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HAMAP rule MF_03181

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General rule information [?]

Accession MF_03181
Dates 21-FEB-2014 (Created)
19-NOV-2022 (Last updated, Version 8)
Name PAN3
Scope(s) Eukaryota
Template(s) Q7SDP4 (PAN3_NEUCR); P36102 (PAN3_YEAST); Q58A45 (PAN3_HUMAN); Q95RR8 (PAN3_DROME); G0S0Y3 (PAN3_CHATD); [ Recover all ]
Triggered by HAMAP; MF_03181 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier PAN3
Protein name RecName: Full=PAN2-PAN3 deadenylation complex subunit PAN3;
AltName: Full=PAB1P-dependent poly(A)-specific ribonuclease;
AltName: Full=Poly(A)-nuclease deadenylation complex subunit 3;
                 Short=PAN deadenylation complex subunit 3;
Gene name Name=PAN3;

Comments [?]

case <OC:Metazoa>
FUNCTIONRegulatory 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. 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.
else case <OC:Fungi>
FUNCTIONRegulatory 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. @gn(PAN3) acts as a positive regulator for PAN activity, recruiting the catalytic subunit @gn(PAN2) to mRNA via its interaction with RNA and with @gn(PAB1).
else
FUNCTIONRegulatory 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. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP.
end case
case <OC:Vertebrata>
SUBUNITHomodimer. Forms a heterotrimer with a catalytic subunit @gn(PAN2) to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein @gn(PABPC1) (via PABC domain), conferring substrate specificity of the enzyme complex. Interacts with the GW182 family proteins @gn(TNRC6A), @gn(TNRC6B) and @gn(TNRC6C).
else case <OC:Metazoa>
SUBUNITHomodimer. Forms a heterotrimer with a catalytic subunit @gn(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.
else case <OC:Fungi>
SUBUNITHomodimer. Forms a heterotrimer with a catalytic subunit @gn(PAN2) to form the poly(A)-nuclease (PAN) deadenylation complex. Interacts (via PAM-2 motif) with poly(A)-binding protein @gn(PAB1) (via PABC domain), conferring substrate specificity of the enzyme complex.
else
SUBUNITHomodimer. 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.
end case
case <OC:Metazoa>
SUBCELLULAR LOCATIONCytoplasm, P-body.
else
SUBCELLULAR LOCATIONCytoplasm.
end case
DOMAINThe N-terminal zinc finger binds to poly(A) RNA.
DOMAINContains 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 @gn(PAN2) nuclease in vitro. The nucleotide-binding site is juxtaposed to the RNase active site of @gn(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.
DOMAINThe 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 @gn(PAN2).
SIMILARITYBelongs to the protein kinase superfamily. PAN3 family.

Keywords [?]


Gene Ontology [?]

case <OCellular component:Metazoa>
GO:0000932; Cellular component:P-body
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
case <Feature:PS50103>
GO:0046872; Molecular function:metal ion binding
end case
GO:0031251; Cellular component:PAN complex
GO:0005524; Molecular function:ATP binding
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 PS50011; PROTEIN_KINASE_DOM; 0-1;
PROSITE PS50103; ZF_C3H1; 0-1;
Pfam PF00069; Pkinase; 1;

Features [?]

From: PAN3_HUMAN (Q58A45)
Key From To Description Tag Condition FTGroup
case <OC:Mammalia>
MOTIF 284 299 /note="PABPC-interacting motif-2 (PAM-2)" x(9)-F-x-P-x(4)
end case
From: PAN3_YEAST (P36102)
Key From To Description Tag Condition FTGroup
case <OC:Fungi>
MOTIF 143 163 /note="PABPC-interacting motif-2 (PAM-2)" x(13)-F-x-P-x(5)
end case
REGION 275 548 /note="Pseudokinase domain"
REGION 588 Cter /note="Knob domain"
COILED 549 587
From: PAN3_NEUCR (Q7SDP4)
Key From To Description Tag Condition FTGroup
BINDING 352 359 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[DE]-[YF]-[HYF]-[PA]-x(3)-[ST]
BINDING 412 413 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
x-K
BINDING 302 302 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"
[RK]

Additional information [?]

Size range 589-887 amino acids
Related rules None
Fusion Nter: None Cter: None



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