ID AP4A_RAT Reviewed; 147 AA. AC Q6PEC0; DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-SEP-2026, entry version 125. DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]; DE EC=3.6.1.17 {ECO:0000250|UniProtKB:P50584}; DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase; DE Short=Ap4A hydrolase; DE Short=Ap4Aase; DE Short=Diadenosine tetraphosphatase; DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 2; DE Short=Nudix motif 2; GN Name=Nudt2; 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=Pituitary; 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: Catalyzes the asymmetric hydrolysis of diadenosine 5',5'''- CC P1,P4-tetraphosphate (Ap4A) to yield AMP and ATP (By similarity). CC Exhibits decapping activity towards FAD-capped RNAs and dpCoA-capped CC RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:P50584, CC ECO:0000250|UniProtKB:P56380}. CC -!- CATALYTIC ACTIVITY: CC Reaction=P(1),P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GMP + GTP + CC 2 H(+); Xref=Rhea:RHEA:22484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57553, ChEBI:CHEBI:58115; EC=3.6.1.17; CC Evidence={ECO:0000250|UniProtKB:P50584}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = a 5'-end phospho- CC adenosine-phospho-ribonucleoside in mRNA + (R)-4'-phosphopantetheine CC + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-COMP:15719, Rhea:RHEA- CC COMP:17276, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, CC ChEBI:CHEBI:144051, ChEBI:CHEBI:172371; CC Evidence={ECO:0000250|UniProtKB:P56380}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593; CC Evidence={ECO:0000250|UniProtKB:P56380}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end CC phospho-adenosine-phospho-ribonucleoside in mRNA + FMN + 2 H(+); CC Xref=Rhea:RHEA:67588, Rhea:RHEA-COMP:15719, Rhea:RHEA-COMP:17275, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58210, CC ChEBI:CHEBI:144051, ChEBI:CHEBI:172372; CC Evidence={ECO:0000250|UniProtKB:P56380}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67589; CC Evidence={ECO:0000250|UniProtKB:P56380}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:Q9U2M7}; CC Note=Divalent metal ions. {ECO:0000250|UniProtKB:Q9U2M7}; CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC058156; AAH58156.1; -; mRNA. DR RefSeq; NP_997479.1; NM_207596.2. DR RefSeq; XP_063143372.1; XM_063287302.1. DR RefSeq; XP_063143373.1; XM_063287303.1. DR AlphaFoldDB; Q6PEC0; -. DR SMR; Q6PEC0; -. DR FunCoup; Q6PEC0; 781. DR STRING; 10116.ENSRNOP00000017712; -. DR PhosphoSitePlus; Q6PEC0; -. DR jPOST; Q6PEC0; -. DR PaxDb; 10116-ENSRNOP00000017712; -. DR Ensembl; ENSRNOT00055028534; ENSRNOP00055022973; ENSRNOG00055016807. DR Ensembl; ENSRNOT00060008194; ENSRNOP00060006162; ENSRNOG00060004911. DR Ensembl; ENSRNOT00065006963; ENSRNOP00065004776; ENSRNOG00065004807. DR GeneID; 297998; -. DR KEGG; rno:297998; -. DR UCSC; RGD:1303023; rat. DR AGR; RGD:1303023; -. DR CTD; 318; -. DR RGD; 1303023; Nudt2. DR eggNOG; KOG2839; Eukaryota. DR HOGENOM; CLU_037162_14_5_1; -. DR InParanoid; Q6PEC0; -. DR OMA; WRDYEQA; -. DR OrthoDB; 276276at2759; -. DR PhylomeDB; Q6PEC0; -. DR Reactome; R-RNO-3299685; Detoxification of Reactive Oxygen Species. DR PRO; PR:Q6PEC0; -. DR Proteomes; UP000002494; Chromosome 5. DR Bgee; ENSRNOG00000013110; Expressed in ovary and 19 other cell types or tissues. DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; ISS:UniProtKB. DR GO; GO:0016787; F:hydrolase activity; TAS:RGD. DR GO; GO:0006167; P:AMP biosynthetic process; IBA:GO_Central. DR GO; GO:0006754; P:ATP biosynthetic process; IBA:GO_Central. DR CDD; cd03428; NUDIX_Ap4A_Nudt2; 1. DR FunFam; 3.90.79.10:FF:000037; Nudix hydrolase 2; 1. DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR051325; Nudix_hydrolase_domain. DR InterPro; IPR003565; Tetra_PHTase. DR PANTHER; PTHR21340:SF0; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE [ASYMMETRICAL]; 1. DR PANTHER; PTHR21340; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 1. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR PRINTS; PR01405; TETRPHPHTASE. DR SUPFAM; SSF55811; Nudix; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 2: Evidence at transcript level; KW Acetylation; GTP-binding; Hydrolase; Nucleotide-binding; KW Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P50583" FT CHAIN 2..147 FT /note="Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical]" FT /id="PRO_0000057105" FT DOMAIN 2..139 FT /note="Nudix hydrolase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794" FT MOTIF 43..64 FT /note="Nudix box" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000250|UniProtKB:P50583" SQ SEQUENCE 147 AA; 16929 MW; F17F2BB44D2B9C33 CRC64; MALRACGLII FRRHLIPKVD NTTIEFLLLQ ASDGIHHWTP PKGHVDPGEN DLETALRETQ EETGIEASQL IVLEGFRREL NYVARKKPKT VIYWLAEVKD YDVEIRLSQE HQAYRWLGLD EACQLAQFEE MKATLQEGHQ FLCSTPA //