ID   NUD12_HUMAN             Reviewed;         462 AA.
AC   Q9BQG2; B3KUW2; B4E1W3; Q8TAL7;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 180.
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:31875550};
DE   AltName: Full=NADH pyrophosphatase NUDT12 {ECO:0000305};
DE            EC=3.6.1.22 {ECO:0000269|PubMed:12790796};
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:12790796,
GN   ECO:0000312|HGNC:HGNC:18826};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Amygdala;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye, and Ovary;
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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF 460-PRO--LEU-462.
RX   PubMed=12790796; DOI=10.1042/bj20030441;
RA   Abdelraheim S.R., Spiller D.G., McLennan A.G.;
RT   "Mammalian NADH diphosphatases of the Nudix family: cloning and
RT   characterization of the human peroxisomal NUDT12 protein.";
RL   Biochem. J. 374:329-335(2003).
RN   [6]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
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).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 111-462 IN COMPLEX WITH
RP   7-METHYL-GUANOSINE-5'-TRIPHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH BLMH, METAL-ION BINDING,
RP   AND MUTAGENESIS OF TYR-281; PHE-283; CYS-284; CYS-287; TYR-318; PHE-356;
RP   GLU-370; GLU-374; TYR-384 AND TRP-390.
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).
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:31875550). 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 (PubMed:12790796). May act to regulate the concentration of
CC       peroxisomal nicotinamide nucleotide cofactors required for oxidative
CC       metabolism in this organelle (PubMed:12790796). Regulates the levels of
CC       circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By
CC       similarity). {ECO:0000250|UniProtKB:Q9DCN1,
CC       ECO:0000269|PubMed:12790796, ECO:0000269|PubMed:31101919,
CC       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:31875550};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC         Evidence={ECO:0000305|PubMed:31875550};
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:12790796};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11801;
CC         Evidence={ECO:0000269|PubMed:12790796};
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:0000269|PubMed:12790796};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48869;
CC         Evidence={ECO:0000269|PubMed:12790796};
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:0000269|PubMed:12790796};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60821;
CC         Evidence={ECO:0000269|PubMed:12790796};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000305|PubMed:31875550};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000305|PubMed:31875550};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000305|PubMed:31875550};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305|PubMed:31875550};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11 uM for NADH {ECO:0000269|PubMed:12790796};
CC         KM=16 uM for NADPH {ECO:0000269|PubMed:12790796};
CC         KM=190 uM for NAD {ECO:0000269|PubMed:12790796};
CC       pH dependence:
CC         Optimum pH is 8-9. {ECO:0000269|PubMed:12790796};
CC   -!- SUBUNIT: Homodimer (PubMed:31875550). Homodimerization is essential for
CC       its catalytic activity and protein stability (PubMed:31875550).
CC       Interacts (via ANK repeats) with BLMH (PubMed:31875550).
CC       {ECO:0000269|PubMed:31875550}.
CC   -!- INTERACTION:
CC       Q9BQG2; Q13867: BLMH; NbExp=8; IntAct=EBI-10230612, EBI-718504;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12790796}.
CC       Peroxisome {ECO:0000269|PubMed:12790796}. Cytoplasmic granule
CC       {ECO:0000269|PubMed:31875550}. Note=Localizes to cytoplasmic granules
CC       in the presence of BLMH. {ECO:0000269|PubMed:31875550}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9BQG2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9BQG2-2; Sequence=VSP_060395;
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL136592; CAB66527.1; -; mRNA.
DR   EMBL; AK098066; BAG53574.1; -; mRNA.
DR   EMBL; AK304010; BAG64925.1; -; mRNA.
DR   EMBL; CH471086; EAW49073.1; -; Genomic_DNA.
DR   EMBL; BC026748; AAH26748.1; -; mRNA.
DR   EMBL; BC041099; AAH41099.1; -; mRNA.
DR   CCDS; CCDS4096.1; -. [Q9BQG2-1]
DR   CCDS; CCDS75284.1; -. [Q9BQG2-2]
DR   RefSeq; NP_001287670.1; NM_001300741.1. [Q9BQG2-2]
DR   RefSeq; NP_113626.1; NM_031438.3. [Q9BQG2-1]
DR   RefSeq; XP_005272152.1; XM_005272095.1. [Q9BQG2-1]
DR   RefSeq; XP_005272154.1; XM_005272097.3. [Q9BQG2-2]
DR   PDB; 6SCX; X-ray; 2.92 A; A/B/C=111-462.
