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5'-AMP-activated protein kinase subunit gamma-1 (AMPK gamma1) (AMPK subunit gamma-1) (AMPKg)

 AAKG1_BOVIN             Reviewed;         330 AA.
P58108; Q29RZ6;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
13-JUN-2006, sequence version 2.
30-AUG-2017, entry version 83.
RecName: Full=5'-AMP-activated protein kinase subunit gamma-1;
Short=AMPK gamma1;
Short=AMPK subunit gamma-1;
Short=AMPKg;
Name=PRKAG1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Benkel B., Kollers S., Fries R., Sazanov A., Yoshida E., Davoren J.,
Hickey D.;
"Characterization of the bovine AMPK gamma-1 gene.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=16305752; DOI=10.1186/1471-2164-6-166;
Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
"Characterization of 954 bovine full-CDS cDNA sequences.";
BMC Genomics 6:166-166(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Uterus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: AMP/ATP-binding subunit of AMP-activated protein kinase
(AMPK), an energy sensor protein kinase that plays a key role in
regulating cellular energy metabolism. In response to reduction of
intracellular ATP levels, AMPK activates energy-producing pathways
and inhibits energy-consuming processes: inhibits protein,
carbohydrate and lipid biosynthesis, as well as cell growth and
proliferation. AMPK acts via direct phosphorylation of metabolic
enzymes, and by longer-term effects via phosphorylation of
transcription regulators. Also acts as a regulator of cellular
polarity by remodeling the actin cytoskeleton; probably by
indirectly activating myosin. Gamma non-catalytic subunit mediates
binding to AMP, ADP and ATP, leading to activate or inhibit AMPK:
AMP-binding results in allosteric activation of alpha catalytic
subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and
preventing dephosphorylation of catalytic subunits. ADP also
stimulates phosphorylation, without stimulating already
phosphorylated catalytic subunit. ATP promotes dephosphorylation
of catalytic subunit, rendering the AMPK enzyme inactive (By
similarity). {ECO:0000250}.
-!- SUBUNIT: AMPK is a heterotrimer of an alpha catalytic subunit
(PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-
catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with
FNIP1 and FNIP2 (By similarity). {ECO:0000250}.
-!- DOMAIN: The AMPK pseudosubstrate motif resembles the sequence
around sites phosphorylated on target proteins of AMPK, except the
presence of a non-phosphorylatable residue in place of Ser. In the
absence of AMP this pseudosubstrate sequence may bind to the
active site groove on the alpha subunit (PRKAA1 or PRKAA2),
preventing phosphorylation by the upstream activating kinase
STK11/LKB1 (By similarity). {ECO:0000250}.
-!- DOMAIN: The 4 CBS domains mediate binding to nucleotides. Of the 4
potential nucleotide-binding sites, 3 are occupied, designated as
sites 1, 3, and 4 based on the CBS modules that provide the acidic
residue for coordination with the 2'- and 3'-hydroxyl groups of
the ribose of AMP. Of these, site 4 appears to be a structural
site that retains a tightly held AMP molecule (AMP 3). The 2
remaining sites, 1 and 3, can bind either AMP, ADP or ATP. Site 1
(AMP, ADP or ATP 1) is the high-affinity binding site and likely
accommodates AMP or ADP. Site 3 (AMP, ADP or ATP 2) is the weakest
nucleotide-binding site on the gamma subunit, yet it is
exquisitely sensitive to changes in nucleotide levels and this
allows AMPK to respond rapidly to changes in cellular energy
status. Site 3 is likely to be responsible for protection of a
conserved threonine in the activation loop of the alpha catalytic
subunit through conformational changes induced by binding of AMP
or ADP. {ECO:0000250|UniProtKB:P80385}.
-!- PTM: Phosphorylated by ULK1 and ULK2; leading to negatively
regulate AMPK activity and suggesting the existence of a
regulatory feedback loop between ULK1, ULK2 and AMPK.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
subunit family. {ECO:0000305}.
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EMBL; AF329081; AAK19307.1; -; Genomic_DNA.
EMBL; BT025456; ABF57412.1; -; mRNA.
EMBL; BC113296; AAI13297.1; -; mRNA.
RefSeq; NP_777011.2; NM_174586.2.
UniGene; Bt.5588; -.
ProteinModelPortal; P58108; -.
SMR; P58108; -.
STRING; 9913.ENSBTAP00000043459; -.
PaxDb; P58108; -.
PRIDE; P58108; -.
GeneID; 282324; -.
KEGG; bta:282324; -.
CTD; 5571; -.
eggNOG; KOG1764; Eukaryota.
eggNOG; COG0517; LUCA.
HOGENOM; HOG000176880; -.
HOVERGEN; HBG050431; -.
InParanoid; P58108; -.
KO; K07200; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:AgBase.
GO; GO:0043531; F:ADP binding; ISS:UniProtKB.
GO; GO:0016208; F:AMP binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006468; P:protein phosphorylation; IEA:GOC.
InterPro; IPR000644; CBS_dom.
Pfam; PF00571; CBS; 3.
SMART; SM00116; CBS; 4.
PROSITE; PS51371; CBS; 4.
2: Evidence at transcript level;
ATP-binding; CBS domain; Complete proteome; Fatty acid biosynthesis;
Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 330 5'-AMP-activated protein kinase subunit
gamma-1.
/FTId=PRO_0000204376.
DOMAIN 43 103 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 125 187 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 198 260 CBS 3. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 272 329 CBS 4. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
NP_BIND 87 90 AMP, ADP or ATP 1.
{ECO:0000250|UniProtKB:P80385}.
NP_BIND 151 152 AMP, ADP or ATP 1.
{ECO:0000250|UniProtKB:P80385}.
NP_BIND 226 227 AMP 3. {ECO:0000250|UniProtKB:P80385}.
NP_BIND 242 245 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
NP_BIND 298 299 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
NP_BIND 314 317 AMP 3. {ECO:0000250|UniProtKB:P80385}.
MOTIF 138 159 AMPK pseudosubstrate.
BINDING 70 70 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
BINDING 130 130 AMP, ADP or ATP 1; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P80385}.
BINDING 151 151 AMP 3. {ECO:0000250|UniProtKB:P80385}.
BINDING 170 170 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
BINDING 200 200 AMP 3. {ECO:0000250|UniProtKB:P80385}.
BINDING 205 205 AMP 3; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:P80385}.
BINDING 269 269 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
BINDING 277 277 AMP, ADP or ATP 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P80385}.
BINDING 298 298 AMP 3. {ECO:0000250|UniProtKB:P80385}.
MOD_RES 261 261 Phosphoserine; by ULK1. {ECO:0000250}.
MOD_RES 263 263 Phosphothreonine; by ULK1. {ECO:0000250}.
MOD_RES 270 270 Phosphoserine; by ULK1.
{ECO:0000250|UniProtKB:P80385}.
CONFLICT 121 121 Y -> F (in Ref. 1; AAK19307).
{ECO:0000305}.
SEQUENCE 330 AA; 37497 MW; 40C9C8D5B1798FDA CRC64;
MEAVPSSDSY PAVENEHLQE TPESNNSVYT SFMKSHRCYD LIPTSSKLVV FDTSLQVKKA
FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK SALVQIYELE EHKIETWREV
YLQDSFKPLV CISPNASLFD AVSSLIRNKI HRLPVIDPES GNTLYILTHK RILKFLKLFI
TEFPKPEFMS KSLEELQIGT YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI
YSKFDVINLA AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL
VVVDENDVVK GIVSLSDILQ ALVLTGGEKP


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