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UniProt functional annotation for P53010 | ||
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| UniProt code: P53010. |
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| Organism: | |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). |
| Taxonomy: | |
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. |
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| 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 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 by DCP1-DCP2 and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails, trimming the tails from their synthesized length to the slightly shorter, apparently messenger-specific length found on newly exported mRNAs. PAN cooperates with protein kinase DUN1 in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:11239395, ECO:0000269|PubMed:11953437, ECO:0000269|PubMed:1358757, ECO:0000269|PubMed:15630021, ECO:0000269|PubMed:15894541, ECO:0000269|PubMed:24880344, ECO:0000269|PubMed:8550599, ECO:0000269|PubMed:8816488, ECO:0000269|PubMed:9774670}. |
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| Catalytic activity: | |
Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:1358757, ECO:0000269|PubMed:24880344}; |
| Cofactor: | |
Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24880344}; Note=Binds 2 metal cations per subunit in the catalytic exonuclease domain. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24880344}; |
| Activity regulation: | |
Positively regulated by the regulatory subunit PAN3. Negatively regulated by PAB1-binding protein PBP1. Inhibited under stress conditions. Inhibition of deadenylation under stress increases mRNA stability, which may be a mechanism to retain the majority of the cytoplasmic pool of mRNAs for later reuse and recovery from stress. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:15121841, ECO:0000269|PubMed:16940550, ECO:0000269|PubMed:8816488}. |
| Subunit: | |
Forms a heterotrimer with an asymmetric homodimer of the regulatory subunit PAN3 to form the poly(A)-nuclease (PAN) deadenylation complex. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:15169912, ECO:0000269|PubMed:24872509, ECO:0000269|PubMed:24880344, ECO:0000269|PubMed:8816488}. |
| Subcellular location: | |
Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15894541}. |
| 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. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24880344}. |
| Domain: | |
The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3. {ECO:0000255|HAMAP-Rule:MF_03182, ECO:0000269|PubMed:24872509}. |
| Miscellaneous: | |
Present with 1510 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}. |
| Similarity: | |
Belongs to the peptidase C19 family. PAN2 subfamily. {ECO:0000255|HAMAP-Rule:MF_03182}. |
Annotations taken from UniProtKB at the EBI.