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Database: UniProt
Entry: G3QQ46_GORGO
LinkDB: G3QQ46_GORGO
Original site: G3QQ46_GORGO 
ID   G3QQ46_GORGO            Unreviewed;      1219 AA.
AC   G3QQ46;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Nardilysin convertase {ECO:0000313|Ensembl:ENSGGOP00000004704.2};
GN   Name=NRDC {ECO:0000313|Ensembl:ENSGGOP00000004704.2};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000004704.2, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000004704.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000004704.2, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000004704.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261}.
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DR   EMBL; CABD030003211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030003212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030003213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030003214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_018873978.1; XM_019018433.1.
DR   AlphaFoldDB; G3QQ46; -.
DR   STRING; 9593.ENSGGOP00000004704; -.
DR   MEROPS; M16.005; -.
DR   Ensembl; ENSGGOT00000004824.3; ENSGGOP00000004704.2; ENSGGOG00000004793.3.
DR   GeneID; 101131269; -.
DR   KEGG; ggo:101131269; -.
DR   CTD; 4898; -.
DR   eggNOG; KOG0959; Eukaryota.
DR   GeneTree; ENSGT00940000155026; -.
DR   InParanoid; G3QQ46; -.
DR   OMA; INQVMEH; -.
DR   OrthoDB; 129328at2759; -.
DR   TreeFam; TF106274; -.
DR   Proteomes; UP000001519; Chromosome 1.
DR   Bgee; ENSGGOG00000004793; Expressed in testis and 6 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:UP000001519};
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..205
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   1219 AA;  139399 MW;  C50E2BCE7F078C6E CRC64;
     MLRRVTVAAV CATRRKLCEA GRELAALWGI ETRGRCEDSA AARPFPILAM PGRNKAKSTC
     SCPDLQPNGQ DLGENSRVAR LGADESEEEG RRGSLSNAGD PEIVKSPSDP KQYRYIKLQN
     GLQALLISDL SNMEGKTGNT TDDEEEEEVE EEEEDDDEDS GAEIEDDDEE GFDDEDEFDD
     EHDDDLDTED NELEELEERA EARKKTTEKQ QLQSLFLLWS KLTDRLWFKS TYSKMSSTLL
     VETRNLYGVV GAESRSAPVQ HLAGWQAEEQ QGETDTVLSA AALCVGVGSF ADPDDLPGLA
     HFLEHMVFMG SLKYPDENGF DAFLKKHGGS DNASTDCERT VFQFDVQRKY FKEALDRWAQ
     FFIHPLMIRD AIDREVEAVD SEYQLARPSD ANRKEMLFGS LARPGHPMGK FFWGNAETLK
     HEPKKNNIDT HARLREFWMR YYSSHYMTLV VQSKETLDTL EKWVTEIFSQ IPNNGLPRPN
     FGHLTDPFDT PAFNKLYRVV PIRKIHALTI TWALPPQQQH YRVKPLHYIS WLVGHEGKGS
     ILSFLRKKCW ALALFGGNGE TGFEQNSTYS VFSISITLTD EGYEHFYEVA YTVFQYLKML
     QKLGPEKRIF EEIRKIEDNE FHYQEQTDPV EYVENMCENM QLYPLQDILT GDQLLFEYKP
     EVIGEALNQL VPQKANLVLL SGANEGKCDL KEKWFGTQYS IEDIENSWAE LWNSNFELNP
     DLHLPAENKY IATDFTLKAF DCPETEYPVK IVNTPQGCLW YKKDNKFKIP KAYIRFHLIS
     PLIQKSAANV VLFDIFVNIL THNLAEPAYE ADVAQLEYKL VAGEHGLIIR VKGFNHKLPL
     LFQLIIDYLA EFNSTPAVFT MITEQLKKTY FNILIKPETL AKDVRLLILE YARWSMIDKY
     QALMDGLSLE SLLSFVKEFK SQLFVEGLVQ GNVTSTESMD FLKYVVDKLN FKPLEQEMPV
     QFQVVELPSG HHLCKVKALN KGDANSEVTV YYQSGTRSLR EYTLMELLVM HMEEPCFDFL
     RTKQTLGYHV YPTCRNTSGI LGFSVTVGTQ ATKYNSEVVD KKIEEFLSSF EEKIENLTEE
     AFNTQVTALI KLKECEDTHL GEEVDRNWNE VVTQQYLFDR LAHEIEALKS FSKSDLVNWF
     KAHRGPGSKM LSVHVVGYGK YELEEDGTPS TEDSNSSCEV MQLTYLPTSP LLADCIIPIT
     DIRAFTTTLN LLPYHKIVK
//
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