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
//