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Database: UniProt
Entry: A0A2U4BJX4_TURTR
LinkDB: A0A2U4BJX4_TURTR
Original site: A0A2U4BJX4_TURTR 
ID   A0A2U4BJX4_TURTR        Unreviewed;      1190 AA.
AC   A0A2U4BJX4;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 2.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Nardilysin isoform X2 {ECO:0000313|RefSeq:XP_019793379.2};
GN   Name=NRDC {ECO:0000313|RefSeq:XP_019793379.2};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019793379.2};
RN   [1] {ECO:0000313|RefSeq:XP_019793379.2}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019793379.2};
RG   RefSeq;
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   RefSeq; XP_019793379.2; XM_019937820.2.
DR   AlphaFoldDB; A0A2U4BJX4; -.
DR   Proteomes; UP000245320; Chromosome 1.
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; 5.
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:UP000245320};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          286..414
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          440..625
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          631..912
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          917..1099
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          55..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          134..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..206
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1190 AA;  136174 MW;  512FDEED0BE70033 CRC64;
     MLRRVTVAAV CATRRKLWCE AGRELAALWR IEARGRCEDS AATRPFPILT MPGRNKAKST
     CSCPDRQPNG QDLGESGRVA RLGADESEEE GRRGPVSNVG DPEIVKSPSD PKQYRYIKLR
     NGLQALLISD LSNVEGKMGD ATDDEEEEEE EEEEEEDDDD DDDDDEDSGA EIEDDEEGFD
     DEDEFDDDDE HDDDDLDTED NELEELEERA EARKKTTEKQ QLQSLFLLLS KLTDRLWFKS
     TYTKMSSTLL VETRKLYGVV GAESRSAPLQ HLAGWQEEEQ QGETDTVLSA AALCVGVGSF
     ADPDDLPGLA HFLEHMVFMG SLKYPDENGF DAFLKKHGGS DNASTDCERT VFQFDVQRKY
     FKEALDRWAQ FFIHPLMIRD AIDREVEAVD SEYQLARPSD ANRKEMLFGS LARPGHPMGK
     FFWGNAETLK HEPKRNNIDT HARLREFWMH YYSAHYMTLV VQSKETLDTL EKWVTEIFSQ
     IPNNGLPKPN FGHLTDPFDT PAFNKLYRVV PIRKIHALTI TWALPPQQQH YRVKPLHYIS
     WLVGHEGKGS ILSYLRKKCW ALALFGGNGE TGFEQNSTYS VFSISITLTD EGYEHFYEVA
     HTVFQYLKML QKLGPEKRIF EEIQKIEDNE FHYQEQTDPV EYVENMCENM QLYPLQDFLT
     GDQLLFEYKP EVIAEALNQL VPQKANLVLL SGANEGKCDL KEKWFGTQYS MEDIENSWAE
     LWESNFELNP DLHLPAENKY IATDFMLKAF DCPETEYPVK IVNTPQGCLW YKKDNKFKIP
     KAYIRFHLIS PLIQKSAANV VLFDIFVNIL THNLAEPAYE ADVAQLEYKL VAGEHGLIIR
     VKGFNHKLPL LFQLIIDYLA EFNSTPAVFT MITEQLKKTY FNILIKPETL AKDVRLLILE
     YARWSMIDKY RALMDGLSLE SLLSFVRELK SQLFVEGLVQ GNVTSTESMD FLKYVVDKLN
     FMPLEQEMPV QFQVVELPSG HHLCKVRALN KGDANSEVTV YYQSGARSLK EYTLMELLVM
     HMEEPCFDFL RTKQTLGYHV YPTCRNTSGI LGFSVTVGTQ ATKYNSEVVD KKIEEFLSSF
     EEKIENLTED AFNTQIEALK SFSKSDLVNW FKAHRGPGSK MLSVHVVGFG KYEPEEDGTP
     SGEDSNSSCE VMQLTYLPTS PLLADCTIPV IDIRAFTSRL NLLPYHKIVK
//
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