Reviewed, UniProtKB/Swiss-Prot Q09136 (AAPK1_PIG)

Names and origin

Protein names

Recommended name:
    5'-AMP-activated protein kinase catalytic subunit alpha-1
      Short name=AMPK alpha-1 chain
      Short name=AMPK
    EC=2.7.11.1
Alternative name(s):
    63 kDa subunit

Gene names

Name:	PRKAA1
Synonyms:	AMPK1

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	385 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Binding of AMP results in allosteric activation, inducing phosphorylation on Thr-133 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 an alpha catalytic subunit, a beta and a gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2 By similarity.
Induction	By AMP.
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
Technical term	Direct protein sequencing
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 – ›385	›385	5'-AMP-activated protein kinase catalytic subunit alpha-1		PRO_0000085591
Regions
	Domain	‹1 – 229	›229	Protein kinase
	Nucleotide binding	15 – ›22	›8	ATP By similarity
Sites
	Active site	100	1	Proton acceptor By similarity
Amino acid modifications
	Modified residue	133	1	Phosphothreonine; by STK11 By similarity
	Modified residue	134	1	Phosphoserine By similarity
	Modified residue	219	1	Phosphothreonine By similarity
	Modified residue	277	1	Phosphoserine By similarity
	Modified residue	298	1	Phosphothreonine By similarity
Experimental info
	Non-adjacent residues	22 – 23	2
	Non-adjacent residues	157 – 158	2
	Non-adjacent residues	255 – 256	2
	Non-adjacent residues	270 – 271	2
	Non-adjacent residues	290 – 291	2
	Non-adjacent residues	300 – 301	2
	Non-adjacent residues	323 – 324	2
	Non-adjacent residues	342 – 343	2
	Non-adjacent residues	367 – 368	2
	Non-terminal residue	1	1
	Non-terminal residue	385	1

Sequences

	Sequence		Length	Mass (Da)
	Q09136-1 [UniParc]. Last modified September 2, 2008. Version 2. Checksum: A9B4BC0C935A85A6	FASTA	385	44,226
	10 20 30 40 50 60 DGRVKIGHYI LGDTLGVGTF GKRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG 70 80 90 100 110 120 ELFDYICKNG RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG 130 140 150 160 170 180 LSNMMSDGEF LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV 190 200 210 220 230 240 PTLFKKICDG IFYTPQYLNP SVISLLKHML QVDPMKRATI KDIREHEWFK QDLPKYLFPE 250 260 270 280 290 300 DPSYSXTMID DEALKQDPLA VAYHLIIDNR DFYLATSPPD SFLDDHHLTR VPFLVAETPR 310 320 330 340 350 360 DELNPQKXKH QGVRKAKXHL GIRQLDYEXK VVNPYYLRVR RKKMSLQLYQ VDSRTYLLDF 370 380 RSIDDXIDAE AQGKSSEASL TXSVT

References

[1]	"Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase." Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., Katsis F., Witters L.A., Kemp B.E. J. Biol. Chem. 269:2361-2364(1994) [PubMed: 7905477] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-22; 73-87; 100-157; 222-240 AND 344-361, FUNCTION. Tissue: Liver.
[2]	"Mammalian AMP-activated protein kinase subfamily." Stapleton D., Mitchelhill K.I., Gao G., Widmer J., Michell B.J., Teh T., House C.M., Fernandez C.S., Cox T., Witters L.A., Kemp B.E. J. Biol. Chem. 271:611-614(1996) [PubMed: 8557660] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-22; 73-88; 100-132; 144-156; 209-216; 221-255; 256-270; 271-290; 291-300; 301-323; 324-342; 343-367 AND 368-385. Tissue: Liver.
[3]	"Effect of dietary hemicellulose on growth and energy metabolism of growing pigs." Weber T.E. Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 23-243.

Cross-references

Sequence databases
EMBLGenBankDDBJ	EU622639 mRNA. Translation: ACC78144.1.
PIR	A49958.
3D structure databases
SMR	Q09136. Positions 23-95.
ModBase	Search...
Phylogenomic databases
HOVERGEN	Q09136.
Family and domain databases
InterPro	IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00107. PROTEIN_KINASE_ATP. Partial match. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AAPK1_PIG

Accession

Primary (citable) accession number: Q09136
Secondary accession number(s): B2MV24

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	September 2, 2008
Last modified:	November 25, 2008
This is version 61 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)