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RBG4_ARATH
ID   RBG4_ARATH              Reviewed;         136 AA.
AC   Q9LIS2; A0A6B9JFL3; Q8LDS0;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Glycine-rich RNA-binding protein 4, mitochondrial {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE            Short=AtGR-RBP4 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746};
DE   AltName: Full=AtRBG4 {ECO:0000303|PubMed:20009520};
DE   AltName: Full=Glycine-rich protein 4 {ECO:0000303|PubMed:17169986};
DE            Short=AtGRP4 {ECO:0000303|PubMed:17169986};
DE   AltName: Full=Mitochondrial RNA-binding protein 1b {ECO:0000303|PubMed:11972043};
DE            Short=At-mRBP1b {ECO:0000303|PubMed:11972043};
DE   AltName: Full=Small RNA binding protein 4 {ECO:0000303|PubMed:31812689};
DE            Short=AtSRBP4 {ECO:0000303|PubMed:31812689};
DE   Flags: Precursor;
GN   Name=RBG4 {ECO:0000303|PubMed:20009520};
GN   Synonyms=GR-RBP4 {ECO:0000303|PubMed:11809873, ECO:0000303|PubMed:16207746,
GN   ECO:0000303|PubMed:20009520}, GRP4 {ECO:0000303|PubMed:17169986,
GN   ECO:0000303|PubMed:20009520}, MRBP1B {ECO:0000303|PubMed:11972043},
GN   SRBP4 {ECO:0000303|PubMed:31812689};
GN   OrderedLocusNames=At3g23830 {ECO:0000312|Araport:AT3G23830};
GN   ORFNames=F14O13.2 {ECO:0000312|EMBL:BAB03001.1};
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], FUNCTION, DOMAIN, SUBUNIT, AND GENE FAMILY.
RC   STRAIN=cv. Columbia;
RX   PubMed=31812689; DOI=10.1016/j.molp.2019.12.001;
RA   Yan Y., Ham B.-K., Chong Y.H., Yeh S.-D., Lucas W.J.;
RT   "A plant SMALL RNA-BINDING PROTEIN 1 family mediates cell-to-cell
RT   trafficking of RNAi signals.";
RL   Mol. Plant 13:321-335(2020).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(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.
RN   [6]
RP   GENE FAMILY.
RX   PubMed=11809873; DOI=10.1093/nar/30.3.623;
RA   Lorkovic Z.J., Barta A.;
RT   "Genome analysis: RNA recognition motif (RRM) and K homology (KH) domain
RT   RNA-binding proteins from the flowering plant Arabidopsis thaliana.";
RL   Nucleic Acids Res. 30:623-635(2002).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11972043; DOI=10.1073/pnas.092019599;
RA   Vermel M., Guermann B., Delage L., Grienenberger J.M., Marechal-Drouard L.,
RA   Gualberto J.M.;
RT   "A family of RRM-type RNA-binding proteins specific to plant
RT   mitochondria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:5866-5871(2002).
RN   [8]
RP   TISSUE SPECIFICITY, INDUCTION BY COLD; DEHYDRATION AND SALT, AND FUNCTION.
RX   PubMed=16207746; DOI=10.1093/jxb/eri298;
RA   Kwak K.J., Kim Y.O., Kang H.;
RT   "Characterization of transgenic Arabidopsis plants overexpressing GR-RBP4
RT   under high salinity, dehydration, or cold stress.";
RL   J. Exp. Bot. 56:3007-3016(2005).
RN   [9]
RP   INDUCTION BY COLD.
RX   PubMed=17169986; DOI=10.1093/nar/gkl1076;
RA   Kim J.S., Park S.J., Kwak K.J., Kim Y.O., Kim J.Y., Song J., Jang B.,
RA   Jung C.-H., Kang H.;
RT   "Cold shock domain proteins and glycine-rich RNA-binding proteins from
RT   Arabidopsis thaliana can promote the cold adaptation process in Escherichia
RT   coli.";
RL   Nucleic Acids Res. 35:506-516(2007).
RN   [10]
RP   NOMENCLATURE.
RX   PubMed=20009520; DOI=10.4161/psb.5.2.10336;
RA   Mangeon A., Junqueira R.M., Sachetto-Martins G.;
RT   "Functional diversity of the plant glycine-rich proteins superfamily.";
RL   Plant Signal. Behav. 5:99-104(2010).
CC   -!- FUNCTION: Possibly has a role in RNA transcription or processing during
CC       stress (PubMed:16207746). Binds sequence non-specifically to RNAs and
CC       DNAs (PubMed:16207746). Mediates cell-to-cell trafficking of RNA
CC       interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering
CC       RNA (siRNA) and microRNA (miRNA)) which regulate growth and
CC       development, as well as responses to environmental inputs, including
CC       pathogen attack; can compromise zucchini yellow mosaic virus (ZYMV) and
CC       tobacco rattle virus (TRV) infections at the early stage
CC       (PubMed:31812689). {ECO:0000269|PubMed:16207746,
CC       ECO:0000269|PubMed:31812689}.
