RBG5_ARATH
ID RBG5_ARATH Reviewed; 289 AA.
AC Q9C909;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glycine-rich RNA-binding protein 5, mitochondrial {ECO:0000303|PubMed:11809873};
DE Short=AtGR-RBP5 {ECO:0000303|PubMed:11809873};
DE AltName: Full=AtRBG5 {ECO:0000303|PubMed:20009520};
DE AltName: Full=Mitochondrial RNA-binding protein 2b {ECO:0000303|PubMed:11972043};
DE Short=At-mRBP2b {ECO:0000303|PubMed:11972043};
DE AltName: Full=Organelle RRM domain-containing protein 4 {ECO:0000303|PubMed:26578708};
DE Flags: Precursor;
GN Name=RBG5 {ECO:0000303|PubMed:20009520};
GN Synonyms=GR-RBP5 {ECO:0000303|PubMed:11809873},
GN MRBP2B {ECO:0000303|PubMed:11972043}, ORRM4 {ECO:0000303|PubMed:26578708};
GN OrderedLocusNames=At1g74230 {ECO:0000312|Araport:AT1G74230};
GN ORFNames=F1O17.10 {ECO:0000312|EMBL:AAG52402.1};
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;
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 [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 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 [5]
RP SUBCELLULAR LOCATION, AND FUNCTION.
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 [6]
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).
RN [7]
RP FUNCTION, HOMODIMERIZATION, INTERACTION WITH MORF8/RIP1 AND RBG3/ORRM3,
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26578708; DOI=10.1104/pp.15.01280;
RA Shi X., Germain A., Hanson M.R., Bentolila S.;
RT "RNA recognition motif-containing protein ORRM4 broadly affects
RT mitochondrial RNA editing and impacts plant development and flowering.";
RL Plant Physiol. 170:294-309(2016).
RN [8]
RP INTERACTION WITH RBG2/ORRM5.
RC STRAIN=cv. Columbia;
RX PubMed=28549172; DOI=10.1093/jxb/erx139;
RA Shi X., Castandet B., Germain A., Hanson M.R., Bentolila S.;
RT "ORRM5, an RNA recognition motif-containing protein, has a unique effect on
RT mitochondrial RNA editing.";
RL J. Exp. Bot. 68:2833-2847(2017).
CC -!- FUNCTION: Possibly has a role in RNA transcription or processing during
CC stress (By similarity). Binds RNAs and DNAs sequence with a preference
CC to single-stranded nucleic acids. Displays strong affinity to poly(U)
CC sequence (PubMed:11972043). Involved in C-to-U editing of mitochondrial
CC RNA. Functions as major mitochondrial editing factor. Controls 44
CC percent of the mitochondrial editing sites (PubMed:26578708).
CC {ECO:0000250|UniProtKB:Q9LIS2, ECO:0000269|PubMed:11972043,
CC ECO:0000269|PubMed:26578708}.
CC -!- SUBUNIT: Homodimer (PubMed:26578708). Interacts with MORF8/RIP1 AND
CC RBG3/ORRM3 (PubMed:26578708). Binds to RBG2/ORRM5 (PubMed:28549172).
CC {ECO:0000269|PubMed:26578708, ECO:0000269|PubMed:28549172}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11972043,
CC ECO:0000269|PubMed:26578708}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth rate and delayed flowering.
CC {ECO:0000269|PubMed:26578708}.
CC -!- SIMILARITY: Belongs to the GR-RBP family. {ECO:0000305}.
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DR EMBL; AC020579; AAG52402.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35568.1; -; Genomic_DNA.
DR EMBL; BT002037; AAN72048.1; -; mRNA.
DR EMBL; BT006315; AAP13423.1; -; mRNA.
DR PIR; F96770; F96770.
DR RefSeq; NP_177563.1; NM_106083.5.
DR AlphaFoldDB; Q9C909; -.
DR SMR; Q9C909; -.
DR STRING; 3702.AT1G74230.1; -.
DR PaxDb; Q9C909; -.
DR PRIDE; Q9C909; -.
DR ProteomicsDB; 236508; -.
DR EnsemblPlants; AT1G74230.1; AT1G74230.1; AT1G74230.
DR GeneID; 843763; -.
DR Gramene; AT1G74230.1; AT1G74230.1; AT1G74230.
DR KEGG; ath:AT1G74230; -.
DR Araport; AT1G74230; -.
DR TAIR; locus:2019622; AT1G74230.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_012062_13_1_1; -.
DR InParanoid; Q9C909; -.
DR OMA; QTEVGPD; -.
DR OrthoDB; 1579773at2759; -.
DR PRO; PR:Q9C909; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C909; baseline and differential.
DR Genevisible; Q9C909; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:TAIR.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:TAIR.
DR GO; GO:0016554; P:cytidine to uridine editing; IMP:UniProtKB.
DR GO; GO:0080156; P:mitochondrial mRNA modification; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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; mRNA processing; Reference proteome; RNA-binding;
KW Transit peptide.
FT TRANSIT 1..31
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 32..289
FT /note="Glycine-rich RNA-binding protein 5, mitochondrial"
FT /id="PRO_0000421676"
FT DOMAIN 34..111
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 219..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 28728 MW; 5D14263809060747 CRC64;
MAFLSKVGRL FSQTSSHVTA SSSMLQSIRC MSSSKIFVGG ISYSTDEFGL REAFSKYGEV
VDAKIIVDRE TGRSRGFAFV TFTSTEEASN AMQLDGQDLH GRRIRVNYAT ERGSGFGGRG
FGGPGGGYGA SDGGYGAPAG GYGGGAGGYG GNSSYSGNAG GGGGYGGNSS YGGNAGGYGG
NPPYSGNAVG GGGGYGSNFG GGGGYGVAGG VGGSENFAQG SSTNAGFDDK FESNQPLGND
TDHQTESGLG GDEQFGGSDN QFGDAENGNT ENGPVGFDQT DDGDVAKRA
