NUD12_HUMAN
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 03-AUG-2022, entry version 171.
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, 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 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: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; 36.
DR IntAct; Q9BQG2; 15.
DR MINT; Q9BQG2; -.
DR STRING; 9606.ENSP00000230792; -.
DR iPTMnet; Q9BQG2; -.
DR PhosphoSitePlus; Q9BQG2; -.
DR BioMuta; NUDT12; -.
DR DMDM; 68565930; -.
DR EPD; Q9BQG2; -.
DR jPOST; Q9BQG2; -.
DR MassIVE; Q9BQG2; -.
DR MaxQB; Q9BQG2; -.
DR PaxDb; Q9BQG2; -.
DR PeptideAtlas; Q9BQG2; -.
DR PRIDE; Q9BQG2; -.
DR ProteomicsDB; 78677; -.
DR ABCD; Q9BQG2; 4 sequenced antibodies.
DR Antibodypedia; 25275; 191 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 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; DWNTRNT; -.
DR OrthoDB; 1436400at2759; -.
DR PhylomeDB; Q9BQG2; -.
DR TreeFam; TF106352; -.
DR PathwayCommons; Q9BQG2; -.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR SignaLink; Q9BQG2; -.
DR BioGRID-ORCS; 83594; 7 hits in 1081 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 172 other tissues.
DR Genevisible; Q9BQG2; HS.
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 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_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 NAD-
FT capped RNAs. Loss of homodimerization; when associated with
FT 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
