AAKG_KLULA
ID AAKG_KLULA Reviewed; 328 AA.
AC Q9P869; Q6CKG9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=5'-AMP-activated protein kinase subunit gamma;
DE Short=AMPK gamma;
DE Short=AMPK subunit gamma;
DE AltName: Full=Nuclear protein SNF4;
GN Name=SNF4; OrderedLocusNames=KLLA0F10769g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Tomasini L., Ferrero I., Goffrini P.;
RT "Molecular characterization of KlSNF4 gene.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Adenine nucleotides-binding subunit gamma of AMP-activated
CC protein kinase (AMPK), an energy sensor protein kinase that plays a key
CC role in regulating cellular energy metabolism. In response to reduction
CC of intracellular ATP levels, AMPK activates energy-producing pathways
CC and inhibits energy-consuming processes: inhibits protein, carbohydrate
CC and lipid biosynthesis, as well as cell growth and proliferation. AMPK
CC acts via direct phosphorylation of metabolic enzymes, and by longer-
CC term effects via phosphorylation of transcription regulators. Gamma
CC non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to
CC activate or inhibit AMPK: AMP-binding results in allosteric activation
CC of alpha catalytic subunit (SNF1) both by inducing phosphorylation and
CC preventing dephosphorylation of catalytic subunits.
CC {ECO:0000250|UniProtKB:P12904}.
CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit, a beta
CC and a gamma non-catalytic subunits. {ECO:0000250|UniProtKB:P12904}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12904}. Cytoplasm
CC {ECO:0000250|UniProtKB:P12904}.
CC -!- DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4
CC potential nucleotide-binding sites, 2 are occupied, designated as sites
CC 2 (or A), and 3 (or B) based on the CBS modules that provide the acidic
CC residue for coordination with the 2'- and 3'-hydroxyl groups of the
CC ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP
CC 2). Site 2 binds specifically ADP (ADP 1) and is likely to be
CC responsible for protection of a conserved threonine in the activation
CC loop of the alpha catalytic subunit through conformational changes
CC induced by binding of ADP. {ECO:0000250|UniProtKB:Q10343}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC subunit family. {ECO:0000305}.
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DR EMBL; AJ277480; CAB89520.1; -; Genomic_DNA.
DR EMBL; CR382126; CAG98278.1; -; Genomic_DNA.
DR RefSeq; XP_455570.1; XM_455570.1.
DR AlphaFoldDB; Q9P869; -.
DR SMR; Q9P869; -.
DR STRING; 28985.XP_455570.1; -.
DR EnsemblFungi; CAG98278; CAG98278; KLLA0_F10769g.
DR GeneID; 2895004; -.
DR KEGG; kla:KLLA0_F10769g; -.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_021740_1_0_1; -.
DR InParanoid; Q9P869; -.
DR OMA; TCSEDDR; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005641; C:nuclear envelope lumen; IEA:EnsemblFungi.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:EnsemblFungi.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR GO; GO:0016208; F:AMP binding; IEA:EnsemblFungi.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:EnsemblFungi.
DR GO; GO:0006914; P:autophagy; IEA:EnsemblFungi.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0030447; P:filamentous growth; IEA:EnsemblFungi.
DR GO; GO:0007031; P:peroxisome organization; IEA:EnsemblFungi.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:EnsemblFungi.
DR GO; GO:2000217; P:regulation of invasive growth in response to glucose limitation; IEA:EnsemblFungi.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR Gene3D; 3.10.580.10; -; 2.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR Pfam; PF00571; CBS; 2.
DR SMART; SM00116; CBS; 4.
DR SUPFAM; SSF54631; SSF54631; 2.
DR PROSITE; PS51371; CBS; 4.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; CBS domain; Cytoplasm;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..328
FT /note="5'-AMP-activated protein kinase subunit gamma"
FT /id="PRO_0000204388"
FT DOMAIN 42..103
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 123..186
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 199..259
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 268..328
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 47
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 150
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 150
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 151
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 171..174
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 227..228
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 227..228
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 227..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 297..299
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 313..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 315..318
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT BINDING 315..318
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:Q10343"
FT CONFLICT 283..284
FT /note="ND -> KH (in Ref. 1; CAB89520)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 328 AA; 37127 MW; B12ED3F8518D927E CRC64;
MPASSDKLQP KDQQTIELEQ KLAVQSIRVF LQSKTSYDVL PVSYRLIVLD TSLLVKKSLN
ILLQNNVVSA PLWDAQTSKF AGLLTSSDFI NVIQYYFHNP DKFELVDKLQ LNGLKDIERA
IGIQPYDTRS IHPFRPLYEA CVKMIESRSR RIPLIDQDEE TQREIVVSVL TQYRILKFVA
LNCKEIRYLK RPLRELDIIS TNNIMSCQMS TPVIDVIQLL TLAGGVSSVP IVDEQGKLVN
VYEAVDVLGL IKGGIYNDLS LSVGEALMRR SDDFEGVFTC TENDKLSSIL DTVRKSRVHR
FFVVDSNGFL TGVLTLSDIL KYILFAES
