R7UIQ4 · R7UIQ4_CAPTE

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.

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 site1043a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1045a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1152a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1204a 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
      CAPTEDRAFT_225482

Organism names

  • Taxonomic identifier
  • Strain
    • I ESC-2004
  • Taxonomic lineage
    Eukaryota > Metazoa > Spiralia > Lophotrochozoa > Annelida > Polychaeta > Sedentaria > Scolecida > Capitellidae > Capitella

Accessions

  • Primary accession
    R7UIQ4

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.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-21Disordered
Region422-458Disordered
Compositional bias431-448Polar residues
Domain494-990USP
Compositional bias625-640Polar residues
Region625-701Disordered
Compositional bias661-687Basic and acidic residues
Region1245-1290Disordered
Compositional bias1253-1277Basic 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.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,290
  • Mass (Da)
    147,074
  • Last updated
    2013-07-24 v1
  • Checksum
    AAEC945D5DF87FF8
MEFIPSDIAASSEQSMDPTLSAPVTSFQSPYEEQGFGHEEFFEIKNSMVDGGDRFSVSAVAFDGQEELLWMGNQGGHVTSYYGLDPQKYTSFQVHETNEIRQLLTVDGLVFSLTPDSLRCNSKYGRPQYRHKSDALQDMQCMLLTQPHKILMGGHQPIMVELDIEKRKEIRQVEISEPGCAILRFSTQYICSGDTAGKVTLRDPRSLKTQHVLQAHSGTLSDFDVCNNQLVTCGFSNRMGSLTADRFLMLYDLRYMKATTPMPMTLDPMFLRFIPMYSDRICVVSQIGQFQVMEQGALTPASMTVYNVQTEGASINAFDISPSHQTMAFGDAGGFIHLFGTETPVMNPFSKDTEFAPVETLHASIDVNNLLAPYSLVPMQYPAQGKLASDWPEELCQKTYRKAPRIDPEIIRTVKMVSNVGYAPNPGGRRRNQMQRPTASSHKTTHKNSVPDSPLDRDDPFIKIPKRYRKVEIKYSKLGVEDFDFWYYNKTNFAGLETQIPNAYCNAMVQVLYTIEPLRVALIGHLCDREFCLACELGFLFHMLDLQKGKACQASNFLRAFRTIPEASALSLVLNDAEESMGKVNLRRLIQNWNRFLLQQIHTECSELSDISSILEKSGLQPLSPVSRTQSWSEDPNIEDHPLTSASPLPSLDEDEIEEKDEKEEKKAKGTVPEPLELKKQRLDSLSSEDGKPPQGGHAKDSAVKSLFGLDLENVFTCNKCGAVMKRSMTSSANDLSYPELMQDRVEKQYLFAEVLQRSLCSEQNTQAWCNVCKKYQPHVQTKVIESLPDILSLNCHLESTRELEFWRAQEAFVRKKYEGETTSAASITRSAVKLCRYGLACTRKDCKFRHDNDGDRSSLRFDEAASEDKRSVYDHSWLPVGLQAKLLDDGKVLFHNIEDENDIPSKWAEPDLSYYELHATVAYIKDQKTGGHLISHVNMGERYHQRKERVTCTQWYLFNDFAIQPIERQEAVSFNLDWKIPCVVYYMRKDITARHSTTIQNPITADVLFTDSTLVTPRRKHVMFAPLDRPEIPVEGEVVGLDAEFVTLNQEEAELRSDGTRSTIKPSHLSVARITCIRGKGPLMYEPFIDDYISTQEAVVDYLTQFSGIQPGDLDAAISQKHLTTLKSTYLKLRYLIDRGCLFVGHGLKKDFRVINLVIKSDQVIDTVDLFHLPRQRMISLKFLAWYFLGTTIQSDMHDSIEDARTALRLYHKYQEMCKEGMDMVRETLKEMYETGRKLQWKVTDAPSPVEIAADRAREEEEKRKKEEKEKEEKEDEKEKEEEEEEETE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias431-448Polar residues
Compositional bias625-640Polar residues
Compositional bias661-687Basic and acidic residues
Compositional bias1253-1277Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AMQN01008379
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KB302988
EMBL· GenBank· DDBJ
ELU03678.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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