AAKG_SCHPO
ID AAKG_SCHPO Reviewed; 334 AA.
AC Q10343; Q9UTJ1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=5'-AMP-activated protein kinase subunit gamma;
DE Short=AMPK gamma;
DE Short=AMPK subunit gamma;
GN Name=cbs2; ORFNames=SPAC1556.08c, SPAC1F12.01c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3] {ECO:0007744|PDB:2OOX, ECO:0007744|PDB:2OOY}
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 3-334 IN COMPLEXES WITH AMP AND
RP ATP, AND SUBUNIT.
RX PubMed=17289942; DOI=10.1126/science.1137503;
RA Townley R., Shapiro L.;
RT "Crystal structures of the adenylate sensor from fission yeast AMP-
RT activated protein kinase.";
RL Science 315:1726-1729(2007).
RN [4] {ECO:0007744|PDB:2QR1, ECO:0007744|PDB:2QRC, ECO:0007744|PDB:2QRD, ECO:0007744|PDB:2QRE}
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 3-334 IN COMPLEXES WITH ADP; AMP
RP AND ATP.
RX PubMed=17937917; DOI=10.1016/j.str.2007.07.017;
RA Jin X., Townley R., Shapiro L.;
RT "Structural insight into AMPK regulation: ADP comes into play.";
RL Structure 15:1285-1295(2007).
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 (ssp2) 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 (ssp2), a
CC beta (amk2) and a gamma non-catalytic subunits (cbs2). Forms a dimer of
CC trimers. {ECO:0000269|PubMed:17289942}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}.
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:0000269|PubMed:17289942,
CC ECO:0000269|PubMed:17937917}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC subunit family. {ECO:0000305}.
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DR EMBL; CU329670; CAB61219.1; -; Genomic_DNA.
DR PIR; T38059; S67444.
DR PIR; T50087; T50087.
DR RefSeq; XP_001713093.1; XM_001713041.2.
DR PDB; 2OOX; X-ray; 2.60 A; E/G=3-334.
DR PDB; 2OOY; X-ray; 2.88 A; E/G=3-334.
DR PDB; 2QR1; X-ray; 2.70 A; E/G=3-334.
DR PDB; 2QRC; X-ray; 2.70 A; E/G=3-334.
DR PDB; 2QRD; X-ray; 2.41 A; E/G=3-334.
DR PDB; 2QRE; X-ray; 3.01 A; E/G=3-334.
DR PDBsum; 2OOX; -.
DR PDBsum; 2OOY; -.
DR PDBsum; 2QR1; -.
DR PDBsum; 2QRC; -.
DR PDBsum; 2QRD; -.
DR PDBsum; 2QRE; -.
DR AlphaFoldDB; Q10343; -.
DR SMR; Q10343; -.
DR BioGRID; 858067; 28.
DR DIP; DIP-29522N; -.
DR IntAct; Q10343; 2.
DR STRING; 4896.SPAC1556.08c.1; -.
DR SwissPalm; Q10343; -.
DR MaxQB; Q10343; -.
DR PaxDb; Q10343; -.
DR EnsemblFungi; SPAC1556.08c.1; SPAC1556.08c.1:pep; SPAC1556.08c.
DR PomBase; SPAC1556.08c; cbs2.
DR VEuPathDB; FungiDB:SPAC1556.08c; -.
DR eggNOG; KOG1764; Eukaryota.
DR HOGENOM; CLU_021740_1_0_1; -.
DR InParanoid; Q10343; -.
DR OMA; ACVKMLE; -.
DR PhylomeDB; Q10343; -.
DR Reactome; R-SPO-1632852; Macroautophagy.
DR Reactome; R-SPO-163680; AMPK inhibits chREBP transcriptional activation activity.
DR Reactome; R-SPO-200425; Carnitine metabolism.
DR Reactome; R-SPO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR Reactome; R-SPO-5628897; TP53 Regulates Metabolic Genes.
DR EvolutionaryTrace; Q10343; -.
DR PRO; PR:Q10343; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0016208; F:AMP binding; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IDA:PomBase.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:PomBase.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0042149; P:cellular response to glucose starvation; IBA:GO_Central.
DR GO; GO:0010514; P:induction of conjugation with cellular fusion; EXP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0050790; P:regulation of catalytic activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:PomBase.
DR GO; GO:0007165; P:signal transduction; NAS:PomBase.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; CBS domain; Cytoplasm;
KW Nucleotide-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..334
FT /note="5'-AMP-activated protein kinase subunit gamma"
FT /id="PRO_0000204390"
FT DOMAIN 29..89
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 115..177
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 187..247
FT /note="CBS 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 262..319
FT /note="CBS 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 35
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 141
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 141
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOX"
FT BINDING 141
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2OOY"
FT BINDING 142
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 162..165
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 191
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 191
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOX"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOY"
FT BINDING 196
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 196
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOX"
FT BINDING 196
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOY"
FT BINDING 217..218
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 217..218
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOX"
FT BINDING 217..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOY"
FT BINDING 287..289
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0000269|PubMed:17937917, ECO:0007744|PDB:2OOY"
FT BINDING 303..308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOY"
FT BINDING 305..308
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:17937917,
FT ECO:0007744|PDB:2QR1"
FT BINDING 305..308
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:17289942,
FT ECO:0007744|PDB:2OOX"
FT HELIX 4..21
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 24..27
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:2QRD"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 128..137
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:2QRD"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 184..186
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 204..214
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:2OOX"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:2OOX"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 306..314
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:2OOX"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2OOX"
SQ SEQUENCE 334 AA; 37427 MW; 8D32CC6CE53F7916 CRC64;
MTDVQETQKG ALKEIQAFIR SRTSYDVLPT SFRLIVFDVT LFVKTSLSLL TLNNIVSAPL
WDSEANKFAG LLTMADFVNV IKYYYQSSSF PEAIAEIDKF RLLGLREVER KIGAIPPETI
YVHPMHSLMD ACLAMSKSRA RRIPLIDVDG ETGSEMIVSV LTQYRILKFI SMNCKETAML
RVPLNQMTIG TWSNLATASM ETKVYDVIKM LAEKNISAVP IVNSEGTLLN VYESVDVMHL
IQDGDYSNLD LSVGEALLKR PANFDGVHTC RATDRLDGIF DAIKHSRVHR LFVVDENLKL
EGILSLADIL NYIIYDKTTT PGVPEQTDNF ESAV
