AP4A_RAT
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 03-AUG-2022, entry version 110.
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=H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = 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 = (R)-4'-
CC phosphopantetheine + a 5'-end phospho-adenosine-phospho-
CC ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-
CC COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051,
CC ChEBI:CHEBI:172371; 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}.
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DR EMBL; BC058156; AAH58156.1; -; mRNA.
DR RefSeq; NP_997479.1; NM_207596.1.
DR AlphaFoldDB; Q6PEC0; -.
DR SMR; Q6PEC0; -.
DR STRING; 10116.ENSRNOP00000017712; -.
DR jPOST; Q6PEC0; -.
DR PaxDb; Q6PEC0; -.
DR PRIDE; Q6PEC0; -.
DR Ensembl; ENSRNOT00000017712; ENSRNOP00000017712; ENSRNOG00000013110.
DR GeneID; 297998; -.
DR KEGG; rno:297998; -.
DR UCSC; RGD:1303023; rat.
DR CTD; 318; -.
DR RGD; 1303023; Nudt2.
DR eggNOG; KOG2839; Eukaryota.
DR GeneTree; ENSGT00390000002416; -.
DR HOGENOM; CLU_037162_14_5_1; -.
DR InParanoid; Q6PEC0; -.
DR OMA; DYKWIHS; -.
DR OrthoDB; 1107148at2759; -.
DR PhylomeDB; Q6PEC0; -.
DR TreeFam; TF105958; -.
DR PRO; PR:Q6PEC0; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000013110; Expressed in ovary and 19 other tissues.
DR Genevisible; Q6PEC0; RN.
DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
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; Ap4A_hydrolase_human_like; 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; IPR003565; Tetra_PHTase.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR PRINTS; PR01405; TETRPHPHTASE.
DR SUPFAM; SSF55811; SSF55811; 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
