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Details on Person UniProt:Q95RR8 PAN3
| Class:Id | ReferenceGeneProduct:5433714 |
|---|---|
| _chainChangeLog | chain:1-790 added on Sat February 7 2015 |
| _displayName | UniProt:Q95RR8 PAN3 |
| _timestamp | 2025-08-15 22:18:01 |
| chain | chain:1-790 |
| checksum | 19555B56DAA43E21 |
| comment | FUNCTION Regulatory 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 deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins.SUBUNIT Homodimer. Forms a heterotrimer with a catalytic subunit PAN2 to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein (via PABC domain), conferring substrate specificity of the enzyme complex (PubMed:23932717). Interacts with the GW182 family protein gw (PubMed:21981923, PubMed:23172285). Interacts with Gyf (PubMed:31114929).INTERACTION The N-terminal zinc finger binds to poly(A) RNA.DOMAIN Contains a pseudokinase domain. The protein kinase domain is predicted to be catalytically inactive because some of the residues important for catalytic activity are substituted and it lacks the equivalent of the binding site for a peptide substrate. However, it has retained an ATP-binding site and ATP-binding is required for mRNA degradation, stimulating the activity of the PAN2 nuclease in vitro (PubMed:23932717). The nucleotide-binding site is juxtaposed to the RNase active site of PAN2 in the complex and may actually bind nucleosides of a poly(A) RNA rather than ATP, feeding the poly(A)-tail to the active site of the deadenylase and thus increasing the efficiency with which this distributive enzyme degrades oligo(A) RNAs (By similarity).DOMAIN The pseudokinase domain, the coiled-coil (CC), and C-terminal knob domain (CK) form a structural unit (PKC) that forms an extensive high-affinity interaction surface for PAN2.SIMILARITY Belongs to the protein kinase superfamily. PAN3 family. |
| created | [InstanceEdit:5433710] Weiser, JD |
| description | recommendedName: fullName evidence="1"PAN2-PAN3 deadenylation complex subunit PAN3 alternativeName: fullName evidence="1"PAB1P-dependent poly(A)-specific ribonuclease alternativeName: fullName evidence="1"Poly(A)-nuclease deadenylation complex subunit 3 shortName evidence="1"PAN deadenylation complex subunit 3 |
| geneName | PAN3 CG11486 |
| identifier | Q95RR8 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure ATP-binding Coiled coil Cytoplasm mRNA processing Nucleotide-binding Reference proteome |
| modified | [InstanceEdit:5618415] Weiser, JD [InstanceEdit:5634237] Weiser, JD [InstanceEdit:5673015] Weiser, JD [InstanceEdit:9027688] Weiser, JD [InstanceEdit:9037114] Weiser, JD [InstanceEdit:9637257] Weiser, JD [InstanceEdit:9657908] Weiser, JD [InstanceEdit:9676415] Weiser, JD [InstanceEdit:9730071] Weiser, JD [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | PAN3 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| secondaryIdentifier | PAN3_DROME |
| sequenceLength | 790 |
| species | [Species:56210] Drosophila melanogaster |
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No pathways have been reviewed or authored by UniProt:Q95RR8 PAN3 (5433714)
