A0A0D1DWZ5 · RRM4_USTMA

Function

function

Key RNA-binding protein involved in the formation of polar-growing hyphae which is essential for infection by the plant pathogen (PubMed:15643068, PubMed:17105762, PubMed:19494833).
During filamentation, assembles into particles that shuttle bidirectionally along microtubules to both poles (PubMed:17105762, PubMed:19494833, PubMed:30738139).
The RRM4 transport particles are part of the endosomal mRNP transport that regulates polarity of the infectious hyphae by transporting distinct mRNAs encoding, for example, the ubiquitin fusion protein UBI1, the small G protein RHO3, or the septin CDC3, from the nucleus to cell poles (PubMed:17105762, PubMed:19494833, PubMed:22357951, PubMed:24355572, PubMed:25985087, PubMed:30738139).
Recognizes a broad spectrum of cargo mRNAs and precisely binds at stop codons, which constitute landmark sites of translation, suggesting an intimate connection of mRNA transport and translation (PubMed:30552148).
Binds also to the specific binding motif UAUG of cargo mRNAs via its third RRM (PubMed:30552148).
Plus-end-directed KIN3, a kinesin-3 type motor, mediates anterograde transport of RRM4-containing mRNPs whereas split dynein DYM1-DYN2 functions in retrograde movement of mRNPs (PubMed:22357951).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasmic stress granule
Cellular Componentcytoskeleton
Cellular Componentcytosol
Cellular Componentendosome
Cellular Componentnucleus
Cellular Componentribonucleoprotein complex
Molecular FunctionmRNA 3'-UTR binding
Molecular Functionpoly(A) binding
Molecular Functionpoly(U) RNA binding
Biological ProcessmRNA transport

Keywords

Community curation (6)

Key RNA binding protein for endosome meditated mRNA transport.

Key RNA binding protein for microtubule-dependent mRNA transport.

Key RNA binding protein for endosome meditated mRNA transport.

Key RNA binding protein for endosome meditated mRNA transport.

Key RNA binding protein for endosome meditated mRNA transport.

It is a key mRNA transporting protein, mediating the mRNA transport to the growing tip of the cell.

Names & Taxonomy

Protein names

  • Recommended name
    RNA-binding protein RRM4

Gene names

    • Name
      RRM4
    • ORF names
      UMAG_10836
Community curation (6)

Organism names

Accessions

  • Primary accession
    A0A0D1DWZ5

Proteomes

Organism-specific databases

Subcellular Location

Endosome
Note: Assembles into particles that shuttle along microtubules to both poles (PubMed:17105762, PubMed:19494833).
Shuttles with RAB5A-positive endosomes along microtubules (PubMed:22357951, PubMed:25985087).

Keywords

Phenotypes & Variants

Disruption phenotype

Reduces filamentous growth and virulence (PubMed:15643068).
Disturbs polar growth of filaments (PubMed:17105762, PubMed:25985087).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis116-119Leads to a reduction of RNA-binding.
Mutagenesis365-368Leads to a reduction of RNA-binding.
Mutagenesis740Leads to a reduction of RNA-binding; when associated with A-743, G-751 and A-753.
Mutagenesis743Leads to a reduction of RNA-binding; when associated with A-740, G-751 and A-753.
Mutagenesis751Leads to a reduction of RNA-binding; when associated with A-740, A-743 and A-753.
Mutagenesis753Leads to a reduction of RNA-binding; when associated with A-740, A-743 and G-753.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004543421-792RNA-binding protein RRM4

Interaction

Subunit

Part of large ribonucleoprotein complexes (mRNPs) containing RNA-binding proteins RRM4 and PAB1, endosome-binding protein UPA1, core scaffold protein UPA2 and associated factor GRP1 (PubMed:17105762, PubMed:19494833, PubMed:22357951, PubMed:30738139, PubMed:31338952).
Interacts (via PABC domain) with UPA1 (via PAM2 domain) (PubMed:25985087).

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias37-51Polar residues
Region37-60Disordered
Domain72-145RRM 1
Domain154-235RRM 2
Domain321-398RRM 3
Region412-438Disordered
Region630-649Disordered
Domain715-792PABC

Domain

The RRM1, RRM3 and PABC domains are important for RNA_binding and polar growth (PubMed:17105762, PubMed:19494833).
RRM3 recognizes the specific binding motif UAUG of cargo mRNAs (PubMed:30552148).

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    792
  • Mass (Da)
    84,663
  • Last updated
    2015-04-29 v1
  • Checksum
    4977FDC429CC8815
MSDSIYAPHNKHKLEAARAADAAADDAATVSALVEPTDSTAQASHAAEQTIDAHQQAGDVEPERCHPHLTRPLLYLSGVDATMTDKELAGLVFDQVLPVRLKIDRTVGEGQTASGTVEFQTLDKAEKAYATVRPPIQLRINQDASIREPHPSAKPRLVKQLPPTSDDAFVYDLFRPFGPLRRAQCLLTNPAGIHTGFKGMAVLEFYSEQDAQRAESEMHCSEVGGKSISVAIDTATRKVSAAAAEFRPSAAAFVPAGSMSPSAPSFDPYPAGSRSVSTGSAASIYATSGAAPTHDTRNGAQKGARVPLQYSSQASTYVDPCNLFIKNLDPNMESNDLFDTFKRFGHIVSARVMRDDNGKSREFGFVSFTTPDEAQQALQAMDNAKLGTKKIIVRLHEPKTMRQEKLAARYNAANADNSDMSSNSPPTEARKADKRQSRSYFKAGVPSDASGLVDEEQLRSLSTVVRNELLSGEFTRRIPKVSSVTEAQLDDVVGELLSLKLADAVEALNNPISLIQRISDAREQLAQKSASTLTAPSPAPLSAEHPAMLGIQAQRSVSSASSTGEGGASVKERERLLKAVISVTESGAPVEDITDMIASLPKKDRALALFNPEFLKQKVDEAKDILDITDESGEDLSPPRASSGSAPVPLSVQTPASAIFKDASNGQSSISPGAAEAYTLSTLAALPAAEIVRLANSQSSSGLPLPKADPATVKATDDFIDSLQGKAAHDQKQKLGDQLFKKIRTFGVKGAPKLTIHLLDSEDLRALAHLMNSYEDVLKEKVQHKVAAGLNK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias37-51Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CM003147
EMBL· GenBank· DDBJ
KIS68744.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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