ID   RBP45_NICPL             Reviewed;         409 AA.
AC   Q9LEB4;
DT   22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Polyadenylate-binding protein RBP45;
DE            Short=Poly(A)-binding protein RBP45;
DE   AltName: Full=RNA-binding protein 45;
DE            Short=NplRBP45;
GN   Name=RBP45;
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).
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   -!- SUBUNIT: Interacts with the poly(A) tail of mRNA in nucleus.
CC       {ECO:0000269|PubMed:11105760}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11105760}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in leaves, roots, and
CC       stems. {ECO:0000269|PubMed:11105760}.
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding RBP45 family.
CC       {ECO:0000305}.
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DR   EMBL; AJ292767; CAC01237.1; -; mRNA.
DR   AlphaFoldDB; Q9LEB4; -.
DR   SMR; Q9LEB4; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008143; F:poly(A) binding; 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.
FT   CHAIN           1..409
FT                   /note="Polyadenylate-binding protein RBP45"
FT                   /id="PRO_0000415761"
FT   DOMAIN          84..164
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          176..255
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          282..354
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..82
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  45243 MW;  145EE701A89AF01D CRC64;
     MMPQSGVAQP PMAPMSMDQH QYQQQAPPPT QQQQWMMPPQ QPQQPQFQPQ SQPAWAQQPS
     QQQYGAMATT NPNPSPTGNP NEVRSLWIGD LQYWMDENYL STCFYHTGEL VSAKVIRNKQ
     TGQSEGYGFL EFRSHAAAET ILQTYNGTLM PNVEQNFRMN WASLGAGERR DDSAEHTIFV
     GDLAADVTDY ILQETFKSVY SSVRGAKVVT DRITGRSKGY GFVKFADESE QLRAMTEMNG
     VLCSTRPMRI GPAANKKPVG TPQKATYQNP QATQGESDPN NTTIFVGGLD PTVAEEHLRQ
     VFSPYGELVH VKIVAGKRCG FVQFGTRASA EQALSSLNGT QLGGQSIRLS WGRSPSSKQT
     DQTQWGGSGG AYYGYGQGYE AYGYAPPAQD PNMYYGNYPG YANYQQPQQ