AAKB_SCHPO
ID AAKB_SCHPO Reviewed; 298 AA.
AC P78789; Q1L851; Q9UU43;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=5'-AMP-activated protein kinase subunit beta;
DE Short=AMPK subunit beta;
GN Name=amk2; ORFNames=SPCC1919.03c {ECO:0000312|PomBase:SPCC1919.03c};
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 MRNA].
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 97-117.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 203-298, 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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) OF 203-298 IN COMPLEX WITH ADP.
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: Beta subunit of AMP-activated protein kinase (AMPK), which is
CC required for transcriptional, metabolic, and developmental adaptations
CC in response to glucose limitation. Has a structural role, mediating
CC heterotrimer formation, and a regulatory role, defining carbon source-
CC regulated subcellular location and substrate specificity of the AMPK
CC kinase complex. {ECO:0000250|UniProtKB:P34164}.
CC -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (ssp2), a
CC beta (amk2) and a gamma non-catalytic subunits (cbs2). The beta subunit
CC serves as a bridge between the catalytic and the regulatory subunit.
CC {ECO:0000250|UniProtKB:P34164}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13800.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D89138; BAA13800.1; ALT_INIT; mRNA.
DR EMBL; CU329672; CAA22634.1; -; Genomic_DNA.
DR EMBL; AB027823; BAA87127.1; -; Genomic_DNA.
DR PIR; T41228; T41228.
DR PIR; T42415; T42415.
DR RefSeq; NP_588485.1; NM_001023476.2.
DR PDB; 2OOX; X-ray; 2.60 A; B/D=203-298.
DR PDB; 2OOY; X-ray; 2.88 A; B/D=203-298.
DR PDB; 2QR1; X-ray; 2.70 A; B/D=203-298.
DR PDB; 2QRC; X-ray; 2.70 A; B/D=203-298.
DR PDB; 2QRD; X-ray; 2.41 A; B/D=203-298.
DR PDB; 2QRE; X-ray; 3.01 A; B/D=203-298.
DR PDBsum; 2OOX; -.
DR PDBsum; 2OOY; -.
DR PDBsum; 2QR1; -.
DR PDBsum; 2QRC; -.
DR PDBsum; 2QRD; -.
DR PDBsum; 2QRE; -.
DR AlphaFoldDB; P78789; -.
DR SMR; P78789; -.
DR BioGRID; 275702; 631.
DR DIP; DIP-29521N; -.
DR IntAct; P78789; 2.
DR STRING; 4896.SPCC1919.03c.1; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; P78789; -.
DR SwissPalm; P78789; -.
DR MaxQB; P78789; -.
DR PaxDb; P78789; -.
DR PRIDE; P78789; -.
DR EnsemblFungi; SPCC1919.03c.1; SPCC1919.03c.1:pep; SPCC1919.03c.
DR GeneID; 2539130; -.
DR KEGG; spo:SPCC1919.03c; -.
DR PomBase; SPCC1919.03c; amk2.
DR VEuPathDB; FungiDB:SPCC1919.03c; -.
DR eggNOG; KOG1616; Eukaryota.
DR HOGENOM; CLU_070949_2_1_1; -.
DR InParanoid; P78789; -.
DR OMA; PPHKPWE; -.
DR PhylomeDB; P78789; -.
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; P78789; -.
DR PRO; PR:P78789; -.
DR Proteomes; UP000002485; Chromosome III.
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:0005886; C:plasma membrane; ISO:PomBase.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0019887; F:protein kinase regulator activity; ISO:PomBase.
DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; IC:PomBase.
DR GO; GO:0010514; P:induction of conjugation with cellular fusion; EXP:PomBase.
DR GO; GO:0045859; P:regulation of protein kinase activity; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR032640; AMPK1_CBM.
DR InterPro; IPR006828; ASC_dom.
DR InterPro; IPR037256; ASC_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR030077; SIP2/GAL83.
DR PANTHER; PTHR10343:SF84; PTHR10343:SF84; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR Pfam; PF04739; AMPKBI; 1.
DR SMART; SM01010; AMPKBI; 1.
DR SUPFAM; SSF160219; SSF160219; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Reference proteome.
FT CHAIN 1..298
FT /note="5'-AMP-activated protein kinase subunit beta"
FT /id="PRO_0000339125"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250..252
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with subunit gamma"
FT /evidence="ECO:0007744|PDB:2QR1, ECO:0007744|PDB:2QRC,
FT ECO:0007744|PDB:2QRD"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2OOX"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:2QR1"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:2QRD"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:2OOX"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 271..283
FT /evidence="ECO:0007829|PDB:2QRD"
FT STRAND 286..294
FT /evidence="ECO:0007829|PDB:2QRD"
SQ SEQUENCE 298 AA; 32970 MW; B9D5A078C166E730 CRC64;
MGNVQSQEGE TRAHAVPSQD ATTTPDNANN VPKEPRAQSM ISIAADDLNQ EGEMSDDNQQ
EGGNNRTSQN GTSGSSGHTK RRSQTSGKKT HQPYSGPCVP TIIRWRGGGE VVYVTGSFSR
WKKKIQLLKS EDYTVLLQLR PGTQRFKFLV DGIWCCSSDF PTATDAEGNL YNYLEVEANE
KLGASIDERL SQVHTDLPME EKSESEQYST EIPAFLTSNT LQELKLPKPP SLPPHLEKCI
LNSNTAYKED QSVLPNPNHV LLNHLAAANT QLGVLALSAT TRYHRKYVTT AMFKNFDV
