HESO1_ARATH
ID HESO1_ARATH Reviewed; 511 AA.
AC Q5XET5; O22284; Q0WSQ3;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein HESO1 {ECO:0000303|PubMed:22464194};
DE EC=2.7.7.52 {ECO:0000269|PubMed:22464194};
DE AltName: Full=HEN1 suppressor 1 {ECO:0000303|PubMed:22464194};
DE AltName: Full=RNA uridylyltransferase {ECO:0000305};
GN Name=HESO1 {ECO:0000303|PubMed:22464194};
GN OrderedLocusNames=At2g39740 {ECO:0000312|Araport:AT2G39740};
GN ORFNames=T5I7.4 {ECO:0000312|EMBL:AAB87123.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:AAU95417.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=22464194; DOI=10.1016/j.cub.2012.02.051;
RA Zhao Y., Yu Y., Zhai J., Ramachandran V., Dinh T.T., Meyers B.C., Mo B.,
RA Chen X.;
RT "The Arabidopsis nucleotidyl transferase HESO1 uridylates unmethylated
RT small RNAs to trigger their degradation.";
RL Curr. Biol. 22:689-694(2012).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22464191; DOI=10.1016/j.cub.2012.02.052;
RA Ren G., Chen X., Yu B.;
RT "Uridylation of miRNAs by hen1 suppressor1 in Arabidopsis.";
RL Curr. Biol. 22:695-700(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH AGO1.
RX PubMed=24733911; DOI=10.1073/pnas.1405083111;
RA Ren G., Xie M., Zhang S., Vinovskis C., Chen X., Yu B.;
RT "Methylation protects microRNAs from an AGO1-associated activity that
RT uridylates 5' RNA fragments generated by AGO1 cleavage.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:6365-6370(2014).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25928341; DOI=10.1371/journal.pgen.1005091;
RA Wang X., Zhang S., Dou Y., Zhang C., Chen X., Yu B., Ren G.;
RT "Synergistic and independent actions of multiple terminal nucleotidyl
RT transferases in the 3' tailing of small RNAs in Arabidopsis.";
RL PLoS Genet. 11:E1005091-E1005091(2015).
RN [9]
RP FUNCTION.
RX PubMed=25928405; DOI=10.1371/journal.pgen.1005119;
RA Tu B., Liu L., Xu C., Zhai J., Li S., Lopez M.A., Zhao Y., Yu Y.,
RA Ramachandran V., Ren G., Yu B., Li S., Meyers B.C., Mo B., Chen X.;
RT "Distinct and cooperative activities of HESO1 and URT1 nucleotidyl
RT transferases in microRNA turnover in Arabidopsis.";
RL PLoS Genet. 11:E1005119-E1005119(2015).
RN [10]
RP FUNCTION.
RX PubMed=30364210; DOI=10.3389/fpls.2018.01438;
RA Zuber H., Scheer H., Joly A.C., Gagliardi D.;
RT "Respective contributions of URT1 and HESO1 to the uridylation of 5'
RT fragments produced from RISC-cleaved mRNAs.";
RL Front. Plant Sci. 9:1438-1438(2018).
CC -!- FUNCTION: Uridylates small RNAs to trigger their degradation
CC (PubMed:22464191, PubMed:22464194, PubMed:25928341). Catalyzes the
CC uridylation of 5' fragments produced by AGO1-mediated cleavage of miRNA
CC target RNAs (PubMed:24733911). Acts synergistically with URT1 in
CC unmethylated miRNA uridylation, leading to their degradation
CC (PubMed:25928341). URT1 and HESO1 prefer substrates with different 3'
CC end nucleotides and act cooperatively to tail different forms of the
CC same miRNAs (PubMed:25928405). URT1 and HESO1 act sequentially, with
CC URT1 mono-uridylating the miRNAs followed by their further uridylation
CC by HESO1 (PubMed:25928405). URT1 and HESO1 are involved in the
CC uridylation and clearance of RISC-generated 5' mRNA fragments
CC (PubMed:30364210). Able to act on AGO1-bound miRNAs and the uridylated
CC species stay associated with AGO1 (PubMed:24733911, PubMed:25928405).
CC {ECO:0000269|PubMed:22464191, ECO:0000269|PubMed:22464194,
CC ECO:0000269|PubMed:24733911, ECO:0000269|PubMed:25928341,
CC ECO:0000269|PubMed:25928405, ECO:0000269|PubMed:30364210}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + UTP = diphosphate + RNA(n)-3'-uridine ribonucleotide;
CC Xref=Rhea:RHEA:14785, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17348,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:46398, ChEBI:CHEBI:140395,
CC ChEBI:CHEBI:173116; EC=2.7.7.52;
CC Evidence={ECO:0000269|PubMed:22464194};
CC -!- ACTIVITY REGULATION: Completely inhibited by 2'-O-methylation on the
CC substrate RNA. {ECO:0000269|PubMed:22464194}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22464191}.
