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Protein HESO1 (EC 2.7.7.52) (HEN1 suppressor 1) (RNA uridylyltransferase)

 HESO1_ARATH             Reviewed;         511 AA.
Q5XET5; O22284; Q0WSQ3;
14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
23-NOV-2004, sequence version 1.
07-JUN-2017, entry version 88.
RecName: Full=Protein HESO1 {ECO:0000303|PubMed:22464194};
EC=2.7.7.52 {ECO:0000269|PubMed:22464194};
AltName: Full=HEN1 suppressor 1 {ECO:0000303|PubMed:22464194};
AltName: Full=RNA uridylyltransferase {ECO:0000305};
Name=HESO1 {ECO:0000303|PubMed:22464194};
OrderedLocusNames=At2g39740 {ECO:0000312|Araport:AT2G39740};
ORFNames=T5I7.4 {ECO:0000312|EMBL:AAB87123.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702 {ECO:0000312|EMBL:AAU95417.1};
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617197; DOI=10.1038/45471;
Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
Venter J.C.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis
thaliana.";
Nature 402:761-768(1999).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AND DISRUPTION
PHENOTYPE.
PubMed=22464194; DOI=10.1016/j.cub.2012.02.051;
Zhao Y., Yu Y., Zhai J., Ramachandran V., Dinh T.T., Meyers B.C.,
Mo B., Chen X.;
"The Arabidopsis nucleotidyl transferase HESO1 uridylates unmethylated
small RNAs to trigger their degradation.";
Curr. Biol. 22:689-694(2012).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22464191; DOI=10.1016/j.cub.2012.02.052;
Ren G., Chen X., Yu B.;
"Uridylation of miRNAs by hen1 suppressor1 in Arabidopsis.";
Curr. Biol. 22:695-700(2012).
[7]
FUNCTION, AND INTERACTION WITH AGO1.
PubMed=24733911; DOI=10.1073/pnas.1405083111;
Ren G., Xie M., Zhang S., Vinovskis C., Chen X., Yu B.;
"Methylation protects microRNAs from an AGO1-associated activity that
uridylates 5' RNA fragments generated by AGO1 cleavage.";
Proc. Natl. Acad. Sci. U.S.A. 111:6365-6370(2014).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25928341; DOI=10.1371/journal.pgen.1005091;
Wang X., Zhang S., Dou Y., Zhang C., Chen X., Yu B., Ren G.;
"Synergistic and independent actions of multiple terminal nucleotidyl
transferases in the 3' tailing of small RNAs in Arabidopsis.";
PLoS Genet. 11:E1005091-E1005091(2015).
[9]
FUNCTION.
PubMed=25928405; DOI=10.1371/journal.pgen.1005119;
Tu B., Liu L., Xu C., Zhai J., Li S., Lopez M.A., Zhao Y., Yu Y.,
Ramachandran V., Ren G., Yu B., Li S., Meyers B.C., Mo B., Chen X.;
"Distinct and cooperative activities of HESO1 and URT1 nucleotidyl
transferases in microRNA turnover in Arabidopsis.";
PLoS Genet. 11:E1005119-E1005119(2015).
-!- FUNCTION: Uridylates small RNAs to trigger their degradation
(PubMed:25928341, PubMed:22464191, PubMed:22464194). Catalyzes the
uridylation of 5' fragments produced by AGO1-mediated cleavage of
miRNA target RNAs (PubMed:24733911). Acts synergistically with
URT1 in unmethylated miRNA uridylation, leading to their
degradation (PubMed:25928341). URT1 and HESO1 prefer substrates
with different 3' end nucleotides and act cooperatively to tail
different forms of the same miRNAs (PubMed:25928405). URT1 and
HESO1 act sequentially, with URT1 mono-uridylating the miRNAs
followed by their further uridylation by HESO1 (PubMed:25928405).
Able to act on AGO1-bound miRNAs and the uridylated species stay
associated with AGO1 (PubMed:25928405, PubMed:24733911).
{ECO:0000269|PubMed:22464191, ECO:0000269|PubMed:22464194,
ECO:0000269|PubMed:24733911, ECO:0000269|PubMed:25928341,
ECO:0000269|PubMed:25928405}.
-!- CATALYTIC ACTIVITY: UTP + RNA(n) = diphosphate + RNA(n+1).
{ECO:0000269|PubMed:22464194}.
-!- ENZYME REGULATION: Completely inhibited by 2'-O-methylation on the
substrate RNA. {ECO:0000269|PubMed:22464194}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22464191}.
Cytoplasm, P-body {ECO:0000269|PubMed:25928341}. Nucleus
{ECO:0000269|PubMed:22464191, ECO:0000269|PubMed:25928341}.
-!- DISRUPTION PHENOTYPE: No effect on miRNA accumulation in the wild-
type background, but increased abundance of the heterogeneous
miRNA species in a hen1 background. Reduced 3' uridylation of
miRNAs without affecting the 3' truncation.
{ECO:0000269|PubMed:22464194}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB87123.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC003000; AAB87123.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002685; AEC09717.1; -; Genomic_DNA.
EMBL; CP002685; ANM62240.1; -; Genomic_DNA.
EMBL; CP002685; ANM62241.1; -; Genomic_DNA.
EMBL; BT015881; AAU95417.1; -; mRNA.
EMBL; BT020198; AAV59264.1; -; mRNA.
EMBL; AK227869; BAE99845.1; -; mRNA.
PIR; T01004; T01004.
RefSeq; NP_001318386.1; NM_001336793.1.
RefSeq; NP_001324414.1; NM_001336794.1.
RefSeq; NP_181504.2; NM_129532.4.
UniGene; At.21484; -.
UniGene; At.37137; -.
ProteinModelPortal; Q5XET5; -.
IntAct; Q5XET5; 6.
STRING; 3702.AT2G39740.1; -.
PaxDb; Q5XET5; -.
EnsemblPlants; AT2G39740.1; AT2G39740.1; AT2G39740.
EnsemblPlants; AT2G39740.2; AT2G39740.2; AT2G39740.
EnsemblPlants; AT2G39740.3; AT2G39740.3; AT2G39740.
GeneID; 818559; -.
Gramene; AT2G39740.1; AT2G39740.1; AT2G39740.
Gramene; AT2G39740.2; AT2G39740.2; AT2G39740.
Gramene; AT2G39740.3; AT2G39740.3; AT2G39740.
KEGG; ath:AT2G39740; -.
Araport; AT2G39740; -.
TAIR; locus:2063937; AT2G39740.
eggNOG; KOG2277; Eukaryota.
eggNOG; COG5260; LUCA.
HOGENOM; HOG000082987; -.
OMA; NNHPQAY; -.
OrthoDB; EOG09360MXX; -.
PhylomeDB; Q5XET5; -.
PRO; PR:Q5XET5; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q5XET5; baseline and differential.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
GO; GO:0016779; F:nucleotidyltransferase activity; IDA:TAIR.
GO; GO:0050265; F:RNA uridylyltransferase activity; IDA:UniProtKB.
GO; GO:0060964; P:regulation of gene silencing by miRNA; IDA:UniProtKB.
GO; GO:0071076; P:RNA 3' uridylation; IDA:UniProtKB.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Nucleus; Reference proteome;
Transferase.
CHAIN 1 511 Protein HESO1.
/FTId=PRO_0000434143.
COMPBIAS 377 442 Gln-rich. {ECO:0000255|PROSITE-
ProRule:PRU00006}.
CONFLICT 89 89 T -> I (in Ref. 4; BAE99845).
{ECO:0000305}.
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


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