NUDT9_MOUSE
ID NUDT9_MOUSE Reviewed; 350 AA.
AC Q8BVU5; A2AH31; Q3TZ68; Q8K1J4;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=ADP-ribose pyrophosphatase, mitochondrial;
DE EC=3.6.1.13;
DE AltName: Full=ADP-ribose diphosphatase;
DE AltName: Full=ADP-ribose phosphohydrolase;
DE AltName: Full=Adenosine diphosphoribose pyrophosphatase;
DE Short=ADPR-PPase;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 9;
DE Short=Nudix motif 9;
DE Flags: Precursor;
GN Name=Nudt9;
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=Head, and Inner ear;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, 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: Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.13;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. Interacts with GLOD4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily.
CC {ECO:0000305}.
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DR EMBL; AK076500; BAC36366.1; -; mRNA.
DR EMBL; AK158058; BAE34342.1; -; mRNA.
DR EMBL; AL714024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033921; AAH33921.1; -; mRNA.
DR CCDS; CCDS19482.1; -.
DR RefSeq; NP_083070.2; NM_028794.4.
DR AlphaFoldDB; Q8BVU5; -.
DR SMR; Q8BVU5; -.
DR BioGRID; 216542; 1.
DR STRING; 10090.ENSMUSP00000031250; -.
DR iPTMnet; Q8BVU5; -.
DR PhosphoSitePlus; Q8BVU5; -.
DR EPD; Q8BVU5; -.
DR MaxQB; Q8BVU5; -.
DR PaxDb; Q8BVU5; -.
DR PeptideAtlas; Q8BVU5; -.
DR PRIDE; Q8BVU5; -.
DR ProteomicsDB; 289951; -.
DR Antibodypedia; 14458; 268 antibodies from 26 providers.
DR DNASU; 74167; -.
DR Ensembl; ENSMUST00000031250; ENSMUSP00000031250; ENSMUSG00000029310.
DR GeneID; 74167; -.
DR KEGG; mmu:74167; -.
DR UCSC; uc008yka.1; mouse.
DR CTD; 53343; -.
DR MGI; MGI:1921417; Nudt9.
DR VEuPathDB; HostDB:ENSMUSG00000029310; -.
DR eggNOG; KOG4195; Eukaryota.
DR GeneTree; ENSGT00390000017405; -.
DR HOGENOM; CLU_067226_0_0_1; -.
DR InParanoid; Q8BVU5; -.
DR OMA; PQWNQLD; -.
DR OrthoDB; 1186086at2759; -.
DR PhylomeDB; Q8BVU5; -.
DR TreeFam; TF106351; -.
DR Reactome; R-MMU-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR BioGRID-ORCS; 74167; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Nudt9; mouse.
DR PRO; PR:Q8BVU5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BVU5; protein.
DR Bgee; ENSMUSG00000029310; Expressed in saccule of membranous labyrinth and 257 other tissues.
DR ExpressionAtlas; Q8BVU5; baseline and differential.
DR Genevisible; Q8BVU5; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IDA:MGI.
DR GO; GO:0046032; P:ADP catabolic process; IDA:MGI.
DR GO; GO:0046709; P:IDP catabolic process; IDA:MGI.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR039989; NUDT9.
DR PANTHER; PTHR13030; PTHR13030; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Manganese; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..350
FT /note="ADP-ribose pyrophosphatase, mitochondrial"
FT /id="PRO_0000019951"
FT DOMAIN 178..334
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 53..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 215..237
FT /note="Nudix box"
FT COMPBIAS 53..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW91"
FT CONFLICT 343
FT /note="H -> R (in Ref. 3; AAH33921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 38604 MW; EDD9371307AB3373 CRC64;
MAGRSLGQAV ATVSLSVALA SVTVRSSACR AVPAPRNTFP TCGFHLNANI MSGSNGAKEN
SHNKARTSPY PGSKVERSQV PNEKVGWLVE WQDYNPVEYT AVSVLAGPQW ADPQISESNF
SPKFNEKDGH VERKSQNGLY EIENGRPRNP AGRTGLVGRG LLGRWGPNHA ADPIITRWKR
DESGNKITHP VSGKCILQFV AIKRKDCGEW AIPGGMVDPG EKISATLKRE FGEEALNSLQ
KSSAEKREIE EKLHALFSQE HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE TGETMDNLTL
EAGDDAGKVK WVDISDQLKL YASHSQFIKL VAEKRDAHWS EDHAADSRGL
