DXO_HUMAN
ID DXO_HUMAN Reviewed; 396 AA.
AC O77932; A2CER3; B0UZ80; O15004; O78127; O78128; Q5ST60; Q6IPZ2; Q9NPK4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Decapping and exoribonuclease protein {ECO:0000303|PubMed:29601584};
DE Short=DXO {ECO:0000303|PubMed:29601584};
DE EC=3.6.1.- {ECO:0000269|PubMed:29601584};
DE AltName: Full=5'-3' exoribonuclease DXO {ECO:0000305};
DE EC=3.1.13.- {ECO:0000269|PubMed:29601584};
DE AltName: Full=Dom-3 homolog Z {ECO:0000303|PubMed:9799600};
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:0000303|PubMed:29601584, ECO:0000312|HGNC:HGNC:2992};
GN Synonyms=DOM3L, DOM3Z {ECO:0000303|PubMed:9799600}, NG6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT THR-28, AND TISSUE SPECIFICITY.
RX PubMed=9799600; DOI=10.1006/geno.1998.5499;
RA Yang Z., Shen L., Dangel A.W., Wu L.-C., Yu C.Y.;
RT "Four ubiquitously expressed genes, RD (D6S45)-SKI2W (SKIV2L)-DOM3Z-RP1
RT (D6S60E), are present between complement component genes factor B and C4 in
RT the class III region of the HLA.";
RL Genomics 53:338-347(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-261.
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neuroblastoma, and Retinoblastoma;
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).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-106, AND VARIANT THR-28.
RX PubMed=10686478; DOI=10.1159/000019119;
RA Yang Z., Yu C.Y.;
RT "Organizations and gene duplications of the human and mouse MHC complement
RT gene clusters.";
RL Exp. Clin. Immunogenet. 17:1-17(2000).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21750099; DOI=10.1261/rna.2789611;
RA Zheng D., Chen C.Y., Shyu A.B.;
RT "Unraveling regulation and new components of human P-bodies through a
RT protein interaction framework and experimental validation.";
RL RNA 17:1619-1634(2011).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28283058; DOI=10.1016/j.cell.2017.02.019;
RA Jiao X., Doamekpor S.K., Bird J.G., Nickels B.E., Tong L., Hart R.P.,
RA Kiledjian M.;
RT "5' end nicotinamide adenine dinucleotide cap in human cells promotes RNA
RT decay through DXO-mediated deNADding.";
RL Cell 168:1015-1027(2017).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 7-LYS-ARG-8; ASP-236 AND GLU-253.
RX PubMed=29601584; DOI=10.1371/journal.pone.0193804;
RA Picard-Jean F., Brand C., Tremblay-Letourneau M., Allaire A.,
RA Beaudoin M.C., Boudreault S., Duval C., Rainville-Sirois J., Robert F.,
RA Pelletier J., Geiss B.J., Bisaillon M.;
RT "2'-O-methylation of the mRNA cap protects RNAs from decapping and
RT degradation by DXO.";
RL PLoS ONE 13:E0193804-E0193804(2018).
RN [10]
RP FUNCTION.
RX PubMed=31101919; DOI=10.1038/s41589-019-0293-7;
RA Grudzien-Nogalska E., Wu Y., Jiao X., Cui H., Mateyak M.K., Hart R.P.,
RA Tong L., Kiledjian M.;
RT "Structural and mechanistic basis of mammalian Nudt12 RNA deNADding.";
RL Nat. Chem. Biol. 15:575-582(2019).
RN [11]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32374864; DOI=10.1093/nar/gkaa297;
RA Doamekpor S.K., Grudzien-Nogalska E., Mlynarska-Cieslak A., Kowalska J.,
RA Kiledjian M., Tong L.;
RT "DXO/Rai1 enzymes remove 5'-end FAD and dephospho-CoA caps on RNAs.";
RL Nucleic Acids Res. 48:6136-6148(2020).
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 (PubMed:28283058). The NAD-cap is present at the 5'-end of some RNAs
CC and snoRNAs (PubMed:28283058). In contrast to the canonical 5'-end N7
CC methylguanosine (m7G) cap, the NAD cap promotes mRNA decay
CC (PubMed:28283058). Preferentially acts on NAD-capped transcripts in
CC response to environmental stress (PubMed:31101919). Also acts as a non-
CC canonical decapping enzyme that removes the entire cap structure of m7G
CC capped or incompletely capped RNAs and mediates their subsequent
CC degradation (By similarity). Specifically degrades pre-mRNAs with a
CC defective 5'-end m7G cap and is part of a pre-mRNA capping quality
CC control (By similarity). Has decapping activity toward incomplete 5'-
CC end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while
CC it has no activity toward 2'-O-ribose methylated m7G cap (cap1)
CC (PubMed:29601584). In contrast to canonical decapping enzymes DCP2 and
CC NUDT16, which cleave the cap within the triphosphate linkage, the
CC decapping activity releases the entire cap structure GpppN and a 5'-end
CC monophosphate RNA (By similarity). Also has 5'-3' exoribonuclease
CC activities: The 5'-end monophosphate RNA is then degraded by the 5'-3'
CC exoribonuclease activity, enabling this enzyme to decap and degrade
CC incompletely capped mRNAs (PubMed:29601584). 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 (PubMed:32374864). Exhibits decapping activity
CC towards dpCoA-capped RNAs in vitro (By similarity).
