RRM4_USTMA
ID RRM4_USTMA Reviewed; 792 AA.
AC A0A0D1DWZ5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=RNA-binding protein RRM4 {ECO:0000303|PubMed:17105762};
GN Name=RRM4 {ECO:0000303|PubMed:17105762}; ORFNames=UMAG_10836;
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, AND DISRUPTION PHENOTYPE.
RX PubMed=15643068; DOI=10.1128/ec.4.1.121-133.2005;
RA Becht P., Vollmeister E., Feldbruegge M.;
RT "Role for RNA-binding proteins implicated in pathogenic development of
RT Ustilago maydis.";
RL Eukaryot. Cell 4:121-133(2005).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, DOMAIN, SUBUNIT, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 116-THR--PHE-119; 365-PHE--PHE-368; PHE-740; ILE-743;
RP ALA-751 AND LYS-753.
RX PubMed=17105762; DOI=10.1242/jcs.03287;
RA Becht P., Koenig J., Feldbruegge M.;
RT "The RNA-binding protein Rrm4 is essential for polarity in Ustilago maydis
RT and shuttles along microtubules.";
RL J. Cell Sci. 119:4964-4973(2006).
RN [5]
RP FUNCTION, DOMAIN, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19494833; DOI=10.1038/emboj.2009.145;
RA Koenig J., Baumann S., Koepke J., Pohlmann T., Zarnack K., Feldbruegge M.;
RT "The fungal RNA-binding protein Rrm4 mediates long-distance transport of
RT ubi1 and rho3 mRNAs.";
RL EMBO J. 28:1855-1866(2009).
RN [6]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22357951; DOI=10.1242/jcs.101212;
RA Baumann S., Pohlmann T., Jungbluth M., Brachmann A., Feldbruegge M.;
RT "Kinesin-3 and dynein mediate microtubule-dependent co-transport of mRNPs
RT and endosomes.";
RL J. Cell Sci. 125:2740-2752(2012).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24355572; DOI=10.1002/embr.201338037;
RA Baumann S., Koenig J., Koepke J., Feldbruegge M.;
RT "Endosomal transport of septin mRNA and protein indicates local translation
RT on endosomes and is required for correct septin filamentation.";
RL EMBO Rep. 15:94-102(2014).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH UPA1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=25985087; DOI=10.7554/elife.06041;
RA Pohlmann T., Baumann S., Haag C., Albrecht M., Feldbruegge M.;
RT "A FYVE zinc finger domain protein specifically links mRNA transport to
RT endosome trafficking.";
RL Elife 4:0-0(2015).
RN [9]
RP FUNCTION, DOMAIN, AND 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).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=31338952; DOI=10.15252/embr.201847381;
RA Jankowski S., Pohlmann T., Baumann S., Muentjes K., Devan S.K., Zander S.,
RA Feldbruegge M.;
RT "The multi PAM2 protein Upa2 functions as novel core component of endosomal
RT mRNA transport.";
RL EMBO Rep. 20:e47381-e47381(2019).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=30738139; DOI=10.1016/j.fgb.2019.01.013;
RA Mueller J., Pohlmann T., Feldbruegge M.;
RT "Core components of endosomal mRNA transport are evolutionarily conserved
RT in fungi.";
RL Fungal Genet. Biol. 126:12-16(2019).
CC -!- FUNCTION: Key RNA-binding protein involved in the formation of polar-
CC growing hyphae which is essential for infection by the plant pathogen
CC (PubMed:15643068, PubMed:17105762, PubMed:19494833). During
CC filamentation, assembles into particles that shuttle bidirectionally
CC along microtubules to both poles (PubMed:17105762, PubMed:19494833,
CC PubMed:30738139). The RRM4 transport particles are part of the
CC endosomal mRNP transport that regulates polarity of the infectious
CC hyphae by transporting distinct mRNAs encoding, for example, the
CC ubiquitin fusion protein UBI1, the small G protein RHO3, or the septin
CC CDC3, from the nucleus to cell poles (PubMed:17105762, PubMed:19494833,
CC PubMed:22357951, PubMed:24355572, PubMed:25985087, PubMed:30738139).
CC Recognizes a broad spectrum of cargo mRNAs and precisely binds at stop
CC codons, which constitute landmark sites of translation, suggesting an
CC intimate connection of mRNA transport and translation
CC (PubMed:30552148). Binds also to the specific binding motif UAUG of
CC cargo mRNAs via its third RRM (PubMed:30552148). Plus-end-directed
CC KIN3, a kinesin-3 type motor, mediates anterograde transport of RRM4-
CC containing mRNPs whereas split dynein DYM1-DYN2 functions in retrograde
CC movement of mRNPs (PubMed:22357951). {ECO:0000269|PubMed:15643068,
CC ECO:0000269|PubMed:17105762, ECO:0000269|PubMed:19494833,
CC ECO:0000269|PubMed:22357951, ECO:0000269|PubMed:24355572,
CC ECO:0000269|PubMed:25985087, ECO:0000269|PubMed:30552148,
CC ECO:0000269|PubMed:30738139}.
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 (PubMed:17105762,
CC PubMed:19494833, PubMed:22357951, PubMed:31338952, PubMed:30738139).
CC Interacts (via PABC domain) with UPA1 (via PAM2 domain)
CC (PubMed:25985087). {ECO:0000269|PubMed:17105762,
CC ECO:0000269|PubMed:19494833, ECO:0000269|PubMed:22357951,
CC ECO:0000269|PubMed:25985087, ECO:0000269|PubMed:30738139,
CC ECO:0000269|PubMed:31338952}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17105762, ECO:0000269|PubMed:19494833,
CC ECO:0000269|PubMed:25985087}. Endosome {ECO:0000269|PubMed:22357951,
CC ECO:0000269|PubMed:24355572, ECO:0000269|PubMed:25985087}.
CC Note=Assembles into particles that shuttle along microtubules to both
CC poles (PubMed:17105762, PubMed:19494833). Shuttles with RAB5A-positive
CC endosomes along microtubules (PubMed:22357951, PubMed:25985087).
CC {ECO:0000269|PubMed:17105762, ECO:0000269|PubMed:19494833,
CC ECO:0000269|PubMed:22357951, ECO:0000269|PubMed:25985087}.
CC -!- DOMAIN: The RRM1, RRM3 and PABC domains are important for RNA_binding
CC and polar growth (PubMed:17105762, PubMed:19494833). RRM3 recognizes
CC the specific binding motif UAUG of cargo mRNAs (PubMed:30552148).
CC {ECO:0000269|PubMed:17105762, ECO:0000269|PubMed:19494833,
CC ECO:0000269|PubMed:30552148}.
CC -!- DISRUPTION PHENOTYPE: Reduces filamentous growth and virulence
CC (PubMed:15643068). Disturbs polar growth of filaments (PubMed:17105762,
CC PubMed:25985087). {ECO:0000269|PubMed:15643068,
CC ECO:0000269|PubMed:17105762, ECO:0000269|PubMed:25985087}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003147; KIS68744.1; -; Genomic_DNA.
DR RefSeq; XP_011389820.1; XM_011391518.1.
DR STRING; 5270.UM03311P0; -.
DR EnsemblFungi; KIS68744; KIS68744; UMAG_10836.
DR GeneID; 23566810; -.
DR KEGG; uma:UMAG_10836; -.
DR VEuPathDB; FungiDB:UMAG_10836; -.
DR eggNOG; KOG0123; Eukaryota.
DR OrthoDB; 795608at2759; -.
DR Proteomes; UP000000561; Chromosome 8.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0005686; C:U2 snRNP; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF63570; SSF63570; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Endosome; mRNA transport; Reference proteome;
KW Repeat; RNA-binding; Transport.
FT CHAIN 1..792
FT /note="RNA-binding protein RRM4"
FT /id="PRO_0000454342"
FT DOMAIN 72..145
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 154..235
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 321..398
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 715..792
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 37..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..438
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 116..119
FT /note="TVEF->AAAA: Leads to a reduction of RNA-binding."
FT /evidence="ECO:0000269|PubMed:17105762"
FT MUTAGEN 365..368
FT /note="FVSF->AAAA: Leads to a reduction of RNA-binding."
FT /evidence="ECO:0000269|PubMed:17105762"
FT MUTAGEN 740
FT /note="F->A: Leads to a reduction of RNA-binding; when
FT associated with A-743, G-751 and A-753."
FT /evidence="ECO:0000269|PubMed:17105762"
FT MUTAGEN 743
FT /note="I->A: Leads to a reduction of RNA-binding; when
FT associated with A-740, G-751 and A-753."
FT /evidence="ECO:0000269|PubMed:17105762"
FT MUTAGEN 751
FT /note="A->G: Leads to a reduction of RNA-binding; when
FT associated with A-740, A-743 and A-753."
FT /evidence="ECO:0000269|PubMed:17105762"
FT MUTAGEN 753
FT /note="K->A: Leads to a reduction of RNA-binding; when
FT associated with A-740, A-743 and G-753."
FT /evidence="ECO:0000269|PubMed:17105762"
SQ SEQUENCE 792 AA; 84663 MW; 4977FDC429CC8815 CRC64;
MSDSIYAPHN KHKLEAARAA DAAADDAATV SALVEPTDST AQASHAAEQT IDAHQQAGDV
EPERCHPHLT RPLLYLSGVD ATMTDKELAG LVFDQVLPVR LKIDRTVGEG QTASGTVEFQ
TLDKAEKAYA TVRPPIQLRI NQDASIREPH PSAKPRLVKQ LPPTSDDAFV YDLFRPFGPL
RRAQCLLTNP AGIHTGFKGM AVLEFYSEQD AQRAESEMHC SEVGGKSISV AIDTATRKVS
AAAAEFRPSA AAFVPAGSMS PSAPSFDPYP AGSRSVSTGS AASIYATSGA APTHDTRNGA
QKGARVPLQY SSQASTYVDP CNLFIKNLDP NMESNDLFDT FKRFGHIVSA RVMRDDNGKS
REFGFVSFTT PDEAQQALQA MDNAKLGTKK IIVRLHEPKT MRQEKLAARY NAANADNSDM
SSNSPPTEAR KADKRQSRSY FKAGVPSDAS GLVDEEQLRS LSTVVRNELL SGEFTRRIPK
VSSVTEAQLD DVVGELLSLK LADAVEALNN PISLIQRISD AREQLAQKSA STLTAPSPAP
LSAEHPAMLG IQAQRSVSSA SSTGEGGASV KERERLLKAV ISVTESGAPV EDITDMIASL
PKKDRALALF NPEFLKQKVD EAKDILDITD ESGEDLSPPR ASSGSAPVPL SVQTPASAIF
KDASNGQSSI SPGAAEAYTL STLAALPAAE IVRLANSQSS SGLPLPKADP ATVKATDDFI
DSLQGKAAHD QKQKLGDQLF KKIRTFGVKG APKLTIHLLD SEDLRALAHL MNSYEDVLKE
KVQHKVAAGL NK
