ID   GRP1_USTMA              Reviewed;         175 AA.
AC   A0A0D1C8Z4; A0A0D1CTT4;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 28.
DE   RecName: Full=Glycine-rich RNA-binding protein 1 {ECO:0000303|PubMed:30552148};
GN   Name=GRP1 {ECO:0000303|PubMed:30552148}; ORFNames=UMAG_02412;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   MRNA-BINDING.
RX   PubMed=30552148; DOI=10.15252/embr.201846588;
RA   Olgeiser L., Haag C., Boerner S., Ule J., Busch A., Koepke J., Koenig J.,
RA   Feldbruegge M., Zarnack K.;
RT   "The key protein of endosomal mRNP transport Rrm4 binds translational
RT   landmark sites of cargo mRNAs.";
RL   EMBO Rep. 20:0-0(2019).
CC   -!- FUNCTION: Component of endosomal mRNA transport that regulates polarity
CC       of the infectious hyphae by transporting a broad spectrum of cargo
CC       mRNAs from the nucleus to cell poles. {ECO:0000269|PubMed:30552148}.
CC   -!- SUBUNIT: Part of large ribonucleoprotein complexes (mRNPs) containing
CC       RNA-binding proteins RRM4 and PAB1, endosome-binding protein UPA1, core
CC       scaffold protein UPA2 and associated factor GRP1.
CC       {ECO:0000269|PubMed:30552148}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:30552148}. Note=The
CC       endosomal localization of GRP1 depends on RRM4.
CC       {ECO:0000269|PubMed:30552148}.
CC   -!- DISRUPTION PHENOTYPE: In the yeast form, results in slower
CC       proliferation as well as increased cell size (PubMed:30552148). Does
CC       not cause an increased amount of bipolar cells and leads to
CC       significantly longer hyphae and empty sections at the basal pole
CC       (PubMed:30552148). {ECO:0000269|PubMed:30552148}.
CC   -!- SIMILARITY: Belongs to the glycine-rich RNA-binding protein family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=KIS69898.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM003144; KIS69898.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM003144; KIS69897.1; -; Genomic_DNA.
DR   RefSeq; XP_011388704.1; XM_011390402.1.
DR   RefSeq; XP_011388705.1; XM_011390403.1.
DR   STRING; 5270.UM02412P0; -.
DR   EnsemblFungi; KIS69897; KIS69897; UMAG_02412.
DR   EnsemblFungi; KIS69898; KIS69898; UMAG_02412.
DR   GeneID; 23563163; -.
DR   KEGG; uma:UMAG_02412; -.
DR   VEuPathDB; FungiDB:UMAG_02412; -.
DR   eggNOG; KOG0118; Eukaryota.
DR   OMA; GWEDRSY; -.
DR   OrthoDB; 1579773at2759; -.
DR   Proteomes; UP000000561; Chromosome 5.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
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   Endosome; mRNA transport; Reference proteome; RNA-binding; Transport.
FT   CHAIN           1..175
FT                   /note="Glycine-rich RNA-binding protein 1"
FT                   /id="PRO_0000454343"
FT   DOMAIN          3..81
FT                   /note="RRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          114..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   175 AA;  18115 MW;  73F24B76655FA661 CRC64;
     MAAKVYVGNL SWNTTDDSLA HAFSTYGQLT DYIVMKDRET GRSRGFGFVT FATQAEADAA
     IAALNEQELD GRRIRVNMAN SRPAGGMGGG YGGVTGQYGA NAYGAQGGYG GYGGQPGGFQ
     QPGGFQQQGG YPQQGGYGGY QQPGFQPQQG GYGAPQQGYG APQQGGYGGY NGQSQ