG AEIQDDDEEG
     FDDEEEFDDD EHDDDDLDNE 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
     LNSDLHLPAE NKYIATDFTL KAFDCPETEY PAKIVNTPQG CLWYKKDNKF KIPKAYIRFH
     LISPLIQKSA ANVVLFDIFV NILTHNLAEP AYEADVAQLE YKLVAGEHGL IIRVKGFNHK
     LPLLFQLIID YLTEFSSTPA VFTMITEQLK KTYFNILIKP ETLAKDVRLL ILEYSRWSMI
     DKYRALMDGL SLESLLNFVK DFKSQLFVEG LVQGNVTSTE SMDFLRYVVD KLNFVPLERE
     MPVQFQVVEL PSGHHLCKVR ALNKGDANSE VTVYYQSGTR SLREYTLMEL LVMHMEEPCF
     DFLRTKQTLG YHVYPTCRNT SGILGFSVTV GTQATKYNSE TVDKKIEEFL SSFEEKIENL
     TEDAFNTQVT ALIKLKECED THLGEEVDRN WNEVVTQQYL FDRLAHEIEA LKSFSKSDLV
     SWFKAHRGPG SKMLSVHVVG YGKYELEEDG APVCEDPNSR EGMQLIYLPP SPLLAESTTP
     ITDIRAFTAT LSLFPYHKIV K