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Ribonuclease TUDOR 2 (AtTudor2) (TUDOR-SN protein 2) (EC 3.1.-.-) (100 kDa coactivator-like protein)

 TSN2_ARATH              Reviewed;         985 AA.
Q9FLT0; Q0WLY7; Q0WM01; Q0WVT1;
02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 129.
RecName: Full=Ribonuclease TUDOR 2 {ECO:0000303|PubMed:20396901};
Short=AtTudor2 {ECO:0000303|PubMed:20396901};
Short=TUDOR-SN protein 2 {ECO:0000303|PubMed:20396901};
EC=3.1.-.- {ECO:0000269|PubMed:25736060};
AltName: Full=100 kDa coactivator-like protein;
Name=TSN2 {ECO:0000303|PubMed:20396901};
OrderedLocusNames=At5g61780 {ECO:0000312|Araport:AT5G61780};
ORFNames=MAC9.10 {ECO:0000312|EMBL:BAB10078.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9628582; DOI=10.1093/dnares/5.1.41;
Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. IV.
Sequence features of the regions of 1,456,315 bp covered by nineteen
physically assigned P1 and TAC clones.";
DNA Res. 5:41-54(1998).
[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;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-347 AND 374-985.
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-971, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Root;
PubMed=18433157; DOI=10.1021/pr8000173;
de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C.,
Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
Hirt H.;
"Site-specific phosphorylation profiling of Arabidopsis proteins by
mass spectrometry and peptide chip analysis.";
J. Proteome Res. 7:2458-2470(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-961; TYR-966 AND
SER-971, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
STRAIN=cv. Columbia;
PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
Andreasson E., Rathjen J.P., Peck S.C.;
"Phosphoproteomic analysis of nuclei-enriched fractions from
Arabidopsis thaliana.";
J. Proteomics 72:439-451(2009).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-971, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19376835; DOI=10.1104/pp.109.138677;
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
Grossmann J., Gruissem W., Baginsky S.;
"Large-scale Arabidopsis phosphoproteome profiling reveals novel
chloroplast kinase substrates and phosphorylation networks.";
Plant Physiol. 150:889-903(2009).
[8]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, GENE FAMILY, AND NOMENCLATURE.
STRAIN=cv. Columbia;
PubMed=20396901; DOI=10.1007/s00425-010-1167-0;
Liu S., Jia J., Gao Y., Zhang B., Han Y.;
"The AtTudor2, a protein with SN-Tudor domains, is involved in control
of seed germination in Arabidopsis.";
Planta 232:197-207(2010).
[9]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=cv. Columbia;
PubMed=20484005; DOI=10.1105/tpc.109.070680;
Frei dit Frey N., Muller P., Jammes F., Kizis D., Leung J.,
Perrot-Rechenmann C., Bianchi M.W.;
"The RNA binding protein Tudor-SN is essential for stress tolerance
and stabilizes levels of stress-responsive mRNAs encoding secreted
proteins in Arabidopsis.";
Plant Cell 22:1575-1591(2010).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[11]
FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DOMAIN, AND
ENZYME REGULATION.
STRAIN=cv. Columbia;
PubMed=25736060; DOI=10.1105/tpc.114.134494;
Gutierrez-Beltran E., Moschou P.N., Smertenko A.P., Bozhkov P.V.;
"Tudor staphylococcal nuclease links formation of stress granules and
processing bodies with mRNA catabolism in Arabidopsis.";
Plant Cell 27:926-943(2015).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=cv. Columbia, and cv. Landsberg erecta;
PubMed=26237081; DOI=10.1080/15592324.2015.1071005;
Gutierrez-Beltran E., Bozhkov P.V., Moschou P.N.;
"Tudor staphylococcal nuclease plays two antagonistic roles in RNA
metabolism under stress.";
Plant Signal. Behav. 10:E1071005-E1071005(2015).
-!- FUNCTION: Cytoprotective ribonuclease (RNase) required for
resistance to abiotic stresses, acting as a positive regulator of
mRNA decapping during stress (PubMed:25736060). Essential for the
integrity and function of cytoplasmic messenger ribonucleoprotein
(mRNP) complexes called stress granules (SGs) and processing
bodies (PBs), sites of post-transcriptional gene regulation during
stress (e.g. salt and heat) (PubMed:25736060). Involved in
gibberellic acid (GA) biosynthesis and seed germination
(PubMed:20396901). Essential for stress tolerance, probably by
regulating mRNAs entering the secretory pathway (PubMed:20484005).
Component of stress granules (SGs) that regulates growth under
salt stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3
mRNA (By similarity). May inhibit the degradation of mRNAs
involved in stress adaptation (PubMed:26237081).
