A0A7T6XIS3 · A0A7T6XIS3_PENDI

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.

164950100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site303ATP (UniProtKB | ChEBI)
Binding site352-359ATP (UniProtKB | ChEBI)
Binding site412-413ATP (UniProtKB | ChEBI)

GO annotations

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

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
      PAN3
    • ORF names
      Pdw03_4762

Organism names

  • Taxonomic identifier
  • Strain
    • PdW03
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Penicillium

Accessions

  • Primary accession
    A0A7T6XIS3

Proteomes

Organism-specific databases

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 region, compositional bias, domain, zinc finger, coiled coil.

Type
IDPosition(s)Description
Region1-29Disordered
Compositional bias13-29Basic and acidic residues
Domain26-55C3H1-type
Zinc finger26-55C3H1-type
Region90-123Disordered
Compositional bias102-123Polar residues
Domain274-649Protein kinase
Coiled coil513-551
Region552-649Knob 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    649
  • Mass (Da)
    72,187
  • Last updated
    2021-06-02 v1
  • Checksum
    20AA7F6641867532
MASTGKPPLEDARRTTGSPKMKSRENAKDTLCRNVTIYGRCRYEDKGCAFNHDPTKLNANQSDSKKRFNVDSPSFTPSLLSGNVASAPKKSTAISPKAASAAPFQPRTTSSRSNTSTPTTRSEAAQDWAVADVQEFVPQGFEHVTPLQGNGNGGITPTGAFDPFVTTPTPMTPGAVGPVSANPYSHDPTGTMGGAFFANQTGFQQPIQYHLYAPIGPHSQNTLGYQRNVHDLFIPNDLREELQKKSAATLQTLPNTQLPAQVDYFHSLVPLDLSHQKNAATFGYPSWIYKAQSSKDGTFYALRRLEGFRLTNEKAIRSVQAWKRVCNASVVTIHDAFTSRSFQDSSLIFVTDYHPLSKTLADQHLNTGTRFPGRHTNAHIPEQVLWGYMTQIANGLKAIHTNGLAARVLEPSKVLLTAKTRVRINACAILDVVQFDTQRTLADLQRQDLVNFGQLIVTLGANSPIVIHNPTKAMEHFTRSYSPQLKNSVFWLLNGQQKDQERTIDTFITGISSQLMSTFDSALHLDDQLNYDLGRELENGRIVRLLSKLGLINERPEYELDQRWSESGERYFLKLFRDYVFHSVDSQGEAVVDLGHVLTCLNKLDAGIDEKIHLVSRDEQSSFIVSYKEVKKALESSFQALMKPARRMH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias13-29Basic and acidic residues
Compositional bias102-123Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP060774
EMBL· GenBank· DDBJ
QQK41908.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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