A0A0D1DWZ5 · RRM4_USTMA
- ProteinRNA-binding protein RRM4
- GeneRRM4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids792 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic stress granule | |
Cellular Component | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | endosome | |
Cellular Component | nucleus | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | poly(A) binding | |
Molecular Function | poly(U) RNA binding | |
Biological Process | mRNA transport |
Keywords
- Molecular function
- Biological process
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 nameRNA-binding protein RRM4
Gene names
- Community suggested namesRrm4; rrm4; UMAG_10836.
- Community suggested namesRrm4; rrm4; UMAG_10836.
- Community suggested namesRrm4; rrm4; UMAG_10836.
- Community suggested namesRrm4; rrm4; UMAG_10836.
- Community suggested namesRrm4; rrm4; UMAG_10836.
- Community suggested namesRrm4
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Ustilaginomycotina > Ustilaginomycetes > Ustilaginales > Ustilaginaceae > Ustilago
Accessions
- Primary accessionA0A0D1DWZ5
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Reduces filamentous growth and virulence (PubMed:15643068).
Disturbs polar growth of filaments (PubMed:17105762, PubMed:25985087).
Disturbs polar growth of filaments (PubMed:17105762, PubMed:25985087).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 116-119 | Leads to a reduction of RNA-binding. | ||||
Sequence: TVEF → AAAA | ||||||
Mutagenesis | 365-368 | Leads to a reduction of RNA-binding. | ||||
Sequence: FVSF → AAAA | ||||||
Mutagenesis | 740 | Leads to a reduction of RNA-binding; when associated with A-743, G-751 and A-753. | ||||
Sequence: F → A | ||||||
Mutagenesis | 743 | Leads to a reduction of RNA-binding; when associated with A-740, G-751 and A-753. | ||||
Sequence: I → A | ||||||
Mutagenesis | 751 | Leads to a reduction of RNA-binding; when associated with A-740, A-743 and A-753. | ||||
Sequence: A → G | ||||||
Mutagenesis | 753 | Leads to a reduction of RNA-binding; when associated with A-740, A-743 and G-753. | ||||
Sequence: K → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000454342 | 1-792 | RNA-binding protein RRM4 | |||
Sequence: MSDSIYAPHNKHKLEAARAADAAADDAATVSALVEPTDSTAQASHAAEQTIDAHQQAGDVEPERCHPHLTRPLLYLSGVDATMTDKELAGLVFDQVLPVRLKIDRTVGEGQTASGTVEFQTLDKAEKAYATVRPPIQLRINQDASIREPHPSAKPRLVKQLPPTSDDAFVYDLFRPFGPLRRAQCLLTNPAGIHTGFKGMAVLEFYSEQDAQRAESEMHCSEVGGKSISVAIDTATRKVSAAAAEFRPSAAAFVPAGSMSPSAPSFDPYPAGSRSVSTGSAASIYATSGAAPTHDTRNGAQKGARVPLQYSSQASTYVDPCNLFIKNLDPNMESNDLFDTFKRFGHIVSARVMRDDNGKSREFGFVSFTTPDEAQQALQAMDNAKLGTKKIIVRLHEPKTMRQEKLAARYNAANADNSDMSSNSPPTEARKADKRQSRSYFKAGVPSDASGLVDEEQLRSLSTVVRNELLSGEFTRRIPKVSSVTEAQLDDVVGELLSLKLADAVEALNNPISLIQRISDAREQLAQKSASTLTAPSPAPLSAEHPAMLGIQAQRSVSSASSTGEGGASVKERERLLKAVISVTESGAPVEDITDMIASLPKKDRALALFNPEFLKQKVDEAKDILDITDESGEDLSPPRASSGSAPVPLSVQTPASAIFKDASNGQSSISPGAAEAYTLSTLAALPAAEIVRLANSQSSSGLPLPKADPATVKATDDFIDSLQGKAAHDQKQKLGDQLFKKIRTFGVKGAPKLTIHLLDSEDLRALAHLMNSYEDVLKEKVQHKVAAGLNK |
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).
Interacts (via PABC domain) with UPA1 (via PAM2 domain) (PubMed:25985087).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 37-51 | Polar residues | ||||
Sequence: TDSTAQASHAAEQTI | ||||||
Region | 37-60 | Disordered | ||||
Sequence: TDSTAQASHAAEQTIDAHQQAGDV | ||||||
Domain | 72-145 | RRM 1 | ||||
Sequence: PLLYLSGVDATMTDKELAGLVFDQVLPVRLKIDRTVGEGQTASGTVEFQTLDKAEKAYATVRPPIQLRINQDAS | ||||||
Domain | 154-235 | RRM 2 | ||||
Sequence: KPRLVKQLPPTSDDAFVYDLFRPFGPLRRAQCLLTNPAGIHTGFKGMAVLEFYSEQDAQRAESEMHCSEVGGKSISVAIDTA | ||||||
Domain | 321-398 | RRM 3 | ||||
Sequence: CNLFIKNLDPNMESNDLFDTFKRFGHIVSARVMRDDNGKSREFGFVSFTTPDEAQQALQAMDNAKLGTKKIIVRLHEP | ||||||
Region | 412-438 | Disordered | ||||
Sequence: AANADNSDMSSNSPPTEARKADKRQSR | ||||||
Region | 630-649 | Disordered | ||||
Sequence: DESGEDLSPPRASSGSAPVP | ||||||
Domain | 715-792 | PABC | ||||
Sequence: ATDDFIDSLQGKAAHDQKQKLGDQLFKKIRTFGVKGAPKLTIHLLDSEDLRALAHLMNSYEDVLKEKVQHKVAAGLNK |
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).
RRM3 recognizes the specific binding motif UAUG of cargo mRNAs (PubMed:30552148).
Sequence similarities
Belongs to the polyadenylate-binding protein type-1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length792
- Mass (Da)84,663
- Last updated2015-04-29 v1
- Checksum4977FDC429CC8815
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 37-51 | Polar residues | ||||
Sequence: TDSTAQASHAAEQTI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CM003147 EMBL· GenBank· DDBJ | KIS68744.1 EMBL· GenBank· DDBJ | Genomic DNA |