CC {ECO:0000250|UniProtKB:O70348, ECO:0000269|PubMed:28283058,
CC ECO:0000269|PubMed:29601584, ECO:0000269|PubMed:31101919,
CC ECO:0000269|PubMed:32374864}.
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:0000269|PubMed:28283058, ECO:0000269|PubMed:31101919};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60881;
CC Evidence={ECO:0000305|PubMed:28283058};
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:0000269|PubMed:29601584};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66929;
CC Evidence={ECO:0000305|PubMed:29601584};
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:0000269|PubMed:32374864};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67493;
CC Evidence={ECO:0000269|PubMed:32374864};
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:0000269|PubMed:21750099,
CC ECO:0000269|PubMed:29601584}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9799600}.
CC -!- SIMILARITY: Belongs to the DXO/Dom3Z family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67983.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB89306.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF059252; AAC78603.1; -; mRNA.
DR EMBL; AF019413; AAB67983.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049547; CAB89305.1; -; Genomic_DNA.
DR EMBL; AL049547; CAB89306.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL662849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR759782; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR753845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471081; EAX03558.1; -; Genomic_DNA.
DR EMBL; BC009344; AAH09344.1; -; mRNA.
DR EMBL; BC019083; AAH19083.1; -; mRNA.
DR EMBL; AF059253; AAC78604.1; -; mRNA.
DR EMBL; AF059254; AAC78605.1; -; mRNA.
DR CCDS; CCDS4732.1; -.
DR RefSeq; NP_005501.2; NM_005510.3.
DR RefSeq; XP_006715068.1; XM_006715005.3.
DR AlphaFoldDB; O77932; -.
DR SMR; O77932; -.
DR BioGRID; 108132; 20.
DR IntAct; O77932; 14.
DR MINT; O77932; -.
DR STRING; 9606.ENSP00000364498; -.
DR iPTMnet; O77932; -.
DR PhosphoSitePlus; O77932; -.
DR BioMuta; DXO; -.
DR EPD; O77932; -.
DR jPOST; O77932; -.
DR MassIVE; O77932; -.
DR MaxQB; O77932; -.
DR PaxDb; O77932; -.
DR PeptideAtlas; O77932; -.
DR PRIDE; O77932; -.
DR ProteomicsDB; 50418; -.
DR Antibodypedia; 45412; 133 antibodies from 23 providers.
DR DNASU; 1797; -.
DR Ensembl; ENST00000337523.10; ENSP00000337759.5; ENSG00000204348.10.
DR Ensembl; ENST00000375349.7; ENSP00000364498.3; ENSG00000204348.10.
DR Ensembl; ENST00000375356.7; ENSP00000364505.3; ENSG00000204348.10.
DR Ensembl; ENST00000383330.4; ENSP00000372820.4; ENSG00000206346.8.
DR Ensembl; ENST00000399936.5; ENSP00000382818.1; ENSG00000206346.8.
DR Ensembl; ENST00000399937.5; ENSP00000382819.1; ENSG00000206346.8.
DR Ensembl; ENST00000414092.2; ENSP00000391123.2; ENSG00000236765.6.
DR Ensembl; ENST00000419797.6; ENSP00000391532.2; ENSG00000234798.6.
DR Ensembl; ENST00000426498.5; ENSP00000394167.1; ENSG00000225682.6.
DR Ensembl; ENST00000427627.1; ENSP00000413860.1; ENSG00000234798.6.
DR Ensembl; ENST00000427690.5; ENSP00000406143.1; ENSG00000225682.6.
DR Ensembl; ENST00000432110.5; ENSP00000401315.1; ENSG00000236765.6.
DR Ensembl; ENST00000439989.5; ENSP00000395262.1; ENSG00000224313.6.
DR Ensembl; ENST00000443250.5; ENSP00000415675.1; ENSG00000224313.6.
DR Ensembl; ENST00000446967.5; ENSP00000391349.1; ENSG00000234798.6.
