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Q8BGM7 (AAKG3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
5'-AMP-activated protein kinase subunit gamma-3
Short name=AMPK gamma3
Short name=AMPK subunit gamma-3
Gene names
Name:Prkag3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length489 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

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.

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.

The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP By similarity.

Post-translational modification

Phosphorylated by ULK1; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1 and AMPK. Ref.5

Sequence similarities

Belongs to the 5'-AMP-activated protein kinase gamma subunit family.

Contains 4 CBS domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BGM7-1)

Also known as: Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8BGM7-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4894895'-AMP-activated protein kinase subunit gamma-3
PRO_0000204385

Regions

Domain197 – 25862CBS 1
Domain280 – 34061CBS 2
Domain355 – 41561CBS 3
Domain427 – 48660CBS 4
Motif293 – 31422AMPK pseudosubstrate

Sites

Binding site2251AMP 1 By similarity
Binding site2251ATP 1 By similarity
Binding site3061AMP 2 By similarity
Binding site3061AMP 3 By similarity
Binding site3061ATP 2 By similarity
Binding site3071ATP 1 By similarity
Binding site3071ATP 2 By similarity
Binding site3251AMP 1 By similarity
Binding site3251ATP 1 By similarity
Binding site4531AMP 3 By similarity
Binding site4541AMP 1 By similarity
Binding site4541ATP 1 By similarity

Natural variations

Alternative sequence1 – 2525Missing in isoform 2.
VSP_015588

Experimental info

Sequence conflict3901G → GS in AAP22981. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 85C9F71D8BDBDA5D

FASTA48953,849
        10         20         30         40         50         60 
MEPELEHTLP GTLTWSHSGG PESQEMDFLE QGENSWPSPA VATSSERTCA IRGVKASRWT 

        70         80         90        100        110        120 
RQEAVEEAEP PGLGEGAQSR PAAESTRQEA TFPKATPLAQ AVPLAEAETS PTGWDLLLPD 

       130        140        150        160        170        180 
CAASAGGSST GDLELTIEFP APEAWDCELE GLGKDRPRPG PSPQAPLLGL SWDDELQKPG 

       190        200        210        220        230        240 
AQVYMHFMQE HTCYDAMATS SKLVIFDTTL EIKKAFFAMV ANGVRAAPLW DSKKQSFVGM 

       250        260        270        280        290        300 
LTITDFILVL HRYYRSPLVQ IYEIEEHKIE TWREIYLQGC FKPLVSISPN DSLFEAVYAL 

       310        320        330        340        350        360 
IKNRIHRLPV LDPVSGTVLY ILTHKRLLKF LHIFGALLPR PSFLCRTIQD LGIGTFRDLA 

       370        380        390        400        410        420 
VVLETAPVLT ALDIFVDRRV SALPVVNESG QVVGLYSRFD VIHLAAQQTY NHLDMSVGEA 

       430        440        450        460        470        480 
LRQRTLCLEG VLSCQPHESL GEVIDRIARE QVHRLVLVDE TQHLLGVVSL SDILQALVLS 


PAGIDALSA

« Hide

Isoform 2 (Short) [UniParc].

Checksum: CEC324A5855C3F2E
Show »

FASTA46451,117

References

« Hide 'large scale' references
[1]"Cloning and characterization of mouse 5'-AMP-activated protein kinase gamma3 subunit."
Yu H., Fujii N., Hirshman M.F., Pomerleau J.M., Goodyear L.J.
Am. J. Physiol. 286:C283-C292(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Strain: BALB/c.
Tissue: Skeletal muscle.
[2]"Comparative sequence analysis of the PRKAG3 region between human and pig: evolution of repetitive sequences and potential new exons."
Amarger V., Erlandsson R., Pielberg G., Jeon J.-T., Andersson L.
Cytogenet. Genome Res. 102:163-172(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: C57BL/6J.
Tissue: Bone.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[5]"Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory feedback loop."
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.
Autophagy 7:696-706(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY ULK1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF525500 mRNA. Translation: AAN47137.1.
AF525501 mRNA. Translation: AAN47138.1.
AY263402 Genomic DNA. Translation: AAP22981.1.
AK036585 mRNA. Translation: BAC29492.1.
BC116749 mRNA. Translation: AAI16750.1.
BC116777 mRNA. Translation: AAI16778.1.
IPIIPI00221645.
IPI00468404.
RefSeqNP_714966.1. NM_153744.3.
UniGeneMm.166501.
Mm.453463.

3D structure databases

ProteinModelPortalQ8BGM7.
SMRQ8BGM7. Positions 181-480.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000080342.

PTM databases

PhosphoSiteQ8BGM7.

Proteomic databases

PaxDbQ8BGM7.
PRIDEQ8BGM7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081636; ENSMUSP00000080342; ENSMUSG00000006542.
ENSMUST00000113672; ENSMUSP00000109302; ENSMUSG00000006542.
ENSMUST00000160732; ENSMUSP00000125344; ENSMUSG00000006542.
GeneID241113.
KEGGmmu:241113.
UCSCuc007bnb.2. mouse.
uc007bnc.1. mouse.

Organism-specific databases

CTD53632.
MGIMGI:1891343. Prkag3.

Phylogenomic databases

eggNOGCOG0517.
GeneTreeENSGT00390000009849.
HOGENOMHOG000176880.
HOVERGENHBG050431.
InParanoidQ0VG42.
KOK07200.
OMAYMRFMQE.
OrthoDBEOG47H5PV.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_88307. Membrane Trafficking.

Gene expression databases

ArrayExpressQ8BGM7.
BgeeQ8BGM7.
GenevestigatorQ8BGM7.
GermOnlineENSMUSG00000006542. Mus musculus.

Family and domain databases

InterProIPR000644. Cysta_beta_synth_core.
[Graphical view]
PfamPF00571. CBS. 3 hits.
[Graphical view]
SMARTSM00116. CBS. 4 hits.
[Graphical view]
PROSITEPS51371. CBS. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio384884.
SOURCESearch...

Entry information

Entry nameAAKG3_MOUSE
AccessionPrimary (citable) accession number: Q8BGM7
Secondary accession number(s): Q0VG42, Q80WK8, Q8CJ41
Entry history
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents