ID   RBP47_NICPL             Reviewed;         428 AA.
AC   Q9LEB3;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Polyadenylate-binding protein RBP47;
DE            Short=Poly(A)-binding protein RBP47;
DE   AltName: Full=RNA-binding protein 47;
DE            Short=NplRBP47;
GN   Name=RBP47;
OS   Nicotiana plumbaginifolia (Leadwort-leaved tobacco) (Tex-Mex tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBUNIT,
RP   SUBCELLULAR LOCATION, 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   [2]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18643965; DOI=10.1111/j.1365-313x.2008.03623.x;
RA   Weber C., Nover L., Fauth M.;
RT   "Plant stress granules and mRNA processing bodies are distinct from heat
RT   stress granules.";
RL   Plant J. 56:517-530(2008).
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:0000269|PubMed:11105760,
CC       ECO:0000269|PubMed:18643965}.
CC   -!- SUBUNIT: Interacts with the poly(A) tail of mRNA in nucleus.
CC       {ECO:0000269|PubMed:11105760}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasmic granule. Note=Relocalizes
CC       from nucleus to cytoplasmic stress granules (SGs) under heat stress.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in leaves, roots, and
CC       stems. {ECO:0000269|PubMed:11105760}.
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding RBP47 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ292768; CAC01238.1; -; mRNA.
DR   AlphaFoldDB; Q9LEB3; -.
DR   SMR; Q9LEB3; -.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; IDA:UniProtKB.
DR   GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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; Repeat; RNA-binding; Stress response.
FT   CHAIN           1..428
FT                   /note="Polyadenylate-binding protein RBP47"
FT                   /id="PRO_0000415765"
FT   DOMAIN          84..164
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          177..256
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          295..367
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
SQ   SEQUENCE   428 AA;  47374 MW;  E5579F481C40523D CRC64;
     MNGGDMNQQQ QQQQQQHQQQ QQQWLAMQQY QQQWMAMQYP AAAMAMQQQM MYGQQYMPYY
     QQHQQQQKMQ QSPTQIQSSS EDNKTIWIGD LQQWMDESYL HSCFSQAGEV ISVKIIRNKQ
     TGQSERYGFV EFNTHAAAEK VLQSYNGTMM PNTEQPFRLN WAGFSTGEKR AETGSDFSIF
     VGDLASDVTD TMLRDTFASR YPSLKGAKVV VDANTGHSKG YGFVRFGDES ERSRAMTEMN
     GVYCSSRAMR IGVATPKKPS AHEQYSSQAV ILSGGYASNG AATHGSQSDG DSSNTTIFVG
     GLDSEVTDEE LRQSFNQFGE VVSVKIPAGK GCGFVQFSDR SSAQEAIQKL SGAIIGKQAV
     RLSWGRSPAN KQMRTDSGSQ WNGGYNGRQN YGGYGYGASQ NQDSGMYATG AAYGASSNRY
     GNHQQPVS