RB47B_ARATH
ID RB47B_ARATH Reviewed; 435 AA.
AC Q0WW84; Q8LFI9; Q9LJL7;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Polyadenylate-binding protein RBP47B;
DE Short=Poly(A)-binding protein RBP47B;
DE AltName: Full=RNA-binding protein 47B;
DE Short=AtRBP47B;
GN Name=RBP47B; OrderedLocusNames=At3g19130; ORFNames=MVI11.3;
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=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 [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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF Clones.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 TISSUE SPECIFICITY, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11105760; DOI=10.1017/s1355838200001163;
RA Lorkovic Z.J., Wieczorek Kirk D.A., Klahre U., Hemmings-Mieszczak M.,
RA Filipowicz W.;
RT "RBP45 and RBP47, two oligouridylate-specific hnRNP-like proteins
RT interacting with poly(A)+ RNA in nuclei of plant cells.";
RL RNA 6:1610-1624(2000).
RN [7]
RP INDUCTION BY OZONE, AND GENE FAMILY.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=21120628; DOI=10.1007/s10059-011-0001-2;
RA Peal L., Jambunathan N., Mahalingam R.;
RT "Phylogenetic and expression analysis of RNA-binding proteins with triple
RT RNA recognition motifs in plants.";
RL Mol. Cells 31:55-64(2011).
CC -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein
CC binding the poly(A) tail of mRNA and probably involved in some steps of
CC pre-mRNA maturation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the poly(A) tail of mRNA in nucleus.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q0WW84; Q9SHZ6: UBA1A; NbExp=3; IntAct=EBI-25522105, EBI-346271;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasmic granule
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in leaves, stems, flowers,
CC and seedlings. {ECO:0000269|PubMed:11105760}.
CC -!- INDUCTION: Repressed by ozone-induced oxidative stress.
CC {ECO:0000269|PubMed:21120628}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding RBP47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM67293.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB02953.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP000419; BAB02953.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76196.1; -; Genomic_DNA.
DR EMBL; AK226472; BAE98614.1; -; mRNA.
DR EMBL; BT026489; ABH04596.1; -; mRNA.
DR EMBL; AY084821; AAM67293.1; ALT_INIT; mRNA.
DR RefSeq; NP_188544.1; NM_112800.4.
DR AlphaFoldDB; Q0WW84; -.
DR SMR; Q0WW84; -.
DR BioGRID; 6780; 1.
DR IntAct; Q0WW84; 1.
DR STRING; 3702.AT3G19130.1; -.
DR iPTMnet; Q0WW84; -.
DR PaxDb; Q0WW84; -.
DR PRIDE; Q0WW84; -.
DR ProteomicsDB; 236988; -.
DR EnsemblPlants; AT3G19130.1; AT3G19130.1; AT3G19130.
DR GeneID; 821447; -.
DR Gramene; AT3G19130.1; AT3G19130.1; AT3G19130.
DR KEGG; ath:AT3G19130; -.
DR Araport; AT3G19130; -.
DR TAIR; locus:2094098; AT3G19130.
DR eggNOG; KOG0118; Eukaryota.
DR HOGENOM; CLU_016304_2_1_1; -.
DR InParanoid; Q0WW84; -.
DR OMA; INTSHYR; -.
DR OrthoDB; 775799at2759; -.
DR PhylomeDB; Q0WW84; -.
DR PRO; PR:Q0WW84; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q0WW84; baseline and differential.
DR Genevisible; Q0WW84; AT.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0008143; F:poly(A) binding; ISS:UniProtKB.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0034063; P:stress granule assembly; IEP:TAIR.
DR Gene3D; 3.30.70.330; -; 3.
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; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 3.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..435
FT /note="Polyadenylate-binding protein RBP47B"
FT /id="PRO_0000415767"
FT DOMAIN 108..188
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 202..281
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 321..393
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 31..32
FT /note="Missing (in Ref. 5; AAM67293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 435 AA; 48119 MW; 327DA6727EA7767E CRC64;
MQTTNGSDST LATSGATPPN QQTPPPPQQW QQQQQQQQQW MAAMQYPPAA AMMMMQQQQM
LMYPHQYVPY NQGPYQQHHP QLHQYGSYQQ HQHQQHKAID RGSGDDVKTL WVGDLLHWMD
ETYLHSCFSH TGEVSSVKVI RNKLTSQSEG YGFVEFLSRA AAEEVLQNYS GSVMPNSDQP
FRINWASFST GEKRAVENGP DLSVFVGDLS PDVTDVLLHE TFSDRYPSVK SAKVVIDSNT
GRSKGYGFVR FGDENERSRA LTEMNGAYCS NRQMRVGIAT PKRAIANQQQ HSSQAVILAG
GHGSNGSMGY GSQSDGESTN ATIFVGGIDP DVIDEDLRQP FSQFGEVVSV KIPVGKGCGF
VQFADRKSAE DAIESLNGTV IGKNTVRLSW GRSPNKQWRG DSGQQWNGGY SRGHGYNNGG
GYANHHDSNN YHGEN
