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5'-AMP-activated protein kinase subunit gamma-3 (AMPK gamma3) (AMPK subunit gamma-3)

 AAKG3_MOUSE             Reviewed;         489 AA.
Q8BGM7; Q0VG42; Q80WK8; Q8CJ41;
13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
22-NOV-2017, entry version 103.
RecName: Full=5'-AMP-activated protein kinase subunit gamma-3;
Short=AMPK gamma3;
Short=AMPK subunit gamma-3;
Name=Prkag3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
PubMed=14512293; DOI=10.1152/ajpcell.00319.2003;
Yu H., Fujii N., Hirshman M.F., Pomerleau J.M., Goodyear L.J.;
"Cloning and characterization of mouse 5'-AMP-activated protein kinase
gamma3 subunit.";
Am. J. Physiol. 286:C283-C292(2004).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=14970697; DOI=10.1159/000075743;
Amarger V., Erlandsson R., Pielberg G., Jeon J.-T., Andersson L.;
"Comparative sequence analysis of the PRKAG3 region between human and
pig: evolution of repetitive sequences and potential new exons.";
Cytogenet. Genome Res. 102:163-172(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Bone;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PHOSPHORYLATION BY ULK1.
PubMed=21460634; DOI=10.4161/auto.7.7.15451;
Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
"Ulk1-mediated phosphorylation of AMPK constitutes a negative
regulatory feedback loop.";
Autophagy 7:696-706(2011).
-!- 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}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=Q8BGM7-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=Q8BGM7-2; Sequence=VSP_015588;
-!- 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; leading to negatively regulate AMPK
activity and suggesting the existence of a regulatory feedback
loop between ULK1 and AMPK. {ECO:0000269|PubMed:21460634}.
-!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
subunit family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF525500; AAN47137.1; -; mRNA.
EMBL; AF525501; AAN47138.1; -; mRNA.
EMBL; AY263402; AAP22981.1; -; Genomic_DNA.
EMBL; AK036585; BAC29492.1; -; mRNA.
EMBL; BC116749; AAI16750.1; -; mRNA.
EMBL; BC116777; AAI16778.1; -; mRNA.
CCDS; CCDS15055.1; -. [Q8BGM7-1]
RefSeq; NP_714966.1; NM_153744.3. [Q8BGM7-1]
RefSeq; XP_006496051.1; XM_006495988.3. [Q8BGM7-1]
RefSeq; XP_006496052.1; XM_006495989.3. [Q8BGM7-1]
UniGene; Mm.166501; -.
UniGene; Mm.453463; -.
ProteinModelPortal; Q8BGM7; -.
SMR; Q8BGM7; -.
STRING; 10090.ENSMUSP00000080342; -.
iPTMnet; Q8BGM7; -.
PhosphoSitePlus; Q8BGM7; -.
PaxDb; Q8BGM7; -.
PRIDE; Q8BGM7; -.
Ensembl; ENSMUST00000081636; ENSMUSP00000080342; ENSMUSG00000006542. [Q8BGM7-1]
Ensembl; ENSMUST00000113672; ENSMUSP00000109302; ENSMUSG00000006542. [Q8BGM7-2]
Ensembl; ENSMUST00000160732; ENSMUSP00000125344; ENSMUSG00000006542. [Q8BGM7-1]
Ensembl; ENSMUST00000188073; ENSMUSP00000139909; ENSMUSG00000006542. [Q8BGM7-1]
GeneID; 241113; -.
KEGG; mmu:241113; -.
UCSC; uc007bnb.2; mouse. [Q8BGM7-1]
CTD; 53632; -.
MGI; MGI:1891343; Prkag3.
eggNOG; KOG1764; Eukaryota.
eggNOG; COG0517; LUCA.
GeneTree; ENSGT00390000009849; -.
HOGENOM; HOG000176880; -.
HOVERGEN; HBG050431; -.
InParanoid; Q8BGM7; -.
KO; K07200; -.
OMA; AKASRWT; -.
OrthoDB; EOG091G0CZV; -.
