AC   MF_03182;
DC   Protein; auto
TR   HAMAP; MF_03182; -; 1; level=0
XX
Names: PAN2
XX
ID   PAN2
DE   RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit PAN2;
DE            EC=3.1.13.4;
DE   AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease;
DE   AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2;
DE            Short=PAN deadenylation complex subunit 2;
case <OC:Vertebrata>
DE   + AltName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 52;
end case
GN   Name=PAN2;
XX
case <OC:Mammalia>
CC   -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC       complex, one of two cytoplasmic mRNA deadenylases involved in general
CC       and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A)
CC       tails of RNA and the activity is stimulated by poly(A)-binding protein
CC       (PABP). PAN deadenylation is followed by rapid degradation of the
CC       shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are
CC       then degraded by two alternative mechanisms, namely exosome-mediated
CC       3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA
CC       decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. Also
CC       acts as an important regulator of the HIF1A-mediated hypoxic response.
CC       Required for HIF1A mRNA stability independent of poly(A) tail length
CC       regulation.
else case <OC:Fungi>
CC   -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC       complex, one of two cytoplasmic mRNA deadenylases involved in mRNA
CC       turnover. PAN specifically shortens poly(A) tails of RNA and the
CC       activity is stimulated by poly(A)-binding protein @gn(PAB1). PAN
CC       deadenylation is followed by rapid degradation of the shortened mRNA
CC       tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by
CC       two alternative mechanisms, namely exosome-mediated 3'-5'
CC       exonucleolytic degradation, or deadenlyation-dependent mRNA decaping
CC       and subsequent 5'-3' exonucleolytic degradation by @gn(XRN1). May also
CC       be involved in post-transcriptional maturation of mRNA poly(A) tails.
else case <OC:Metazoa>
CC   -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC       complex, one of two cytoplasmic mRNA deadenylases involved in general
CC       and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A)
CC       tails of RNA and the activity is stimulated by poly(A)-binding protein
CC       (PABP). PAN deadenylation is followed by rapid degradation of the
CC       shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are
CC       then degraded by two alternative mechanisms, namely exosome-mediated
CC       3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA
CC       decaping and subsequent 5'-3' exonucleolytic degradation by XRN1.
else
CC   -!- FUNCTION: Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation
CC       complex, one of two cytoplasmic mRNA deadenylases involved in mRNA
CC       turnover. PAN specifically shortens poly(A) tails of RNA and the
CC       activity is stimulated by poly(A)-binding protein (PABP). PAN
CC       deadenylation is followed by rapid degradation of the shortened mRNA
CC       tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by
CC       two alternative mechanisms, namely exosome-mediated 3'-5'
CC       exonucleolytic degradation, or deadenlyation-dependent mRNA decaping
CC       and subsequent 5'-3' exonucleolytic degradation by XRN1.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC       Note=Binds 2 metal cations per subunit in the catalytic exonuclease
CC       domain
CC   -!- ACTIVITY REGULATION: Positively regulated by the regulatory subunit
CC       @gn(PAN3).
case <OC:Mammalia>
CC   -!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the
CC       regulatory subunit PAN3 to form the poly(A)-nuclease (PAN)
CC       deadenylation complex. Interacts with ZFP36.
else
CC   -!- SUBUNIT: Forms a heterotrimer with an asymmetric homodimer of the
CC       regulatory subunit @gn(PAN3) to form the poly(A)-nuclease (PAN)
CC       deadenylation complex.
end case
case <OC:Metazoa>
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body. Nucleus. Note=Shuttles between
CC       nucleus and cytoplasm.
else
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
end case
CC   -!- DOMAIN: The linker, or PAN3 interaction domain (PID), between the WD40
CC       repeats and the pseudo-UCH domain mediates interaction with PAN3.
CC   -!- DOMAIN: Contains a pseudo-UCH domain. This ubiquitin C-terminal
CC       hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain
CC       is predicted to be catalytically inactive because it lacks the active
CC       site catalytic triad characteristic of thiol proteases, with residues
CC       at the equivalent structural positions that are incompatible with
CC       catalysis, and it cannot bind ubiquitin. It functions as a structural
CC       scaffold for intra- and intermolecular interactions in the complex.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
XX
DR   PROSITE; PS50235; USP_3; 0-1; trigger=no
DR   Pfam; PF00929; RNase_T; 1; trigger=yes
DR   Pfam; PF13423; UCH_1; 1; trigger=no
DR   REP; Repeat_WD40; WD40; 1-6; trigger=yes
XX
case <OC:Metazoa>
KW   Nucleus
end case
KW   Cytoplasm
KW   Exonuclease
KW   Hydrolase
KW   mRNA processing
KW   Metal-binding
KW   Nuclease
XX
case <OC:Metazoa>
GO   GO:0000932; C:P-body
GO   GO:0005634; C:nucleus
GO   GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly
else
GO   GO:0005737; C:cytoplasm
end case
GO   GO:0004535; F:poly(A)-specific ribonuclease activity
GO   GO:0031251; C:PAN complex
GO   GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay
GO   GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening
XX
FT   From: PAN2_YEAST (P53010)
FT   DOMAIN          474..855
FT                   /note="USP"
FT   REGION          337..473
FT                   /note="Linker"
FT   BINDING         910
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT   Condition: D
FT   BINDING         912
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT   Condition: E
FT   BINDING         1020
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT   Condition: D
FT   BINDING         1071
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT   Condition: D
XX
Size: 1008-1310;
Related: None;
Template: P53010; Q504Q3; Q8BGF7; G0SAK8; A1Z7K9;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.12 2022/11/19
//