DR   PDBsum; 6SCX; -.
DR   AlphaFoldDB; Q9BQG2; -.
DR   SMR; Q9BQG2; -.
DR   BioGRID; 123690; 43.
DR   IntAct; Q9BQG2; 16.
DR   MINT; Q9BQG2; -.
DR   STRING; 9606.ENSP00000230792; -.
DR   iPTMnet; Q9BQG2; -.
DR   PhosphoSitePlus; Q9BQG2; -.
DR   SwissPalm; Q9BQG2; -.
DR   BioMuta; NUDT12; -.
DR   DMDM; 68565930; -.
DR   EPD; Q9BQG2; -.
DR   jPOST; Q9BQG2; -.
DR   MassIVE; Q9BQG2; -.
DR   MaxQB; Q9BQG2; -.
DR   PaxDb; 9606-ENSP00000230792; -.
DR   PeptideAtlas; Q9BQG2; -.
DR   ProteomicsDB; 78677; -.
DR   Pumba; Q9BQG2; -.
DR   ABCD; Q9BQG2; 4 sequenced antibodies.
DR   Antibodypedia; 25275; 246 antibodies from 25 providers.
DR   DNASU; 83594; -.
DR   Ensembl; ENST00000230792.7; ENSP00000230792.2; ENSG00000112874.10. [Q9BQG2-1]
DR   Ensembl; ENST00000507423.1; ENSP00000424521.1; ENSG00000112874.10. [Q9BQG2-2]
DR   GeneID; 83594; -.
DR   KEGG; hsa:83594; -.
DR   MANE-Select; ENST00000230792.7; ENSP00000230792.2; NM_031438.4; NP_113626.1.
DR   UCSC; uc003koi.4; human. [Q9BQG2-1]
DR   AGR; HGNC:18826; -.
DR   CTD; 83594; -.
DR   GeneCards; NUDT12; -.
DR   HGNC; HGNC:18826; NUDT12.
DR   HPA; ENSG00000112874; Low tissue specificity.
DR   MIM; 609232; gene.
DR   neXtProt; NX_Q9BQG2; -.
DR   OpenTargets; ENSG00000112874; -.
DR   PharmGKB; PA38699; -.
DR   VEuPathDB; HostDB:ENSG00000112874; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG3084; Eukaryota.
DR   GeneTree; ENSGT00940000157592; -.
DR   InParanoid; Q9BQG2; -.
DR   OMA; EARWFPR; -.
DR   OrthoDB; 3024612at2759; -.
DR   PhylomeDB; Q9BQG2; -.
DR   TreeFam; TF106352; -.
DR   PathwayCommons; Q9BQG2; -.
DR   Reactome; R-HSA-197264; Nicotinamide salvaging.
DR   SignaLink; Q9BQG2; -.
DR   BioGRID-ORCS; 83594; 8 hits in 1160 CRISPR screens.
DR   ChiTaRS; NUDT12; human.
DR   GeneWiki; NUDT12; -.
DR   GenomeRNAi; 83594; -.
DR   Pharos; Q9BQG2; Tbio.
DR   PRO; PR:Q9BQG2; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9BQG2; Protein.
DR   Bgee; ENSG00000112874; Expressed in islet of Langerhans and 174 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR   GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0000210; F:NAD+ diphosphatase activity; IDA:UniProtKB.
DR   GO; GO:0035529; F:NADH pyrophosphatase activity; IDA:UniProtKB.
DR   GO; GO:1990174; F:phosphodiesterase decapping endonuclease activity; IMP:UniProtKB.
DR   GO; GO:0110153; F:RNA NAD-cap (NMN-forming) hydrolase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0110156; P:methylguanosine-cap decapping; IDA:UniProtKB.
DR   GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; TAS:Reactome.
DR   GO; GO:0019677; P:NAD catabolic process; IDA:UniProtKB.
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; IDA:UniProtKB.
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; Q9BQG2; HS.
