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HAMAP rule MF_03182

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General rule information [?]

Accession MF_03182
Dates 24-FEB-2014 (Created)
19-NOV-2022 (Last updated, Version 12)
Name PAN2
Scope
Eukaryota
Templates P53010 (PAN2_YEAST); Q504Q3 (PAN2_HUMAN); Q8BGF7 (PAN2_MOUSE); G0SAK8 (PAN2_CHATD); A1Z7K9 (PAN2_DROME): [Recover all]
Triggered by

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
PAN2
Protein name
RecName: Full=PAN2-PAN3 deadenylation complex catalytic subunit PAN2;
EC 3.1.13.4;
AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease;
AltName: Full=Poly(A)-nuclease deadenylation complex subunit 2;
Short=PAN deadenylation complex subunit 2;
case <OC:Vertebrata>
Protein name
Full=Inactive ubiquitin carboxyl-terminal hydrolase 52;
end case
Gene name
PAN2

Comments [?]

case <OC:Mammalia>
Function Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). 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. Also acts as an important regulator of the HIF1A-mediated hypoxic response. Required for HIF1A mRNA stability independent of poly(A) tail length regulation.
else case <OC:Fungi>
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 @gn(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 @gn(XRN1). May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
else case <OC:Metazoa>
Function Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). 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.
else
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 (PABP). 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.
end case
Catalytic activity Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
Cofactor a divalent metal cation
Note: Binds 2 metal cations per subunit in the catalytic exonuclease domain
Activity regulation Positively regulated by the regulatory subunit @gn(PAN3).
case <OC:Mammalia>
Subunit Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts with ZFP36.
else
Subunit Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit @gn(PAN3) to form the poly(A)-nuclease (PAN) deadenylation complex.
end case
case <OC:Metazoa>
Subcellular location Cytoplasm, P-body. Nucleus. Note=Shuttles between nucleus and cytoplasm.
else
Subcellular location Cytoplasm.
end case
Domain The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
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.
Similarity Belongs to the peptidase C19 family. PAN2 subfamily.

Keywords [?]

case <OC:Metazoa>
Nucleus
end case
Cytoplasm
Exonuclease
Hydrolase
mRNA processing
Metal-binding
Nuclease

Gene Ontology [?]

case <OC:Metazoa>
GO:0000932; Cellular component: P-body.
GO:0005634; Cellular component: nucleus.
GO:0010606; Biological process: positive regulation of cytoplasmic mRNA processing body assembly.
else
GO:0005737; Cellular component: cytoplasm.
end case
GO:0004535; Molecular function: poly(A)-specific ribonuclease activity.
GO:0031251; Cellular component: PAN complex.
GO:0000288; Biological process: nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay.
GO:0000289; Biological process: nuclear-transcribed mRNA poly(A) tail shortening.

Cross-references [?]

PROSITE PS50235; USP_3; 0-1;
Pfam PF00929; RNase_T; 1; trigger=Yes;
PF13423; UCH_1; 1;

Computed features [?]

REP Repeat_WD40; WD40; 1-6; trigger=yes;

Features [?]

From: PAN2_YEAST (P53010)
Key     From     To       Description   Tag   Condition   FTGroup
DOMAIN     474     855       USP        
REGION     337     473       Linker        
BINDING     910     910       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="catalytic     D  
BINDING     912     912       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="catalytic     E  
BINDING     1020     1020       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="catalytic     D  
BINDING     1071     1071       /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_note="catalytic     D  

Additional information [?]

Size range 1008-1310 amino acids
Related rules None
Fusion None


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