A0A5M9MBJ0 · A0A5M9MBJ0_9EURO

  • 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 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.
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).

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 site1469a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1471a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1578a divalent metal cation (UniProtKB | ChEBI); catalytic
Binding site1637a divalent metal cation (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentendosome membrane
Cellular ComponentPAN complex
Molecular Functionmetal ion binding
Molecular Functionnucleic acid binding
Molecular Functionphosphatidylinositol binding
Molecular Functionpoly(A)-specific ribonuclease activity
Molecular Functionubiquitin binding
Biological Processendosomal transport
Biological Processintracellular protein transport
Biological ProcessmRNA processing
Biological Processnuclear-transcribed mRNA poly(A) tail shortening
Biological Processvacuolar transport

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
      ATNIH1004_008489

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NIH1004
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati

Accessions

  • Primary accession
    A0A5M9MBJ0

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Endosome membrane
; Peripheral membrane protein
Membrane
; Peripheral membrane protein

Keywords

Interaction

Subunit

Component of the ESCRT-0 complex composed of HSE1 and VPS27.
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 domain, region, compositional bias.

TypeIDPosition(s)Description
Domain16-145VHS
Domain203-262SH3
Region359-499Disordered
Compositional bias382-414Polar residues
Region520-557Disordered
Compositional bias533-552Pro residues
Domain1079-1417USP
Region1672-1750Disordered
Compositional bias1683-1704Polar residues
Compositional bias1724-1738Polar 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 STAM family.
Belongs to the peptidase C19 family. PAN2 subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,750
  • Mass (Da)
    195,546
  • Last updated
    2020-02-26 v1
  • Checksum
    529712DD5E54D5BC
MFRAQQNAFDDAVAKATDENLTSENWEYILDVCDKVAAEESGAKDAVAALIKRLAHRNANVQLYTLELGNALAQNCGPKIHRELASRSFTDALLRLASDRNTHQQVKSKILERMQEWTEMFSSNPDFGIMEQAYMKLKTQNPNLQASIEAGENGDYRRRNPVPAPPPPLRLQSSRLNLAPVPVLLIRSKERLHKLFRQVLPLLRSPASERFSTFNRQNRVNCNFERGDVIAVLESVYKDWWKGSLRGQTGIFPLNYVEKLPDPTVEELQREAQMETEVFGQIKNVEKLLTLLSTRGSEPNVQDNEEITNLYHSTLAIRPKLIELIGKYSQKKDEFTQLNEKFIKARRDYEALLEASMSHPPQAQFGRPGQSQYGYPGPALSIGYSQGSSQADAQRYFSPRPQGEENQPVQPNTAPYYGGDQAPVYPPASQSPDMRNRTPPAGPVYPQQPQQPQQPAADSYQPVHHRPESTYEHPQELGTSVYDSPVEHPANQRLPYPVGQIPGAVQHFQQQQQEYSNLVYPPEDAANKPPGQQAPYPSTPASHQPPPMPSAAIPGSATNYPVNPASGGYQAYNPTQSGVPNSNPASYYRCDADTMEADWDELSRIPVPAPSSHSLPTIATTVAFDDVMELLWTGNEYGRITSFYGPELQRYTSVRAHPVSEGLVRQILFHERGVISLSSKSVHMITRRGLTQWHIDHEEMTDLRCMSFTAQTNRIIVAGCQGVMFTIDIDKGIIIDKLQTEFQYTMMKKSRYLCAATDTGSVNALSLTDFQVVKSWKAHGTAVNDMDARNDLLVTCGFSVRHLGSPIVDPLANVYDLKTLSPLPPIPFHAGAAYVRMHPKLHTTSFVASQTGQLQVVDLMNPNAINLRQANVSFMLGIDISPSGEALAINDAECSIHLWGSPAKVHFNEMSKETEFADVAPRPPPLEWSSETPLSMIGMPYYHERLLSAWPSHLLFEIGSPPAPIDQAVIPYLRPAEIGHYAPNPKKTRRYQVENTRALSTAEPALIAPKFLSEKAREQQSRAKSEGSISDTAEALAGVKLNGETEDDPLLKYSNVEIKYSRFGVDDFDFRFYNQTDFSGLETHIANSFTNALLQLLKFIPLVRNLALSHAASSCIYENCLLCEMGYLFDMLEKANGQNCQATNLLKTFSSFREASNLGLFEENLTNKSLSSAIQAVNRFFLSQIAHDFRMILPSSDDFDQRLATIASEAIRCMFCQNEIVRPGNSLANELIYPAIDIKQARRNPAFRFSNILRASIERETQNRGWCNYCRRYQQVAIRKSVHRMPLALILNASLSNPLYRRLWAIPGWLPEEIGIVVDGGQVLCFEGEDLQLRKQGNMPGLLVYELVGLVSEIDIPEHQKPHLVSFINVSISSREPDPGSRWHLFNDFLVTEVDKDEALRFSQPWKQPCVLAYQVRDARHAIDDAWKNFLDTSLLFRDWSLNAGRPVESLVTLAEGEKPNPGTPVALDTEFVDLEKAEIDVKADGSQEIVRPSKSGLARVSVLRGSGAREGVPFIDDYITIKEPIVDYVTQYSGIKPGDLDPRISQHTLVPLKVAYKKLWLLLNLGCVFVGHGLASDFRQINIQVPKNQTVDSQYLFFHPGKNRRLSLRYLAWAVFKEYIQEEPADNNDGHDSIEDARMALRLWKKFQEYEDAGIVSQILEEIFREGSKLGFRPPPRNGTATVLSRPGTAVTLQNNSGRNTPSAPDVGGAASAPATPRQAFRRSIALTPSNGTFTGPGAGDFFSGSPLK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias382-414Polar residues
Compositional bias533-552Pro residues
Compositional bias1683-1704Polar residues
Compositional bias1724-1738Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QUQM01000006
EMBL· GenBank· DDBJ
KAA8644288.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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