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RBP11_ARATH
ID   RBP11_ARATH             Reviewed;         146 AA.
AC   Q9FFZ6;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=Small RNA-binding protein 11, chloroplastic {ECO:0000303|PubMed:24413693};
DE   Flags: Precursor;
GN   Name=S-RBP11 {ECO:0000303|PubMed:24413693};
GN   OrderedLocusNames=At5g06210 {ECO:0000312|Araport:AT5G06210};
GN   ORFNames=MBL20.9 {ECO:0000312|EMBL:BAB09686.1};
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RA   Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. XI.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [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., 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   [4]
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   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY METHYL
RP   VIOLOGEN, AND DISRUPTION PHENOTYPE.
RX   PubMed=24413693; DOI=10.1007/s00299-013-1560-9;
RA   Lee S.Y., Seok H.Y., Tarte V.N., Woo D.H., Le D.H., Lee E.H., Moon Y.H.;
RT   "The Arabidopsis chloroplast protein S-RBP11 is involved in oxidative and
RT   salt stress responses.";
RL   Plant Cell Rep. 33:837-847(2014).
CC   -!- FUNCTION: Probable RNA-binding protein that may be involved in salt and
CC       oxidative stress tolerance. {ECO:0000269|PubMed:24413693}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:24413693}.
CC   -!- TISSUE SPECIFICITY: Expressed in rosette leaves, cauline leaves, stems
CC       and flowers. {ECO:0000269|PubMed:24413693}.
CC   -!- INDUCTION: Induced by methyl viologen. {ECO:0000269|PubMed:24413693}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC       conditions, but mutant plants exhibit increased sensitivity to salt
CC       stress. {ECO:0000269|PubMed:24413693}.
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DR   EMBL; AP002544; BAB09686.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90984.1; -; Genomic_DNA.
DR   EMBL; AY062714; AAL32792.1; -; mRNA.
DR   EMBL; AY093349; AAM13348.1; -; mRNA.
DR   EMBL; AY087577; AAM65119.1; -; mRNA.
DR   RefSeq; NP_196239.1; NM_120703.3.
DR   AlphaFoldDB; Q9FFZ6; -.
DR   SMR; Q9FFZ6; -.
DR   STRING; 3702.AT5G06210.1; -.
DR   iPTMnet; Q9FFZ6; -.
DR   PaxDb; Q9FFZ6; -.
DR   PRIDE; Q9FFZ6; -.
DR   ProteomicsDB; 236529; -.
DR   EnsemblPlants; AT5G06210.1; AT5G06210.1; AT5G06210.
DR   GeneID; 830508; -.
DR   Gramene; AT5G06210.1; AT5G06210.1; AT5G06210.
DR   KEGG; ath:AT5G06210; -.
DR   Araport; AT5G06210; -.
DR   TAIR; locus:2160752; AT5G06210.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_012062_28_4_1; -.
DR   InParanoid; Q9FFZ6; -.
DR   OMA; NASGSCF; -.
DR   OrthoDB; 1579773at2759; -.
DR   PhylomeDB; Q9FFZ6; -.
DR   PRO; PR:Q9FFZ6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FFZ6; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:1901002; P:positive regulation of response to salt stress; IMP:UniProtKB.
DR   Gene3D; 3.30.70.330; -; 1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF54928; SSF54928; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Chloroplast; Phosphoprotein; Plastid; Reference proteome; RNA-binding;
KW   Stress response; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..146
FT                   /note="Small RNA-binding protein 11, chloroplastic"
FT                   /id="PRO_0000439871"
FT   DOMAIN          34..112
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8RWN5"
SQ   SEQUENCE   146 AA;  15422 MW;  A06C0BD661D9301B CRC64;
     MAALARIGGR HLKSVCLINS SASCFFTQRR GVASKLFIGG LSFCTTEQGL SEAFSKCGQV
     VEAQIVMDRV SDRSKGFGFV TFASADEAQK ALMEFNGQQL NGRTIFVDYA KAKQSLGGGG
     GYPIARGPPD PAVIAATRTT ETSKSD
 
 
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