NUD12_MOUSE
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 03-AUG-2022, entry version 157.
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, 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 3',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:58343, ChEBI:CHEBI:90832;
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}.
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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 iPTMnet; Q9DCN1; -.
DR PhosphoSitePlus; Q9DCN1; -.
DR SwissPalm; Q9DCN1; -.
DR jPOST; Q9DCN1; -.
DR MaxQB; Q9DCN1; -.
DR PaxDb; Q9DCN1; -.
DR PeptideAtlas; Q9DCN1; -.
DR PRIDE; Q9DCN1; -.
DR ProteomicsDB; 293806; -. [Q9DCN1-1]
DR ProteomicsDB; 293807; -. [Q9DCN1-2]
DR Antibodypedia; 25275; 191 antibodies from 25 providers.
DR DNASU; 67993; -.
DR Ensembl; ENSMUST00000025065; ENSMUSP00000025065; ENSMUSG00000024228. [Q9DCN1-1]
DR Ensembl; ENSMUST00000174122; ENSMUSP00000133678; ENSMUSG00000024228. [Q9DCN1-2]
DR GeneID; 67993; -.
DR KEGG; mmu:67993; -.
DR UCSC; uc008dfc.1; mouse. [Q9DCN1-1]
DR UCSC; uc008dfd.1; mouse. [Q9DCN1-2]
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; DWNTRNT; -.
DR OrthoDB; 1436400at2759; -.
DR PhylomeDB; Q9DCN1; -.
DR TreeFam; TF106352; -.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR BioGRID-ORCS; 67993; 5 hits in 74 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 219 other tissues.
DR Genevisible; Q9DCN1; MM.
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 Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR015375; NADH_PPase-like_N.
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 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; SSF48403; 1.
DR SUPFAM; SSF55811; SSF55811; 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.
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
