ID   F7IIA1_CALJA            Unreviewed;      1136 AA.
AC   F7IIA1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Nardilysin convertase {ECO:0000313|Ensembl:ENSCJAP00000047233.2};
GN   Name=NRDC {ECO:0000313|Ensembl:ENSCJAP00000047233.2};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000047233.2, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000047233.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000047233.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR   AlphaFoldDB; F7IIA1; -.
DR   Ensembl; ENSCJAT00000058181.3; ENSCJAP00000047233.2; ENSCJAG00000021578.5.
DR   GeneTree; ENSGT00940000155026; -.
DR   Proteomes; UP000008225; Chromosome 7.
DR   Bgee; ENSCJAG00000021578; Expressed in frontal cortex and 6 other cell types or tissues.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
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   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          203..336
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          362..547
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          553..834
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          839..1005
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          81..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..186
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..186
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1136 AA;  129808 MW;  824A4DD187D97719 CRC64;
     MLRRVTVAAV CATRRKLCEA GRELAALWGI EKRGQCEDSA AARPFPILAM PGRNKAKSTC
     SFPDLQPNGQ DLGENSRVAR LGADESEEEG RRGSLSNAGD PEIVKSPSDP KQYRYIKLQN
     GLQALLISDL SNIEGKTGNT TDDDDEEEEE VEEEEDDDED SGAETQDDEE GFDDEDEFDD
     EHDDDIDTEN NELEELEERA EARKKTTEKQ SAAALCVGVG SFADPDDLPG LAHFLEHMVF
     MGSLKYPDEN GFDAFLKKHG GSDNASTDCE RTVFQFDVQR KYFKEALDRW AQFFIHPLMI
     RDAIDREVEA VDSEYQLARP SDANRKEMLF GSLARPGHPM GKFFWGNAET LKHEPKKNNI
     DTHSRLKEFW TRYYSAHYMT LVVQSKETLD TLEKWVTEIF SEIPNNGLPK PNFGHLTDPF
     DTPAFNKLYR VVPIRKIHAL TITWALPPQQ QHYRVKPLHY ISWLVGHEGK GSILSFLRKK
     CWALALFGGN GETGFEQNST YSVFSISITL TDEGYEHFYE VAYTVFQYLK MLQKLGPEKR
     IFEEIRKIED NEFHYQEQTD PVEYVENMCE NMQLYPLQDI LTGDQLLFEY NPEVIAEALN
     QLVPQKANLV LLSGANEGKC DLKEKWFGTQ YSIEDIENSW AELWNSNFEL NPDLHLPAEN
     KYIAKDFTLK AFDCPETEYP VKIVNTPQGC LWYKKDNKFK IPKAYIRFHL ISPLIQKSAA
     NVVLFDIFVN ILTHNLAEPA YEADVAQLEY KLVAGEYGLV IRVKGFNHKL PLLFQLIINY
     LAEFSSTPAV FTMITEQLKK TYFNILIKPE TLAKDVRLLI LEYARWSMID KYQALMDGLT
     LECLLSFVKE FKSQLFVEGL VQGNVTSTVS VRCSQEMPVQ FQVVELPRGH HLCKVKALNK
     GDANSEVTVY YQVSWGWADG QYVELQMHME EPCFDFLRTK QTLGYHVYPT CRNTSGILGF
     SVTVGTQATK YNSEVVDKKI EEFLSSFEEK IENLTEDAFN TQVTALIKLK ECEDTHLGEE
     VDRNWNEVVT QQYLFDRLAH EIEALKSFSK SDLVNWFKAH RGPGNKMLSV HVVGYGKYEL
     EEDGTHSGED SNSSCEVMEL TYLPTSPLLA DCIIPITDIR AFTSTLNLLP YHKIVK
//