UniProt functional annotation for Q10343



	UniProt functional annotation for Q10343

UniProt code: Q10343.

Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.

Function: Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer- term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (ssp2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. {ECO:0000250|UniProtKB:P12904}.

Subunit: AMPK is a heterotrimer of an alpha catalytic subunit (ssp2), a beta (amk2) and a gamma non-catalytic subunits (cbs2). Forms a dimer of trimers. {ECO:0000269|PubMed:17289942}.

Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.

Domain: The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 2 are occupied, designated as sites 2 (or A), and 3 (or B) based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP 2). Site 2 binds specifically ADP (ADP 1) and is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of ADP. {ECO:0000269|PubMed:17289942, ECO:0000269|PubMed:17937917}.

Similarity: Belongs to the 5'-AMP-activated protein kinase gamma subunit family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.



Function:		Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer- term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (ssp2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. {ECO:0000250\|UniProtKB:P12904}.


Subunit:		AMPK is a heterotrimer of an alpha catalytic subunit (ssp2), a beta (amk2) and a gamma non-catalytic subunits (cbs2). Forms a dimer of trimers. {ECO:0000269\|PubMed:17289942}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:16823372}. Cytoplasm {ECO:0000269\|PubMed:16823372}.
Domain:		The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 2 are occupied, designated as sites 2 (or A), and 3 (or B) based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP 2). Site 2 binds specifically ADP (ADP 1) and is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of ADP. {ECO:0000269\|PubMed:17289942, ECO:0000269\|PubMed:17937917}.
Similarity:		Belongs to the 5'-AMP-activated protein kinase gamma subunit family. {ECO:0000305}.