UniProt functional annotation for P39517



	UniProt functional annotation for P39517

UniProt code: P39517.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1 (PubMed:11780629, PubMed:12032091, PubMed:11696541, PubMed:12730603, PubMed:15703442. PubMed:15706350). Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs (PubMed:15166134). May also have a role in translation and mRNA nuclear export (PubMed:12930949). Required for sporulation (PubMed:12930949). Blocks autophagy in nutrient-rich conditions by, at least partly, binding and repressing the expression of a set of ATG genes, including ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 (PubMed:26098573). {ECO:0000269|PubMed:11696541, ECO:0000269|PubMed:11780629, ECO:0000269|PubMed:12032091, ECO:0000269|PubMed:12730603, ECO:0000269|PubMed:12930949, ECO:0000269|PubMed:15166134, ECO:0000269|PubMed:15703442, ECO:0000269|PubMed:15706350, ECO:0000269|PubMed:26098573}.

Catalytic activity: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000305};

Subunit: Associated with the CCR4-NOT complex and possibly other big complexes (PubMed:9504907, PubMed:12930949). Interacts with CDC39/NOT1 (PubMed:11696541). Interacts with DCP1, LSM1, and POP2 (PubMed:9504907, PubMed:11780629). Interacts with IGO1 (PubMed:20471941). Interacts with PAT1 and with KEM1, the major 5'-3' exonuclease (PubMed:11780629, PubMed:12032091). {ECO:0000269|PubMed:11696541, ECO:0000269|PubMed:11780629, ECO:0000269|PubMed:12032091, ECO:0000269|PubMed:12930949, ECO:0000269|PubMed:20471941, ECO:0000269|PubMed:9504907}.

Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:12032091, ECO:0000269|PubMed:12730603, ECO:0000269|PubMed:12930949, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15706350}.

Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Disruption phenotype: Leads to an increased in autophagy flux (PubMed:26098573). Causes an accumulation of ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 transcripts in nutrient-replete conditions (PubMed:26098573). {ECO:0000269|PubMed:26098573}.

Miscellaneous: Present with 42900 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1 (PubMed:11780629, PubMed:12032091, PubMed:11696541, PubMed:12730603, PubMed:15703442. PubMed:15706350). Is involved in G1/S DNA-damage checkpoint recovery, probably through the regulation of the translational status of a subset of mRNAs (PubMed:15166134). May also have a role in translation and mRNA nuclear export (PubMed:12930949). Required for sporulation (PubMed:12930949). Blocks autophagy in nutrient-rich conditions by, at least partly, binding and repressing the expression of a set of ATG genes, including ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 (PubMed:26098573). {ECO:0000269\|PubMed:11696541, ECO:0000269\|PubMed:11780629, ECO:0000269\|PubMed:12032091, ECO:0000269\|PubMed:12730603, ECO:0000269\|PubMed:12930949, ECO:0000269\|PubMed:15166134, ECO:0000269\|PubMed:15703442, ECO:0000269\|PubMed:15706350, ECO:0000269\|PubMed:26098573}.


Catalytic activity:		Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000305};
Subunit:		Associated with the CCR4-NOT complex and possibly other big complexes (PubMed:9504907, PubMed:12930949). Interacts with CDC39/NOT1 (PubMed:11696541). Interacts with DCP1, LSM1, and POP2 (PubMed:9504907, PubMed:11780629). Interacts with IGO1 (PubMed:20471941). Interacts with PAT1 and with KEM1, the major 5'-3' exonuclease (PubMed:11780629, PubMed:12032091). {ECO:0000269\|PubMed:11696541, ECO:0000269\|PubMed:11780629, ECO:0000269\|PubMed:12032091, ECO:0000269\|PubMed:12930949, ECO:0000269\|PubMed:20471941, ECO:0000269\|PubMed:9504907}.
Subcellular location:		Cytoplasm, P-body {ECO:0000269\|PubMed:12032091, ECO:0000269\|PubMed:12730603, ECO:0000269\|PubMed:12930949, ECO:0000269\|PubMed:14562095, ECO:0000269\|PubMed:15706350}.
Domain:		The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Disruption phenotype:		Leads to an increased in autophagy flux (PubMed:26098573). Causes an accumulation of ATG3, ATG7, ATG8, ATG19, ATG20, ATG22 and SNX4/ATG24 transcripts in nutrient-replete conditions (PubMed:26098573). {ECO:0000269\|PubMed:26098573}.
Miscellaneous:		Present with 42900 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the DEAD box helicase family. DDX6/DHH1 subfamily. {ECO:0000305}.