PhylomeDB; Q8BGM7; -.
TreeFam; TF313247; -.
Reactome; R-MMU-1632852; Macroautophagy.
Reactome; R-MMU-380972; Energy dependent regulation of mTOR by LKB1-AMPK.
Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
PRO; PR:Q8BGM7; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000006542; -.
ExpressionAtlas; Q8BGM7; baseline and differential.
Genevisible; Q8BGM7; MM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0031588; C:nucleotide-activated protein kinase complex; IEA:Ensembl.
GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0015758; P:glucose transport; IMP:MGI.
GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0007005; P:mitochondrion organization; TAS:Reactome.
InterPro; IPR000644; CBS_dom.
Pfam; PF00571; CBS; 3.
SMART; SM00116; CBS; 4.
PROSITE; PS51371; CBS; 4.
1: Evidence at protein level;
Alternative splicing; ATP-binding; CBS domain; Complete proteome;
Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
Lipid metabolism; Nucleotide-binding; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 489 5'-AMP-activated protein kinase subunit
gamma-3.
/FTId=PRO_0000204385.
DOMAIN 197 258 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 280 340 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 355 415 CBS 3. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 427 486 CBS 4. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
NP_BIND 242 245 AMP, ADP or ATP 1.
{ECO:0000250|UniProtKB:P80385}.
NP_BIND 306 307 AMP, ADP or ATP 1.
{ECO:0000250|UniProtKB:P80385}.
NP_BIND 381 382 AMP 3. {ECO:0000250|UniProtKB:P80385}.
NP_BIND 397 400 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
NP_BIND 453 454 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
NP_BIND 469 472 AMP 3. {ECO:0000250|UniProtKB:P80385}.
MOTIF 293 314 AMPK pseudosubstrate.
BINDING 225 225 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
BINDING 285 285 AMP, ADP or ATP 1; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P80385}.
BINDING 306 306 AMP 3. {ECO:0000250|UniProtKB:P80385}.
BINDING 325 325 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
BINDING 355 355 AMP 3. {ECO:0000250|UniProtKB:P80385}.
BINDING 360 360 AMP 3; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:P80385}.
BINDING 424 424 AMP, ADP or ATP 2.
{ECO:0000250|UniProtKB:P80385}.
BINDING 432 432 AMP, ADP or ATP 2; via amide nitrogen and
carbonyl oxygen.
{ECO:0000250|UniProtKB:P80385}.
BINDING 453 453 AMP 3. {ECO:0000250|UniProtKB:P80385}.
VAR_SEQ 1 25 Missing (in isoform 2).
{ECO:0000303|PubMed:14512293,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015588.
CONFLICT 390 390 G -> GS (in Ref. 2; AAP22981).
{ECO:0000305}.
SEQUENCE 489 AA; 53849 MW; 85C9F71D8BDBDA5D CRC64;
MEPELEHTLP GTLTWSHSGG PESQEMDFLE QGENSWPSPA VATSSERTCA IRGVKASRWT
RQEAVEEAEP PGLGEGAQSR PAAESTRQEA TFPKATPLAQ AVPLAEAETS PTGWDLLLPD
CAASAGGSST GDLELTIEFP APEAWDCELE GLGKDRPRPG PSPQAPLLGL SWDDELQKPG
AQVYMHFMQE HTCYDAMATS SKLVIFDTTL EIKKAFFAMV ANGVRAAPLW DSKKQSFVGM
LTITDFILVL HRYYRSPLVQ IYEIEEHKIE TWREIYLQGC FKPLVSISPN DSLFEAVYAL
IKNRIHRLPV LDPVSGTVLY ILTHKRLLKF LHIFGALLPR PSFLCRTIQD LGIGTFRDLA
VVLETAPVLT ALDIFVDRRV SALPVVNESG QVVGLYSRFD VIHLAAQQTY NHLDMSVGEA
LRQRTLCLEG VLSCQPHESL GEVIDRIARE QVHRLVLVDE TQHLLGVVSL SDILQALVLS
PAGIDALSA


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