DXO_BOVIN
ID DXO_BOVIN Reviewed; 397 AA.
AC Q5E9Y5; Q58CY4; Q58D18; Q5BIQ5; Q5E9U5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Decapping and exoribonuclease protein {ECO:0000250|UniProtKB:O77932};
DE Short=DXO {ECO:0000250|UniProtKB:O77932};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:O70348};
DE AltName: Full=5'-3' exoribonuclease DXO {ECO:0000305};
DE EC=3.1.13.- {ECO:0000250|UniProtKB:O70348};
DE AltName: Full=Dom-3 homolog Z {ECO:0000250|UniProtKB:O77932};
DE AltName: Full=NAD-capped RNA hydrolase DXO {ECO:0000305};
DE Short=DeNADding enzyme DXO {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:O70348};
GN Name=DXO {ECO:0000250|UniProtKB:O77932};
GN Synonyms=DOM3Z {ECO:0000250|UniProtKB:O77932};
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] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes
CC the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs
CC by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA.
CC The NAD-cap is present at the 5'-end of some RNAs and snoRNAs. In
CC contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD
CC cap promotes mRNA decay (By similarity). Preferentially acts on NAD-
CC capped transcripts in response to environmental stress (By similarity).
CC Also acts as a non-canonical decapping enzyme that removes the entire
CC cap structure of m7G capped or incompletely capped RNAs and mediates
CC their subsequent degradation. Specifically degrades pre-mRNAs with a
CC defective 5'-end m7G cap and is part of a pre-mRNA capping quality
CC control. Has decapping activity toward incomplete 5'-end m7G cap mRNAs
CC such as unmethylated 5'-end-capped RNA (cap0), while it has no activity
CC toward 2'-O-ribose methylated m7G cap (cap1). In contrast to canonical
CC decapping enzymes DCP2 and NUDT16, which cleave the cap within the
CC triphosphate linkage, the decapping activity releases the entire cap
CC structure GpppN and a 5'-end monophosphate RNA. Also has 5'-3'
CC exoribonuclease activities: The 5'-end monophosphate RNA is then
CC degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to
CC decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-
CC pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to
CC release pyrophosphates (By similarity). Exhibits decapping activity
CC towards FAD-capped RNAs (By similarity). Exhibits decapping activity
CC towards dpCoA-capped RNAs in vitro (By similarity).
CC {ECO:0000250|UniProtKB:O70348, ECO:0000250|UniProtKB:O77932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in mRNA + H2O = a 5'-
CC end phospho-ribonucleoside in mRNA + H(+) + NAD(+);
CC Xref=Rhea:RHEA:60880, Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:15698,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:144029;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end NAD(+)-phospho-ribonucleoside in snoRNA + H2O = a 5'-
CC end phospho-ribonucleoside in snoRNA + H(+) + NAD(+);
CC Xref=Rhea:RHEA:60892, Rhea:RHEA-COMP:15699, Rhea:RHEA-COMP:15700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:138282, ChEBI:CHEBI:144029;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60893;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside-
CC ribonucleotide in mRNA + H2O = a (N(7)-methyl 5'-triphospho-
CC guanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA +
CC H(+); Xref=Rhea:RHEA:66928, Rhea:RHEA-COMP:15692, Rhea:RHEA-
CC COMP:17313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172876, ChEBI:CHEBI:172877;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end
CC phospho-ribonucleoside in mRNA + FAD + H(+); Xref=Rhea:RHEA:67492,
CC Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17275, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172372; Evidence={ECO:0000250|UniProtKB:O70348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67493;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = 3'-dephospho-CoA +
CC a 5'-end phospho-ribonucleoside in mRNA + H(+); Xref=Rhea:RHEA:67496,
CC Rhea:RHEA-COMP:15692, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57328, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:172371; Evidence={ECO:0000250|UniProtKB:O70348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67497;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O70348};
CC Note=Binds 2 magnesium ions. {ECO:0000250|UniProtKB:O70348};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O77932}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5E9Y5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5E9Y5-2; Sequence=VSP_020556;
CC Name=3;
CC IsoId=Q5E9Y5-3; Sequence=VSP_020558;
CC Name=4;
CC IsoId=Q5E9Y5-4; Sequence=VSP_020555, VSP_020557;
CC -!- SIMILARITY: Belongs to the DXO/Dom3Z family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAX46626.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT020784; AAX08801.1; -; mRNA.
