ID   NUD12_MOUSE             Reviewed;         462 AA.
AC   Q9DCN1; Q6PFA5;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=NAD-capped RNA hydrolase NUDT12 {ECO:0000305};
DE            Short=DeNADding enzyme NUDT12 {ECO:0000305};
DE            EC=3.6.1.- {ECO:0000269|PubMed:31101919, ECO:0000269|PubMed:32432673};
DE   AltName: Full=NADH pyrophosphatase NUDT12 {ECO:0000305};
DE            EC=3.6.1.22 {ECO:0000250|UniProtKB:Q9BQG2};
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 12 {ECO:0000305};
DE            Short=Nudix motif 12 {ECO:0000305};
GN   Name=Nudt12 {ECO:0000303|PubMed:31101919,
GN   ECO:0000312|MGI:MGI:1915243};
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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] (ISOFORM 2).
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Liver, Lung, 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).
RN   [4]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-10; LYS-185 AND LYS-292, 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, 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).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=31875550; DOI=10.1016/j.celrep.2019.11.108;
RA   Wu H., Li L., Chen K.M., Homolka D., Gos P., Fleury-Olela F.,
RA   McCarthy A.A., Pillai R.S.;
RT   "Decapping Enzyme NUDT12 Partners with BLMH for Cytoplasmic Surveillance of
RT   NAD-Capped RNAs.";
RL   Cell Rep. 29:4422-4434(2019).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 131-457 IN COMPLEX WITH AMP;
RP   MAGNESIUM AND ZINC, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND
RP   MUTAGENESIS OF 373-GLU-GLU-374.
RX   PubMed=31101919; DOI=10.1038/s41589-019-0293-7;
RA   Grudzien-Nogalska E., Wu Y., Jiao X., Cui H., Mateyak M.K., Hart R.P.,
RA   Tong L., Kiledjian M.;
RT   "Structural and mechanistic basis of mammalian Nudt12 RNA deNADding.";
RL   Nat. Chem. Biol. 15:575-582(2019).
CC   -!- FUNCTION: mRNA decapping enzyme that specifically removes the
CC       nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by
CC       hydrolyzing the diphosphate linkage to produce nicotinamide
CC       mononucleotide (NMN) and 5' monophosphate mRNA (PubMed:31101919,
CC       PubMed:32432673). The NAD-cap is present at the 5'-end of some RNAs; in
CC       contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap
CC       promotes mRNA decay (PubMed:31101919). Preferentially acts on NAD-
CC       capped transcripts in response to nutrient stress (PubMed:31101919).
CC       Also acts on free nicotinamide adenine dinucleotide molecules:
CC       hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-
CC       ADP (By similarity). May act to regulate the concentration of
CC       peroxisomal nicotinamide nucleotide cofactors required for oxidative
CC       metabolism in this organelle (By similarity). Regulates the levels of
CC       circadian clock components PER1, PER2, PER3 and CRY2 in the liver
CC       (PubMed:31875550). {ECO:0000250|UniProtKB:Q9BQG2,
CC       ECO:0000269|PubMed:31101919, ECO:0000269|PubMed:31875550}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC         end phospho-adenosine-phospho-ribonucleoside in mRNA + beta-
CC         nicotinamide D-ribonucleotide + 2 H(+); Xref=Rhea:RHEA:60876,
CC         Rhea:RHEA-COMP:15698, Rhea:RHEA-COMP:15719, ChEBI:CHEBI:14649,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:144029,
CC         ChEBI:CHEBI:144051; Evidence={ECO:0000269|PubMed:31101919,
CC         ECO:0000269|PubMed:32432673};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC         Evidence={ECO:0000269|PubMed:31101919};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NAD(+) = AMP + beta-nicotinamide D-ribonucleotide + 2
CC         H(+); Xref=Rhea:RHEA:11800, ChEBI:CHEBI:14649, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:456215;
CC         EC=3.6.1.22; Evidence={ECO:0000269|PubMed:31101919};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11801;
CC         Evidence={ECO:0000269|PubMed:31101919};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADH = AMP + 2 H(+) + reduced beta-nicotinamide D-
CC         ribonucleotide; Xref=Rhea:RHEA:48868, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57945, ChEBI:CHEBI:90832,
CC         ChEBI:CHEBI:456215; EC=3.6.1.22;
CC         Evidence={ECO:0000250|UniProtKB:Q9BQG2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48869;
CC         Evidence={ECO:0000250|UniProtKB:Q9BQG2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + NADPH = adenosine 2',5'-bisphosphate + 2 H(+) + reduced
CC         beta-nicotinamide D-ribonucleotide; Xref=Rhea:RHEA:60820,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:90832, ChEBI:CHEBI:194156;
CC         Evidence={ECO:0000250|UniProtKB:Q9BQG2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60821;
CC         Evidence={ECO:0000250|UniProtKB:Q9BQG2};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:31101919};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:31101919};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:31101919};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:31101919};
CC   -!- SUBUNIT: Homodimer (PubMed:31101919). Homodimerization is essential for
CC       its catalytic activity and protein stability (By similarity). Interacts
CC       (via ANK repeats) with BLMH (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BQG2, ECO:0000269|PubMed:31101919}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BQG2}.
