NUD12_BOVIN
ID NUD12_BOVIN Reviewed; 444 AA.
AC Q29RH3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=NAD-capped RNA hydrolase NUDT12 {ECO:0000305};
DE Short=DeNADding enzyme NUDT12 {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9DCN1};
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:0000250|UniProtKB:Q9BQG2};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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. The NAD-cap is present
CC at the 5'-end of some RNAs; in contrast to the canonical N7
CC methylguanosine (m7G) cap, the NAD cap promotes mRNA decay.
CC Preferentially acts on NAD-capped transcripts in response to nutrient
CC stress (By similarity). Also acts on free nicotinamide adenine
CC dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and
CC NADPH into NMNH and 2',5'-ADP. 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q9BQG2,
CC ECO:0000250|UniProtKB:Q9DCN1}.
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:0000250|UniProtKB:Q9DCN1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60877;
CC Evidence={ECO:0000250|UniProtKB:Q9DCN1};
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:0000250|UniProtKB:Q9BQG2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11801;
CC Evidence={ECO:0000250|UniProtKB:Q9BQG2};
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:0000250|UniProtKB:Q9DCN1};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9DCN1};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9DCN1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9DCN1};
CC -!- SUBUNIT: Homodimer (By similarity). 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:0000250|UniProtKB:Q9DCN1}.
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 -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudC subfamily.
CC {ECO:0000305}.
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DR EMBL; BC114173; AAI14174.1; -; mRNA.
DR RefSeq; NP_001040073.1; NM_001046608.1.
DR AlphaFoldDB; Q29RH3; -.
DR SMR; Q29RH3; -.
DR STRING; 9913.ENSBTAP00000039749; -.
DR PaxDb; Q29RH3; -.
DR PRIDE; Q29RH3; -.
DR Ensembl; ENSBTAT00000039965; ENSBTAP00000039749; ENSBTAG00000027728.
DR GeneID; 617720; -.
DR KEGG; bta:617720; -.
DR CTD; 83594; -.
DR VEuPathDB; HostDB:ENSBTAG00000027728; -.
DR VGNC; VGNC:32326; NUDT12.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG3084; Eukaryota.
DR GeneTree; ENSGT00940000157592; -.
DR HOGENOM; CLU_037162_0_2_1; -.
DR InParanoid; Q29RH3; -.
DR OMA; DWNTRNT; -.
DR OrthoDB; 1436400at2759; -.
DR TreeFam; TF106352; -.
DR Reactome; R-BTA-197264; Nicotinamide salvaging.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000027728; Expressed in liver and 107 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0000210; F:NAD+ diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IBA:GO_Central.
DR GO; GO:1990174; F:phosphodiesterase decapping endonuclease activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0019677; P:NAD catabolic process; IBA:GO_Central.
DR GO; GO:0110155; P:NAD-cap decapping; ISS:UniProtKB.
DR GO; GO:0006734; P:NADH metabolic process; IBA:GO_Central.
DR GO; GO:0006742; P:NADP catabolic process; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
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; PF00293; NUDIX; 1.
DR Pfam; PF09296; NUDIX-like; 1.
DR Pfam; PF09297; zf-NADH-PPase; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW ANK repeat; Cytoplasm; Hydrolase; Magnesium; Metal-binding; NAD; NADP;
KW Peroxisome; Reference proteome; Repeat; Zinc.
FT CHAIN 1..444
FT /note="NAD-capped RNA hydrolase NUDT12"
FT /id="PRO_0000260768"
FT REPEAT 11..40
FT /note="ANK 1"
FT REPEAT 60..80
FT /note="ANK 2"
FT DOMAIN 301..435
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 337..358
FT /note="Nudix box"
FT MOTIF 442..444
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG2"
FT BINDING 266
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 300
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 336..338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 352
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 352
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 356
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 397
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 397
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT BINDING 397
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT MOD_RES 167
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
FT MOD_RES 274
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCN1"
SQ SEQUENCE 444 AA; 50119 MW; D9352B6AFCD6F21B CRC64;
MSSVKRSLNQ EIISQFHYSA AEGDIAKLTA ILSHSPSLLN ETSENGWSAL ICDRSIVNKS
RQTALDIAKF WGYKHIANLL ANAKGGKKPW FLTNEVEECE NYFSKTLLDR KSEKRNNSDW
LLAKESHPAT VYILFSDLNP LVTLGGNKES FQQPEVRLCQ LNYTDIKDYL AQPEKITLIF
LGVELEMKKE FFNYAGEISK EEEDGLVAWF ALGIDTVAAE EFKQRHENCY FLHPPMPALL
QLKEKEAGVV AQARSVLAWH SRYKFCPTCG NATKIEEGGY KRVCLKEDCP SLHGVHNTSY
PRVDPVVIMQ VIHPDGTKCL LGRQKRFPPG MFTCLAGFIE PGETIEDAVR REVEEESGVK
VGHVQYVSCQ PWPMPSSLMI GCLAVAVSTE IKVDKNEIED ARWFTREQVV DVLTKGKQQA
FFVPPSRAIA HQLIKHWIGM NPNL
