Q9FQ03 · XRN3_ARATH

Function

function

Possesses 5'->3' exoribonuclease activity (PubMed:11106401).
Acts as an endogenous post-transcriptional gene silencing (PTGS) suppressor. Degrades miRNA-derived loops, excised during miRNA maturation in the nucleus. Required for proper development (PubMed:17993620).
Involved in pre-rRNA processing. Involved with XRN2 in the 5'-end exonucleolytic processing of 5.8S and 25S rRNAs. Contributes with XRN2 to polyadenylation-dependent nuclear RNA surveillance. Involved in the degradation of aberrant polyadenylated pre-rRNA through 5'-end processing (PubMed:20338880).

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnucleus
Molecular Function5'-3' RNA exonuclease activity
Molecular Functionnucleic acid binding
Molecular Functionzinc ion binding
Biological ProcessmiRNA catabolic process
Biological ProcessmRNA processing
Biological Processnegative regulation of post-transcriptional gene silencing
Biological Processnuclear polyadenylation-dependent rRNA catabolic process
Biological ProcessrRNA 5'-end processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5'-3' exoribonuclease 3
  • EC number
  • Short names
    AtXRN3
  • Alternative names
    • Protein EXORIBONUCLEASE 3

Gene names

    • Name
      XRN3
    • ORF names
      F10A5.15
    • Ordered locus names
      At1g75660

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q9FQ03
  • Secondary accessions
    • Q8L7A3
    • Q9LR05

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Embryonic lethality.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 48 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003489551-10205'-3' exoribonuclease 3

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in roots, leaves, stems and flowers.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, zinc finger, coiled coil.

TypeIDPosition(s)Description
Region113-144Disordered
Compositional bias117-144Basic and acidic residues
Zinc finger262-279CCHC-type
Compositional bias411-436Basic and acidic residues
Region411-440Disordered
Region452-483Disordered
Compositional bias453-469Polar residues
Coiled coil487-523
Region831-859Disordered
Compositional bias836-855Polar residues
Region875-897Disordered
Region911-1020Disordered
Compositional bias938-988Polar residues
Compositional bias1002-1020Basic residues

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q9FQ03-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,020
  • Mass (Da)
    116,826
  • Last updated
    2001-03-01 v1
  • Checksum
    E383AB94A0A758D3
MGVPSFYRWLAEKYPLLVADVIEEEPVEIEGIKIPVDTSKPNPNNLEYDNLYLDMNGIIHPCFHPEDRPSPTTFEEVFQCMFDYIDRLFVMVRPRKLLYMAIDGVAPRAKMNQQRSRRFRSAKDASDAAAEEERLREEFEREGRRLPPKVDSQVFDSNVITPGTEFMGVLSIALQYYVHLRLNHDVGWKNIKVILSDANVPGEGEHKIMSYIRLQRNLPGFDPNTRHCLYGLDADLIMLGLATHEVHFSILREVVYTPGQQERCFLCGQMGHFASNCEGKPKKRAGESDEKGDGNDFVKKPYQFLHIWVLREYLELEMRIPNPPFEIDLERIVDDFIFICFFVGNDFLPHMPTLEIREGAINLLMAVYKKEFRSFDGYLTDGCKPNLKRVEQFIQAVGSFEDKIFQKRAMQHQRQAERVKRDKAGKATKRMDDEAPTVQPDLVPVARFSGSRLASAPTPSPFQSNDGRSAPHQKVRRLSPGSSVGAAIVDVENSLESDERENKEELKTKLKELIREKSDAFNSDTTEEDKVKLGQPGWRERYYEEKFSVVTPEEMERVRKDVVLKYTEGLCWVMHYYMEGVCSWQWFYPYHYAPFASDLKDLGEMDIKFELGTPFKPFNQLLGVFPAASSHALPERYRTLMTDPNSPIIDFYPTDFEVDMNGKRFSWQGIAKLPFIDERRLLEAVSEVEFTLTDEEKRRNSRMCDMLFIATSHRLAELVFSLDNHCRQLSARERVDFKVKIKPKLSDGMNGYLTPCSGETHPPVFRSPMEGMEDILTNQVICCIYRLPDAHEHITRPPPGVIFPKKTVDIGDLKPPPALWHEDNGRRPMHNNHGMHNNHGMHNNQGRQNPPGSVSGRHLGNAAHRLVSNSLQMGTDRYQTPTDVPAPGYGYNPPQYVPPIPYQHGGYMAPPGAQGYAQPAPYQNRGGYQPRGPSGRFPSEPYQSQSREGQHASRGGGYSGNHQNQHQQQQWHGQGGSEQNNPRGYNGQHHHQQGGDHDRRGRGRGSHHHHDQGGNPRHRY

Q9FQ03-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence AAF87130.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias117-144Basic and acidic residues
Compositional bias411-436Basic and acidic residues
Compositional bias453-469Polar residues
Alternative sequenceVSP_035194746-763in isoform 2
Alternative sequenceVSP_035195764-1020in isoform 2
Compositional bias836-855Polar residues
Compositional bias938-988Polar residues
Compositional bias1002-1020Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF286719
EMBL· GenBank· DDBJ
AAG40732.1
EMBL· GenBank· DDBJ
mRNA
AC006434
EMBL· GenBank· DDBJ
AAF87130.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002684
EMBL· GenBank· DDBJ
AEE35742.1
EMBL· GenBank· DDBJ
Genomic DNA
AY136383
EMBL· GenBank· DDBJ
AAM97049.1
EMBL· GenBank· DDBJ
mRNA
BT000175
EMBL· GenBank· DDBJ
AAN15494.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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