A0AAE0SBW6 · A0AAE0SBW6_9BIVA

  • Protein
    PAN2-PAN3 deadenylation complex catalytic subunit PAN2
  • Gene
    PAN2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • Exonucleolytic cleavage of poly(A) to 5'-AMP.
    EC:3.1.13.4 (UniProtKB | ENZYME | Rhea)

Cofactor

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

Note: Binds 2 metal cations per subunit in the catalytic exonuclease domain.

Activity regulation

Positively regulated by the regulatory subunit PAN3.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site1068a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1070a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1177a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1229a divalent metal cation (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentnucleus
Cellular ComponentP-body
Cellular ComponentPAN complex
Molecular Functionmetal ion binding
Molecular Functionnucleic acid binding
Molecular Functionpoly(A)-specific ribonuclease activity
Biological ProcessmRNA processing
Biological Processnuclear-transcribed mRNA poly(A) tail shortening
Biological Processpositive regulation of cytoplasmic mRNA processing body assembly

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    PAN2-PAN3 deadenylation complex catalytic subunit PAN2
  • EC number
  • Alternative names
    • PAB1P-dependent poly(A)-specific ribonuclease
    • Poly(A)-nuclease deadenylation complex subunit 2
      (PAN deadenylation complex subunit 2
      )

Gene names

    • Name
      PAN2
    • ORF names
      CHS0354_007971

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CHS0354
  • Taxonomic lineage
    Eukaryota > Metazoa > Spiralia > Lophotrochozoa > Mollusca > Bivalvia > Autobranchia > Heteroconchia > Palaeoheterodonta > Unionida > Unionoidea > Unionidae > Ambleminae > Lampsilini > Potamilus

Accessions

  • Primary accession
    A0AAE0SBW6

Proteomes

Subcellular Location

Cytoplasm, P-body
Nucleus
Note: Shuttles between nucleus and cytoplasm.

Keywords

Interaction

Subunit

Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex.

Family & Domains

Features

Showing features for region, domain, compositional bias.

Type
IDPosition(s)Description
Region466-485Disordered
Domain519-1015USP
Region642-720Disordered
Compositional bias647-672Polar residues
Compositional bias687-703Basic and acidic residues

Domain

Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex.
The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.

Sequence similarities

Belongs to the peptidase C19 family. PAN2 subfamily.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,284
  • Mass (Da)
    146,263
  • Last updated
    2024-05-29 v1
  • Checksum
    722916876BB55E1C
MQRMNMDFNHMPTSSLNVGFPSGPVEMNPGVGMIPPVMMPEHFQQQAPPGMFPTHPDTVHAGGEYREIHSVLVDGGSHYGVSSVCFDTQELLWMGNHGGHVTSYCGLDLQKYTSFQIHASDEIRQIMPLGEKGVMFLTRGNLRCSNRRGLNVFRYTNAAMHDMQCMIQMNPSSVLIGGHQTEVLELDLVKLQPKNMFTVAEPGCAIFRETGRYLTVGDTSGKVTLYDCNTMKAEHFLNAHSGTLSDFDIHGNTLITCGYSSRHGTLTADRYLMVYDLRMMRAMTPIQVIIEPTFLRFVHTYCPKLAVVSQVGQFQLIEGTADMSKFVYSVNVNDGLIMSFDVSKNYQAMAFGDSHGCMHLFATGNQIHFNNHIVSPEYADPVEPVPPIHIRDELTPLSVIPMTYPRSGRLLSDWPEHLCKKVYRKPKKIDPEILRTMKVYQNVGYAPNPGKERRNQIPYILEDKNAKKKGKKNVPESPVGRGDDPLMQTPQTYRKVILKYSKLGLEDFDFRHYNKTPFAGLETHIPNAYCNCMLQVFFFIEPLRCALLNHLCKREFCLSCELAFLFHMLDKQKGHSCQASNFLRAFRTLPEASALSLILGESEEILLRVNLGHLIQSWQRFIHQQIHSETFTKITVSVEEEKPPQATVPDITSSSGVTLADEKSSETTLSSSSSKSKKKKKKSKKKEREEKEKEKKEQREESPQNVEVPIPPPVQEEKTVNETEKSIITDLFGLDQVSTLTCRCGQETSRNTKPTLINLRYPDCSPQGPNKAPVHFSFSQVLEHSLSVEQNTQAWCNVCESYQPHNQTKKIESLPDVLALNCQLENERNQEFWKIQLMLLKQKEEMEGSFSTSSSPIPQSFSPVMCRYGRNCTRKGCRFRHETDMTCEGSDDLFRSKPEIGPVWVPMGLKVTLSADGKPQIDEISDEEILPKIHPLRTKYYEIFATVLHVKDAKTGGHLVSHIKVGETYHQRKENVTCTQWYLMNDFSITPIEKYEAVQLNLDWKVPCTIYFIRRNIVKYYNLAVKNPITSDVFFDDSSILNPKRRKVTFTPLDPKELPKEGTIVGLDAEFVSLNQEESELRSDGTRSTIKPSHLSVARITCIRGDGEQAGVPFLDDYIATHEQVVDYLTQYSGIQHGDLNPVISSKHLTTLKSTYIKLRYLIDAGVIFVGHGLKKDFRVINIMVPKDQIIDTVELFYIPRQRMISLKFLAWYFLKLNIQSATHDSVEDARTALHLYFKYQEMSKEGMDRVRATINEMYEFGRKNQWKISEIEEDNVEDTIAVL

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0AAE0SBK9A0AAE0SBK9_9BIVAPAN21316

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias647-672Polar residues
Compositional bias687-703Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEAOA010000537
EMBL· GenBank· DDBJ
KAK3589026.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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