A0A5M9MBJ0 · A0A5M9MBJ0_9EURO
- ProteinPAN2-PAN3 deadenylation complex catalytic subunit PAN2
- GenePAN2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1750 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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).
Catalytic activity
Cofactor
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 1469 | a divalent metal cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 1471 | a divalent metal cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 1578 | a divalent metal cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 1637 | a divalent metal cation (UniProtKB | ChEBI); catalytic | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endosome membrane | |
Cellular Component | PAN complex | |
Molecular Function | metal ion binding | |
Molecular Function | nucleic acid binding | |
Molecular Function | phosphatidylinositol binding | |
Molecular Function | poly(A)-specific ribonuclease activity | |
Molecular Function | ubiquitin binding | |
Biological Process | endosomal transport | |
Biological Process | intracellular protein transport | |
Biological Process | mRNA processing | |
Biological Process | nuclear-transcribed mRNA poly(A) tail shortening | |
Biological Process | vacuolar transport |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePAN2-PAN3 deadenylation complex catalytic subunit PAN2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA0A5M9MBJ0
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endosome membrane ; Peripheral membrane protein
Membrane ; Peripheral membrane protein
Keywords
- Cellular component
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.
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 16-145 | VHS | ||||
Sequence: ATDENLTSENWEYILDVCDKVAAEESGAKDAVAALIKRLAHRNANVQLYTLELGNALAQNCGPKIHRELASRSFTDALLRLASDRNTHQQVKSKILERMQEWTEMFSSNPDFGIMEQAYMKLKTQNPNLQ | ||||||
Domain | 203-262 | SH3 | ||||
Sequence: LRSPASERFSTFNRQNRVNCNFERGDVIAVLESVYKDWWKGSLRGQTGIFPLNYVEKLPD | ||||||
Region | 359-499 | Disordered | ||||
Sequence: HPPQAQFGRPGQSQYGYPGPALSIGYSQGSSQADAQRYFSPRPQGEENQPVQPNTAPYYGGDQAPVYPPASQSPDMRNRTPPAGPVYPQQPQQPQQPAADSYQPVHHRPESTYEHPQELGTSVYDSPVEHPANQRLPYPVG | ||||||
Compositional bias | 382-414 | Polar residues | ||||
Sequence: IGYSQGSSQADAQRYFSPRPQGEENQPVQPNTA | ||||||
Region | 520-557 | Disordered | ||||
Sequence: YPPEDAANKPPGQQAPYPSTPASHQPPPMPSAAIPGSA | ||||||
Compositional bias | 533-552 | Pro residues | ||||
Sequence: QAPYPSTPASHQPPPMPSAA | ||||||
Domain | 1079-1417 | USP | ||||
Sequence: SGLETHIANSFTNALLQLLKFIPLVRNLALSHAASSCIYENCLLCEMGYLFDMLEKANGQNCQATNLLKTFSSFREASNLGLFEENLTNKSLSSAIQAVNRFFLSQIAHDFRMILPSSDDFDQRLATIASEAIRCMFCQNEIVRPGNSLANELIYPAIDIKQARRNPAFRFSNILRASIERETQNRGWCNYCRRYQQVAIRKSVHRMPLALILNASLSNPLYRRLWAIPGWLPEEIGIVVDGGQVLCFEGEDLQLRKQGNMPGLLVYELVGLVSEIDIPEHQKPHLVSFINVSISSREPDPGSRWHLFNDFLVTEVDKDEALRFSQPWKQPCVLAYQVR | ||||||
Region | 1672-1750 | Disordered | ||||
Sequence: GFRPPPRNGTATVLSRPGTAVTLQNNSGRNTPSAPDVGGAASAPATPRQAFRRSIALTPSNGTFTGPGAGDFFSGSPLK | ||||||
Compositional bias | 1683-1704 | Polar residues | ||||
Sequence: TVLSRPGTAVTLQNNSGRNTPS | ||||||
Compositional bias | 1724-1738 | Polar residues | ||||
Sequence: RSIALTPSNGTFTGP |
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
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,750
- Mass (Da)195,546
- Last updated2020-02-26 v1
- Checksum529712DD5E54D5BC
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 382-414 | Polar residues | ||||
Sequence: IGYSQGSSQADAQRYFSPRPQGEENQPVQPNTA | ||||||
Compositional bias | 533-552 | Pro residues | ||||
Sequence: QAPYPSTPASHQPPPMPSAA | ||||||
Compositional bias | 1683-1704 | Polar residues | ||||
Sequence: TVLSRPGTAVTLQNNSGRNTPS | ||||||
Compositional bias | 1724-1738 | Polar residues | ||||
Sequence: RSIALTPSNGTFTGP |