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   27-MAR-2024, entry version 157.
DE   RecName: Full=Ribonuclease 2;
DE            EC=4.6.1.19 {ECO:0000255|PROSITE-ProRule:PRU10046};
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}.
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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.P42814; -.
DR   PaxDb; 3702-AT2G39780-1; -.
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; AT2G39780; RNS2.
DR   eggNOG; KOG1642; Eukaryota.
DR   HOGENOM; CLU_069912_3_0_1; -.
DR   InParanoid; P42814; -.
DR   OMA; NFANEIM; -.
DR   OrthoDB; 878940at2759; -.
DR   PhylomeDB; P42814; -.
DR   PRO; PR:P42814; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P42814; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0010168; C:ER body; IDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0005773; C:vacuole; 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:0004521; F:RNA endonuclease activity; IDA:TAIR.
DR   GO; GO:0010507; P:negative regulation of autophagy; IMP:TAIR.
DR   GO; GO:0016075; P:rRNA catabolic process; IMP:TAIR.
DR   CDD; cd01061; RNase_T2_euk; 1.
DR   Gene3D; 3.90.730.10; Ribonuclease T2-like; 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:SF89; RIBONUCLEASE 2; 1.
DR   PANTHER; PTHR11240; RIBONUCLEASE T2; 1.
DR   Pfam; PF00445; Ribonuclease_T2; 1.
DR   SUPFAM; SSF55895; Ribonuclease Rh-like; 1.
DR   PROSITE; PS00530; RNASE_T2_1; 1.
DR   PROSITE; PS00531; RNASE_T2_2; 1.
DR   Genevisible; P42814; AT.
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                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SID5,
FT                   ECO:0000255|PROSITE-ProRule:PRU10045"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   ACT_SITE        133
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SID5,
FT                   ECO:0000255|PROSITE-ProRule:PRU10045"
FT   BINDING         40
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   BINDING         71
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   BINDING         125
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   BINDING         128..129
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   BINDING         132..133
FT                   /ligand="RNA"
FT                   /ligand_id="ChEBI:CHEBI:33697"
FT                   /ligand_part="a 3'-terminal ribonucleotide 3'-phosphate
FT                   residue"
FT                   /ligand_part_id="ChEBI:CHEBI:83062"
FT                   /evidence="ECO:0000250|UniProtKB:P23540"
FT   DISULFID        46..58
FT                   /evidence="ECO:0000250|UniProtKB:Q7SID5"
FT   DISULFID        86..136
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   DISULFID        198..231
FT                   /evidence="ECO:0000250|UniProtKB:P08056"
FT   DISULFID        209..219
FT                   /evidence="ECO:0000250|UniProtKB:Q7SID5"
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
//