RNS2_ARATH
ID RNS2_ARATH Reviewed; 259 AA.
AC P42814; Q42136;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Ribonuclease 2;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNS2; OrderedLocusNames=At2g39780; ORFNames=T5I7.8;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8506358; DOI=10.1073/pnas.90.11.5118;
RA Taylor C.B., Bariola P.A., Delcardayre S.B., Raines R.T., Green P.J.;
RT "RNS2: a senescence-associated RNase of Arabidopsis that diverged from the
RT S-RNases before speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5118-5122(1993).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-259.
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
CC -!- FUNCTION: May remobilize phosphate, particularly when cells senesce or
CC when phosphate becomes limiting.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10045, ECO:0000255|PROSITE-ProRule:PRU10046};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P42814-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Most highly expressed in flowers, but also
CC expressed in roots, stems, and leaves.
CC -!- INDUCTION: By phosphate starvation.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {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; M98336; AAA51406.1; -; mRNA.
DR EMBL; AC003000; AAB87127.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC09723.1; -; Genomic_DNA.
DR EMBL; Z26559; CAA81330.1; -; mRNA.
DR PIR; T01008; T01008.
DR RefSeq; NP_030524.1; NM_129536.5. [P42814-1]
DR AlphaFoldDB; P42814; -.
DR SMR; P42814; -.
DR STRING; 3702.AT2G39780.1; -.
DR PaxDb; P42814; -.
DR PRIDE; P42814; -.
DR ProteomicsDB; 227968; -. [P42814-1]
DR DNASU; 818563; -.
DR EnsemblPlants; AT2G39780.1; AT2G39780.1; AT2G39780. [P42814-1]
DR GeneID; 818563; -.
DR Gramene; AT2G39780.1; AT2G39780.1; AT2G39780. [P42814-1]
DR KEGG; ath:AT2G39780; -.
DR Araport; AT2G39780; -.
DR TAIR; locus:2063964; AT2G39780.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_069912_3_0_1; -.
DR InParanoid; P42814; -.
DR OMA; WHQWKKH; -.
DR PhylomeDB; P42814; -.
DR PRO; PR:P42814; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P42814; baseline and differential.
DR Genevisible; P42814; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0010168; C:ER body; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005773; C:vacuole; IDA:TAIR.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:TAIR.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:TAIR.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0016075; P:rRNA catabolic process; IMP:TAIR.
DR CDD; cd01061; RNase_T2_euk; 1.
DR Gene3D; 3.90.730.10; -; 1.
DR InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR InterPro; IPR001568; RNase_T2-like.
DR InterPro; IPR036430; RNase_T2-like_sf.
DR InterPro; IPR018188; RNase_T2_His_AS_1.
DR InterPro; IPR033130; RNase_T2_His_AS_2.
DR PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00530; RNASE_T2_1; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW Nuclease; Reference proteome; Signal; Stress response.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..259
FT /note="Ribonuclease 2"
FT /id="PRO_0000030967"
FT ACT_SITE 71
FT /evidence="ECO:0000250"
FT ACT_SITE 129
FT /evidence="ECO:0000250"
FT ACT_SITE 133
FT /evidence="ECO:0000250"
FT DISULFID 86..136
FT /evidence="ECO:0000250"
FT CONFLICT 210
FT /note="F -> S (in Ref. 4; CAA81330)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 259 AA; 29153 MW; FE6DCD6926428942 CRC64;
MASRLCLLLL VACIAGAFAG DVIELNRSQR EFDYFALSLQ WPGTYCRGTR HCCSKNACCR
GSDAPTQFTI HGLWPDYNDG SWPSCCYRSD FKEKEISTLM DGLEKYWPSL SCGSPSSCNG
GKGSFWGHEW EKHGTCSSPV FHDEYNYFLT TLNLYLKHNV TDVLYQAGYV ASNSEKYPLG
GIVTAIQNAF HITPEVVCKR DAIDEIRICF YKDFKPRDCV GSQDLTSRKS CPKYVSLPEY
TPLDGEAMVL KMPTEREAL