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-174 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).
SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. SNF1 subfamily.
SIMILARITY: Contains 1 protein kinase domain.

Copyright

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Cross-references

Sequence databases

EMBL

CR857935; CAH90182.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q5RDH5; 12-280.

ModBase

Q5RDH5.

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 of domain structure.

PANTHER

PTHR22982:SF61; AMPK; 1.

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]

SMART

SM00220; S_TKc; 1.
SMART graphical view of domain structure.

PROSITE

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

BLOCKS

Q5RDH5.

Phylogenomic databases

HOVERGEN

Q5RDH5; -.

Other

ProtoNet

Q5RDH5.

UniRef

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

Keywords

ATP-binding; Cholesterol biosynthesis; 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`	`1 550`	`550`	`5'-AMP-activated protein kinase catalytic subunit alpha-1.`	`PRO_0000085592`
`DOMAIN`	`18 270`	`253`	`Protein kinase.`
`NP_BIND`	`24 32`	`9`	`ATP (By similarity).`
`ACT_SITE`	`141 141`		`Proton acceptor (By similarity).`
`BINDING`	`47 47`		`ATP (By similarity).`
`MOD_RES`	`174 174`		`Phosphothreonine; by STK11 (By similarity).`
`MOD_RES`	`175 175`		`Phosphoserine (By similarity).`
`MOD_RES`	`260 260`		`Phosphothreonine (By similarity).`
`MOD_RES`	`373 373`		`Phosphothreonine (By similarity).`
`MOD_RES`	`433 433`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`487 487`		`Phosphoserine (By similarity).`
`MOD_RES`	`499 499`		`Phosphoserine (By similarity).`

Sequence information

Length: 550 AA [This is the length of the unprocessed precursor]

Molecular weight: 62836 Da [This is the MW of the unprocessed precursor]

CRC64: FC2F12DDD858B1C2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATAEKQKHD GRVRIGHYIL GDTLGVGTFG KVKVGKHELT GHKVAVKILN RQKIRSLDVV 

        70         80         90        100        110        120 
GKIRREIQNL KLFRHPHIIK LYQVISTPSD IFMVMEYVSG GELFDYICKN GRLDEKESRR 

       130        140        150        160        170        180 
LFQQILSGVD YCHRHMVVHR DLKPENVLLD AHMNAKIADF GLSNMMSDGE FLRTSCGSPN 

       190        200        210        220        230        240 
YAAPEVISGR LYAGPEVDIW SSGVILYALL CGTLPFDDDH VPTLFKKICD GIFYTPQYLN 

       250        260        270        280        290        300 
PSVISLLKHM LQVDPMKRAT IKDIREHEWF KQDLPKYLFP EDPSYSSTMI DDEALKEVCE 

       310        320        330        340        350        360 
KFECSEEEVL SCLYNRNHQD PLAVAYHLII DNRRIMNEAK DFYLATSPPD SFLDDHHLTR 

       370        380        390        400        410        420 
PHPERVPFLV AETPRARHTL DELNPQKSKH QGVRKAKWHL GIRSQSRPND IMAEVCRAIK 

       430        440        450        460        470        480 
QLDYEWKVVN PYYLRVRRKN PVTSTYSKMS LQLYQVDSRT YLLDFRSIDD EITEAKSGTA 

       490        500        510        520        530        540 
TPQRSGSVSN YRSCQRSDSD AEAQGKSSEV SLTSSVTSLD SSPVDLTPRP GSHTIEFFEM 

       550 
CANLIKILAQ

Q5RDH5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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