{ECO:0000250|UniProtKB:Q8VZG7, ECO:0000269|PubMed:20396901,
ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25736060,
ECO:0000269|PubMed:26237081}.
-!- ENZYME REGULATION: Repressed by the specific inhibitor 3',5'-
deoxythymidine bisphosphate (pdTp); this RNase activity inhibition
impairs subcellular relocation upon abiotic stress and leads to
reduced stress resistance. {ECO:0000269|PubMed:25736060}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20484005,
ECO:0000269|PubMed:25736060}. Cytoplasm, perinuclear region
{ECO:0000269|PubMed:20484005}. Endoplasmic reticulum
{ECO:0000269|PubMed:20484005}. Cytoplasmic granule
{ECO:0000269|PubMed:25736060}. Note=Accumulates heterogeneously in
the cytosol, in patches around the nucleus and in the cell
periphery, and relocates transiently to a diffuse pattern in
response to salt stress (PubMed:20484005). Accumulates in
cytoplasmic stress granules (SGs) and processing bodies (PBs) in
response to abiotic stresses (e.g. salt and heat)
(PubMed:25736060). {ECO:0000269|PubMed:20484005,
ECO:0000269|PubMed:25736060}.
-!- TISSUE SPECIFICITY: Mostly expressed in seeds, and, to a lower
extent, in leaves, flowers, roots and siliques (at protein level)
(PubMed:20396901, PubMed:20484005). Accumulates strongly in the
cap and elongation zone of the root apices (at protein level)
(PubMed:20484005). {ECO:0000269|PubMed:20396901,
ECO:0000269|PubMed:20484005}.
-!- DEVELOPMENTAL STAGE: In mature seeds, accumulates highly both in
cotyledons and radicals. {ECO:0000269|PubMed:20396901}.
-!- DOMAIN: TNase-like domains are required for relocation to
cytoplasmic foci upon abiotic stresses.
{ECO:0000269|PubMed:25736060}.
-!- DISRUPTION PHENOTYPE: Normal vegetative growth, flowering time and
flower morphology, but delayed seed germination after
vernalization (at 4 degrees Celsius); this phenotype is reversed
by gibberellic acid (GA-3) but increased by paclobutrazol, a GA
biosynthesis inhibitor. Reduced expression of enzyme involved in
GA biosynthesis leading to reduced levels of GA-4 (e.g. GA20OX3)
(PubMed:20396901). The double mutant tsn1 tsn2 exhibits severe
alteration in germination, growth, and survival under high
salinity stress. In normal conditions, moderate reduction in root
growth due to cell elongation defect. Reduced levels of stress-
regulated mRNAs encoding secreted proteins (PubMed:20484005).
Abnormal stress granules (SGs) and processing bodies (PBs)
assembly accompanied by reduced uncapped RNAs levels in heat-
stressed double mutant tsn1 tsn2 (PubMed:25736060). The double
mutant tsn1 tsn2 is also showing enriched uncapping and subsequent
degradation of mRNAs involved in stress adaptation
(PubMed:26237081). {ECO:0000269|PubMed:20396901,
ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25736060,
ECO:0000269|PubMed:26237081}.
-----------------------------------------------------------------------
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EMBL; AB010069; BAB10078.1; -; Genomic_DNA.
EMBL; CP002688; AED97517.1; -; Genomic_DNA.
EMBL; BT002044; AAN72055.1; -; mRNA.
EMBL; AK226659; BAE98767.1; -; mRNA.
EMBL; AK230034; BAF01856.1; -; mRNA.
EMBL; AK230048; BAF01870.1; -; mRNA.
RefSeq; NP_200986.1; NM_125572.3.
UniGene; At.21985; -.
ProteinModelPortal; Q9FLT0; -.
SMR; Q9FLT0; -.
STRING; 3702.AT5G61780.1; -.
iPTMnet; Q9FLT0; -.
PaxDb; Q9FLT0; -.
EnsemblPlants; AT5G61780.1; AT5G61780.1; AT5G61780.
GeneID; 836300; -.
Gramene; AT5G61780.1; AT5G61780.1; AT5G61780.
KEGG; ath:AT5G61780; -.
Araport; AT5G61780; -.
TAIR; locus:2159218; AT5G61780.
eggNOG; KOG2039; Eukaryota.
eggNOG; COG1525; LUCA.
HOGENOM; HOG000173592; -.
KO; K15979; -.
OMA; AGMFYVQ; -.
OrthoDB; EOG093601G3; -.
PhylomeDB; Q9FLT0; -.
BRENDA; 3.1.31.1; 399.
PRO; PR:Q9FLT0; -.
Proteomes; UP000006548; Chromosome 5.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
GO; GO:0000932; C:P-body; IDA:TAIR.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0016442; C:RISC complex; IEA:InterPro.
GO; GO:0003729; F:mRNA binding; IDA:TAIR.
GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
GO; GO:0009686; P:gibberellin biosynthetic process; IMP:TAIR.
GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
GO; GO:0010372; P:positive regulation of gibberellin biosynthetic process; IMP:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009651; P:response to salt stress; IGI:TAIR.
GO; GO:0009845; P:seed germination; IMP:TAIR.
Gene3D; 2.40.50.90; -; 5.
InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
InterPro; IPR035437; SNase_OB-fold/TUDOR_sf.
InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
InterPro; IPR002999; Tudor.
Pfam; PF00565; SNase; 4.
Pfam; PF00567; TUDOR; 1.
PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
SMART; SM00318; SNc; 4.
SMART; SM00333; TUDOR; 1.
SUPFAM; SSF50199; SSF50199; 6.
PROSITE; PS50830; TNASE_3; 4.
PROSITE; PS50304; TUDOR; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Endoplasmic reticulum;
Hydrolase; Nuclease; Phosphoprotein; Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895}.
CHAIN 2 985 Ribonuclease TUDOR 2.
/FTId=PRO_0000437884.
DOMAIN 10 153 TNase-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00272}.
DOMAIN 188 368 TNase-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00272}.
DOMAIN 382 552 TNase-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00272}.
DOMAIN 582 711 TNase-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00272}.
DOMAIN 778 843 Tudor. {ECO:0000255|PROSITE-
ProRule:PRU00211}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895}.
MOD_RES 961 961 Phosphothreonine.
{ECO:0000244|PubMed:19245862}.
MOD_RES 966 966 Phosphotyrosine.
{ECO:0000244|PubMed:19245862}.
MOD_RES 971 971 Phosphoserine.
{ECO:0000244|PubMed:18433157,
ECO:0000244|PubMed:19245862,
ECO:0000244|PubMed:19376835}.
CONFLICT 921 921 A -> T (in Ref. 4; BAF01856).
{ECO:0000305}.
SEQUENCE 985 AA; 107742 MW; 1A66E660099EF887 CRC64;
MATGAATENQ WLKGRVKAVT SGDCLVITAL THNRAGPPPE KTITLSSLMA PKMARRGGID
EPFAWESREF LRKLCIGKEV AFKVDYKVEA IAGREFGSVY LGNENLAKLV VQNGWAKVRR
PGQQNQDKVS PYIAELEQLE EQAQQEGFGR WSKVPGAAEA SIRNLPPSAV GDSGNFDAMG
LLAASKGKPM EGIVEQVRDG STIRVYLLPE FQFVQVFVAG LQAPSMGRRQ STQEAVVDPD
VTATSNGDAS AETRGPLTTA QRLAASAASS VEVSSDPFAM EAKYFTELRV LNRDVRIVLE
GVDKFNNLIG SVYYSDGDTV KDLGLELVEN GLAKYVEWSA NMLDEEAKKK LKATELQCKK
NRVKMWANYV PPASNSKAIH DQNFTGKVVE VVSGDCLVVA DDSIPFGSPM AERRVCLSSI
RSPKMGNPRR EEKPAPYARE AKEFLRQKLI GMEVIVQMEY SRKISPGDGV TTSGAGDRVM
DFGSVFLPSP TKGDTAVAAA ATPGANIAEL IISRGLGTVV RHRDFEERSN HYDALLAAEA
RAIAGKKNIH SAKDSPALHI ADLTVASAKK AKDFLPSLQR INQISAVVEY VLSGHRFKLY
IPKESCSIAF AFSGVRCPGR GEPYSEEAIA LMRRKIMQRD VEIVVENVDR TGTFLGSMWE
KNSKTNAGTY LLEAGLAKMQ TGFGADRIPE AHILEMAERS AKNQKLKIWE NYVEGEEVVN
GSSKVETRQK ETLKVVVTEV LGGGRFYVQT VGDQKVASIQ NQLAALSLKD APIIGSFNPK
KGDIVLAQFS LDNSWNRAMI VNGPRGAVQS PEEEFEVFYI DYGNQEIVPY SAIRPVDPSV
SSAPGLAQLC RLAYIKVPGK EEDFGRDAGE YLHTVTLESG KEFRAVVEER DTSGGKVKGQ
GTGTELVVTL IAVDDEISVN AAMLQEGIAR MEKRRRWEPK DKQAALDALE KFQDEARKSR
TGIWEYGDIQ SDDEDNVPVR KPGRG


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