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Glycine-rich RNA-binding protein 4, mitochondrial (AtGR-RBP4) (AtRBG4) (Glycine-rich protein 4) (AtGRP4) (Mitochondrial RNA-binding protein 1b) (At-mRBP1b)

 RBG4_ARATH              Reviewed;         136 AA.
Q9LIS2; Q8LDS0;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 118.
RecName: Full=Glycine-rich RNA-binding protein 4, mitochondrial;
Short=AtGR-RBP4;
AltName: Full=AtRBG4;
AltName: Full=Glycine-rich protein 4;
Short=AtGRP4;
AltName: Full=Mitochondrial RNA-binding protein 1b;
Short=At-mRBP1b;
Flags: Precursor;
Name=RBG4; Synonyms=GR-RBP4, GRP4, MRBP1B;
OrderedLocusNames=At3g23830; ORFNames=F14O13_2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[5]
GENE FAMILY.
PubMed=11809873; DOI=10.1093/nar/30.3.623;
Lorkovic Z.J., Barta A.;
"Genome analysis: RNA recognition motif (RRM) and K homology (KH)
domain RNA-binding proteins from the flowering plant Arabidopsis
thaliana.";
Nucleic Acids Res. 30:623-635(2002).
[6]
SUBCELLULAR LOCATION.
PubMed=11972043; DOI=10.1073/pnas.092019599;
Vermel M., Guermann B., Delage L., Grienenberger J.M.,
Marechal-Drouard L., Gualberto J.M.;
"A family of RRM-type RNA-binding proteins specific to plant
mitochondria.";
Proc. Natl. Acad. Sci. U.S.A. 99:5866-5871(2002).
[7]
TISSUE SPECIFICITY, INDUCTION BY COLD; DEHYDRATION AND SALT, AND
FUNCTION.
PubMed=16207746; DOI=10.1093/jxb/eri298;
Kwak K.J., Kim Y.O., Kang H.;
"Characterization of transgenic Arabidopsis plants overexpressing GR-
RBP4 under high salinity, dehydration, or cold stress.";
J. Exp. Bot. 56:3007-3016(2005).
[8]
INDUCTION BY COLD.
PubMed=17169986; DOI=10.1093/nar/gkl1076;
Kim J.S., Park S.J., Kwak K.J., Kim Y.O., Kim J.Y., Song J., Jang B.,
Jung C.-H., Kang H.;
"Cold shock domain proteins and glycine-rich RNA-binding proteins from
Arabidopsis thaliana can promote the cold adaptation process in
Escherichia coli.";
Nucleic Acids Res. 35:506-516(2007).
[9]
NOMENCLATURE.
PubMed=20009520; DOI=10.4161/psb.5.2.10336;
Mangeon A., Junqueira R.M., Sachetto-Martins G.;
"Functional diversity of the plant glycine-rich proteins
superfamily.";
Plant Signal. Behav. 5:99-104(2010).
-!- FUNCTION: Possibly has a role in RNA transcription or processing
during stress. Binds sequence non-specifically to RNAs and DNAs.
{ECO:0000269|PubMed:16207746}.
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11972043}.
-!- TISSUE SPECIFICITY: Abundantly expressed in young plants, root
tips, and flowers, but weakly in mature leaves and stems, implying
highly expression in actively proliferating organs.
{ECO:0000269|PubMed:16207746}.
-!- INDUCTION: Up-regulated by cold stress and down-regulated by salt
stress and dehydration stress. {ECO:0000269|PubMed:16207746,
ECO:0000269|PubMed:17169986}.
-!- MISCELLANEOUS: Plants overexpressing RBG4 display retarded
germination under salt and dehydration stress.
-!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
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EMBL; AP001297; BAB03001.1; -; Genomic_DNA.
EMBL; CP002686; AEE76819.1; -; Genomic_DNA.
EMBL; CP002686; AEE76820.1; -; Genomic_DNA.
EMBL; AY070755; AAL50093.1; -; mRNA.
EMBL; AY097374; AAM19890.1; -; mRNA.
EMBL; AY085838; AAM63053.1; -; mRNA.
RefSeq; NP_189025.1; NM_113288.3.
RefSeq; NP_850629.1; NM_180298.4.
UniGene; At.8272; -.
ProteinModelPortal; Q9LIS2; -.
SMR; Q9LIS2; -.
STRING; 3702.AT3G23830.1; -.
SwissPalm; Q9LIS2; -.
PaxDb; Q9LIS2; -.
EnsemblPlants; AT3G23830.1; AT3G23830.1; AT3G23830.
EnsemblPlants; AT3G23830.2; AT3G23830.2; AT3G23830.
GeneID; 821966; -.
Gramene; AT3G23830.1; AT3G23830.1; AT3G23830.
Gramene; AT3G23830.2; AT3G23830.2; AT3G23830.
KEGG; ath:AT3G23830; -.
Araport; AT3G23830; -.
TAIR; locus:2076096; AT3G23830.
eggNOG; KOG0118; Eukaryota.
eggNOG; COG0724; LUCA.
HOGENOM; HOG000276232; -.
InParanoid; Q9LIS2; -.
OMA; CEDSANN; -.
OrthoDB; EOG09360WQH; -.
PhylomeDB; Q9LIS2; -.
PRO; PR:Q9LIS2; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LIS2; baseline and differential.
Genevisible; Q9LIS2; AT.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:TAIR.
GO; GO:0003723; F:RNA binding; IDA:TAIR.
GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
GO; GO:1900864; P:mitochondrial RNA modification; IGI:TAIR.
GO; GO:0009409; P:response to cold; IEP:UniProtKB.
GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
GO; GO:0009651; P:response to salt stress; IMP:TAIR.
GO; GO:0009414; P:response to water deprivation; IEP:UniProtKB.
Gene3D; 3.30.70.330; -; 1.
InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 1.
SMART; SM00360; RRM; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
2: Evidence at transcript level;
Complete proteome; Mitochondrion; Phosphoprotein; Reference proteome;
RNA-binding; Transit peptide.
TRANSIT 1 33 Mitochondrion. {ECO:0000255}.
CHAIN 34 136 Glycine-rich RNA-binding protein 4,
mitochondrial.
/FTId=PRO_0000421675.
DOMAIN 35 113 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 123 135 Gly-rich.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:Q8RWN5}.
CONFLICT 17 17 Q -> H (in Ref. 4; AAM63053).
{ECO:0000305}.
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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