AP4A_PIG
ID AP4A_PIG Reviewed; 147 AA.
AC P50584;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical];
DE EC=3.6.1.17 {ECO:0000269|PubMed:9147133};
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; Synonyms=APAH1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC TISSUE=Small intestine;
RX PubMed=9147133; DOI=10.1016/s1357-2725(96)00153-7;
RA Hankin S., Winteroe A.K., McLennan A.G.;
RT "Molecular cloning of diadenosine tetraphosphatase from pig small
RT intestinal mucosa and identification of sequence blocks common to
RT diadenosine polyphosphate hydrolases and phosphorylases.";
RL Int. J. Biochem. Cell Biol. 29:317-323(1997).
CC -!- FUNCTION: Catalyzes the asymmetric hydrolysis of diadenosine 5',5'''-
CC P1,P4-tetraphosphate (Ap4A) to yield AMP and ATP (PubMed:9147133).
CC Exhibits decapping activity towards FAD-capped RNAs and dpCoA-capped
CC RNAs in vitro (By similarity). {ECO:0000250|UniProtKB:P56380,
CC ECO:0000269|PubMed:9147133}.
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:0000269|PubMed:9147133};
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 -!- ACTIVITY REGULATION: Inhibited by fluoride ions.
CC {ECO:0000269|PubMed:9147133}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 uM for P(1),P(4)-bis(5'-guanosyl) tetraphosphate
CC {ECO:0000269|PubMed:9147133};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; U38619; AAB61380.1; -; mRNA.
DR RefSeq; NP_999474.1; NM_214309.2.
DR RefSeq; XP_005668113.1; XM_005668056.2.
DR RefSeq; XP_005668114.1; XM_005668057.2.
DR RefSeq; XP_013835621.1; XM_013980167.1.
DR AlphaFoldDB; P50584; -.
DR SMR; P50584; -.
DR STRING; 9823.ENSSSCP00000011711; -.
DR PaxDb; P50584; -.
DR PeptideAtlas; P50584; -.
DR PRIDE; P50584; -.
DR Ensembl; ENSSSCT00000012019; ENSSSCP00000011711; ENSSSCG00000010981.
DR Ensembl; ENSSSCT00015019567; ENSSSCP00015007675; ENSSSCG00015014742.
DR Ensembl; ENSSSCT00015019611; ENSSSCP00015007694; ENSSSCG00015014742.
DR Ensembl; ENSSSCT00030070607; ENSSSCP00030032215; ENSSSCG00030050634.
DR Ensembl; ENSSSCT00035066313; ENSSSCP00035026891; ENSSSCG00035049766.
DR Ensembl; ENSSSCT00040041110; ENSSSCP00040017214; ENSSSCG00040030545.
DR Ensembl; ENSSSCT00045003594; ENSSSCP00045002269; ENSSSCG00045002295.
DR Ensembl; ENSSSCT00055031600; ENSSSCP00055025148; ENSSSCG00055016025.
DR Ensembl; ENSSSCT00065050378; ENSSSCP00065021827; ENSSSCG00065036918.
DR Ensembl; ENSSSCT00070038135; ENSSSCP00070031914; ENSSSCG00070019290.
DR Ensembl; ENSSSCT00070038146; ENSSSCP00070031926; ENSSSCG00070019290.
DR Ensembl; ENSSSCT00070038150; ENSSSCP00070031930; ENSSSCG00070019290.
DR GeneID; 397577; -.
DR KEGG; ssc:397577; -.
DR CTD; 318; -.
DR VGNC; VGNC:96457; NUDT2.
DR eggNOG; KOG2839; Eukaryota.
DR GeneTree; ENSGT00390000002416; -.
DR HOGENOM; CLU_037162_14_5_1; -.
DR InParanoid; P50584; -.
DR OMA; WRDYEQA; -.
DR OrthoDB; 1107148at2759; -.
DR TreeFam; TF105958; -.
DR Reactome; R-SSC-3299685; Detoxification of Reactive Oxygen Species.
DR Proteomes; UP000008227; Chromosome 10.
DR Proteomes; UP000314985; Chromosome 10.
DR Bgee; ENSSSCG00000010981; Expressed in longissimus lumborum muscle and 46 other tissues.
DR ExpressionAtlas; P50584; baseline and differential.
DR Genevisible; P50584; SS.
DR GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0006167; P:AMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0006754; P:ATP biosynthetic process; IBA:GO_Central.
DR CDD; cd03428; Ap4A_hydrolase_human_like; 1.
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; PR01405; TETRPHPHTASE.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein 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_0000057104"
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; 16835 MW; 332B6F3C185A7379 CRC64;
MALRACGLII FRRRLIPKVD NTAIEFLLLQ ASNGIHHWTP PKGHVEPGES DLQTALRETQ
EEAGIDAGQL TIIEGFRKEL NYVAWEKPKT VIYWLAEVKD YDVEVRLSRE HQAYRWLGLD
EACQLAQFKD MKAVLQEGHQ FLCSMAA
