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RNS1_ARATH
ID   RNS1_ARATH              Reviewed;         230 AA.
AC   P42813; A0MEM0; Q1PF62; Q42188; Q6LAC8; Q8LC78;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 151.
DE   RecName: Full=Ribonuclease 1;
DE            EC=4.6.1.19;
DE   Flags: Precursor;
GN   Name=RNS1; OrderedLocusNames=At2g02990; ORFNames=T17M13.16;
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=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].
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].
RC   STRAIN=cv. Columbia;
RX   PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA   Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT   "Simultaneous high-throughput recombinational cloning of open reading
RT   frames in closed and open configurations.";
RL   Plant Biotechnol. J. 4:317-324(2006).
RN   [6]
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.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-225.
RC   STRAIN=cv. Columbia; TISSUE=Green siliques;
RA   Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT   "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PROTEIN SEQUENCE OF 23-41.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
RA   Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
RA   Slabas A.R.;
RT   "Differential extraction and protein sequencing reveals major differences
RT   in patterns of primary cell wall proteins from plants.";
RL   J. Biol. Chem. 272:15841-15848(1997).
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   -!- INDUCTION: By phosphate starvation.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK28493.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U05206; AAC48925.1; -; mRNA.
DR   EMBL; AC004138; AAC32917.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC05652.1; -; Genomic_DNA.
DR   EMBL; AY072413; AAL62405.1; -; mRNA.
DR   EMBL; AY114710; AAM48029.1; -; mRNA.
DR   EMBL; DQ446504; ABE65814.1; -; mRNA.
DR   EMBL; DQ652992; ABK28493.1; ALT_SEQ; mRNA.
DR   EMBL; AY086747; AAM63798.1; -; mRNA.
DR   EMBL; Z27289; CAA81782.1; -; mRNA.
DR   EMBL; Z27290; CAA81783.1; -; mRNA.
DR   PIR; A84443; A84443.
DR   RefSeq; NP_178399.1; NM_126351.3.
DR   AlphaFoldDB; P42813; -.
DR   SMR; P42813; -.
DR   BioGRID; 230; 6.
DR   IntAct; P42813; 6.
DR   STRING; 3702.AT2G02990.1; -.
DR   PaxDb; P42813; -.
DR   PRIDE; P42813; -.
DR   ProteomicsDB; 227967; -.
DR   EnsemblPlants; AT2G02990.1; AT2G02990.1; AT2G02990.
DR   GeneID; 814828; -.
DR   Gramene; AT2G02990.1; AT2G02990.1; AT2G02990.
DR   KEGG; ath:AT2G02990; -.
DR   Araport; AT2G02990; -.
DR   TAIR; locus:2056755; AT2G02990.
DR   eggNOG; KOG1642; Eukaryota.
DR   HOGENOM; CLU_069912_2_1_1; -.
DR   InParanoid; P42813; -.
DR   OMA; DMRRYWP; -.
DR   OrthoDB; 994722at2759; -.
DR   PhylomeDB; P42813; -.
DR   PRO; PR:P42813; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P42813; baseline and differential.
DR   Genevisible; P42813; AT.
DR   GO; GO:0005576; C:extracellular region; IDA:TAIR.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0004540; F:ribonuclease 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:0009718; P:anthocyanin-containing compound biosynthetic process; IMP:TAIR.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR   GO; GO:0009611; P:response to wounding; IEP:TAIR.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW   Nuclease; Reference proteome; Signal; Stress response.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:9188482"
FT   CHAIN           23..230
FT                   /note="Ribonuclease 1"
FT                   /id="PRO_0000030966"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        119
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        123
FT                   /evidence="ECO:0000250"
FT   DISULFID        80..126
FT                   /evidence="ECO:0000250"
FT   DISULFID        186..221
FT                   /evidence="ECO:0000250"
FT   CONFLICT        39..41
FT                   /note="WPG -> GXP (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="A -> D (in Ref. 6; AAM63798)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130..131
FT                   /note="VI -> GY (in Ref. 7; CAA81782)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        203
FT                   /note="V -> A (in Ref. 7; CAA81782)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   230 AA;  25397 MW;  DFD132D39F02505A CRC64;
     MKILLASLCL ISLLVILPSV FSASSSSEDF DFFYFVQQWP GSYCDTQKKC CYPNSGKPAA
     DFGIHGLWPN YKDGTYPSNC DASKPFDSST ISDLLTSMKK SWPTLACPSG SGEAFWEHEW
     EKHGTCSESV IDQHEYFQTA LNLKQKTNLL GALTKAGINP DGKSYSLESI RDSIKESIGF
     TPWVECNRDG SGNSQLYQVY LCVDRSGSGL IECPVFPHGK CGAEIEFPSF
 
 
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