CC       Peroxisome {ECO:0000250|UniProtKB:Q9BQG2}. Cytoplasmic granule
CC       {ECO:0000250|UniProtKB:Q9BQG2}. Note=Localizes to cytoplasmic granules
CC       in the presence of BLMH. {ECO:0000250|UniProtKB:Q9BQG2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DCN1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DCN1-2; Sequence=VSP_014280, VSP_014281;
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in the liver and kidney.
CC       {ECO:0000269|PubMed:31875550}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK002641; BAB22253.1; -; mRNA.
DR   EMBL; BC057657; AAH57657.1; -; mRNA.
DR   CCDS; CCDS28933.1; -. [Q9DCN1-1]
DR   RefSeq; NP_080773.1; NM_026497.2. [Q9DCN1-1]
DR   PDB; 6O3P; X-ray; 1.60 A; A/B=126-460.
DR   PDBsum; 6O3P; -.
DR   AlphaFoldDB; Q9DCN1; -.
DR   SMR; Q9DCN1; -.
DR   BioGRID; 212586; 1.
DR   STRING; 10090.ENSMUSP00000025065; -.
DR   GlyGen; Q9DCN1; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9DCN1; -.
DR   PhosphoSitePlus; Q9DCN1; -.
DR   SwissPalm; Q9DCN1; -.
DR   jPOST; Q9DCN1; -.
DR   MaxQB; Q9DCN1; -.
DR   PaxDb; 10090-ENSMUSP00000025065; -.
DR   PeptideAtlas; Q9DCN1; -.
DR   ProteomicsDB; 293806; -. [Q9DCN1-1]
DR   ProteomicsDB; 293807; -. [Q9DCN1-2]
DR   Pumba; Q9DCN1; -.
DR   Antibodypedia; 25275; 246 antibodies from 25 providers.
DR   DNASU; 67993; -.
DR   Ensembl; ENSMUST00000025065.12; ENSMUSP00000025065.6; ENSMUSG00000024228.13. [Q9DCN1-1]
DR   Ensembl; ENSMUST00000174122.2; ENSMUSP00000133678.2; ENSMUSG00000024228.13. [Q9DCN1-2]
DR   GeneID; 67993; -.
DR   KEGG; mmu:67993; -.
DR   UCSC; uc008dfc.1; mouse. [Q9DCN1-1]
DR   UCSC; uc008dfd.1; mouse. [Q9DCN1-2]
DR   AGR; MGI:1915243; -.
DR   CTD; 83594; -.
DR   MGI; MGI:1915243; Nudt12.
DR   VEuPathDB; HostDB:ENSMUSG00000024228; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG3084; Eukaryota.
DR   GeneTree; ENSGT00940000157592; -.
DR   HOGENOM; CLU_037162_0_2_1; -.
DR   InParanoid; Q9DCN1; -.
DR   OMA; EARWFPR; -.
DR   OrthoDB; 3024612at2759; -.
DR   PhylomeDB; Q9DCN1; -.
DR   TreeFam; TF106352; -.
DR   Reactome; R-MMU-197264; Nicotinamide salvaging.
DR   BioGRID-ORCS; 67993; 5 hits in 79 CRISPR screens.
DR   PRO; PR:Q9DCN1; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q9DCN1; Protein.
DR   Bgee; ENSMUSG00000024228; Expressed in left lobe of liver and 222 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005777; C:peroxisome; ISO:MGI.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0000210; F:NAD+ diphosphatase activity; ISO:MGI.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; ISO:MGI.
DR   GO; GO:1990174; F:phosphodiesterase decapping endonuclease activity; ISO:MGI.
