RNS3_ARATH
ID RNS3_ARATH Reviewed; 222 AA.
AC P42815;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ribonuclease 3;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNS3; OrderedLocusNames=At1g26820; ORFNames=T24P13.23, T2P11.1;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8000425; DOI=10.1046/j.1365-313x.1994.6050673.x;
RA Bariola P.A., Howard C.J., Taylor C.B., Verburg M.T., Jaglan V.D.,
RA Green P.J.;
RT "The Arabidopsis ribonuclease gene RNS1 is tightly controlled in response
RT to phosphate limitation.";
RL Plant J. 6:673-685(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR EMBL; U05207; AAC48926.1; -; mRNA.
DR EMBL; AC005508; AAD14489.1; -; Genomic_DNA.
DR EMBL; AC006535; AAF87036.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30746.1; -; Genomic_DNA.
DR EMBL; AY063844; AAL36200.1; -; mRNA.
DR EMBL; AY117288; AAM51363.1; -; mRNA.
DR EMBL; AY088821; AAM67130.1; -; mRNA.
DR PIR; H86394; H86394.
DR RefSeq; NP_564264.1; NM_102446.3.
DR AlphaFoldDB; P42815; -.
DR SMR; P42815; -.
DR STRING; 3702.AT1G26820.1; -.
DR PaxDb; P42815; -.
DR PRIDE; P42815; -.
DR ProteomicsDB; 227974; -.
DR EnsemblPlants; AT1G26820.1; AT1G26820.1; AT1G26820.
DR GeneID; 839225; -.
DR Gramene; AT1G26820.1; AT1G26820.1; AT1G26820.
DR KEGG; ath:AT1G26820; -.
DR Araport; AT1G26820; -.
DR TAIR; locus:2200665; AT1G26820.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_069912_2_1_1; -.
DR InParanoid; P42815; -.
DR OMA; DNEASCC; -.
DR OrthoDB; 994722at2759; -.
DR PhylomeDB; P42815; -.
DR PRO; PR:P42815; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P42815; baseline and differential.
DR Genevisible; P42815; AT.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
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 Disulfide bond; Endonuclease; Hydrolase; Lyase; Nuclease;
KW Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..222
FT /note="Ribonuclease 3"
FT /id="PRO_0000030968"
FT ACT_SITE 57
FT /evidence="ECO:0000250"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT ACT_SITE 115
FT /evidence="ECO:0000250"
FT DISULFID 72..118
FT /evidence="ECO:0000250"
FT DISULFID 178..213
FT /evidence="ECO:0000250"
SQ SEQUENCE 222 AA; 25626 MW; 4CA54957D6C2DFEC CRC64;
MKFFIFILAL QQLYVQSFAQ DFDFFYFVLQ WPGAYCDSRH SCCYPQTGKP AADFGIHGLW
PNYKTGGWPQ NCNPDSRFDD LRVSDLMSDL QREWPTLSCP SNDGMKFWTH EWEKHGTCAE
SELDQHDYFE AGLKLKQKAN LLHALTNAGI KPDDKFYEMK DIENTIKQVV GFAPGIECNK
DSSHNSQLYQ IYLCVDTSAS KFINCPVMPH GRCDSRVQFP KF
