Entry euk: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   10-MAY-2017, entry version 125.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.
RT   Sequence features of the regions of 1,456,315 bp covered by nineteen
RT   physically assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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.,
RA   Hayashizaki Y., 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] {ECO:0000244|PubMed:18433157}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.,
RA   Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
RA   Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by
RT   mass spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
RN   [6] {ECO:0000244|PubMed:19245862}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,
RA   Andreasson E., Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from
RT   Arabidopsis thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [7] {ECO:0000244|PubMed:19376835}
RP   IDENTIFICATION BY 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
RP   STAGE, 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
RT   of 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
RT   and stabilizes levels of stress-responsive mRNAs encoding secreted
RT   proteins in Arabidopsis.";
RL   Plant Cell 22:1575-1591(2010).
RN   [10] {ECO:0000244|PubMed:22223895}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.M111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
RA   Meinnel T., 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
RP   ENZYME 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
CC       resistance to abiotic stresses, acting as a positive regulator of
CC       mRNA decapping during stress (PubMed:25736060). Essential for the
CC       integrity and function of cytoplasmic messenger ribonucleoprotein
CC       (mRNP) complexes called stress granules (SGs) and processing
CC       bodies (PBs), sites of post-transcriptional gene regulation during
CC       stress (e.g. salt and heat) (PubMed:25736060). Involved in
CC       gibberellic acid (GA) biosynthesis and seed germination
CC       (PubMed:20396901). Essential for stress tolerance, probably by
CC       regulating mRNAs entering the secretory pathway (PubMed:20484005).
CC       Component of stress granules (SGs) that regulates growth under
CC       salt stress by modulating levels of GA20OX3 mRNA. Binds GA20OX3
CC       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   -!- ENZYME 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
CC       reduced 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
CC       the cytosol, in patches around the nucleus and in the cell
CC       periphery, and relocates transiently to a diffuse pattern in
CC       response to salt stress (PubMed:20484005). Accumulates in
CC       cytoplasmic stress granules (SGs) and processing bodies (PBs) in
CC       response to abiotic stresses (e.g. salt and heat)
CC       (PubMed:25736060). {ECO:0000269|PubMed:20484005,
CC       ECO:0000269|PubMed:25736060}.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in seeds, and, to a lower
CC       extent, in leaves, flowers, roots and siliques (at protein level)
CC       (PubMed:20396901, PubMed:20484005). Accumulates strongly in the
CC       cap and 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
CC       cytoplasmic foci upon abiotic stresses.
CC       {ECO:0000269|PubMed:25736060}.
CC   -!- DISRUPTION PHENOTYPE: Normal vegetative growth, flowering time and
CC       flower morphology, but delayed seed germination after
CC       vernalization (at 4 degrees Celsius); this phenotype is reversed
CC       by gibberellic acid (GA-3) but increased by paclobutrazol, a GA
CC       biosynthesis inhibitor. Reduced expression of enzyme involved in
CC       GA biosynthesis leading to reduced levels of GA-4 (e.g. GA20OX3)
CC       (PubMed:20396901). The double mutant tsn1 tsn2 exhibits severe
CC       alteration in germination, growth, and survival under high
CC       salinity stress. In normal conditions, moderate reduction in root
CC       growth due to cell elongation defect. Reduced levels of stress-
CC       regulated mRNAs encoding secreted proteins (PubMed:20484005).
CC       Abnormal stress granules (SGs) and processing bodies (PBs)
CC       assembly accompanied by reduced uncapped RNAs levels in heat-
CC       stressed double mutant tsn1 tsn2 (PubMed:25736060). The double
CC       mutant tsn1 tsn2 is also showing enriched uncapping and subsequent
CC       degradation of mRNAs involved in stress adaptation
CC       (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   UniGene; At.21985; -.
DR   ProteinModelPortal; Q9FLT0; -.
DR   SMR; Q9FLT0; -.
DR   STRING; 3702.AT5G61780.1; -.
DR   PaxDb; Q9FLT0; -.
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   eggNOG; COG1525; LUCA.
DR   HOGENOM; HOG000173592; -.
DR   KO; K15979; -.
DR   OMA; PGANIAE; -.
DR   OrthoDB; EOG093601G3; -.
DR   PhylomeDB; Q9FLT0; -.
DR   BRENDA; 3.1.31.1; 399.
DR   PRO; PR:Q9FLT0; -.
DR   Proteomes; UP000006548; Chromosome 5.
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:0000932; C:P-body; IDA:TAIR.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009506; C:plasmodesma; IDA: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   InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR   InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR   InterPro; IPR002999; Tudor.
DR   Pfam; PF00565; SNase; 5.
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; 6.
DR   PROSITE; PS50830; TNASE_3; 4.
DR   PROSITE; PS50304; TUDOR; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW   Nuclease; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN         1    985       Ribonuclease TUDOR 2.
FT                                /FTId=PRO_0000437884.
FT   DOMAIN       10    153       TNase-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      188    368       TNase-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      382    552       TNase-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      582    711       TNase-like 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00272}.
FT   DOMAIN      778    843       Tudor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00211}.
FT   MOD_RES     971    971       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8VZG7}.
FT   CONFLICT    921    921       A -> T (in Ref. 4; BAF01856).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       730    853       ipfam:TUDOR [T]
FT   MYHIT       382    552       iprf:TNASE_3 [T]
FT   MYHIT       188    368       iprf:TNASE_3 [T]
FT   MYHIT       382    552       ismart:SNc [T]
FT   MYHIT       777    841       ismart:TUDOR [T]
FT   MYHIT       778    843       iprf:TUDOR [T]
FT   MYHIT       582    711       ismart:SNc [T]
FT   MYHIT       582    711       iprf:TNASE_3 [T]
FT   MYHIT        10    153       iprf:TNASE_3 [T]
FT   MYHIT       188    368       ismart:SNc [T]
FT   MYHIT       612    711       ipfam:SNase [T]
FT   MYHIT        10    153       ismart:SNc [T]
FT   MYHIT       414    549       ipfam:SNase [T]
FT   MYHIT       274    367       ipfam:SNase [T]
FT   MYHIT        42    153       ipfam:SNase [T]
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
//