Skip Header

 
Contribute Send feedback

Reviewed, UniProtKB/Swiss-Prot Q09137 (AAPK2_RAT)

Last modified November 25, 2008. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    5'-AMP-activated protein kinase catalytic subunit alpha-2
      Short name=AMPK alpha-2 chain
    EC=2.7.11.1
Gene names
Name: Prkaa2
Synonyms: Ampk, Ampk2
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

Protein attributes

Sequence length552 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Responsible for the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase. It also regulates cholesterol synthesis via phosphorylation and inactivation of hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase. Appears to act as a metabolic stress-sensing protein kinase switching off biosynthetic pathways when cellular ATP levels are depleted and when 5'-AMP rises in response to fuel limitation and/or hypoxia. This is a catalytic subunit.

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Cofactor

Magnesium.

Enzyme regulation

Binding of AMP results in allosteric activation, inducing phosphorylation on Thr-172 by STK11 in complex with STE20-related adapter-alpha (STRAD alpha) pseudo kinase and CAB39. Also activated by phosphorylation by CAMKK2 triggered by a rise in intracellular calcium ions, without detectable changes in the AMP/ATP ratio.

Subunit structure

Heterotrimer of a catalytic subunit, a beta and a gamma non-catalytic subunits.

Tissue specificity

Skeletal muscle, lower levels in liver, heart and kidney.

Induction

By AMP.

Sequence similarities

Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.

Contains 1 protein kinase domain.

Hide | Top

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q09137-1)

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 Short (identifier: Q09137-2)

The sequence of this isoform differs from the canonical sequence as follows:
     32-388: Missing.
     392-552: Missing.
Notes: Lacks the sequence parts essential for kinase activity and is therefore inactive.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 5525525'-AMP-activated protein kinase catalytic subunit alpha-2
PRO_0000085597

Regions

Domain16 – 268253Protein kinase
Nucleotide binding22 – 309ATP By similarity

Sites

Active site1391Proton acceptor By similarity
Binding site451ATP By similarity

Amino acid modifications

Modified residue1721Phosphothreonine; by STK11 By similarity
Modified residue1731Phosphoserine By similarity
Modified residue1761Phosphoserine By similarity
Modified residue2581Phosphothreonine
Modified residue3771Phosphoserine By similarity
Modified residue4911Phosphoserine
Modified residue5001Phosphoserine By similarity

Natural variations

Alternative sequence32 – 388357Missing in isoform Short.
VSP_004949
Alternative sequence392 – 552161Missing in isoform Short.
VSP_004950

Experimental info

Sequence conflict3551M → S in AAA85033. Ref.2
Sequence conflict4621N → D in AAA85033. Ref.2

Hide | Top

Sequences

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

Last modified February 1, 1995. Version 1.
Checksum: 2829E07F674D89B1

FASTA55262,258
        10         20         30         40         50         60 
MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK 

        70         80         90        100        110        120 
IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEVEARRLF 

       130        140        150        160        170        180 
QQILSAVDYC HRHMVVHRDL KPENVLLDAQ MNAKIADFGL SNMMSDGEFL RTSCGSPNYA 

       190        200        210        220        230        240 
APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPEYLNRS 

       250        260        270        280        290        300 
IATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF 

       310        320        330        340        350        360 
ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPTGS FMDDMAMHIP 

       370        380        390        400        410        420 
PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KPYDIMAEVY 

       430        440        450        460        470        480 
RAMKQLDFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DNRSYLLDFK SIDDEVVEQR 

       490        500        510        520        530        540 
SGSSTPQRSC SAAGLHRPRS SVDSSTAENH SLSGSLTGSL TGSTLSSASP RLGSHTMDFF 

       550 
EMCASLITAL AR

« Hide

Isoform Short [UniParc].

Checksum: 4BF6E5CF5CF23F3B
Show »

343,700

Hide | Top

References

[1]"Mammalian AMP-activated protein kinase is homologous to yeast and plant protein kinases involved in the regulation of carbon metabolism."
Carling D., Aguan K., Woods A., Verhoeven A.J.M., Beri R.K., Brennan C.H., Sidebottom C., Davison M.D., Scott J.
J. Biol. Chem. 269:11442-11448(1994) [PubMed: 7908907] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Catalytic subunits of the porcine and rat 5'-AMP-activated protein kinase are members of the SNF1 protein kinase family."
Gao G., Widmer J., Stapleton D., Teh T., Cox T., Kemp B.E., Witters L.A.
Biochim. Biophys. Acta 1266:73-82(1995) [PubMed: 7718624] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
[3]"Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade."
Hawley S.A., Boudeau J., Reid J.L., Mustard K.J., Udd L., Makela T.P., Alessi D.R., Hardie D.G.
J. Biol. 2:28.1-28.16(2003) [PubMed: 14511394] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[4]"Identification of phosphorylation sites in AMP-activated protein kinase (AMPK) for upstream AMPK kinases and study of their roles by site-directed mutagenesis."
Woods A., Vertommen D., Neumann D., Turk R., Bayliss J., Schlattner U., Wallimann T., Carling D., Rider M.H.
J. Biol. Chem. 278:28434-28442(2003) [PubMed: 12764152] [Abstract]
Cited for: PHOSPHORYLATION AT THR-258 AND SER-491, MASS SPECTROMETRY.
[5]"Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase."
Hawley S.A., Pan D.A., Mustard K.J., Ross L., Bain J., Edelman A.M., Frenguelli B.G., Hardie D.G.
Cell Metab. 2:9-19(2005) [PubMed: 16054095] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.

Hide | Top

Cross-references

Sequence databases

Z29486 mRNA. Translation: CAA82620.1.
U12149 mRNA. Translation: AAA85033.1.
PIRA53621.
RefSeqNP_076481.1.
UniGeneRn.64583

3D structure databases

HSSPHSSP built from PDB template 1A06 based on UniProtKB Q63450.
SMRQ09137. Positions 10-278.
ModBaseSearch...

PTM databases

PhosphoSiteQ09137.

Genome annotation databases

EnsemblENSRNOG00000007706. Rattus norvegicus. [Contig view]
GeneID78975.
KEGGrno:78975.

Organism-specific databases

RGD620893. Prkaa2.

Phylogenomic databases

HOVERGENQ09137.

Gene expression databases

ArrayExpressQ09137.
GermOnlineENSRNOG00000007706. Rattus norvegicus.

Family and domain databases

InterProIPR015741. AMPK.
IPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_bd_CS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
IPR002290. Ser_thr_pkinase.
[Graphical view]
PANTHERPTHR22982:SF61. AMPK. 1 hit.
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio614450.

Hide | Top

Entry information

Entry nameAAPK2_RAT
AccessionPrimary (citable) accession number: Q09137
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: November 25, 2008
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents