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A0A0W0EMY7 · A0A0W0EMY7_CANGB

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.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Features

Showing features for binding site.

1717100200300400500600700
TypeIDPosition(s)Description
Binding site378ATP (UniProtKB | ChEBI)
Binding site428-435ATP (UniProtKB | ChEBI)
Binding site482-483ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular ComponentP-body
Cellular ComponentPAN complex
Molecular FunctionATP binding
Molecular Functionmetal ion binding
Molecular Functionpoly(A) binding
Biological ProcessmRNA processing
Biological Processnuclear-transcribed mRNA poly(A) tail shortening
Biological Processpostreplication repair

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
      AO440_005236
      , AO440_005769

Organism names

Accessions

  • Primary accession
    A0A0W0EMY7

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

Type
IDPosition(s)Description
Domain8-37C3H1-type
Zinc finger8-37C3H1-type
Region37-100Disordered
Compositional bias44-100Polar residues
Coiled coil586-624
Region625-717Knob 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
    717
  • Mass (Da)
    79,820
  • Last updated
    2016-03-16 v1
  • MD5 Checksum
    B3AA31C5A2FFBA4AAF4988237F09CB38
MDKINPDWARDVPCRNVIIYGFCKKKTEGCPFKHDDDDIATPTSTPKVADTVPAPSGVIQQPSKISVSSLPSLNSQPSSTVPTSAPNATAHTGSKSQVPKFNAKASASFTPMSKAADGTQETQAPYLESPVAGSPGPILKAGTPVSFMQPNIYSTTPVPSPASMAMPNVVMPPNDMGSPDLGLQQQSHMVNLDGSIQQNYQERPNVLMRDSSMPLTMGTSGSRPMLDQQIHSISGLSNTSGSQPPGLLQSMNGASMDMGLPMNLRYPTIYPPTHSILQYHLYAPDPPPQLEIALKENERTPRMLFIPNDLREELVKRNLASLQLFPSGGNLPHIVKDYFGLVPLDFHQRSSVKDRYKKHKNSLYKVFSNVDGRIYLLRRIHDVNISDPTIISKTFQKWSKIDSSNVVALKDLFLTTAFGDSSLGIVYDYYPNATSLYEAHFVNYPTVEVTEDLLWSYAVQILNGLREIHNTNGVNIGDLDCDKIILTGKGRIKISAGAEYDIMNMCCPEDNEDDDNEEKLRKRNFVDLGEILFKLASKMCNCHGKDVANLAQVSEKLKNLIKSLAFEQLHDYVNVATIIEKYIGLDVVFKVMEAQQTYSEYAENVLSRELENGRLFRLICKLNFIFGRVENRLDINWSEPGDKFVIVLFYDYVFHQIDPNTGKPVTDLTHVLRCLNKLDAGVEENILLVTPDELNTAVVSYKKVKELVDKTFRAMTL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias44-100Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LLZZ01000154
EMBL· GenBank· DDBJ
KTA98031.1
EMBL· GenBank· DDBJ
Genomic DNA
LLZZ01000013
EMBL· GenBank· DDBJ
KTB13256.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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