DR Ensembl; ENST00000453742.2; ENSP00000410404.2; ENSG00000225682.6.
DR Ensembl; ENST00000454430.2; ENSP00000411380.2; ENSG00000224313.6.
DR Ensembl; ENST00000458308.5; ENSP00000400173.1; ENSG00000236765.6.
DR GeneID; 1797; -.
DR KEGG; hsa:1797; -.
DR MANE-Select; ENST00000337523.10; ENSP00000337759.5; NM_005510.4; NP_005501.2.
DR UCSC; uc003nyp.2; human.
DR CTD; 1797; -.
DR DisGeNET; 1797; -.
DR GeneCards; DXO; -.
DR HGNC; HGNC:2992; DXO.
DR HPA; ENSG00000204348; Low tissue specificity.
DR MIM; 605996; gene.
DR neXtProt; NX_O77932; -.
DR OpenTargets; ENSG00000204348; -.
DR PharmGKB; PA27458; -.
DR VEuPathDB; HostDB:ENSG00000204348; -.
DR eggNOG; KOG1982; Eukaryota.
DR GeneTree; ENSGT00390000006425; -.
DR HOGENOM; CLU_024877_1_2_1; -.
DR InParanoid; O77932; -.
DR OMA; MAYWGYK; -.
DR OrthoDB; 1034620at2759; -.
DR PhylomeDB; O77932; -.
DR TreeFam; TF322812; -.
DR PathwayCommons; O77932; -.
DR SignaLink; O77932; -.
DR BioGRID-ORCS; 1797; 45 hits in 1057 CRISPR screens.
DR ChiTaRS; DXO; human.
DR GeneWiki; DOM3Z; -.
DR GenomeRNAi; 1797; -.
DR Pharos; O77932; Tbio.
DR PRO; PR:O77932; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O77932; protein.
DR Bgee; ENSG00000204348; Expressed in left testis and 92 other tissues.
DR ExpressionAtlas; O77932; baseline and differential.
DR Genevisible; O77932; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; IDA:UniProtKB.
DR GO; GO:0110155; P:NAD-cap decapping; IDA: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 1: Evidence at protein level;
KW Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..396
FT /note="Decapping and exoribonuclease protein"
FT /id="PRO_0000249822"
FT REGION 1..37
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:0000305|PubMed:29601584"
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:0000305|PubMed:29601584"
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 VARIANT 28
FT /note="S -> T (in dbSNP:rs1056694)"
FT /evidence="ECO:0000269|PubMed:10686478,
FT ECO:0000269|PubMed:9799600"
FT /id="VAR_027492"
FT VARIANT 63
FT /note="D -> E (in dbSNP:rs2746396)"
FT /id="VAR_027493"
FT VARIANT 261
FT /note="H -> Q (in dbSNP:rs17207867)"
FT /evidence="ECO:0000269|PubMed:14574404"
FT /id="VAR_027494"
FT VARIANT 332
FT /note="A -> V (in dbSNP:rs12205138)"
FT /id="VAR_027495"
FT MUTAGEN 7..8
FT /note="KR->AA: Impaired subcellular location, leading to
FT localization both in cytoplasm and nucleus."
FT /evidence="ECO:0000269|PubMed:29601584"
FT MUTAGEN 236
FT /note="D->A: Abolishes the decapping activity on incomplete
FT m7G cap mRNAs; when associated with A-253."
FT /evidence="ECO:0000269|PubMed:29601584"
FT MUTAGEN 253
FT /note="E->A: Abolishes the decapping activity on incomplete
FT m7G cap mRNAs; when associated with A-236."
FT /evidence="ECO:0000269|PubMed:29601584"
SQ SEQUENCE 396 AA; 44929 MW; 17C8119037EB6892 CRC64;
MDPRGTKRGA EKTEVAEPRN KLPRPAPSLP TDPALYSGPF PFYRRPSELG CFSLDAQRQY
HGDARALRYY SPPPTNGPGP NFDLRDGYPD RYQPRDEEVQ ERLDHLLCWL LEHRGRLEGG
PGWLAEAIVT WRGHLTKLLT TPYERQEGWQ LAASRFQGTL YLSEVETPNA RAQRLARPPL
LRELMYMGYK FEQYMCADKP GSSPDPSGEV NTNVAFCSVL RSRLGSHPLL FSGEVDCTDP
QAPSTQPPTC YVELKTSKEM HSPGQWRSFY RHKLLKWWAQ SFLPGVPNVV AGFRNPDGFV
SSLKTFPTMK MFEYVRNDRD GWNPSVCMNF CAAFLSFAQS TVVQDDPRLV HLFSWEPGGP
VTVSVHQDAP YAFLPIWYVE AMTQDLPSPP KTPSPK
