ID   GRP_HORVU               Reviewed;         161 AA.
AC   Q43472;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Glycine-rich RNA-binding protein blt801 {ECO:0000250|UniProtKB:Q03250, ECO:0000303|PubMed:8639753};
DE   AltName: Full=Low temperature-responsive RNA-binding protein {ECO:0000312|EMBL:AAB07749.1};
GN   Name=blt801 {ECO:0000303|PubMed:8639753, ECO:0000312|EMBL:AAB07749.1};
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAB07749.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, AND PHOSPHORYLATION AT
RP   SER-87.
RC   STRAIN=cv. Igri {ECO:0000269|PubMed:8639753};
RC   TISSUE=Leaf meristem {ECO:0000312|EMBL:AAB07749.1};
RX   PubMed=8639753; DOI=10.1007/bf00020806;
RA   Dunn M.A., Brown K., Lightowlers R., Hughes M.A.;
RT   "A low-temperature-responsive gene from barley encodes a protein with
RT   single-stranded nucleic acid-binding activity which is phosphorylated in
RT   vitro.";
RL   Plant Mol. Biol. 30:947-959(1996).
CC   -!- FUNCTION: Binds single-stranded DNA and homoribopolymers of guanine,
CC       uracil and adenine, but not cytosine. Also binds RNA, with a preference
CC       for RNA containing a high proportion of adenine within an open loop
CC       structure. Possibly has a role in RNA transcription or processing
CC       during stress. {ECO:0000250|UniProtKB:Q03250,
CC       ECO:0000269|PubMed:8639753}.
CC   -!- INDUCTION: Induced by low temperature stress or foliar application of
CC       the phytohormone abscisic acid (ABA). {ECO:0000269|PubMed:8639753}.
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DR   EMBL; U49482; AAB07749.1; -; mRNA.
DR   PIR; S71453; S71453.
DR   AlphaFoldDB; Q43472; -.
DR   SMR; Q43472; -.
DR   iPTMnet; Q43472; -.
DR   PRIDE; Q43472; -.
DR   ExpressionAtlas; Q43472; baseline and differential.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0009737; P:response to abscisic acid; IDA:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IDA:UniProtKB.
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   DNA-binding; mRNA processing; Phosphoprotein; RNA-binding; Stress response;
KW   Transcription.
FT   CHAIN           1..161
FT                   /note="Glycine-rich RNA-binding protein blt801"
FT                   /id="PRO_0000390499"
FT   DOMAIN          6..84
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          72..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         87
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000269|PubMed:8639753"
SQ   SEQUENCE   161 AA;  15926 MW;  4D8A803EC5D0E9E6 CRC64;
     MADVEYRCFV GGLRWATDDQ SLQNAFSKYG DVIDSKIITD RETGRSRGFG FVTFASDEAM
     RQAIEAMNGQ DLDGRNITVN EAQSRRSDGG GGFGGGGGGY GGQRREGGGG GYGGGGGGYG
     GGRSGGGGGY GSRDGGGGGY GGGGGGYGGS RGGSGGGNWR E