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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//