ID A0A3P9P0P0_POERE Unreviewed; 1166 AA.
AC A0A3P9P0P0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Nardilysin convertase {ECO:0000313|Ensembl:ENSPREP00000015375.1};
GN Name=NRDC {ECO:0000313|Ensembl:ENSPREP00000015375.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000015375.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000015375.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000015375.1};
RG Ensembl;
RL Submitted (SEP-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; A0A3P9P0P0; -.
DR STRING; 8081.ENSPREP00000015375; -.
DR Ensembl; ENSPRET00000015532.1; ENSPREP00000015375.1; ENSPREG00000010372.1.
DR GeneTree; ENSGT00940000155026; -.
DR OMA; VEPWYCT; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000010372; Expressed in head and 1 other cell type or tissue.
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:UP000242638};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 213..339
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 366..550
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 556..837
FT /note="Peptidase M16 middle/third"
FT /evidence="ECO:0000259|Pfam:PF16187"
FT DOMAIN 842..1021
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 60..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..183
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1166 AA; 132457 MW; E95B6643EA2673CA CRC64;
MLLFTIFLFV FDARRVFFII ALFRLTRRVA ALTTKFPVTA SCPVVYSRAL LSVRCAKASS
PLPRMPQTNK STSSPAADSP GSVQAEAPAS CEESRAAKDD GGGEDNVGDS EIIKSPSDPK
QYRYIVLDNG LAALLISDFS GPVVSEHDDL DKEEEGEDDD DDDEEEEEED EDDEEEHEDE
ADVDECREDK KRAKKKRGSA DKQGITDRSA FFQSAAALCV GVGSFSDPSD LPGLAHFLEH
MVFMGSEKYP SENGFDAFLK KHGGSDNAST DCERTIFQFD VQRKSFKEAL DRWAQFFICP
LMIRDAINRE VEAVDSEYQL AKPSDSHRKE MLFGSLAKPG HPMGKFCWGN AETLKQEPKK
KKINVYKRLF AFWKEHYSAH YMTLAVQSKE KLDTLEKWVR EIFSKVPNNG LPKPDFSNLP
DPFDTPAFCK LYRVIPVRKV HALTISWALP PQEKHYRVKP LHYISWLVGH EGAGSILSVL
RKKCWALALY GGNSETGFDQ NTTYSIFSVS ITLTNEGFQN IYEVTDLVFQ YLKMLQKLGP
RQRIYEEIQR IEANEFHYQE QIDPIENVED ICECMQLFPK EDFLTGDHLM FEYNPEVISA
ALSLLTPEKA NLMLLSPEHE GQCPLREKWF GTQYSVEDIE KKWTERWSGN MEPNGDLHLP
AANEFIATDF TLKPSDCPDT DFPVRIATSN EGCLWYKKDN KFKIPKAYIR FHLISPIIQK
SAKNIVLFDL MVNILGHNLA KPAYEAEVAQ LDHKLVAGEH GLIFKVKGFN HKLPLLFHLI
VDHLADFSAS DDVFSMFAEQ LKKTYFNILI KPEKLGKDVR LLILEHSRWS MVEKYQALTA
GLTCKELLEF SRSFKTELFA EGLVQGNVSR AESVEFLKYV TDKLQFSKLP AEVPVMFRVV
ELPQKHHICK VKSLNKGDAN SEVTVYYQSG LKALRQHTLM ELLVMHMEEP CFDFLRTKET
LGYHVSPTCR NTSGVLGFSI TVETQATKFN SELVELKIEE FLASYGKELG DLTEEAFSTQ
VTALVQLKEC EDTHLGEEVN RNWQEVLTQQ YVFDRLNKEI AALKQMSRDE LLSWFQKHRD
ESSRKLSVHV VGFGAEENDG DGEGKKKQKG KAEADNEEEV TESAYGEVSK LTLLPASSKI
EGAIPIMDIP DFIKGLPLFP YHKILE
//
