AAKB1_PIG
ID AAKB1_PIG Reviewed; 122 AA.
AC P80387;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 108.
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;
DE Flags: Fragment;
GN Name=PRKAB1;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE OF 15-120, AND PROTEIN SEQUENCE OF 1-21; 23-86 AND
RP 92-122.
RC 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).
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). Interacts with FNIP1 and FNIP2 (By
CC similarity). {ECO:0000250}.
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. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta subunit
CC family. {ECO:0000305}.
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DR AlphaFoldDB; P80387; -.
DR SMR; P80387; -.
DR STRING; 9823.ENSSSCP00000010503; -.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR PaxDb; P80387; -.
DR eggNOG; KOG1616; Eukaryota.
DR HOGENOM; CLU_070949_2_0_1; -.
DR InParanoid; P80387; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P80387; SS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR10343:SF89; PTHR10343:SF89; 1.
DR Pfam; PF16561; AMPK1_CBM; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Phosphoprotein; Reference proteome.
FT CHAIN <1..>122
FT /note="5'-AMP-activated protein kinase subunit beta-1"
FT /id="PRO_0000204365"
FT REGION 33..>122
FT /note="Glycogen-binding domain"
FT /evidence="ECO:0000250"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P80386"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R078"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y478"
FT CONFLICT 65
FT /note="W -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 122
SQ SEQUENCE 122 AA; 13877 MW; C86CA259EC94A54F CRC64;
ILMDSPEDAD LYHSEEIKAP EKEEFLAWQH DLEVNDKASA QARPTVFRWT GGGKEVYLSG
SFNNWSKLPL TRSHNNFVAI LDLPEGEHQY KFLVDGQWTH DPSEPVVTSQ LGTVNNIIQV
KK
