ID   AAKB2_RAT               Reviewed;         271 AA.
AC   Q9QZH4;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 139.
DE   RecName: Full=5'-AMP-activated protein kinase subunit beta-2;
DE            Short=AMPK subunit beta-2;
GN   Name=Prkab2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT SER-183.
RC   STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle;
RX   PubMed=10544261; DOI=10.1016/s0014-5793(99)01371-x;
RA   Chen Z., Heierhorst J., Mann R.J., Mitchelhill K.I., Michell B.J.,
RA   Witters L.A., Lynch G.S., Kemp B.E., Stapleton D.;
RT   "Expression of the AMP-activated protein kinase beta1 and beta2 subunits in
RT   skeletal muscle.";
RL   FEBS Lett. 460:343-348(1999).
RN   [2]
RP   PHOSPHORYLATION BY ULK1 AND ULK2, AND PHOSPHORYLATION AT SER-38; THR-39;
RP   SER-68 AND SER-173.
RX   PubMed=21460634; DOI=10.4161/auto.7.7.15451;
RA   Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
RA   Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
RT   "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory
RT   feedback loop.";
RL   Autophagy 7:696-706(2011).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Non-catalytic subunit of AMP-activated protein kinase (AMPK),
CC       an energy sensor protein kinase that plays a key role in regulating
CC       cellular energy metabolism. In response to reduction of intracellular
CC       ATP levels, AMPK activates energy-producing pathways and inhibits
CC       energy-consuming processes: inhibits protein, carbohydrate and lipid
CC       biosynthesis, as well as cell growth and proliferation. AMPK acts via
CC       direct phosphorylation of metabolic enzymes, and by longer-term effects
CC       via phosphorylation of transcription regulators. Also acts as a
CC       regulator of cellular polarity by remodeling the actin cytoskeleton;
CC       probably by indirectly activating myosin. Beta non-catalytic subunit
CC       acts as a scaffold on which the AMPK complex assembles, via its C-
CC       terminus that bridges alpha (PRKAA1 or PRKAA2) and gamma subunits
CC       (PRKAG1, PRKAG2 or PRKAG3) (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1
CC       or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic
CC       subunits (PRKAG1, PRKAG2 or PRKAG3). {ECO:0000250}.
CC   -!- PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1
CC       or PRKAA2). Phosphorylated by ULK1 and ULK2; leading to negatively
CC       regulate AMPK activity and suggesting the existence of a regulatory
CC       feedback loop between ULK1, ULK2 and AMPK.
CC       {ECO:0000269|PubMed:10544261, ECO:0000269|PubMed:21460634}.
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC       family. {ECO:0000305}.
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DR   EMBL; AF182717; AAF01293.1; -; mRNA.
DR   RefSeq; NP_072149.1; NM_022627.2.
DR   PDB; 2LU3; NMR; -; A=67-163.
DR   PDB; 2LU4; NMR; -; A=67-163.
DR   PDB; 4Y0G; X-ray; 1.60 A; A/B=74-155.
DR   PDB; 4YEE; X-ray; 2.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=74-155.
DR   PDBsum; 2LU3; -.
DR   PDBsum; 2LU4; -.
DR   PDBsum; 4Y0G; -.
DR   PDBsum; 4YEE; -.
DR   AlphaFoldDB; Q9QZH4; -.
DR   BMRB; Q9QZH4; -.
DR   SMR; Q9QZH4; -.
DR   STRING; 10116.ENSRNOP00000069519; -.
DR   BindingDB; Q9QZH4; -.
DR   ChEMBL; CHEMBL4523617; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   iPTMnet; Q9QZH4; -.
DR   PhosphoSitePlus; Q9QZH4; -.
DR   PaxDb; 10116-ENSRNOP00000062137; -.
DR   DNASU; 64562; -.
DR   GeneID; 64562; -.
DR   KEGG; rno:64562; -.
DR   AGR; RGD:620905; -.
DR   CTD; 5565; -.
DR   RGD; 620905; Prkab2.
DR   eggNOG; KOG1616; Eukaryota.
DR   InParanoid; Q9QZH4; -.
DR   OrthoDB; 120305at2759; -.
DR   PhylomeDB; Q9QZH4; -.
DR   BRENDA; 2.7.11.31; 5301.
DR   Reactome; R-RNO-1632852; Macroautophagy.
DR   Reactome; R-RNO-163680; AMPK inhibits chREBP transcriptional activation activity.
DR   Reactome; R-RNO-200425; Carnitine metabolism.
DR   Reactome; R-RNO-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
DR   Reactome; R-RNO-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-RNO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR   PRO; PR:Q9QZH4; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:RGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR   GO; GO:0031669; P:cellular response to nutrient levels; ISO:RGD.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd02859; E_set_AMPKbeta_like_N; 1.
DR   Gene3D; 6.20.250.60; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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   PANTHER; PTHR10343; 5'-AMP-ACTIVATED PROTEIN KINASE , BETA SUBUNIT; 1.
DR   PANTHER; PTHR10343:SF92; 5'-AMP-ACTIVATED PROTEIN KINASE SUBUNIT BETA-2; 1.
DR   Pfam; PF16561; AMPK1_CBM; 1.
DR   Pfam; PF04739; AMPKBI; 1.
DR   SMART; SM01010; AMPKBI; 1.
DR   SUPFAM; SSF160219; AMPKBI-like; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Phosphoprotein; Reference proteome.
FT   CHAIN           1..271
FT                   /note="5'-AMP-activated protein kinase subunit beta-2"
FT                   /id="PRO_0000204370"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..37
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         38
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000269|PubMed:21460634,
FT                   ECO:0007744|PubMed:22673903"
FT   MOD_RES         39
FT                   /note="Phosphothreonine; by ULK1"
FT                   /evidence="ECO:0000269|PubMed:21460634"
FT   MOD_RES         68
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000269|PubMed:21460634"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43741"
FT   MOD_RES         107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43741"
FT   MOD_RES         147
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O43741"
FT   MOD_RES         157
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43741"
FT   MOD_RES         169
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43741"
FT   MOD_RES         173
FT                   /note="Phosphoserine; by ULK1"
FT                   /evidence="ECO:0000269|PubMed:21460634"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:10544261"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:2LU4"
FT   STRAND          76..82
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   STRAND          89..93
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   HELIX           94..96
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   STRAND          110..117
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   STRAND          119..128
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   STRAND          131..133
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:2LU3"
FT   STRAND          140..142
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   STRAND          148..154
FT                   /evidence="ECO:0007829|PDB:4Y0G"
FT   STRAND          157..160
FT                   /evidence="ECO:0007829|PDB:2LU3"
SQ   SEQUENCE   271 AA;  30227 MW;  D881451A03287BEA CRC64;
     MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS KLPGDKEFVP
     WQQDLDDSVK PTQQARPTVI RWSEGGKEVF ISGSFNNWST KIPLIKSHND FVAILDLPEG
     EHQYKFFVDG QWVHDPSEPV VTSQLGTINN LIHVKKSDFE VFDALKLDSM ESSETSCRDL
     SSSPPGPYGQ EMYVFRSEER FKSPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL
     YALSTKDSVM VLSATHRYKK KYVTTLLYKP I
//