NRDC_MOUSE
ID NRDC_MOUSE Reviewed; 1161 AA.
AC Q8BHG1;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Nardilysin;
DE EC=3.4.24.61;
DE AltName: Full=N-arginine dibasic convertase;
DE Short=NRD convertase;
DE Short=NRD-C;
DE AltName: Full=Nardilysin convertase {ECO:0000250|UniProtKB:O43847};
DE Flags: Precursor;
GN Name=Nrdc {ECO:0000250|UniProtKB:O43847}; Synonyms=Nrd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cleaves peptide substrates on the N-terminus of arginine
CC residues in dibasic pairs.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of polypeptides, preferably at -Xaa-|-Arg-Lys-, and
CC less commonly at -Arg-|-Arg-Xaa-, in which Xaa is not Arg or Lys.;
CC EC=3.4.24.61;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; AK031548; BAC27445.1; -; mRNA.
DR EMBL; BC036128; AAH36128.1; -; mRNA.
DR CCDS; CCDS18460.1; -.
DR RefSeq; NP_666262.2; NM_146150.2.
DR AlphaFoldDB; Q8BHG1; -.
DR SMR; Q8BHG1; -.
DR BioGRID; 230982; 12.
DR STRING; 10090.ENSMUSP00000068328; -.
DR MEROPS; M16.005; -.
DR iPTMnet; Q8BHG1; -.
DR PhosphoSitePlus; Q8BHG1; -.
DR EPD; Q8BHG1; -.
DR jPOST; Q8BHG1; -.
DR MaxQB; Q8BHG1; -.
DR PaxDb; Q8BHG1; -.
DR PRIDE; Q8BHG1; -.
DR Antibodypedia; 19043; 160 antibodies from 25 providers.
DR DNASU; 230598; -.
DR Ensembl; ENSMUST00000065977; ENSMUSP00000068328; ENSMUSG00000053510.
DR GeneID; 230598; -.
DR KEGG; mmu:230598; -.
DR UCSC; uc008ubw.1; mouse.
DR CTD; 230598; -.
DR MGI; MGI:1201386; Nrd1.
DR VEuPathDB; HostDB:ENSMUSG00000053510; -.
DR eggNOG; KOG0959; Eukaryota.
DR GeneTree; ENSGT00940000155026; -.
DR HOGENOM; CLU_004639_1_0_1; -.
DR InParanoid; Q8BHG1; -.
DR OMA; INQVMEH; -.
DR PhylomeDB; Q8BHG1; -.
DR TreeFam; TF106274; -.
DR BRENDA; 3.4.24.61; 3474.
DR BioGRID-ORCS; 230598; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Nrd1; mouse.
DR PRO; PR:Q8BHG1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8BHG1; protein.
DR Bgee; ENSMUSG00000053510; Expressed in seminiferous tubule of testis and 259 other tissues.
DR ExpressionAtlas; Q8BHG1; baseline and differential.
DR Genevisible; Q8BHG1; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0120163; P:negative regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0052548; P:regulation of endopeptidase activity; ISO:MGI.
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 Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR Pfam; PF16187; Peptidase_M16_M; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1161
FT /note="Nardilysin"
FT /id="PRO_0000026756"
FT REGION 49..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..207
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43847"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43847"
SQ SEQUENCE 1161 AA; 132891 MW; 21334221632A5122 CRC64;
MLRRVAVAAV CVTGRKLRCE AGRELTALGR IEARGLCEES SKPFPTLTMP GRNKAKSTCS
CPDLQPNGQD LGESGRLARL GADESEEEGR SFSNVGDPEI IKSPSDPKQY RYIKLQNGLQ
ALLISDLSNV EGKTGNATDE EEEEEEEEEE EDDDDDDDDD DDDEDSGAEI QDDDEEGFDD
EEEFDDDDDD EHDDDDLENE ENELEELEER VEARKKTTEK QSAAALCVGV GSFADPDDLP
GLAHFLEHMV FMGSLKYPDE NGFDAFLKKH GGSDNASTDC ERTVFQFDVQ RKYFKEALDR
WAQFFIHPLM IRDAIDREVE AVDSEYQLAR PSDANRKEML FGSLARPGHP MGKFFWGNAE
TLKHEPKKNN IDTHARLREF WMRYYSAHYM TLVVQSKETL DTLEKWVTEI FSQIPNNGLP
KPNFSHLTDP FDTPAFNKLY RVVPIRKIHA LTITWALPPQ QQHYRVKPLH YISWLVGHEG
KGSILSYLRK KCWALALFGG NGETGFEQNS TYSVFSISIT LTDEGYEHFY EVAHTVFQYL
KMLQKLGPEK RVFEEIQKIE DNEFHYQEQT DPVEYVENMC ENMQLYPRQD FLTGDQLLFE
YKPEVIAEAL NQLVPQKANL VLLSGANEGR CDLKEKWFGT QYSIEDIENS WTELWKSNFD
LNPDLHLPAE NKYIATDFTL KAFDCPETEY PAKIVNTAQG CLWYKKDNKF KIPKAYIRFH
LISPLIQKSA ANVVLFDIFV NILTHNLAEP AYEADVAQLE YKLVAGEHGL IIRVKGFNHK
LPLLFQLIID YLTEFSSTPA VFTMITEQLK KTYFNILIKP ETLAKDVRLL ILEYSRWSMI
DKYQALMDGL SLDSLLNFVK DFKSQLFVEG LVQGNVTSTE SMDFLKYVVD KLNFAPLERE
MPVQFQVVEL PSGHHLCKVR ALNKGDANSE VTVYYQSGTR SLREYTLMEL LVMHMEEPCF
DFLRTKQTLG YHVYPTCRNT SGILGFSVTV GTQATKYNSE TVDKKIEEFL SSFEEKIENL
TEDAFNTQVT ALIKLKECED THLGEEVDRN WNEVVTQQYL FDRLAHEIEA LKSFSKSDLV
SWFKAHRGPG SKMLSVHVVG YGKYELEEDG APFGEDSNSR EGMQLTYLPP SPVLAESTTP
ITDIRAFTAT LSLFPYHKIV K
