NUDT8_MOUSE
ID NUDT8_MOUSE Reviewed; 210 AA.
AC Q9CR24; Q3TDQ2;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Mitochondrial coenzyme A diphosphatase NUDT8;
DE EC=3.6.1.-;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 8;
DE Short=Nudix motif 8;
GN Name=Nudt8;
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, and NOD; TISSUE=Kidney, and Tongue;
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=C57BL/6J; TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, and Pancreas;
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).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-70 AND LYS-96, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=31004344; DOI=10.1002/1873-3468.13392;
RA Kerr E.W., Shumar S.A., Leonardi R.;
RT "Nudt8 is a novel CoA diphosphohydrolase that resides in the
RT mitochondria.";
RL FEBS Lett. 593:1133-1143(2019).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32432673; DOI=10.1093/nar/gkaa402;
RA Sharma S., Grudzien-Nogalska E., Hamilton K., Jiao X., Yang J., Tong L.,
RA Kiledjian M.;
RT "Mammalian Nudix proteins cleave nucleotide metabolite caps on RNAs.";
RL Nucleic Acids Res. 48:6788-6798(2020).
CC -!- FUNCTION: Acyl-CoA diphosphatase that mediates the hydrolysis of a wide
CC range of CoA and CoA esters yielding 3',5'-ADP and the corresponding
CC 4'-phosphopantetheine derivative as products (PubMed:31004344).
CC Hydrolyzes short- and medium-chain acyl-CoAs, exhibiting the highest
CC activity toward free CoA, hexanoyl-CoA, and octanoyl-CoA and the lowest
CC activity against acetyl-CoA (PubMed:31004344). Exhibits decapping
CC activity towards dpCoA-capped RNAs in vitro (PubMed:32432673).
CC {ECO:0000269|PubMed:31004344, ECO:0000269|PubMed:32432673}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl-CoA + H2O = adenosine 3',5'-bisphosphate + an acyl-4'-
CC phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58342, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:132023; Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50045;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CoA + H2O = (R)-4'-phosphopantetheine + adenosine 3',5'-
CC bisphosphate + 2 H(+); Xref=Rhea:RHEA:64988, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:61723; Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64989;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-
CC acetyl-4'-phosphopantetheine; Xref=Rhea:RHEA:64992,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:156266;
CC Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64993;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=butanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-butanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49976,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57371,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132011;
CC Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49977;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC hexanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:49980,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:62620, ChEBI:CHEBI:132012;
CC Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49981;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + octanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-octanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50016,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132013;
CC Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50017;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + propanoyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC propanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67464,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57392,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172362;
CC Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67465;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + malonyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC malonyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57384,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172363;
CC Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67469;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + succinyl-CoA = adenosine 3',5'-bisphosphate + 2 H(+) +
CC succinyl-4'-phosphopantetheine; Xref=Rhea:RHEA:67472,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57292,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:172364;
CC Evidence={ECO:0000269|PubMed:31004344};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67473;
CC Evidence={ECO:0000305|PubMed:31004344};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-
CC phosphopantetheine + a 5'-end phospho-adenosine-phospho-
CC ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-
CC COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051,
CC ChEBI:CHEBI:172371; Evidence={ECO:0000305|PubMed:32432673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593;
CC Evidence={ECO:0000305|PubMed:32432673};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:31004344};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:31004344};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=707 uM for acetyl-CoA {ECO:0000269|PubMed:31004344};
CC KM=318 uM for propanol-CoA {ECO:0000269|PubMed:31004344};
CC KM=224 uM for butanoyl-CoA {ECO:0000269|PubMed:31004344};
CC KM=233 uM for malonyl-CoA {ECO:0000269|PubMed:31004344};
CC KM=329 uM for succinyl-CoA {ECO:0000269|PubMed:31004344};
CC KM=251 uM for hexanoyl-CoA {ECO:0000269|PubMed:31004344};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:31004344}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:31004344}.
