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Database: UniProt
Entry: G8F3N6_MACFA
LinkDB: G8F3N6_MACFA
Original site: G8F3N6_MACFA 
ID   G8F3N6_MACFA            Unreviewed;      1194 AA.
AC   G8F3N6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 2.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Nardilysin convertase {ECO:0000313|Ensembl:ENSMFAP00000006666.2};
GN   Name=NRDC {ECO:0000313|Ensembl:ENSMFAP00000006666.2};
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000006666.2, ECO:0000313|Proteomes:UP000233100};
RN   [1] {ECO:0000313|Ensembl:ENSMFAP00000006666.2, ECO:0000313|Proteomes:UP000233100}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSMFAP00000006666.2}
RP   IDENTIFICATION.
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; G8F3N6; -.
DR   STRING; 9541.ENSMFAP00000006666; -.
DR   MEROPS; M16.983; -.
DR   MEROPS; M16.987; -.
DR   Ensembl; ENSMFAT00000025352.2; ENSMFAP00000006666.2; ENSMFAG00000036148.2.
DR   VEuPathDB; HostDB:ENSMFAG00000036148; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   GeneTree; ENSGT00940000155026; -.
DR   OrthoDB; 129328at2759; -.
DR   Proteomes; UP000233100; Chromosome 1.
DR   Bgee; ENSMFAG00000036148; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
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:UP000233100};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          276..404
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          430..615
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          621..902
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          907..1088
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          53..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          133..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..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"
SQ   SEQUENCE   1194 AA;  136612 MW;  8ACEA5BD0D3253AD CRC64;
     MLRRVTVAAV CATRRKLCEA GRELAALWRI ETRGRCEDSA PARSFPILAM PGRNKAKSTC
     SCPDLQPNGQ DLGENSRVAR LGADESEEEG RRGSLSNAGD PEIVKSPSDP KQYRYIKLQN
     GLQALLISDL SNMEGKTGNT TDDEEEEEVE EEDEDDDEDS GAEIEDDDEE GFDDEDEFDD
     EHDDDLDTED NELEELEERA EARKKTTEKQ QSQSLFLLWS KLTDRLWFKS TYSKMSSTLL
     VETRNLYGVV GAESRSAPVQ HLAGWQEEEQ QGETDTVLSA AALCVGVGSF ADPDDLPGLA
     HFLEHMVFMG SLKYPDENGF DAFLKKHGGS DNASTDCERT VFQFDVQRKY FKEALDRWAQ
     FFIHPLMIRD AIDREVEAVD SEYQLARPSD ANRKEMLFGS LARPGHPMGK FFWGNAETLK
     HEPKKNNIDT HARLREFWMR YYSAHYMTLV VQSKETLDTL EKWVTEIFSQ IPNNGLPRPN
     FGHLTDPFDT PAFNKLYRVV PIRKIHALTI TWALPPQQQH YRVKPLHYIS WLVGHEGKGS
     ILSFLRKKCW ALALFGGNGE TGFEQNSTYS VFSISITLTD EGYEHFYEVA YTVFQYLKML
     QKLGPEKRIF EEIRKIEDNE FHYQEQTDPV EYVENMCENM QLYPLQDILT GDQLLFEYKP
     EVIAEALNQL VPQKANLVLL SGANEGKCDL KEKWFGTQYS IEDIENSWAE LWSSNFELNP
     DLHLPAENKY IATDFTLKAF DCPETEYPVK IVNTPQGCLW YKKDNKFKIP KAYIRFHLIS
     PLIQKSAANV VLFDIFVNIL THNLAEPAYE ADVAQLEYKL VAGEHGLIIR VKGFNHKLPL
     LFQLIIDYLA EFNSTPAVFT MITEQLKKTY FNILIKPETL AKDVRLLILE YARWSMIDKY
     QALMDGLSLE SLLSFVKEFK SQLFVEGLVQ GNVTSTESMD FLKYVVDKLN FKPLKQEMPV
     QFQVVELPSG HHLCKVKALN KGDANSEVTV YYQSGTRSLR EYTLMELLVM HMEEPCFDFL
     RTKQTLGYHV YPTCRNTSGI LGFSVTVGTQ ATKYNSEVVD KKIEEFLSSF EEKIENLTEE
     AFNTQVTALI KLKECEDTHL GEEVDRNWNE VVTQQYLFDR LAHEIEALKS FSKSDLVNWF
     KAHRGPGSKM LSVHVVGYGK YELEEDSTSS GEDSNSSCEV MQLTYLPTSP LLAD
//
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