ID   NRDC_PONAB              Reviewed;        1152 AA.
AC   Q5R4H6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves peptide substrates on the N-terminus of arginine
CC       residues in dibasic pairs. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR   EMBL; CR861272; CAH93340.1; -; mRNA.
DR   AlphaFoldDB; Q5R4H6; -.
DR   SMR; Q5R4H6; -.
DR   STRING; 9601.ENSPPYP00000001576; -.
DR   MEROPS; M16.005; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   InParanoid; Q5R4H6; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW   Reference proteome; Signal; Zinc.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1152
FT                   /note="Nardilysin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000045848"
FT   REGION          81..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..95
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..196
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        237
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   BINDING         315
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43847"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43847"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43847"
SQ   SEQUENCE   1152 AA;  131682 MW;  06F4470E12EF609A CRC64;
     MLRKVTVAAV CATRRKLCEA GRELAALWGI ETRGRCEDSA AVRPFPILAM PGRNKAKSTC
     SCPDLQPNGQ DLGENSRVAR LGADESEEEG RRGSLSNAGD PEIVKSPSDP KQYRYIKLQN
     GLQALLISDL SNMEGKTGNT TDDEEEEEVE EEEEDDDEDS GAEIEDDDEE GFDDEDEFDD
     EHDDDLDTED NELEELEERA EARKKKTTEK QSAAALCVGV GSFADPDDLP GLAHFLEHMV
     FMGSLKYPDE NGFDAFLKKH GGSDNASTDC ERTVFQFDVQ RKYFKEALDR WAQFFIHPLM
     IRDAIDREVE AVDSEYQLAR PSDANRKEML FGSLARPGHP MGKFFWGNAE TLKHEPKKNN
     IDTHARLREF WLRYYSAHYM TLVVQSKETL DTLEKWVTEI FSQIPNNGLP RPNFGHLTDP
     FDTPAFNKLY RVVPIRKIHA LTITWALPPQ QQHYRVKPLH YISWLVGHEG KGSILSFLRK
     KCWALALFGG NGETGFEQNS TYSVFSISIT LTDEGYEHFY EVAYTVFQYL KMLQKLGPEK
     RIFEEIQKIE DNEFHYQEQT DPVEYVENMC ENMQPYPLQD ILTGDQLLFE YKPEVIGEAL
     NQLVPQKANL VLLSGANEGK CDLKEKWFGT QYSIEDIENS WAELWNSNFE LNPDLHLPAE
     NKYIATDFTL KAFDCPETEY PVKIVNTPQG CLWYKKDNKF KIPKAYIRFH LISPLIQRSA
     ANVVLFDIFA NILTHNLAEP AYEADVAQLE YKLVAGEHGL IIRVKGFNHK LPLLFQLIVD
     YLAEFNSTPA VFTMITEQLK KTYFNILIKP ETLAKDVRLL ILEYARWSMI DKYQALMDGL
     SLESLLSFVK EFKSQLFVEG LVQGNVTSTE SMDFLKYVVD KLNFKPLEQE MPVQFQVVEL
     PSGHHLCKVK ALNKGDANSE VTVYYQSGTR SLREYTLMEL LVMHMEEPCF DFLRTKQTLG
     YHVYPTCRST SGILGFSVTV GTQATKYNSE VVDKKIEEFL SSFEEKIENL TEEAFNTQVT
     ALIKLKECED THLGEEVDRN WNEVVTQQYL FDRLAHEIEA LKSFSKSDLV NWFKAHRGPG
     SKMLSVHVVG YGKYELEEDG TPSSEDSNSS CEVMQLTYLP TSPLLADCII PITDIRAFTT
     TLNLLPYHKI VK