Reviewed, UniProtKB/Swiss-Prot Q28948 (AAPK2_PIG)

Names and origin

Protein names

Recommended 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:	AMPK2

Organism

Sus scrofa (Pig)

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

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 By similarity.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
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 By similarity.
Subunit structure	Heterotrimer of a catalytic subunit, a beta and a gamma non-catalytic subunits.
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Cholesterol biosynthesis Fatty acid biosynthesis Lipid synthesis Steroid biosynthesis Sterol biosynthesis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	cholesterol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 552	552	5'-AMP-activated protein kinase catalytic subunit alpha-2		PRO_0000085595
Regions
	Domain	16 – 268	253	Protein kinase
	Nucleotide binding	22 – 30	9	ATP By similarity
Sites
	Active site	139	1	Proton acceptor By similarity
	Binding site	45	1	ATP By similarity
Amino acid modifications
	Modified residue	172	1	Phosphothreonine; by STK11 By similarity
	Modified residue	173	1	Phosphoserine By similarity
	Modified residue	176	1	Phosphoserine By similarity
	Modified residue	377	1	Phosphoserine By similarity
	Modified residue	500	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	17	1	V → M in AAA85034. Ref.2
	Sequence conflict	30	1	V → E in AAA85034. Ref.2
	Sequence conflict	144	1	N → K in AAA85034. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q28948-1 [UniParc]. Last modified September 13, 2005. Version 2. Checksum: 628C2529B5D07B02	FASTA	552	62,325
	10 20 30 40 50 60 MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK 70 80 90 100 110 120 IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEMEARRLF 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 VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIDD EAVKEVCEKF 310 320 330 340 350 360 ECTESEVMNS LYSGDPQDQL AVAYHLVIDN RRIMNQASEF YLASSPPTGS FMDDSAMHIP 370 380 390 400 410 420 PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KPYDIMAEVY 430 440 450 460 470 480 RAMKQLDFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DNRSYLLDFK SIDDEVLEQR 490 500 510 520 530 540 SGSSTPQRSC SAAGLHRPRS SLDSVTAESH SLSGSLSGSL TGSMLPSVPP RLGSHTMDFF 550 EMCASLITTL AR

References

[1]	"Molecular cloning and characterization of the porcine AMP-activated protein kinase alpha 2 (AMPKa2) gene." Kim T.-H., Choi B.-H., Park E.-W., Jeon J.-T., Park H.-S., Cheong I.-C. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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] OF 16-144. Tissue: Liver.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY159788 mRNA. Translation: AAO17789.1. U12148 mRNA. Translation: AAA85034.1.
RefSeq	NP_999431.1.
UniGene	Ssc.16257
3D structure databases
SMR	Q28948. Positions 10-278.
ModBase	Search...
Genome annotation databases
GeneID	397504.
KEGG	ssc:397504.
Phylogenomic databases
HOVERGEN	Q28948.
Family and domain databases
InterPro	IPR015741. 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]
PANTHER	PTHR22982:SF61. AMPK. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAPK2_PIG

Accession

Primary (citable) accession number: Q28948
Secondary accession number(s): Q7YRX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 13, 2005
Last modified:	November 25, 2008
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)