ID   UBP1_NICPL              Reviewed;         406 AA.
AC   Q9M427;
DT   19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Oligouridylate-binding protein 1;
DE            Short=NpUBP1;
DE   AltName: Full=Polyuridylate-binding protein UBP1;
DE            Short=Poly(U)-binding protein UBP1;
GN   Name=UBP1;
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, AND SUBCELLULAR LOCATION.
RX   PubMed=10747031; DOI=10.1093/emboj/19.7.1638;
RA   Lambermon M.H., Simpson G.G., Wieczorek Kirk D.A., Hemmings-Mieszczak M.,
RA   Klahre U., Filipowicz W.;
RT   "UBP1, a novel hnRNP-like protein that functions at multiple steps of
RT   higher plant nuclear pre-mRNA maturation.";
RL   EMBO J. 19:1638-1649(2000).
CC   -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)-like protein
CC       that acts as a component of the pre-mRNA processing machinery.
CC       Functions to facilitate the nuclear maturation of plant pre-mRNAs.
CC       Binds with high affinity to RNA molecules that contain AU-rich regions.
CC       May bind to the 3'-UTR and protects the mRNA against exonucleolytic
CC       degradation. Associates with nuclear poly(A)+ RNA in nucleus in vivo.
CC       Does not stimulate transcription or the 3' end cleavage/polyadenylation
CC       reaction. {ECO:0000269|PubMed:10747031}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10747031}.
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DR   EMBL; AJ272011; CAB75429.1; -; mRNA.
DR   AlphaFoldDB; Q9M427; -.
DR   SMR; Q9M427; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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   InterPro; IPR003954; RRM_dom_euk.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   SMART; SM00361; RRM_1; 2.
DR   SUPFAM; SSF54928; SSF54928; 3.
DR   PROSITE; PS50102; RRM; 3.
PE   2: Evidence at transcript level;
KW   mRNA processing; Nucleus; Repeat; RNA-binding.
FT   CHAIN           1..406
FT                   /note="Oligouridylate-binding protein 1"
FT                   /id="PRO_0000425433"
FT   DOMAIN          49..123
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          134..212
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          255..329
FT                   /note="RRM 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          231..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   406 AA;  44088 MW;  7E73C4C766112600 CRC64;
     MMQQQRLKQQ QQQALMQQSL YHPGLLAPPQ IEPILSGNLP PGFDSSTCRS VYVGNIHPQV
     TEPLLQEVFA STGPLEGCKL IRKDKSSYGF VDYFDRRSAA LAIVTLNGRH LFGQPIKVNW
     AYASAQREDT SNHYNIFVGD LSPEVTDATL FACFSVYTSC SDARVMWDQK TGRSRGFGFV
     SFRNQQEAQS AINDLNGKWL GSRQIRCNWA AKGAGAVGEQ NSDAKSVVEL TSGTSDDGQE
     KVVNEDAPEN NPQYTTVYVG NLAPEVTSVD LHRHFHALGA GVIEDVRIQR DKGFGFVRYS
     SHAEAARAIQ LGNARLLFGK PVKCSWGSKP TPPGSSSNPL PPPAIGQIPG LSAMDLAAYQ
     RQLALAKMAG AQAFMQPQGQ RIGAPGQGIY DGGYGGIAST QPPMYF