CC Cytoplasm, P-body {ECO:0000269|PubMed:25928341}. Nucleus
CC {ECO:0000269|PubMed:22464191, ECO:0000269|PubMed:25928341}.
CC -!- DISRUPTION PHENOTYPE: No effect on miRNA accumulation in the wild-type
CC background, but increased abundance of the heterogeneous miRNA species
CC in a hen1 background. Reduced 3' uridylation of miRNAs without
CC affecting the 3' truncation. {ECO:0000269|PubMed:22464194}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB87123.1; Type=Erroneous gene model prediction; Evidence={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; AC003000; AAB87123.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09717.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62240.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62241.1; -; Genomic_DNA.
DR EMBL; BT015881; AAU95417.1; -; mRNA.
DR EMBL; BT020198; AAV59264.1; -; mRNA.
DR EMBL; AK227869; BAE99845.1; -; mRNA.
DR PIR; T01004; T01004.
DR RefSeq; NP_001318386.1; NM_001336793.1.
DR RefSeq; NP_001324414.1; NM_001336794.1.
DR RefSeq; NP_181504.2; NM_129532.4.
DR AlphaFoldDB; Q5XET5; -.
DR SMR; Q5XET5; -.
DR IntAct; Q5XET5; 6.
DR STRING; 3702.AT2G39740.1; -.
DR PaxDb; Q5XET5; -.
DR PRIDE; Q5XET5; -.
DR ProteomicsDB; 230837; -.
DR EnsemblPlants; AT2G39740.1; AT2G39740.1; AT2G39740.
DR EnsemblPlants; AT2G39740.2; AT2G39740.2; AT2G39740.
DR EnsemblPlants; AT2G39740.3; AT2G39740.3; AT2G39740.
DR GeneID; 818559; -.
DR Gramene; AT2G39740.1; AT2G39740.1; AT2G39740.
DR Gramene; AT2G39740.2; AT2G39740.2; AT2G39740.
DR Gramene; AT2G39740.3; AT2G39740.3; AT2G39740.
DR KEGG; ath:AT2G39740; -.
DR Araport; AT2G39740; -.
DR TAIR; locus:2063937; AT2G39740.
DR eggNOG; KOG2277; Eukaryota.
DR HOGENOM; CLU_032695_1_0_1; -.
DR InParanoid; Q5XET5; -.
DR OMA; SNMRWLP; -.
DR OrthoDB; 803033at2759; -.
DR PhylomeDB; Q5XET5; -.
DR BRENDA; 2.7.7.52; 399.
DR PRO; PR:Q5XET5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5XET5; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IDA:TAIR.
DR GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0060964; P:regulation of miRNA-mediated gene silencing; IDA:UniProtKB.
DR GO; GO:0071076; P:RNA 3' uridylation; IDA:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..511
FT /note="Protein HESO1"
FT /id="PRO_0000434143"
FT REGION 378..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 89
FT /note="T -> I (in Ref. 4; BAE99845)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 511 AA; 57592 MW; 9071261E200B77B1 CRC64;
MSRNPFLDPT LQEILQVIKP TRADRDTRIT VIDQLRDVLQ SVECLRGATV QPFGSFVSNL
FTRWGDLDIS VDLFSGSSIL FTGKKQKQTL LGHLLRALRA SGLWYKLQFV IHARVPILKV
VSGHQRISCD ISIDNLDGLL KSRFLFWISE IDGRFRDLVL LVKEWAKAHN INDSKTGTFN
SYSLSLLVIF HFQTCVPAIL PPLRVIYPKS AVDDLTGVRK TAEESIAQVT AANIARFKSE
RAKSVNRSSL SELLVSFFAK FSDINVKAQE FGVCPFTGRW ETISSNTTWL PKTYSLFVED
PFEQPVNAAR SVSRRNLDRI AQVFQITSRR LVSECNRNSI IGILTGQHIQ ESLYRTISLP
SQHHANGMHN VRNLHGQARP QNQQMQQNWS QSYNTPNPPH WPPLTQSRPQ QNWTQNNPRN
LQGQPPVQGQ TWPVITQTQT QQKSPYKSGN RPLKNTSAGS SQNQGHIGKP SGHMNGVNSA
RPAYTNGVNS ARPPSKIPSQ GGQIWRPRHE Q