DR EMBL; BT020825; AAX08842.1; -; mRNA.
DR EMBL; BT021169; AAX31351.1; -; mRNA.
DR EMBL; BT021171; AAX31353.1; -; mRNA.
DR EMBL; BT021779; AAX46626.1; ALT_FRAME; mRNA.
DR EMBL; BT021813; AAX46660.1; -; mRNA.
DR RefSeq; NP_001014872.2; NM_001014872.2.
DR AlphaFoldDB; Q5E9Y5; -.
DR SMR; Q5E9Y5; -.
DR STRING; 9913.ENSBTAP00000007340; -.
DR PaxDb; Q5E9Y5; -.
DR GeneID; 508460; -.
DR KEGG; bta:508460; -.
DR CTD; 1797; -.
DR eggNOG; KOG1982; Eukaryota.
DR InParanoid; Q5E9Y5; -.
DR OrthoDB; 1034620at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0008409; F:5'-3' exonuclease activity; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0110152; F:RNA NAD-cap (NAD-forming) hydrolase activity; ISS:UniProtKB.
DR GO; GO:0034353; F:RNA pyrophosphohydrolase activity; ISS:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0110155; P:NAD-cap decapping; ISS:UniProtKB.
DR GO; GO:0071028; P:nuclear mRNA surveillance; ISS:UniProtKB.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IBA:GO_Central.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; ISS:UniProtKB.
DR GO; GO:0050779; P:RNA destabilization; ISS:UniProtKB.
DR InterPro; IPR013961; RAI1.
DR InterPro; IPR039039; RAI1-like_fam.
DR PANTHER; PTHR12395; PTHR12395; 1.
DR Pfam; PF08652; RAI1; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..397
FT /note="Decapping and exoribonuclease protein"
FT /id="PRO_0000249821"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 131..133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 192
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 253
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6MG77"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70348"
FT VAR_SEQ 198..304
FT /note="DKPGVSPDPSGEVNTNVAFCSVLRSRLGNHPLLFSGEVDCTDPQAPSTQPPT
FT CYVELKTSKEMHSPGQWKSFYRHKLLKWWAQSFLPGVPNVVAGFRNPEGFVCSLK ->
FT GESCPDSAPSPIPRDREPPALAAVSLLVQTNPESPQILLGKLTPTWPSALCYAAAWETT
FT LFFFPGRWTAQTPRPHPHSPPPAMWSSRPPRRCTALANGRASTDTSS (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_020555"
FT VAR_SEQ 271
FT /note="R -> RFRTGVDRMRTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_020556"
FT VAR_SEQ 305..397
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_020557"
FT VAR_SEQ 378..396
FT /note="YVEAVTQDLPSPPKTPSPK -> PPGPHQSAWPQSGPVPPPADGEQRL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_020558"
FT CONFLICT 157
FT /note="R -> Q (in Ref. 1; AAX46626)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="R -> H (in Ref. 1; AAX46626)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="A -> V (in Ref. 1; AAX46626)"
FT /evidence="ECO:0000305"
FT CONFLICT 348
FT /note="R -> G (in Ref. 1; AAX08842)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 45168 MW; C980EF4F38CBACE3 CRC64;
MESRGTKREA GKIEVAEPRN KLPRPAPSLP TDPALYSGPF PFYRRPSELG CFSLDAQRQY
HGDARALRYY SPPPTNGQSP NFDLRDGYPD RYQPRDEEVQ ERLDHLLRWL LEHRGQLEGG
PGWLAGAIVT WRGHLTKLLT TPYERQEGWQ LAASRFRGTL YLSEVETPAA RVQRLTRPPL
LRELMYMGYK FEQYMCADKP GVSPDPSGEV NTNVAFCSVL RSRLGNHPLL FSGEVDCTDP
QAPSTQPPTC YVELKTSKEM HSPGQWKSFY RHKLLKWWAQ SFLPGVPNVV AGFRNPEGFV
CSLKTFPTME MFEYVRNDRD GWNPSVCMNF CAAFLSFAQN TAVQDDPRLV YLFSWEPGGP
VTVSEHRDAP HAFLPPWYVE AVTQDLPSPP KTPSPKD
