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Protein

5'-AMP-activated protein kinase subunit gamma-1

Gene

PRKAG1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

AMP/ATP-binding subunit of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Also acts as a regulator of cellular polarity by remodeling the actin cytoskeleton; probably by indirectly activating myosin. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (PRKAA1 or PRKAA2) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits. ADP also stimulates phosphorylation, without stimulating already phosphorylated catalytic subunit. ATP promotes dephosphorylation of catalytic subunit, rendering the AMPK enzyme inactive (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei70AMP 1By similarity1
Binding sitei70ATP 1By similarity1
Binding sitei151AMP 2By similarity1
Binding sitei151AMP 3By similarity1
Binding sitei151ATP 2By similarity1
Binding sitei152ATP 1By similarity1
Binding sitei152ATP 2By similarity1
Binding sitei170AMP 1By similarity1
Binding sitei170ATP 1By similarity1
Binding sitei298AMP 3By similarity1
Binding sitei299AMP 1By similarity1
Binding sitei299ATP 1By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit gamma-1
Short name:
AMPK gamma1
Short name:
AMPK subunit gamma-1
Short name:
AMPKg
Alternative name(s):
38 kDa subunit
Gene namesi
Name:PRKAG1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002043791 – 3305'-AMP-activated protein kinase subunit gamma-1Add BLAST330

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei261Phosphoserine; by ULK1By similarity1
Modified residuei263Phosphothreonine; by ULK1By similarity1
Modified residuei270Phosphoserine; by ULK1By similarity1

Post-translational modificationi

Phosphorylated by ULK1 and ULK2; leading to negatively regulate AMPK activity and suggesting the existence of a regulatory feedback loop between ULK1, ULK2 and AMPK.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ09138.
PeptideAtlasiQ09138.
PRIDEiQ09138.

Expressioni

Gene expression databases

BgeeiENSSSCG00000000185.
GenevisibleiQ09138. SS.

Interactioni

Subunit structurei

AMPK is a heterotrimer of an alpha catalytic subunit (PRKAA1 or PRKAA2), a beta (PRKAB1 or PRKAB2) and a gamma non-catalytic subunits (PRKAG1, PRKAG2 or PRKAG3). Interacts with FNIP1 and FNIP2 (By similarity).By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000193.

Structurei

3D structure databases

ProteinModelPortaliQ09138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 103CBS 1PROSITE-ProRule annotationAdd BLAST61
Domaini125 – 187CBS 2PROSITE-ProRule annotationAdd BLAST63
Domaini198 – 260CBS 3PROSITE-ProRule annotationAdd BLAST63
Domaini272 – 329CBS 4PROSITE-ProRule annotationAdd BLAST58

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi138 – 159AMPK pseudosubstrateAdd BLAST22

Domaini

The AMPK pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins of AMPK, except the presence of a non-phosphorylatable residue in place of Ser. In the absence of AMP this pseudosubstrate sequence may bind to the active site groove on the alpha subunit (PRKAA1 or PRKAA2), preventing phosphorylation by the upstream activating kinase STK11/LKB1 (By similarity).By similarity
The CBS domains mediate binding to AMP, ADP and ATP. 2 sites bind either AMP or ATP, whereas a third site contains a tightly bound AMP that does not exchange. Under physiological conditions AMPK mainly exists in its inactive form in complex with ATP, which is much more abundant than AMP (By similarity).By similarity

Sequence similaritiesi

Contains 4 CBS domains.PROSITE-ProRule annotation

Keywords - Domaini

CBS domain, Repeat

Phylogenomic databases

eggNOGiKOG1764. Eukaryota.
COG0517. LUCA.
HOGENOMiHOG000176880.
HOVERGENiHBG050431.
InParanoidiQ09138.
KOiK07200.
OrthoDBiEOG091G0CZV.

Family and domain databases

InterProiIPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 3 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q09138-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METVTSSDSS SAVENEHPQD TPESNNSVYT SFMKSHRCYD LIPTSSKLVV
60 70 80 90 100
FDTSLQVKKA FFALVTNGVR AAPLWDSKKQ SFVGMLTITD FINILHRYYK
110 120 130 140 150
SALVQIYELE EHKIETWREV YLQDSFKPLV CISPNASLFD AVSSLIRNKI
160 170 180 190 200
HRLPVIDPES GNTLYILTHK RILKFLKLFI TEFPKPEFMS KSLEELQIGT
210 220 230 240 250
YANIAMVRTT TPVYVALGIF VQHRVSALPV VDEKGRVVDI YSKFDVINLA
260 270 280 290 300
AEKTYNNLDV SVTKALQHRS HYFEGVLKCY LHETLETIIN RLVEAEVHRL
310 320 330
VVVDENDVVK GIVSLSDILQ ALVLTGGEKP
Length:330
Mass (Da):37,415
Last modified:September 13, 2005 - v2
Checksum:iB7A5D65A01F0F2A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY260940 mRNA. Translation: AAP86632.1.
RefSeqiNP_001001642.1. NM_001001642.2.
UniGeneiSsc.26338.

Genome annotation databases

GeneIDi414426.
KEGGissc:414426.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY260940 mRNA. Translation: AAP86632.1.
RefSeqiNP_001001642.1. NM_001001642.2.
UniGeneiSsc.26338.

3D structure databases

ProteinModelPortaliQ09138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000193.

Proteomic databases

PaxDbiQ09138.
PeptideAtlasiQ09138.
PRIDEiQ09138.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi414426.
KEGGissc:414426.

Organism-specific databases

CTDi5571.

Phylogenomic databases

eggNOGiKOG1764. Eukaryota.
COG0517. LUCA.
HOGENOMiHOG000176880.
HOVERGENiHBG050431.
InParanoidiQ09138.
KOiK07200.
OrthoDBiEOG091G0CZV.

Gene expression databases

BgeeiENSSSCG00000000185.
GenevisibleiQ09138. SS.

Family and domain databases

InterProiIPR000644. CBS_dom.
[Graphical view]
PfamiPF00571. CBS. 3 hits.
[Graphical view]
SMARTiSM00116. CBS. 4 hits.
[Graphical view]
PROSITEiPS51371. CBS. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAAKG1_PIG
AccessioniPrimary (citable) accession number: Q09138
Secondary accession number(s): Q6X275
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: September 13, 2005
Last modified: October 5, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.