NUDT7_MOUSE
ID NUDT7_MOUSE Reviewed; 236 AA.
AC Q99P30; Q6IS65; Q8BU08; Q8K260; Q9D0Q3; Q9DBI9;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Peroxisomal coenzyme A diphosphatase NUDT7;
DE EC=3.6.1.-;
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 7;
DE Short=Nudix motif 7;
GN Name=Nudt7 {ECO:0000312|MGI:MGI:1914778};
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, ENZYME ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=11415433; DOI=10.1042/0264-6021:3570033;
RA Gasmi L., McLennan A.G.;
RT "The mouse Nudt7 gene encodes a peroxisomal nudix hydrolase specific for
RT coenzyme A and its derivatives.";
RL Biochem. J. 357:33-38(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Liver, and Mammary gland;
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 ALTERNATIVE SPLICING, FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, INDUCTION BY PEROXISOMAL BETA-OXYDATION (ISOFORM 1),
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18799520; DOI=10.1093/jb/mvn114;
RA Reilly S.J., Tillander V., Ofman R., Alexson S.E., Hunt M.C.;
RT "The nudix hydrolase 7 is an Acyl-CoA diphosphatase involved in regulating
RT peroxisomal coenzyme A homeostasis.";
RL J. Biochem. 144:655-663(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Liver;
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 [6]
RP ABSENCE OF FUNCTION AS A DECAPPING ENZYME, AND RNA-BINDING.
RX PubMed=21070968; DOI=10.1016/j.molcel.2010.10.010;
RA Song M.G., Li Y., Kiledjian M.;
RT "Multiple mRNA decapping enzymes in mammalian cells.";
RL Mol. Cell 40:423-432(2010).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-20 AND LYS-178, 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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, COENZYME A BINDING SITES,
RP MAGNESIUM BINDING SITES, AND MUTAGENESIS OF ARG-60; LYS-65; ARG-66; ASP-79;
RP GLU-92; GLU-95 AND GLU-96.
RX PubMed=29378847; DOI=10.1074/jbc.ra117.001358;
RA Shumar S.A., Kerr E.W., Geldenhuys W.J., Montgomery G.E., Fagone P.,
RA Thirawatananond P., Saavedra H., Gabelli S.B., Leonardi R.;
RT "Nudt19 is a renal CoA diphosphohydrolase with biochemical and regulatory
RT properties that are distinct from the hepatic Nudt7 isoform.";
RL J. Biol. Chem. 293:4134-4148(2018).
RN [9]
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: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes
CC fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-
CC bisphosphate (PubMed:11415433, PubMed:18799520, PubMed:29378847).
CC Cleaves CoA, CoA esters and oxidized CoA with similar efficiencies
CC (PubMed:11415433). Preferentially hydrolyzes medium-chain acyl-CoAs and
CC bile acid-CoAs (PubMed:18799520). Has no activity toward NDP-sugars,
CC CDP-alcohols, (deoxy)nucleoside 5'-triphosphates, nucleoside 5'-di or
CC monophosphates, diadenosine polyphosphates, NAD, NADH, NADP, NADPH or
CC thymidine-5'-monophospho-p-nitrophenyl ester (PubMed:18799520). May be
CC required to eliminate oxidized CoA from peroxisomes, or regulate CoA
CC and acyl-CoA levels in this organelle in response to metabolic demand
CC (PubMed:18799520). Does not play a role in U8 snoRNA decapping activity
CC (PubMed:21070968). Binds U8 snoRNA (PubMed:21070968). Exhibits
CC decapping activity towards dpCoA-capped RNAs in vitro
CC (PubMed:32432673). {ECO:0000269|PubMed:11415433,
CC ECO:0000269|PubMed:18799520, ECO:0000269|PubMed:21070968,
CC ECO:0000269|PubMed:29378847, ECO:0000269|PubMed:32432673}.
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:18799520, ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49981;
CC Evidence={ECO:0000305|PubMed:18799520};
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:18799520, ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50017;
CC Evidence={ECO:0000305|PubMed:18799520};
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:18799520, ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49977;
CC Evidence={ECO:0000305|PubMed:18799520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=decanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + decanoyl-
CC 4'-phosphopantetheine + 2 H(+); Xref=Rhea:RHEA:50020,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:61430, ChEBI:CHEBI:132014;
CC Evidence={ECO:0000269|PubMed:18799520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50021;
CC Evidence={ECO:0000305|PubMed:18799520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) +
CC S-dodecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50024,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57375,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132015;
CC Evidence={ECO:0000269|PubMed:18799520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50025;
CC Evidence={ECO:0000305|PubMed:18799520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + tetradecanoyl-CoA = adenosine 3',5'-bisphosphate + 2
CC H(+) + tetradecanoyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50028,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132017;
CC Evidence={ECO:0000269|PubMed:18799520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50029;
CC Evidence={ECO:0000305|PubMed:18799520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choloyl-CoA + H2O = adenosine 3',5'-bisphosphate + 2 H(+) + S-
CC choloyl-4'-phosphopantetheine; Xref=Rhea:RHEA:50036,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57373,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:132020;
CC Evidence={ECO:0000269|PubMed:18799520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50037;
CC Evidence={ECO:0000305|PubMed:18799520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA +
CC H2O = 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-4'-
CC phosphopantetheine + adenosine 3',5'-bisphosphate + 2 H(+);
CC Xref=Rhea:RHEA:50040, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:63001, ChEBI:CHEBI:132021;
CC Evidence={ECO:0000269|PubMed:18799520};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50041;
CC Evidence={ECO:0000305|PubMed:18799520};
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:18799520, ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64993;
CC Evidence={ECO:0000305|PubMed:18799520};
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:18799520,
CC ECO:0000269|PubMed:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64989;
CC Evidence={ECO:0000305|PubMed:18799520};
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:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67465;
CC Evidence={ECO:0000305|PubMed:29378847};
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:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67469;
CC Evidence={ECO:0000305|PubMed:29378847};
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:29378847};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67473;
CC Evidence={ECO:0000305|PubMed:29378847};
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11415433};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11415433, ECO:0000269|PubMed:29378847};
CC -!- ACTIVITY REGULATION: Inhibited by fluoride.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.240 mM for CoA {ECO:0000269|PubMed:11415433};
CC KM=0.157 mM for CoA {ECO:0000269|PubMed:18799520};
CC KM=0.270 mM for acetyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=92.6 uM for hexanoyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=62.6 uM for octanoyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=34 uM for tetradecanoyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=157.9 uM for butanoyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=242 uM for decanoyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=22.4 uM for dodecanoyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=221.4 uM for propionyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=28.7 uM for palmitoyl-CoA {ECO:0000269|PubMed:18799520};
CC KM=0.430 mM for acetyl-CoA {ECO:0000269|PubMed:11415433};
CC KM=0.235 mM for CoA-S-S-CoA {ECO:0000269|PubMed:11415433};
CC KM=0.330 mM for succinyl-CoA {ECO:0000269|PubMed:11415433};
CC KM=0.480 mM for 3'-dephospho-CoA {ECO:0000269|PubMed:11415433};
CC KM=283 uM for CoA {ECO:0000269|PubMed:29378847};
CC Vmax=0.13 umol/min/mg enzyme toward CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=0.27 umol/min/mg enzyme toward acetyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=0.33 umol/min/mg enzyme toward propionyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=0.49 umol/min/mg enzyme toward butanoyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=0.83 umol/min/mg enzyme toward hexanoyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=1.08 umol/min/mg enzyme toward octanoyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=1.84 umol/min/mg enzyme toward decanoyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=1.06 umol/min/mg enzyme toward dodecanoyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=0.41 umol/min/mg enzyme toward tetradecanoyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC Vmax=0.15 umol/min/mg enzyme toward palmitoyl-CoA
CC {ECO:0000269|PubMed:18799520};
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:11415433};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:29378847}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:11415433,
CC ECO:0000269|PubMed:18799520}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Alpha, Nudt7alpha {ECO:0000303|PubMed:18799520};
CC IsoId=Q99P30-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta, Nudt7beta, Nudt7gamma
CC {ECO:0000303|PubMed:18799520};
CC IsoId=Q99P30-2; Sequence=VSP_014272;
CC Name=3;
CC IsoId=Q99P30-3; Sequence=VSP_014273;
CC Name=4;
CC IsoId=Q99P30-4; Sequence=VSP_014271;
CC Name=5;
CC IsoId=Q99P30-5; Sequence=VSP_014274, VSP_014275;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Highly expressed in liver, brown
CC adipose tissue and heart. Expressed at intermediate level in lung and
CC kidney and at low level in brain. {ECO:0000269|PubMed:11415433,
CC ECO:0000269|PubMed:18799520, ECO:0000269|PubMed:29378847}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in liver, brown adipose
CC tissue and heart at 20 times lower levels than isoform 1.
CC {ECO:0000269|PubMed:18799520}.
CC -!- INDUCTION: [Isoform 1]: Expression decreases in response to peroxisome
CC proliferators. {ECO:0000269|PubMed:18799520}.
CC -!- MISCELLANEOUS: [Isoform 2]: Inactive. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. PCD1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH33046.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF338424; AAK07483.1; -; mRNA.
DR EMBL; AK004924; BAB23675.1; -; mRNA.
DR EMBL; AK011172; BAB27446.1; -; mRNA.
DR EMBL; AK088191; BAC40199.1; -; mRNA.
DR EMBL; BC033046; AAH33046.1; ALT_INIT; mRNA.
DR EMBL; BC069843; AAH69843.1; -; mRNA.
DR CCDS; CCDS22687.1; -. [Q99P30-1]
DR CCDS; CCDS22688.2; -. [Q99P30-3]
DR CCDS; CCDS80934.1; -. [Q99P30-5]
DR CCDS; CCDS80935.1; -. [Q99P30-2]
DR RefSeq; NP_001277109.1; NM_001290180.1.
DR RefSeq; NP_001277110.1; NM_001290181.1. [Q99P30-2]
DR RefSeq; NP_001277111.1; NM_001290182.1. [Q99P30-5]
DR RefSeq; NP_077757.2; NM_024437.4. [Q99P30-1]
DR RefSeq; NP_077766.3; NM_024446.5. [Q99P30-3]
DR AlphaFoldDB; Q99P30; -.
DR SMR; Q99P30; -.
DR BioGRID; 212251; 1.
DR STRING; 10090.ENSMUSP00000073213; -.
DR SwissLipids; SLP:000001595; -. [Q99P30-1]
DR iPTMnet; Q99P30; -.
DR PhosphoSitePlus; Q99P30; -.
DR SwissPalm; Q99P30; -.
DR REPRODUCTION-2DPAGE; Q99P30; -.
DR EPD; Q99P30; -.
DR jPOST; Q99P30; -.
DR MaxQB; Q99P30; -.
DR PaxDb; Q99P30; -.
DR PeptideAtlas; Q99P30; -.
DR PRIDE; Q99P30; -.
DR ProteomicsDB; 291925; -. [Q99P30-1]
DR ProteomicsDB; 291926; -. [Q99P30-2]
DR ProteomicsDB; 291927; -. [Q99P30-3]
DR ProteomicsDB; 291928; -. [Q99P30-4]
DR ProteomicsDB; 291929; -. [Q99P30-5]
DR Antibodypedia; 48153; 28 antibodies from 11 providers.
DR DNASU; 67528; -.
DR Ensembl; ENSMUST00000066514; ENSMUSP00000065791; ENSMUSG00000031767. [Q99P30-4]
DR Ensembl; ENSMUST00000073521; ENSMUSP00000073213; ENSMUSG00000031767. [Q99P30-1]
DR Ensembl; ENSMUST00000109109; ENSMUSP00000104737; ENSMUSG00000031767. [Q99P30-2]
DR Ensembl; ENSMUST00000134593; ENSMUSP00000116868; ENSMUSG00000031767. [Q99P30-5]
DR Ensembl; ENSMUST00000147605; ENSMUSP00000114598; ENSMUSG00000031767. [Q99P30-3]
DR GeneID; 67528; -.
DR KEGG; mmu:67528; -.
DR UCSC; uc009nnv.3; mouse. [Q99P30-5]
DR UCSC; uc009nnw.3; mouse. [Q99P30-1]
DR UCSC; uc009nny.3; mouse. [Q99P30-3]
DR UCSC; uc012glf.2; mouse. [Q99P30-4]
DR UCSC; uc057and.1; mouse. [Q99P30-2]
DR CTD; 283927; -.
DR MGI; MGI:1914778; Nudt7.
DR VEuPathDB; HostDB:ENSMUSG00000031767; -.