DR   GO; GO:0110153; F:RNA NAD-cap (NMN-forming) hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0110156; P:methylguanosine-cap decapping; ISO:MGI.
DR   GO; GO:0006402; P:mRNA catabolic process; IDA:UniProtKB.
DR   GO; GO:0019677; P:NAD catabolic process; ISO:MGI.
DR   GO; GO:0110155; P:NAD-cap decapping; IDA:UniProtKB.
DR   GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR   GO; GO:0006742; P:NADP catabolic process; ISO:MGI.
DR   CDD; cd03429; NADH_pyrophosphatase; 1.
DR   Gene3D; 3.90.79.20; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR015375; NADH_PPase-like_N.
DR   InterPro; IPR049734; NudC-like_C.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR015376; Znr_NADH_PPase.
DR   PANTHER; PTHR42904:SF6; NAD-CAPPED RNA HYDROLASE NUDT12; 1.
DR   PANTHER; PTHR42904; NUDIX HYDROLASE, NUDC SUBFAMILY; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   Pfam; PF09296; NUDIX-like; 1.
DR   Pfam; PF09297; zf-NADH-PPase; 1.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
DR   Genevisible; Q9DCN1; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding; NAD; NADP; Peroxisome; Reference proteome;
KW   Repeat; Zinc.
FT   CHAIN           1..462
FT                   /note="NAD-capped RNA hydrolase NUDT12"
FT                   /id="PRO_0000056957"
FT   REPEAT          11..40
FT                   /note="ANK 1"
FT   REPEAT          45..74
FT                   /note="ANK 2"
FT   REPEAT          78..98
FT                   /note="ANK 3"
FT   DOMAIN          319..453
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   MOTIF           355..376
FT                   /note="Nudix box"
FT   MOTIF           460..462
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BQG2"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         287
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         354..356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         370
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         370
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         374
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         415
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         415
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:31101919,
FT                   ECO:0007744|PDB:6O3P"
FT   MOD_RES         10
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         185
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         292
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   VAR_SEQ         361..367
FT                   /note="ETIEDAV -> KPILTGF (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014280"
FT   VAR_SEQ         368..462
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014281"
FT   MUTAGEN         373..374
FT                   /note="EE->QQ: Abolished deNADding activity."
FT                   /evidence="ECO:0000269|PubMed:31101919"
FT   CONFLICT        78
FT                   /note="A -> G (in Ref. 2; AAH57657)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        290
FT                   /note="A -> V (in Ref. 2; AAH57657)"
FT                   /evidence="ECO:0000305"
FT   HELIX           130..132
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           136..143
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          157..162
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           166..168
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          169..171
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           181..188
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          195..202
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          226..232
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   TURN            234..236
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           238..241
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          247..249
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           262..280
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           295..297
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          299..303
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           308..310
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          322..330
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          334..341
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          353..356
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           363..375
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          379..390
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   TURN            391..394
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          395..405
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          413..415
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   STRAND          417..423
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           424..431
FT                   /evidence="ECO:0007829|PDB:6O3P"
FT   HELIX           447..456
FT                   /evidence="ECO:0007829|PDB:6O3P"
SQ   SEQUENCE   462 AA;  51511 MW;  92C2CBB0FAACEA6D CRC64;
     MSSVKRNPKK EMISELHSSA AEGNVAKLAG ILSHSPSLLN ETSENGWTAL MYAARNGHPD
     VVQFLLEKGC DRSLVNKARQ TALDIAAFWG YRHIANLLAN AKGGKKPWFL TNEVDECENY
     FSRTLLDRRS DKRNNSDWLQ AKESHPTTVY LLFSDLNPLV TLGGNKESSQ QPEVRLCQLN
     YPDVKGYLAQ PEKITLVFLG VELEMRKGSP AQAGGVPEEE EDGLVAWFAL GIEPGAAEEF
     KQRHENCYFL HPPMPALLQL KEKEAGVVAQ ARSVLAWHSR YKFCPTCGSA TKIEEGGYKR
     VCVRETCPSL QGVHNTSYPR VDPVVIMQVI HPDGTKCLLG RQKRFPPGMF TCLAGFIEPG
     ETIEDAVRRE VEEESGVKVG HVQYVSCQPW PMPSSLMIGC LAVAVSTEIK VDKNEIEDAR
     WFTREQVVDV LTKGKQQAFF VPPSRAIAHQ LIKHWVGMNP NL
//