[1]	PROTEIN SEQUENCE OF 1-22; 73-87; 100-157; 222-240 AND 344-361, AND FUNCTION. TISSUE=Liver; PubMed=7905477 [NCBI, ExPASy, EBI, Israel, Japan] Mitchelhill K.I., Stapleton D., Gao G., House C., Michell B., Katsis F., Witters L.A., Kemp B.E.; "Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase."; J. Biol. Chem. 269:2361-2364(1994).
[2]	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; DOI=10.1074/jbc.271.2.611; PubMed=8557660 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Mammalian AMP-activated protein kinase subfamily."; J. Biol. Chem. 271:611-614(1996).
[3]	NUCLEOTIDE SEQUENCE [MRNA] OF 23-243. Weber T.E.; "Effect of dietary hemicellulose on growth and energy metabolism of growing pigs."; Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.

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: Heterotrimer of an alpha catalytic subunit, a beta and a gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2 (By similarity).
INDUCTION: By AMP.
SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

EU622639; ACC78144.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A49958; A49958.

3D structure databases

SMR

Q09136; 23-95.

ModBase

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 of domain structure.

Pfam

PF00069; Pkinase; 1.
Pfam graphical view of domain structure.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00107; PROTEIN_KINASE_ATP; PARTIAL.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; PARTIAL.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q09136.

Phylogenomic databases

HOVERGEN

Q09136; -.

Other

ProtoNet

Q09136.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

ATP-binding; Cholesterol biosynthesis; Direct protein sequencing; Fatty acid biosynthesis; Kinase; Lipid synthesis; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase; Steroid biosynthesis; Sterol biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`<1 >385`	`>385`	`5'-AMP-activated protein kinase catalytic subunit alpha-1.`	`PRO_0000085591`
`DOMAIN`	`<1 229`	`>229`	`Protein kinase.`
`NP_BIND`	`15 >22`	`>8`	`ATP (By similarity).`
`ACT_SITE`	`100 100`		`Proton acceptor (By similarity).`
`MOD_RES`	`133 133`		`Phosphothreonine; by STK11 (By similarity).`
`MOD_RES`	`134 134`		`Phosphoserine (By similarity).`
`MOD_RES`	`219 219`		`Phosphothreonine (By similarity).`
`MOD_RES`	`298 298`		`Phosphothreonine (By similarity).`
`NON_CONS`	`22 23`
`NON_CONS`	`157 158`
`NON_CONS`	`255 256`
`NON_CONS`	`270 271`
`NON_CONS`	`290 291`
`NON_CONS`	`300 301`
`NON_CONS`	`323 324`
`NON_CONS`	`342 343`
`NON_CONS`	`367 368`
`NON_TER`	`1 1`
`NON_TER`	`385 385`

Sequence information

Length: 385 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 44226 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: A9B4BC0C935A85A6 [This is a checksum on the sequence]

        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

Q09136 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools