TSN2_ARATH
ID TSN2_ARATH Reviewed; 985 AA.
AC Q9FLT0; Q0WLY7; Q0WM01; Q0WVT1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 155.
DE RecName: Full=Ribonuclease TUDOR 2 {ECO:0000303|PubMed:20396901};
DE Short=AtTudor2 {ECO:0000303|PubMed:20396901};
DE Short=TUDOR-SN protein 2 {ECO:0000303|PubMed:20396901};
DE EC=3.1.-.- {ECO:0000269|PubMed:25736060};
DE AltName: Full=100 kDa coactivator-like protein;
GN Name=TSN2 {ECO:0000303|PubMed:20396901};
GN OrderedLocusNames=At5g61780 {ECO:0000312|Araport:AT5G61780};
GN ORFNames=MAC9.10 {ECO:0000312|EMBL:BAB10078.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
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;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-347 AND 374-985.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-971, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-961; TYR-966 AND SER-971, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-971, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP GENE FAMILY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=20396901; DOI=10.1007/s00425-010-1167-0;
RA Liu S., Jia J., Gao Y., Zhang B., Han Y.;
RT "The AtTudor2, a protein with SN-Tudor domains, is involved in control of
RT seed germination in Arabidopsis.";
RL Planta 232:197-207(2010).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=20484005; DOI=10.1105/tpc.109.070680;
RA Frei dit Frey N., Muller P., Jammes F., Kizis D., Leung J.,
RA Perrot-Rechenmann C., Bianchi M.W.;
RT "The RNA binding protein Tudor-SN is essential for stress tolerance and
RT stabilizes levels of stress-responsive mRNAs encoding secreted proteins in
RT Arabidopsis.";
RL Plant Cell 22:1575-1591(2010).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, DOMAIN, AND ACTIVITY
RP REGULATION.
RC STRAIN=cv. Columbia;
RX PubMed=25736060; DOI=10.1105/tpc.114.134494;
RA Gutierrez-Beltran E., Moschou P.N., Smertenko A.P., Bozhkov P.V.;
RT "Tudor staphylococcal nuclease links formation of stress granules and
RT processing bodies with mRNA catabolism in Arabidopsis.";
RL Plant Cell 27:926-943(2015).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=26237081; DOI=10.1080/15592324.2015.1071005;
RA Gutierrez-Beltran E., Bozhkov P.V., Moschou P.N.;
RT "Tudor staphylococcal nuclease plays two antagonistic roles in RNA
RT metabolism under stress.";
RL Plant Signal. Behav. 10:E1071005-E1071005(2015).
CC -!- FUNCTION: Cytoprotective ribonuclease (RNase) required for resistance
CC to abiotic stresses, acting as a positive regulator of mRNA decapping
CC during stress (PubMed:25736060). Essential for the integrity and
CC function of cytoplasmic messenger ribonucleoprotein (mRNP) complexes
CC called stress granules (SGs) and processing bodies (PBs), sites of
CC post-transcriptional gene regulation during stress (e.g. salt and heat)
CC (PubMed:25736060). Involved in gibberellic acid (GA) biosynthesis and
CC seed germination (PubMed:20396901). Essential for stress tolerance,
CC probably by regulating mRNAs entering the secretory pathway
CC (PubMed:20484005). Component of stress granules (SGs) that regulates
CC growth under salt stress by modulating levels of GA20OX3 mRNA. Binds
CC GA20OX3 mRNA (By similarity). May inhibit the degradation of mRNAs
CC involved in stress adaptation (PubMed:26237081).
CC {ECO:0000250|UniProtKB:Q8VZG7, ECO:0000269|PubMed:20396901,
CC ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25736060,
CC ECO:0000269|PubMed:26237081}.
CC -!- ACTIVITY REGULATION: Repressed by the specific inhibitor 3',5'-
CC deoxythymidine bisphosphate (pdTp); this RNase activity inhibition
CC impairs subcellular relocation upon abiotic stress and leads to reduced
CC stress resistance. {ECO:0000269|PubMed:25736060}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20484005,
CC ECO:0000269|PubMed:25736060}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:20484005}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:20484005}. Cytoplasmic granule
CC {ECO:0000269|PubMed:25736060}. Note=Accumulates heterogeneously in the
CC cytosol, in patches around the nucleus and in the cell periphery, and
CC relocates transiently to a diffuse pattern in response to salt stress
CC (PubMed:20484005). Accumulates in cytoplasmic stress granules (SGs) and
CC processing bodies (PBs) in response to abiotic stresses (e.g. salt and
CC heat) (PubMed:25736060). {ECO:0000269|PubMed:20484005,
CC ECO:0000269|PubMed:25736060}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seeds, and, to a lower extent,
CC in leaves, flowers, roots and siliques (at protein level)
CC (PubMed:20396901, PubMed:20484005). Accumulates strongly in the cap and
CC elongation zone of the root apices (at protein level)
CC (PubMed:20484005). {ECO:0000269|PubMed:20396901,
CC ECO:0000269|PubMed:20484005}.
CC -!- DEVELOPMENTAL STAGE: In mature seeds, accumulates highly both in
CC cotyledons and radicals. {ECO:0000269|PubMed:20396901}.
CC -!- DOMAIN: TNase-like domains are required for relocation to cytoplasmic
CC foci upon abiotic stresses. {ECO:0000269|PubMed:25736060}.
CC -!- DISRUPTION PHENOTYPE: Normal vegetative growth, flowering time and
CC flower morphology, but delayed seed germination after vernalization (at
CC 4 degrees Celsius); this phenotype is reversed by gibberellic acid (GA-
CC 3) but increased by paclobutrazol, a GA biosynthesis inhibitor. Reduced
CC expression of enzyme involved in GA biosynthesis leading to reduced
CC levels of GA-4 (e.g. GA20OX3) (PubMed:20396901). The double mutant tsn1
CC tsn2 exhibits severe alteration in germination, growth, and survival
CC under high salinity stress. In normal conditions, moderate reduction in
CC root growth due to cell elongation defect. Reduced levels of stress-
CC regulated mRNAs encoding secreted proteins (PubMed:20484005). Abnormal
CC stress granules (SGs) and processing bodies (PBs) assembly accompanied
CC by reduced uncapped RNAs levels in heat-stressed double mutant tsn1
CC tsn2 (PubMed:25736060). The double mutant tsn1 tsn2 is also showing
CC enriched uncapping and subsequent degradation of mRNAs involved in
CC stress adaptation (PubMed:26237081). {ECO:0000269|PubMed:20396901,
CC ECO:0000269|PubMed:20484005, ECO:0000269|PubMed:25736060,
CC ECO:0000269|PubMed:26237081}.
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DR EMBL; AB010069; BAB10078.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97517.1; -; Genomic_DNA.
DR EMBL; BT002044; AAN72055.1; -; mRNA.
DR EMBL; AK226659; BAE98767.1; -; mRNA.
DR EMBL; AK230034; BAF01856.1; -; mRNA.
DR EMBL; AK230048; BAF01870.1; -; mRNA.
DR RefSeq; NP_200986.1; NM_125572.3.
DR AlphaFoldDB; Q9FLT0; -.
DR SMR; Q9FLT0; -.
DR STRING; 3702.AT5G61780.1; -.
DR iPTMnet; Q9FLT0; -.
DR MetOSite; Q9FLT0; -.
DR PaxDb; Q9FLT0; -.
DR PRIDE; Q9FLT0; -.
DR ProteomicsDB; 234649; -.
DR EnsemblPlants; AT5G61780.1; AT5G61780.1; AT5G61780.
DR GeneID; 836300; -.
DR Gramene; AT5G61780.1; AT5G61780.1; AT5G61780.
DR KEGG; ath:AT5G61780; -.
DR Araport; AT5G61780; -.
DR TAIR; locus:2159218; AT5G61780.
DR eggNOG; KOG2039; Eukaryota.
DR HOGENOM; CLU_005966_2_0_1; -.
DR InParanoid; Q9FLT0; -.
DR OMA; FGQEAHD; -.
DR OrthoDB; 227839at2759; -.
DR PhylomeDB; Q9FLT0; -.
DR BRENDA; 3.1.31.1; 399.
DR PRO; PR:Q9FLT0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLT0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005635; C:nuclear envelope; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IDA:TAIR.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0016442; C:RISC complex; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0004518; F:nuclease activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:InterPro.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IMP:TAIR.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IMP:UniProtKB.
DR GO; GO:0010372; P:positive regulation of gibberellin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IGI:TAIR.
DR GO; GO:0009845; P:seed germination; IMP:TAIR.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 2.40.50.90; -; 5.
DR InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR InterPro; IPR035437; SNase_OB-fold_sf.
DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR InterPro; IPR002999; Tudor.
DR Pfam; PF00565; SNase; 4.
DR Pfam; PF00567; TUDOR; 1.
DR PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR SMART; SM00318; SNc; 4.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF50199; SSF50199; 5.
DR PROSITE; PS50830; TNASE_3; 4.
DR PROSITE; PS50304; TUDOR; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Hydrolase; Nuclease;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..985
FT /note="Ribonuclease TUDOR 2"
FT /id="PRO_0000437884"
FT DOMAIN 10..153
FT /note="TNase-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 188..368
FT /note="TNase-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 382..552
FT /note="TNase-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 582..711
FT /note="TNase-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00272"
FT DOMAIN 778..843
FT /note="Tudor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00211"
FT REGION 228..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 961
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 966
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19245862"
FT MOD_RES 971
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT CONFLICT 921
FT /note="A -> T (in Ref. 4; BAF01856)"
FT /evidence="ECO:0000305"
SQ 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