CC   -!- SUBUNIT: Binds to small phloem-mobile single-stranded RNAs (ss-sRNA,
CC       e.g. small interfering RNA (siRNA) and microRNA (miRNA)) in the phloeme
CC       exudate, including viral-derived sRNA (vsiRNA).
CC       {ECO:0000269|PubMed:31812689}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11972043}.
CC       Secreted {ECO:0000269|PubMed:31812689}. Note=Observed in the phloem
CC       translocation stream. {ECO:0000269|PubMed:31812689}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in young plants, root tips,
CC       and flowers, but weakly in mature leaves and stems, implying highly
CC       expression in actively proliferating organs.
CC       {ECO:0000269|PubMed:16207746}.
CC   -!- INDUCTION: Up-regulated by cold stress and down-regulated by salt
CC       stress and dehydration stress. {ECO:0000269|PubMed:16207746,
CC       ECO:0000269|PubMed:17169986}.
CC   -!- DOMAIN: The glycine-rich (GR) domain is necessary and sufficient for
CC       cell-to-cell movement and to interefere with zucchini yellow mosaic
CC       virus (ZYMV) infection. {ECO:0000269|PubMed:31812689}.
CC   -!- MISCELLANEOUS: Plants overexpressing RBG4 display retarded germination
CC       under salt and dehydration stress.
CC   -!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
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DR   EMBL; MN064666; QGZ19401.1; -; mRNA.
DR   EMBL; AP001297; BAB03001.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76819.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76820.1; -; Genomic_DNA.
DR   EMBL; AY070755; AAL50093.1; -; mRNA.
DR   EMBL; AY097374; AAM19890.1; -; mRNA.
DR   EMBL; AY085838; AAM63053.1; -; mRNA.
DR   RefSeq; NP_189025.1; NM_113288.3.
DR   RefSeq; NP_850629.1; NM_180298.4.
DR   AlphaFoldDB; Q9LIS2; -.
DR   SMR; Q9LIS2; -.
DR   STRING; 3702.AT3G23830.2; -.
DR   SwissPalm; Q9LIS2; -.
DR   PaxDb; Q9LIS2; -.
DR   PRIDE; Q9LIS2; -.
DR   ProteomicsDB; 236520; -.
DR   EnsemblPlants; AT3G23830.1; AT3G23830.1; AT3G23830.
DR   EnsemblPlants; AT3G23830.2; AT3G23830.2; AT3G23830.
DR   GeneID; 821966; -.
DR   Gramene; AT3G23830.1; AT3G23830.1; AT3G23830.
DR   Gramene; AT3G23830.2; AT3G23830.2; AT3G23830.
DR   KEGG; ath:AT3G23830; -.
DR   Araport; AT3G23830; -.
DR   TAIR; locus:2076096; AT3G23830.
DR   eggNOG; KOG0118; Eukaryota.
DR   HOGENOM; CLU_012062_28_4_1; -.
DR   InParanoid; Q9LIS2; -.
DR   OMA; FANDKPR; -.
DR   OrthoDB; 1579773at2759; -.
DR   PhylomeDB; Q9LIS2; -.
DR   PRO; PR:Q9LIS2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LIS2; baseline and differential.
DR   Genevisible; Q9LIS2; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
DR   GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:TAIR.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR   GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR   GO; GO:0035197; F:siRNA binding; IDA:UniProtKB.
DR   GO; GO:0006858; P:extracellular transport; IDA:UniProtKB.
DR   GO; GO:1990428; P:miRNA transport; IDA:UniProtKB.
DR   GO; GO:1900864; P:mitochondrial RNA modification; IGI:TAIR.
DR   GO; GO:0050688; P:regulation of defense response to virus; IDA:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEP:UniProtKB.
DR   GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR   GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
DR   GO; GO:0050658; P:RNA transport; IDA: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   1: Evidence at protein level;
KW   Mitochondrion; Phosphoprotein; Reference proteome; RNA-binding; Secreted;
KW   Transit peptide.
FT   TRANSIT         1..33
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..136
FT                   /note="Glycine-rich RNA-binding protein 4, mitochondrial"
FT                   /id="PRO_0000421675"
FT   DOMAIN          35..113
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          113..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..135
FT                   /note="Glycine-rich (GR) required for cell-to-cell
FT                   movement"
FT                   /evidence="ECO:0000305|PubMed:31812689"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8RWN5"
FT   CONFLICT        17
FT                   /note="Q -> H (in Ref. 5; AAM63053)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   136 AA;  14129 MW;  1BE69CF10A48607D CRC64;
     MAFCNKLSGI LRQGVSQSSN GPVTSMLGSL RYMSSKLFVG GLSWGTDDSS LKQAFTSFGE
     VTEATVIADR ETGRSRGFGF VSFSCEDSAN NAIKEMDGKE LNGRQIRVNL ATERSSAPRS
     SFGGGGGYGG GGGGGY
 
 
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