G2WI04 · G2WI04_YEASK

Function

function

Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and with PAB1.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Features

Showing features for binding site.

167950100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site325ATP (UniProtKB | ChEBI)
Binding site376-383ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular ComponentPAN complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionprotein kinase activity
Molecular FunctionRNA binding
Biological ProcessmRNA processing
Biological Processnuclear-transcribed mRNA poly(A) tail shortening

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    PAN2-PAN3 deadenylation complex subunit PAN3
  • Alternative names
    • PAB1P-dependent poly(A)-specific ribonuclease
    • Poly(A)-nuclease deadenylation complex subunit 3
      (PAN deadenylation complex subunit 3
      )

Gene names

    • Name
      K7_PAN3
    • Synonyms
      PAN3
    • ORF names
      SYK7_043251

Organism names

Accessions

  • Primary accession
    G2WI04

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homodimer. Forms a heterotrimer with a catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein PAB1 (via PABC domain), conferring substrate specificity of the enzyme complex.

Family & Domains

Features

Showing features for domain, zinc finger, region, coiled coil.

TypeIDPosition(s)Description
Domain8-37C3H1-type
Zinc finger8-37C3H1-type
Region275-548Pseudokinase domain
Domain299-549Protein kinase
Coiled coil549-587
Region588-679Knob domain

Domain

Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs.
The N-terminal zinc finger binds to poly(A) RNA.
The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.

Sequence similarities

Belongs to the protein kinase superfamily. PAN3 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    679
  • Mass (Da)
    76,384
  • Last updated
    2011-11-16 v1
  • Checksum
    F051C098ABA47B31
MDKINPDWAKDIPCRNITIYGYCKKEKEGCPFKHSDNTTATTINDVPPPIDVGEATTPTMTSVPKFNAKVSASFTPMTVGSDSLTTVTNTTSAATNATGNIAMAATSATASTVNPMINPIVNSSLVNNNNNSSNISISIPTTASSSNYDPFNAPIFTPSSTSSIHTNANAHSFPFPSIANSGGININATDDNSNNMSMANNVPPPMQPPPIESSNLKYPRIYPPPHSLLQYHLYAPEQPSSLKSLLKPNERSADQLFIPNNIREDLTKKNLSILQVCPSSGKVIPSIVQDYFNLVPLNFNNNDFLNKTTLFKVFSNYDGKAYVLKRLPNIDKSMNPNKISKIYQIWSKINCTNLIKFRDIFQTTKFGDLSICLVFDYYPNSLSLYDYHFVNFPKFPITNNYLWIYLVQLTNVINSIHSQNLSIGNTLNWRKVLITGDPGRIKLSHCNFMDLLFNDDTDTVVSSGGSTIEGQQQLDYKYLGELLFNLSINIENSNNNTAPKEYRLEEITPQSIDDMRQIDDKFKDVLKYLISDNGDSKKSIHDLTSHFYDKMFMVLESSQTYTEYMESVLSRELENGRLFRLVNKLNCIFGRIESRIDINWSESGTKFPIILFYDYVFHQVDSNGKPIMDLTHVLRCLNKLDAGIQEKLMLVTPDELNCIIISYKELKDLIESTFRSITQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DG000047
EMBL· GenBank· DDBJ
GAA24697.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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