ID   NUDT9_RAT               Reviewed;         350 AA.
AC   Q5XIG0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ADP-ribose pyrophosphatase, mitochondrial;
DE            EC=3.6.1.13;
DE   AltName: Full=ADP-ribose diphosphatase;
DE   AltName: Full=ADP-ribose phosphohydrolase;
DE   AltName: Full=Adenosine diphosphoribose pyrophosphatase;
DE            Short=ADPR-PPase;
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 9;
DE            Short=Nudix motif 9;
DE   Flags: Precursor;
GN   Name=Nudt9;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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).
CC   -!- FUNCTION: Hydrolyzes ADP-ribose (ADPR) to AMP and ribose 5'-phosphate.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC         Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC         EC=3.6.1.13;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Monomer. Interacts with GLOD4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC083722; AAH83722.1; -; mRNA.
DR   RefSeq; NP_001006992.1; NM_001006991.1.
DR   AlphaFoldDB; Q5XIG0; -.
DR   SMR; Q5XIG0; -.
DR   STRING; 10116.ENSRNOP00000002973; -.
DR   iPTMnet; Q5XIG0; -.
DR   PhosphoSitePlus; Q5XIG0; -.
DR   jPOST; Q5XIG0; -.
DR   PaxDb; Q5XIG0; -.
DR   PRIDE; Q5XIG0; -.
DR   Ensembl; ENSRNOT00000002973; ENSRNOP00000002973; ENSRNOG00000002186.
DR   GeneID; 305149; -.
DR   KEGG; rno:305149; -.
DR   CTD; 53343; -.
DR   RGD; 1359522; Nudt9.
DR   eggNOG; KOG4195; Eukaryota.
DR   GeneTree; ENSGT00390000017405; -.
DR   HOGENOM; CLU_067226_0_0_1; -.
DR   InParanoid; Q5XIG0; -.
DR   OMA; PQWNQLD; -.
DR   OrthoDB; 1186086at2759; -.
DR   PhylomeDB; Q5XIG0; -.
DR   TreeFam; TF106351; -.
DR   Reactome; R-RNO-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR   SABIO-RK; Q5XIG0; -.
DR   PRO; PR:Q5XIG0; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000002186; Expressed in testis and 20 other tissues.
DR   Genevisible; Q5XIG0; RN.
DR   GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR   GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR   GO; GO:0047631; F:ADP-ribose diphosphatase activity; ISO:RGD.
DR   GO; GO:0046032; P:ADP catabolic process; ISO:RGD.
DR   GO; GO:0046709; P:IDP catabolic process; ISO:RGD.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR039989; NUDT9.
DR   PANTHER; PTHR13030; PTHR13030; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; SSF55811; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Manganese; Mitochondrion; Phosphoprotein;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..46
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           47..350
FT                   /note="ADP-ribose pyrophosphatase, mitochondrial"
FT                   /id="PRO_0000019952"
FT   DOMAIN          178..334
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   REGION          53..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          116..153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           215..237
FT                   /note="Nudix box"
FT   COMPBIAS        53..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BW91"
SQ   SEQUENCE   350 AA;  38562 MW;  CB85E68713BD242C CRC64;
     MAGRSLGKAV ATVSLSVALA SVTVRSSGCR AIPAPRNPFP SCGFHLKANI MSGSNGVKDN
     SHNKARTSPY PGSKVERSKV PNEKVGWLVE WQDYNPVEYT AVSVLAGPQW ADPQISESSF
     SPRFNEKDGH VERKSQNGLY EIENGRPRNP AGRTGLVGRG LLGRWGPNHA ADPIITRWKR
     DESGNKITHP VSGKCILQFV AIKRKDCGEW AIPGGMVDPG EKISATLKRE FGEEALNSLQ
     KSSAEKREIE EKLHALFSQE HLVIYKGYVD DPRNTDNAWM ETEAVNYHDE TGETMDNLTL
     EAGDDAGKVK WVDISDQLKL YASHSQFIKL VAEKRDAHWS EDCAADSHGL