Q9FQ02 · XRN2_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 (PubMed:17993620).
Involved in pre-rRNA processing. Involved in the primary exonucleolytic shortening of the 5' external transcribed spacer (5'ETS), required for endonucleolytic processing at site P by the U3 snoRNP complex. Involved with XRN3 in the 5'-end processing of 5.8S and 25S rRNAs. Contributes with XRN3 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 FunctionRNA 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 Processnuclear-transcribed mRNA catabolic process
Biological ProcessrRNA 5'-end processing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    5'-3' exoribonuclease 2
  • EC number
  • Short names
    AtXRN2
  • Alternative names
    • Protein EXORIBONUCLEASE 2

Gene names

    • Name
      XRN2
    • ORF names
      K16E1.1/K16E1.2
    • Ordered locus names
      At5g42540/At5g42550

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
    Q9FQ02
  • Secondary accessions
    • Q56WR6
    • Q570J7
    • Q9AST0
    • Q9FH70
    • Q9FH71

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003489541-10125'-3' exoribonuclease 2

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 zinc finger, region, compositional bias.

Type
IDPosition(s)Description
Zinc finger264-281CCHC-type
Region411-439Disordered
Compositional bias413-434Basic and acidic residues
Region888-976Disordered
Compositional bias895-912Polar residues
Compositional bias914-935Basic and acidic residues
Compositional bias946-967Basic and acidic residues
Region990-1012Disordered

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete

This entry describes 1 isoforms produced by Alternative splicing. A number of isoforms are produced. According to EST sequences.

Q9FQ02-1

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
    1,012
  • Mass (Da)
    116,385
  • Last updated
    2001-03-01 v1
  • Checksum
    9BC6DDC74755265A
MGVPSFYRWLIQRYPLTIQEVIEEEPLEVNGGGVTIPIDSSKPNPNGYEYDNLYLDMNGIIHPCFHPEDKPSPTTFTEVFQCMFDYIDRLFVMVRPRKLLFMAIDGVAPRAKMNQQRARRFRAAKDAAEAAAEEEQLREEFEREGKKLPPKVDSQVFDSNVITPGTEFMATLSFALRYYIHVRLNSDPGWKNIKVILSDANVPGEGEHKIMSYIRCNKNHPGYNPNTHHCLYGLDADLIMLSLATHEIHFSILREVVFFPGEEGKCFLCGQEGHRAADCEGKIKRKTGEMLDNTEADVVVKKPYEFVNIWILREYLEHDMQIPGAKKNLDRLIDDFIFICFFVGNDFLPHMPTLEIREGAIELLMSVYKNKFRSAKKYLTDSSKLNLRNVERFIKAVGMYENQIFQKRAQVQQRQSERFRRDKARDKARDNARDNAQASRQFSGKLVQLDSLDEVSDSLHSSPSRKYLRLSLDDNIGVANVETENSLKAEELDNEEDLKFKLKKLLRDKGDGFRSGNGEQDKVKLNKVGWRERYYEEKFAAKSVEEMEQIRRDVVLKYTEGLCWIMHYYYHGVCSWNWFYPYHYAPFASDLKGLEKLDIKFELGSPFKPFNQLLAVLPSASAHALPECYRSLMTNPDSPIADFYPADFEIDMNGKRYSWQGISKLPFVEEKRLLEAAAQVEKSLTNEEIRRNSALFDMLFVVASHPLGELIRSLNSRTNNLSNEERATIIEKIDPGLSDGMNGYIASCGGDSQPSCFCSTVEGMEDVLTNQVICAIYKLPEDIRGSEITHQIPRLAIPKKTISLVDLKSGGLLWHEDGDKRRAPPKVIKIKRYNPEGSISGGRLGKASHRLVLQTINAQPDYMNINSEPALCPNTVFQNERVPKKIPTFKDNGIQWISPPPSQITPKKMNSPQRQKAWKKDETPQSREKSKKLKSSLKVNPLKMKKTKSPQREFTREKKKENITPQRKLTKAQRQVKHIRMMEEAKMIKQRKKEKYLRKKAKYAQGAPPKTA

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
F4K1L3F4K1L3_ARATHXRN21023

Sequence caution

The sequence AAK32883.1 differs from that shown. Reason: Erroneous termination Truncated C-terminus.
The sequence BAB09325.1 differs from that shown. Reason: Erroneous gene model prediction Was originally thought to correspond to two different genes At5g42540 and At5g42550.
The sequence BAB09326.1 differs from that shown. Reason: Erroneous gene model prediction Was originally thought to correspond to two different genes At5g42540 and At5g42550.
The sequence BAD94484.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict, compositional bias.

Type
IDPosition(s)Description
Sequence conflict390in Ref. 5; BAD93823
Compositional bias413-434Basic and acidic residues
Sequence conflict414in Ref. 5; BAD93823
Compositional bias895-912Polar residues
Compositional bias914-935Basic and acidic residues
Compositional bias946-967Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF286720
EMBL· GenBank· DDBJ
AAG40733.1
EMBL· GenBank· DDBJ
mRNA
AB022210
EMBL· GenBank· DDBJ
BAB09325.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AB022210
EMBL· GenBank· DDBJ
BAB09326.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002688
EMBL· GenBank· DDBJ
AED94824.1
EMBL· GenBank· DDBJ
Genomic DNA
AF367296
EMBL· GenBank· DDBJ
AAK32883.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
AY091687
EMBL· GenBank· DDBJ
AAM10286.1
EMBL· GenBank· DDBJ
mRNA
AK176100
EMBL· GenBank· DDBJ
BAD43863.1
EMBL· GenBank· DDBJ
mRNA
AK220711
EMBL· GenBank· DDBJ
BAD93823.1
EMBL· GenBank· DDBJ
mRNA
AK220893
EMBL· GenBank· DDBJ
BAD94308.1
EMBL· GenBank· DDBJ
mRNA
AK221968
EMBL· GenBank· DDBJ
BAD94484.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help