AAKB1_RAT
ID AAKB1_RAT Reviewed; 270 AA.
AC P80386; Q63048;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=5'-AMP-activated protein kinase subunit beta-1;
DE Short=AMPK subunit beta-1;
DE Short=AMPKb;
DE AltName: Full=5'-AMP-activated protein kinase 40 kDa subunit;
GN Name=Prkab1;
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 PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8621499; DOI=10.1074/jbc.271.15.8675;
RA Gao G., Fernandez C.S., Stapleton D., Auster A.S., Widmer J., Dyck J.R.B.,
RA Kemp B.E., Witters L.A.;
RT "Non-catalytic beta- and gamma-subunit isoforms of the 5'-AMP-activated
RT protein kinase.";
RL J. Biol. Chem. 271:8675-8681(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=8626596; DOI=10.1074/jbc.271.17.10282;
RA Woods A., Cheung P.C.F., Smith F.C., Davison M.D., Scott J., Beri R.K.,
RA Carling D.;
RT "Characterization of AMP-activated protein kinase beta and gamma subunits.
RT Assembly of the heterotrimeric complex in vitro.";
RL J. Biol. Chem. 271:10282-10290(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-159, AND PROTEIN SEQUENCE OF 36-72; 79-83
RP AND 90-159.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=7961907; DOI=10.1016/s0021-9258(18)43879-3;
RA Stapleton D., Gao G., Michell B.J., Widmer J., Mitchelhill K.I., Teh T.,
RA House C.M., Witters L.A., Kemp B.E.;
RT "Mammalian 5'-AMP-activated protein kinase non-catalytic subunits are
RT homologs of proteins that interact with yeast Snf1 protein kinase.";
RL J. Biol. Chem. 269:29343-29346(1994).
RN [5]
RP PARTIAL PROTEIN SEQUENCE, MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT
RP SER-24; SER-25; SER-108 AND SER-182.
RX PubMed=9305909; DOI=10.1074/jbc.272.39.24475;
RA Mitchelhill K.I., Michell B.J., House C.M., Stapleton D., Dyck J.,
RA Gamble J., Ullrich C., Witters L.A., Kemp B.E.;
RT "Posttranslational modifications of the 5'-AMP-activated protein kinase
RT beta1 subunit.";
RL J. Biol. Chem. 272:24475-24479(1997).
RN [6]
RP MUTAGENESIS, MYRISTOYLATION AT GLY-2, AND PHOSPHORYLATION AT SER-24;
RP SER-25; SER-108 AND SER-182.
RX PubMed=11171104; DOI=10.1042/0264-6021:3540275;
RA Warden S.M., Richardson C., O'Donnell J. Jr., Stapleton D., Kemp B.E.,
RA Witters L.A.;
RT "Post-translational modifications of the beta-1 subunit of AMP-activated
RT protein kinase affect enzyme activity and cellular localization.";
RL Biochem. J. 354:275-283(2001).
RN [7]
RP PHOSPHORYLATION AT SER-96; SER-101 AND SER-108.
RX PubMed=12764152; DOI=10.1074/jbc.m303946200;
RA Woods A., Vertommen D., Neumann D., Turk R., Bayliss J., Schlattner U.,
RA Wallimann T., Carling D., Rider M.H.;
RT "Identification of phosphorylation sites in AMP-activated protein kinase
RT (AMPK) for upstream AMPK kinases and study of their roles by site-directed
RT mutagenesis.";
RL J. Biol. Chem. 278:28434-28442(2003).
RN [8]
RP PHOSPHORYLATION BY ULK1.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40 AND SER-108, AND
RP IDENTIFICATION BY 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).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 68-162 IN COMPLEX WITH
RP BETA-CYCLODEXTRIN, DOMAIN GLYCOGEN-BINDING, AND MUTAGENESIS OF TRP-100;
RP LYS-126; LEU-146 AND ASN-150.
RX PubMed=16216577; DOI=10.1016/j.str.2005.07.008;
RA Polekhina G., Gupta A., van Denderen B.J., Feil S.C., Kemp B.E.,
RA Stapleton D., Parker M.W.;
RT "Structural basis for glycogen recognition by AMP-activated protein
RT kinase.";
RL Structure 13:1453-1462(2005).
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).
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). Interacts with FNIP1 and FNIP2.
CC {ECO:0000269|PubMed:16216577}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, heart, white adipose
CC tissue, lung and spleen.
CC -!- DOMAIN: The glycogen-binding domain may target AMPK to glycogen so that
CC other factors like glycogen-bound debranching enzyme or protein
CC phosphatases can directly affect AMPK activity.
CC {ECO:0000269|PubMed:16216577}.
CC -!- PTM: Phosphorylated when associated with the catalytic subunit (PRKAA1
CC or PRKAA2). Phosphorylated by ULK1; leading to negatively regulate AMPK
CC activity and suggesting the existence of a regulatory feedback loop
CC between ULK1 and AMPK. {ECO:0000269|PubMed:11171104,
CC ECO:0000269|PubMed:12764152, ECO:0000269|PubMed:21460634,
CC ECO:0000269|PubMed:9305909}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
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DR EMBL; U42411; AAC52579.1; -; mRNA.
DR EMBL; BC062008; AAH62008.1; -; mRNA.
DR EMBL; X95577; CAA64830.1; -; mRNA.
DR RefSeq; NP_114182.1; NM_031976.1.
DR RefSeq; XP_006249543.1; XM_006249481.3.
DR PDB; 1Z0M; X-ray; 1.91 A; A/B/C=68-163.
DR PDB; 1Z0N; X-ray; 1.49 A; A/B/C=68-163.
DR PDB; 4EAG; X-ray; 2.70 A; B=187-270.
DR PDB; 4EAK; X-ray; 2.50 A; B=200-270.
DR PDB; 4EAL; X-ray; 2.51 A; B=200-270.
DR PDB; 4QFG; X-ray; 3.46 A; B=68-270.
DR PDB; 4QFR; X-ray; 3.34 A; B=68-270.
DR PDB; 4QFS; X-ray; 3.55 A; B=68-270.
DR PDB; 4YEF; X-ray; 1.72 A; A/B/C/D/E/F/G=76-156.
DR PDB; 5KQ5; X-ray; 3.41 A; B=68-270.
DR PDB; 5T5T; X-ray; 3.46 A; B=68-270.
DR PDB; 5UFU; X-ray; 3.45 A; B=67-270.
DR PDB; 6E4T; X-ray; 3.40 A; B=67-270.
DR PDB; 6E4U; X-ray; 3.27 A; B=67-270.
DR PDB; 6E4W; X-ray; 3.35 A; B=67-270.
DR PDBsum; 1Z0M; -.
DR PDBsum; 1Z0N; -.
DR PDBsum; 4EAG; -.
DR PDBsum; 4EAK; -.
DR PDBsum; 4EAL; -.
DR PDBsum; 4QFG; -.
DR PDBsum; 4QFR; -.
DR PDBsum; 4QFS; -.
DR PDBsum; 4YEF; -.
DR PDBsum; 5KQ5; -.
DR PDBsum; 5T5T; -.
DR PDBsum; 5UFU; -.
DR PDBsum; 6E4T; -.
DR PDBsum; 6E4U; -.
DR PDBsum; 6E4W; -.
DR AlphaFoldDB; P80386; -.
DR SMR; P80386; -.
DR BioGRID; 249839; 243.
DR DIP; DIP-59127N; -.
DR IntAct; P80386; 178.
DR STRING; 10116.ENSRNOP00000001508; -.
DR ChEMBL; CHEMBL3885503; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR iPTMnet; P80386; -.
DR PhosphoSitePlus; P80386; -.
DR jPOST; P80386; -.
DR PaxDb; P80386; -.
DR PRIDE; P80386; -.