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_0000056956"
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:0000305|PubMed:12790796"
FT   BINDING         284
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         287
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT   BINDING         354..356
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT   BINDING         370
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         370
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         370
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT   BINDING         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         374
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT   BINDING         415
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         415
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000305|PubMed:31875550,
FT                   ECO:0007744|PDB:6SCX"
FT   BINDING         415
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT   MOD_RES         185
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT   MOD_RES         292
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT   VAR_SEQ         52..69
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060395"
FT   VARIANT         129
FT                   /note="K -> E (in dbSNP:rs35903418)"
FT                   /id="VAR_034157"
FT   VARIANT         235
FT                   /note="I -> V (in dbSNP:rs34468716)"
FT                   /id="VAR_034158"
FT   MUTAGEN         281
FT                   /note="Y->A: Loss of homodimerization; when associated with
FT                   A-283; A-284; A-287 and A-384."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         283
FT                   /note="F->A: Loss of homodimerization; when associated with
FT                   A-281; A-284; A-287 and A-384."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         284
FT                   /note="C->A: Loss of homodimerization; when associated with
FT                   A-281; A-283; A-287 and A-384."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         287
FT                   /note="C->A: Loss of homodimerization; when associated with
FT                   A-281; A-283; A-284 and A-384."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         318
FT                   /note="Y->A: Partial loss of decapping activity towards
FT                   NAD-capped RNAs."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         356
FT                   /note="F->A: Loss of decapping activity towards NAD-capped
FT                   RNAs."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         370
FT                   /note="E->Q: Loss of decapping activity towards NAD-capped
FT                   RNAs."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         374
FT                   /note="E->Q: Loss of decapping activity towards NAD-capped
FT                   RNAs."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         384
FT                   /note="Y->A: No effect on decapping activity towards
FT                   NAD-capped RNAs. Loss of homodimerization; when associated
FT                   with A-281; A-283; A-284 and A-287."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         390
FT                   /note="W->A: Partial loss of decapping activity towards
FT                   NAD-capped RNAs."
FT                   /evidence="ECO:0000269|PubMed:31875550"
FT   MUTAGEN         460..462
FT                   /note="Missing: Abolishes localization to peroxisomes."
FT                   /evidence="ECO:0000269|PubMed:12790796"
FT   CONFLICT        82
FT                   /note="A -> V (in Ref. 2; BAG64925)"
FT                   /evidence="ECO:0000305"
FT   STRAND          125..127
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           130..134
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           136..144
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          157..162
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          174..176
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           181..188
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          195..202
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          226..232
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           234..244
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           253..256
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           257..259
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           262..280
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          290..294
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   TURN            295..298
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          299..302
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           308..310
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           315..317
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          323..330
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          334..341
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          343..345
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          353..356
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           363..375
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          379..389
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          392..394
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          396..405
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          413..415
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   STRAND          417..423
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           424..431
FT                   /evidence="ECO:0007829|PDB:6SCX"
FT   HELIX           447..458
FT                   /evidence="ECO:0007829|PDB:6SCX"
SQ   SEQUENCE   462 AA;  52076 MW;  1A470B93707DB1D5 CRC64;
     MSSVKRSLKQ EIVTQFHCSA AEGDIAKLTG ILSHSPSLLN ETSENGWTAL MYAARNGHPE
     IVQFLLEKGC DRSIVNKSRQ TALDIAVFWG YKHIANLLAT AKGGKKPWFL TNEVEECENY
     FSKTLLDRKS EKRNNSDWLL AKESHPATVF ILFSDLNPLV TLGGNKESFQ QPEVRLCQLN
     YTDIKDYLAQ PEKITLIFLG VELEIKDKLL NYAGEVPREE EDGLVAWFAL GIDPIAAEEF
     KQRHENCYFL HPPMPALLQL KEKEAGVVAQ ARSVLAWHSR YKFCPTCGNA TKIEEGGYKR
     LCLKEDCPSL NGVHNTSYPR VDPVVIMQVI HPDGTKCLLG RQKRFPPGMF TCLAGFIEPG
     ETIEDAVRRE VEEESGVKVG HVQYVACQPW PMPSSLMIGC LALAVSTEIK VDKNEIEDAR
     WFTREQVLDV LTKGKQQAFF VPPSRAIAHQ LIKHWIRINP NL
//