HAMAP rule MF_03182
General rule information
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| Accession | MF_03182 |
| Dates | 24-FEB-2014 (Created)
19-NOV-2022 (Last updated, Version 12) |
| Name | PAN2 |
| Scope(s) |
Eukaryota |
| Template(s) | P53010 (PAN2_YEAST); Q504Q3 (PAN2_HUMAN); Q8BGF7 (PAN2_MOUSE); G0SAK8 (PAN2_CHATD); A1Z7K9 (PAN2_DROME); [ Recover all ] |
| Triggered by |
HAMAP; MF_03182 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| 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 | + AltName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 52; |
| end case | |
| Gene name | Name=PAN2; |
Comments
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| 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 | Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; 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. |
| 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. |
| SIMILARITY | Belongs to the peptidase C19 family. PAN2 subfamily. |
Keywords
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| case <OC:Metazoa> | |
| Nucleus | |
| end case | |
| Cytoplasm | |
| Exonuclease | |
| Hydrolase | |
| mRNA processing | |
| Metal-binding | |
| Nuclease | |
Gene Ontology
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| case <OCellular component: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; https://www.ebi.ac.uk/QuickGO/term/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
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| PROSITE | PS50235; USP_3; 0-1; |
| Pfam | PF00929; RNase_T; 1; |
| Pfam | PF13423; UCH_1; 1; |
| REP | Repeat_WD40; WD40; 1-6; |
Features
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| From: PAN2_YEAST (P53010) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | 474 | 855 | /note="USP" | |||||||||
| REGION | 337 | 473 | /note="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
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| Size range | 1008-1310 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |