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Database: UniProt
Entry: A0A5F9DUX0_RABIT
LinkDB: A0A5F9DUX0_RABIT
Original site: A0A5F9DUX0_RABIT 
ID   A0A5F9DUX0_RABIT        Unreviewed;      1176 AA.
AC   A0A5F9DUX0;
DT   11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Nardilysin convertase {ECO:0000313|Ensembl:ENSOCUP00000049747.1};
GN   Name=NRDC {ECO:0000313|Ensembl:ENSOCUP00000049747.1};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000049747.1, ECO:0000313|Proteomes:UP000001811};
RN   [1] {ECO:0000313|Ensembl:ENSOCUP00000049747.1, ECO:0000313|Proteomes:UP000001811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000049747.1,
RC   ECO:0000313|Proteomes:UP000001811};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSOCUP00000049747.1}
RP   IDENTIFICATION.
RC   STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000049747.1};
RG   Ensembl;
RL   Submitted (NOV-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   EMBL; AAGW02002702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02002703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02002704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02002705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAGW02002706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A5F9DUX0; -.
DR   Ensembl; ENSOCUT00000056296.1; ENSOCUP00000049747.1; ENSOCUG00000004330.4.
DR   GeneTree; ENSGT00940000155026; -.
DR   Proteomes; UP000001811; Chromosome 13.
DR   Bgee; ENSOCUG00000004330; Expressed in testis and 15 other cell types or tissues.
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:UP000001811};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          228..361
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          387..572
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          578..859
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          864..1045
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          58..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          146..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..221
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1176 AA;  134878 MW;  4FEFD0E528B01FA3 CRC64;
     MHFSVNTPSK QQQPWVRVWL RRVTVAAVCA TGRKLWREAG RELAALWRIE ARGRCEDSAR
     PFPTRTMPGR NKAKSTCSCP DLQPNGQDLG ESGRVPRLGA DESEEEGRRG SLSNAGDPEI
     VKSPSDPKQY RYIKLRNGLQ ALLISDLSNM EGKPGNATDD EEEEEEEEEE DDDDDEDSGA
     EIEDDDEEGF DDEDEFDDDD DDDNEHDDDD LDTEDNELEE LEERAEARKK TTEKQSAAAL
     CVGVGSFADP DDLPGLAHFL EHMVFMGSLK YPDENGFDAF LKKHGGSDNA STDCERTVFQ
     FDVQRKYFKE ALDRWAQFFI HPLMIRDAID REVEAVDSEY QLARPSDANR KEMLFGSLAR
     PGHPMGKFFW GNAETLKHEP KKNNIDTHTR LREFWMRYYS AHYMTLVVQS KETLDTLEKW
     VTEIFSQIPN NGLPKPNFGH LTDPFDTPAF NKLYRVVPIR KIHALTITWA LPPQQQHYRV
     KPLHYISWLV GHEGKGSILS YLRKKCWALA LFGGNGETGF EQNSTYSVFS ISITLTDEGY
     EHFYEVAHTV FQYLKMLQKL GPEQRIFEEI QKIEDNEFHY QEQTDPVEYV ENMCENMQLY
     PLQDFLTGDQ LLFEYKPEVI AEALNQLVPQ KANLVLLSGA NEGKCDLKEK WFGTQYSIED
     VENSWNELWK SNFELNPELH LPAENKYIAT DFTLKAFDCP ETEYPVKIVN TPQGCLWYKK
     DNKFKIPKAY IRFHLISPLI QKSAANVVLF DIFVNILTHN LAEPAYEADV AQLEYKLVAG
     EHGLIIRVKG FNHKLPLLFQ LIIDYLAEFN STPAVFTMIT EQLKKTYFNI LIKPETLAKD
     VRLLILEYAR WSMIDKYRAL MDGLSLDSLL SFVKEFKSQL FVEGLVQGNV TSTESMDFLK
     YVVDKLNFVP LEQEMPVQFQ VVELPSGHHL CKVRALNKGD ANSEVTVYYQ SGTRSLREYT
     LMELLVMHME EPCFDFLRTK QTLGYHVYPT CRNTSGILGF SVTVGTQATK YNSEVVDKKI
     EEFLSSFEEK IENLTEDAFN TQVTALIKLK ECEDTHLGEE VDRNWNEVVT QQYLFDRLAH
     EIEALKSFSK SDLVNWFKAH RGPGSKMLSV HVVGYGKYEL EEDSNSSGED SNSSCEVMQL
     TYLPSSPLLA DSTIPITDIR AFTSTLSLLP YHKIVK
//
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