DR eggNOG; KOG3069; Eukaryota.
DR GeneTree; ENSGT00940000159631; -.
DR HOGENOM; CLU_040940_6_0_1; -.
DR InParanoid; Q99P30; -.
DR OMA; CPNPAEV; -.
DR OrthoDB; 1253012at2759; -.
DR PhylomeDB; Q99P30; -.
DR TreeFam; TF106350; -.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 67528; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Nudt7; mouse.
DR PRO; PR:Q99P30; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q99P30; protein.
DR Bgee; ENSMUSG00000031767; Expressed in left lobe of liver and 235 other tissues.
DR Genevisible; Q99P30; MM.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0003986; F:acetyl-CoA hydrolase activity; IBA:GO_Central.
DR GO; GO:0010945; F:CoA pyrophosphatase activity; IDA:MGI.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0030515; F:snoRNA binding; IDA:UniProtKB.
DR GO; GO:0046356; P:acetyl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
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:0009132; P:nucleoside diphosphate metabolic process; IEA:InterPro.
DR GO; GO:1902859; P:propionyl-CoA catabolic process; IDA:UniProtKB.
DR GO; GO:1902858; P:propionyl-CoA metabolic 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 InterPro; IPR000059; NUDIX_hydrolase_NudL_CS.
DR PANTHER; PTHR12992; PTHR12992; 1.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS01293; NUDIX_COA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Peroxisome; Reference proteome; RNA-binding.
FT CHAIN 1..236
FT /note="Peroxisomal coenzyme A diphosphatase NUDT7"
FT /id="PRO_0000057141"
FT DOMAIN 37..169
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 77..98
FT /note="Nudix box"
FT MOTIF 234..236
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000305"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:29378847"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:29378847"
FT SITE 66
FT /note="Important for coenzyme A binding"
FT /evidence="ECO:0000269|PubMed:29378847"
FT MOD_RES 20
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 178
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..63
FT /note="MSRPCGLPEPVRNNLIDDAKARLRKSDVGTRYSHLSSNKFSVLVPLLARGGK
FT LYLMFTVRSDK -> MRVRTICFPKSPAASKRKYCRADVATLWTPGACQ (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014271"
FT VAR_SEQ 1..12
FT /note="MSRPCGLPEPVR -> MVQSLELPQRQPCHFGSWIKRSPSGLTSKSPSQVLG
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11415433,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_014272"
FT VAR_SEQ 97..116
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_014273"
FT VAR_SEQ 117..171
FT /note="NDALVTPVVGFLDHNFQAQPNADEVKEVFFVPLDYFLHPQVYYQKQITQSGR
FT DFI -> VRTGMGPPELSGASTKFPNTLGTEPGELSPCVDSVLCELCGPSHSIQEERGE
FT PPQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014274"
FT VAR_SEQ 172..236
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014275"
FT MUTAGEN 60
FT /note="R->M: 2- to 3-fold increase in Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 65
FT /note="K->A: 3-fold increase in Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 66
FT /note="R->A: 10-fold increase in Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 66
FT /note="R->M: No significant effect on Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 79
FT /note="D->A: No significant effect on Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 92
FT /note="E->A: Loss of fatty acyl-coenzyme A diphosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 95
FT /note="E->A: No significant effect on Km for CoA."
FT /evidence="ECO:0000269|PubMed:29378847"
FT MUTAGEN 96
FT /note="E->A: Loss of fatty acyl-coenzyme A diphosphatase
FT activity."
FT /evidence="ECO:0000269|PubMed:29378847"
FT CONFLICT 161
FT /note="K -> E (in Ref. 1; AAK07483)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 236 AA; 26857 MW; 37A22A9135F8F9ED CRC64;
MSRPCGLPEP VRNNLIDDAK ARLRKSDVGT RYSHLSSNKF SVLVPLLARG GKLYLMFTVR
SDKLKREPGE VCFPGGKRDP VDTDDTATAL REAQEEVGLH PHQVEVVSHL VPYVFDNDAL
VTPVVGFLDH NFQAQPNADE VKEVFFVPLD YFLHPQVYYQ KQITQSGRDF IMHCFEYKDP
ETGVNYLIQG MTSKLAVLVA LIILEQSPAF KIDFDLHDLI PSCERTFLWR YSLSKL
