D6RKN3 · D6RKN3_COPC7

Function

function

Catalytic 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.

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 site848a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site850a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site957a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1010a divalent metal cation (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
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

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
      CC1G_13925

Organism names

Accessions

  • Primary accession
    D6RKN3

Proteomes

Organism-specific databases

Subcellular Location

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 domain.

TypeIDPosition(s)Description
Domain470-818USP

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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,099
  • Mass (Da)
    121,273
  • Last updated
    2010-08-10 v1
  • Checksum
    16CCADDD2FFB66D0
MASYHPLPPLSSPELSNFSRAITALAFDPVSDVLWTGAEDGVVSTYYGHRGLRGVSFPVCKDAPVSKIVAGDSQVNAFCMGSNGVGSWAKGGQNKWFFTAPSNIAAFSNTYHSSHSIAVSLTTLELLFLNSMTGRTVRQIPTSSMLTHLLFSHSSLISGSADGYIRIHDPRTGVTKNGASESLVKAHIGAISGLQATSNFIFSIGMGERHARPFPDPLVKVYDLRTMRALPPIPCSSGPALIHVLPKRSSSIAVASAQGLINIVDASNPSAAGEFYQLDVPSYLTSFAISPTGTYIACGDADGLVHLLSQAEDASLPFNGFDGQPTPWMDTPAPIPEIDWQDDTPLNSIGLPYYETPLLSAWSPVVATAPYFPPPQRIPPQVLNSIKTNDNIAYAPLPKELRGRRNLAIAAPKKENARFRSGKGRKESGSDTTILDDIHIPEFYRKVEIEYSKFGVEDFDFGFYNQTQFSGLETHILNSYTNSLVQVLHYILPIRQLGKSHITTDCSREHCLLCELGFVSRMLEDAKGTNCQSSNFCRTVGVLAHNSNAIELVDFGRETSEVDYAHKIQIFHRFLIDHLSSEGNSFPYNPLLLKPTAANHGELAPAPITQLIGVDAKNIIVCSSCKAVREKDNMTHVIDLIHPRKDTTTAPDFAAILRSSLLRSMTHKATCQSCKHFATFTSQRSIPSSDLPPILALNAAVYNDENIEYWLDSKAGPFLKPQVQVSGQLGDMDDPQVVTYEIRCLVVKITTKGKQSHLVALVKLPPEENDGIEGSWLIFNDFMVPAIIYMERVDLRGRLDLSNLLPAGDPSILTRDTSISQNRDQGSIRHQLLTPDELPKPGTLVAIDAEFVSMQQEETEIRSDGAKKVLRPARLSLARVSVLRGDGPKRGIPFIDDHIHTSEVIVDYLTEYSGIRFGDLDPMLSRYTLTPLKVVYKKLRALVDCGCIFVGHGLSKDFRIINIFVPPEQVIDTVDLYFVKSRQRRLSLRFLAWFVLKKHIQTDTHDSIEDARSALDLYHAYQEMEEEGVFDAKLDEIYKEGRQYNFKPPVVEGSASPILSSPGITHSVAQSYVEHSSPMHMAFHPGQHAVYPPSKSWRS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AACS02000002
EMBL· GenBank· DDBJ
EFI28391.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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