DR DNASU; 83803; -.
DR Ensembl; ENSRNOT00000001508; ENSRNOP00000001508; ENSRNOG00000001142.
DR GeneID; 83803; -.
DR KEGG; rno:83803; -.
DR UCSC; RGD:71057; rat.
DR CTD; 5564; -.
DR RGD; 71057; Prkab1.
DR eggNOG; KOG1616; Eukaryota.
DR GeneTree; ENSGT00940000155307; -.
DR HOGENOM; CLU_070949_2_0_1; -.
DR InParanoid; P80386; -.
DR OMA; NDRAPTQ; -.
DR OrthoDB; 956412at2759; -.
DR PhylomeDB; P80386; -.
DR TreeFam; TF313827; -.
DR BRENDA; 2.7.11.31; 5301.
DR Reactome; R-RNO-1632852; Macroautophagy.
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 EvolutionaryTrace; P80386; -.
DR PRO; PR:P80386; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001142; Expressed in heart and 20 other tissues.
DR Genevisible; P80386; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0004672; F:protein kinase activity; ISO: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:0035878; P:nail development; ISO:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
DR GO; GO:0050790; P:regulation of catalytic 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; IPR039160; AMPKB.
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:SF89; PTHR10343:SF89; 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; Direct protein sequencing; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Lipoprotein;
KW Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..270
FT /note="5'-AMP-activated protein kinase subunit beta-1"
FT /id="PRO_0000204367"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..163
FT /note="Glycogen-binding domain"
FT COMPBIAS 11..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 24
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11171104,
FT ECO:0000269|PubMed:9305909"
FT MOD_RES 25
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11171104,
FT ECO:0000269|PubMed:9305909"
FT MOD_RES 40
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12764152"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12764152"
FT MOD_RES 108
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:11171104,
FT ECO:0000269|PubMed:12764152, ECO:0000269|PubMed:9305909,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11171104,
FT ECO:0000269|PubMed:9305909"
FT MOD_RES 201
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9R078"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:11171104,
FT ECO:0000269|PubMed:9305909"
FT MUTAGEN 100
FT /note="W->G: Abolishes glycogen-binding."
FT /evidence="ECO:0000269|PubMed:16216577"
FT MUTAGEN 100
FT /note="W->L: Partially inhibits glycogen-binding."
FT /evidence="ECO:0000269|PubMed:16216577"
FT MUTAGEN 126
FT /note="K->Q: Abolishes glycogen-binding."
FT /evidence="ECO:0000269|PubMed:16216577"
FT MUTAGEN 146
FT /note="L->A: Significantly reduces glycogen-binding."
FT /evidence="ECO:0000269|PubMed:16216577"
FT MUTAGEN 150
FT /note="N->K: Abolishes glycogen-binding."
FT /evidence="ECO:0000269|PubMed:16216577"
FT MUTAGEN 150
FT /note="N->Q: Significantly reduces glycogen-binding."
FT /evidence="ECO:0000269|PubMed:16216577"
FT CONFLICT 26
FT /note="G -> E (in Ref. 1; AAC52579)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="M -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:1Z0N"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:1Z0N"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1Z0N"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:4YEF"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1Z0N"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:1Z0N"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:1Z0N"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:1Z0N"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1Z0N"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:1Z0N"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:6E4U"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1Z0N"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:4QFG"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:6E4U"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6E4U"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6E4U"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6E4U"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:4EAL"
FT STRAND 248..257
FT /evidence="ECO:0007829|PDB:4EAK"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:4EAK"
SQ SEQUENCE 270 AA; 30394 MW; 62726DD357F36C7C CRC64;
MGNTSSERAA LERQAGHKTP RRDSSGGTKD GDRPKILMDS PEDADIFHTE EMKAPEKEEF
LAWQHDLEVN EKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSQN NFVAILDLPE
GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS
SSPPGPYHQE PYISKPEERF KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY
ALSIKDGVMV LSATHRYKKK YVTTLLYKPI