CC -!- TISSUE SPECIFICITY: Expressed at the highest levels in the kidneys,
CC heart, brown adipose tissue and liver (at protein level)
CC (PubMed:31004344). Expressed at lower levels in the brain, skeletal
CC muscle, and white adipose tissue (at protein level) (PubMed:31004344).
CC {ECO:0000269|PubMed:31004344}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AK002605; BAB22224.1; -; mRNA.
DR EMBL; AK009700; BAB26447.1; -; mRNA.
DR EMBL; AK045197; BAC32259.1; -; mRNA.
DR EMBL; AK170076; BAE41549.1; -; mRNA.
DR EMBL; BC056443; AAH56443.1; -; mRNA.
DR CCDS; CCDS29408.1; -.
DR RefSeq; NP_079805.1; NM_025529.3.
DR AlphaFoldDB; Q9CR24; -.
DR SMR; Q9CR24; -.
DR STRING; 10090.ENSMUSP00000025802; -.
DR iPTMnet; Q9CR24; -.
DR PhosphoSitePlus; Q9CR24; -.
DR SwissPalm; Q9CR24; -.
DR EPD; Q9CR24; -.
DR MaxQB; Q9CR24; -.
DR PaxDb; Q9CR24; -.
DR PeptideAtlas; Q9CR24; -.
DR PRIDE; Q9CR24; -.
DR ProteomicsDB; 287854; -.
DR DNASU; 66387; -.
DR Ensembl; ENSMUST00000025802; ENSMUSP00000025802; ENSMUSG00000110949.
DR Ensembl; ENSMUST00000155405; ENSMUSP00000119218; ENSMUSG00000024869.
DR GeneID; 66387; -.
DR KEGG; mmu:66387; -.
DR UCSC; uc008fyb.1; mouse.
DR CTD; 254552; -.
DR MGI; MGI:1913637; Nudt8.
DR VEuPathDB; HostDB:ENSMUSG00000024869; -.
DR VEuPathDB; HostDB:ENSMUSG00000110949; -.
DR eggNOG; ENOG502SDBZ; Eukaryota.
DR GeneTree; ENSGT00940000162775; -.
DR HOGENOM; CLU_040940_4_0_1; -.
DR InParanoid; Q9CR24; -.
DR OMA; YYIWGAT; -.
DR OrthoDB; 1253012at2759; -.
DR PhylomeDB; Q9CR24; -.
DR TreeFam; TF106350; -.
DR BioGRID-ORCS; 66387; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Nudt8; mouse.
DR PRO; PR:Q9CR24; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CR24; protein.
DR Bgee; ENSMUSG00000024869; Expressed in cortical plate and 54 other tissues.
DR Genevisible; Q9CR24; MM.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0106399; F:acyl-coenzyme A diphosphatase activity; IEA:RHEA.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0046356; P:acetyl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:0044580; P:butyryl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:0015938; P:coenzyme A catabolic process; IDA:UniProtKB.
DR GO; GO:2001294; P:malonyl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:0036114; P:medium-chain fatty-acyl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:1902859; P:propionyl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:1901289; P:succinyl-CoA catabolic process; IDA:UniProtKB.
DR CDD; cd03426; CoAse; 1.
DR InterPro; IPR045121; CoAse.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR PANTHER; PTHR12992; PTHR12992; 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; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..210
FT /note="Mitochondrial coenzyme A diphosphatase NUDT8"
FT /id="PRO_0000019949"
FT DOMAIN 25..172
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 70..91
FT /note="Nudix box"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 96
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 210 AA; 23253 MW; 2E153033C466A6FE CRC64;
MLPDGLSAED EQRCRQLLAR TTARLRSRPA AAAVLVPLCL VRGVPALLYT LRSSRLVGRH
KGEVSFPGGK CDPDDQDVIH TALRETQEEL GLEVPKEHVW GVLQPVYDRE KATIVPVLAN
VGPLDLQSLR PNLEEVDEVF EMSLAHLLQT QNQGYTHFCQ GGHFSYTLPV FLHGPHRVWG
LTAVITELTL KLLAPGFYQP SLAVPELPRG
