Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

5'-AMP-activated protein kinase subunit gamma-3

Gene

PRKAG3

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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 sitei232AMP 1By similarity1
Binding sitei232ATP 1By similarity1
Binding sitei313AMP 2By similarity1
Binding sitei313AMP 3By similarity1
Binding sitei313ATP 2By similarity1
Binding sitei314ATP 1By similarity1
Binding sitei314ATP 2By similarity1
Binding sitei332AMP 1By similarity1
Binding sitei332ATP 1By similarity1
Binding sitei461AMP 3By similarity1
Binding sitei462AMP 1By similarity1
Binding sitei462ATP 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

Enzyme and pathway databases

ReactomeiR-BTA-1632852. Macroautophagy.
R-BTA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-BTA-5628897. TP53 Regulates Metabolic Genes.
R-BTA-6804756. Regulation of TP53 Activity through Phosphorylation.

Names & Taxonomyi

Protein namesi
Recommended name:
5'-AMP-activated protein kinase subunit gamma-3
Short name:
AMPK gamma3
Short name:
AMPK subunit gamma-3
Gene namesi
Name:PRKAG3
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 2

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002401501 – 4975'-AMP-activated protein kinase subunit gamma-3Add BLAST497

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ2LL38.
PRIDEiQ2LL38.

Expressioni

Gene expression databases

BgeeiENSBTAG00000013492.

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

STRINGi9913.ENSBTAP00000017940.

Structurei

3D structure databases

ProteinModelPortaliQ2LL38.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini204 – 265CBS 1PROSITE-ProRule annotationAdd BLAST62
Domaini287 – 345CBS 2PROSITE-ProRule annotationAdd BLAST59
Domaini363 – 423CBS 3PROSITE-ProRule annotationAdd BLAST61
Domaini435 – 494CBS 4PROSITE-ProRule annotationAdd BLAST60

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi300 – 321AMPK 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.
GeneTreeiENSGT00390000009849.
HOVERGENiHBG050431.
InParanoidiQ2LL38.
KOiK07200.
OMAiAKASRWT.
OrthoDBiEOG091G0CZV.
TreeFamiTF313247.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q2LL38-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEPAELEHAL CGSLFSTQTP SWSSFGGPEH QEMSFLEQGD STSWPSPAMT
60 70 80 90 100
TSAEISLGEQ RTKVSRWKSQ EDVEERELPG LEGGPQSRAA AESTGLEATF
110 120 130 140 150
PKATPLAQAT PLSAVGTPTT ERDSLPADCT ASASSSSTDD LDQGIEFSAP
160 170 180 190 200
AAWGDELGLV EERPAQCPSP QVPVLRLGWD DELRKPGAQV YMHFMQEHTC
210 220 230 240 250
YDAMATSSKL VIFDTMLQIK KAFFALVANG VRAAPLWDSK KQSFVGMLTI
260 270 280 290 300
TDFILVLHRY YRSPLVQIYE IEEHKIETWR EIYLQGCFKP LVSISPSDSL
310 320 330 340 350
FEAVYTLIKN RIHRLPVLDP VSGAVLHILT HKRLLKFLHI FQRTLLPRPS
360 370 380 390 400
FLYRTIQDLG IGTFRDLAVV LETAPILTAL DIFVDRRVSA LPVINEAGQV
410 420 430 440 450
VGLYSRFDVI HLAAQQTYNH LDISVGEALR RRTLCLEGVL SCQPHETLGE
460 470 480 490
VIDRIAREQV HRLVLVDETQ HLLGVVSLSD ILQALVLSPA GIDALGA
Length:497
Mass (Da):54,920
Last modified:June 13, 2006 - v2
Checksum:iA0D7B696B8681530
GO
Isoform 2 (identifier: Q2LL38-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     13-18: Missing.

Show »
Length:491
Mass (Da):54,256
Checksum:iA86CCD9DAB7F56CA
GO
Isoform 3 (identifier: Q2LL38-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     342-342: Missing.

Show »
Length:496
Mass (Da):54,792
Checksum:i8E9AE9DCBC0CC0A2
GO
Isoform 4 (identifier: Q2LL38-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     13-18: Missing.
     342-342: Missing.

Show »
Length:490
Mass (Da):54,128
Checksum:i15E1E2CFAB4F3AAC
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti455I → F in AAZ31228 (PubMed:16416094).Curated1
Sequence conflicti455I → F in AAZ31229 (PubMed:16416094).Curated1
Sequence conflicti455I → F in AAZ31230 (PubMed:16416094).Curated1
Sequence conflicti455I → F in AAZ31231 (PubMed:16416094).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti127A → S in strain: Charolais, Holstein and Limousin. 1 Publication1
Natural varianti153W → S in strain: Charolais and Limousin. 1 Publication1
Natural varianti262R → W in strain: Charolais, Holstein and Limousin. 1 Publication1
Natural varianti358D → Y in strain: Charolais. 1 Publication1
Natural varianti373T → M in strain: Limousin. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01929713 – 18Missing in isoform 2 and isoform 4. 1 Publication6
Alternative sequenceiVSP_019298342Missing in isoform 3 and isoform 4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ082732 mRNA. Translation: AAZ31228.1.
DQ082733 mRNA. Translation: AAZ31229.1.
DQ082734 mRNA. Translation: AAZ31230.1.
DQ082735 mRNA. Translation: AAZ31231.1.
DQ082736 Genomic DNA. Translation: AAZ31232.1.
DQ082736 Genomic DNA. Translation: AAZ31233.1.
DQ082736 Genomic DNA. Translation: AAZ31234.1.
DQ082736 Genomic DNA. Translation: AAZ31235.1.
RefSeqiNP_001025473.2. NM_001030302.2. [Q2LL38-1]
NP_001155891.1. NM_001162419.1. [Q2LL38-3]
NP_001155892.1. NM_001162420.1. [Q2LL38-2]
NP_001155893.1. NM_001162421.1. [Q2LL38-4]
UniGeneiBt.42124.

Genome annotation databases

EnsembliENSBTAT00000017940; ENSBTAP00000017940; ENSBTAG00000013492. [Q2LL38-1]
GeneIDi511961.
KEGGibta:511961.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ082732 mRNA. Translation: AAZ31228.1.
DQ082733 mRNA. Translation: AAZ31229.1.
DQ082734 mRNA. Translation: AAZ31230.1.
DQ082735 mRNA. Translation: AAZ31231.1.
DQ082736 Genomic DNA. Translation: AAZ31232.1.
DQ082736 Genomic DNA. Translation: AAZ31233.1.
DQ082736 Genomic DNA. Translation: AAZ31234.1.
DQ082736 Genomic DNA. Translation: AAZ31235.1.
RefSeqiNP_001025473.2. NM_001030302.2. [Q2LL38-1]
NP_001155891.1. NM_001162419.1. [Q2LL38-3]
NP_001155892.1. NM_001162420.1. [Q2LL38-2]
NP_001155893.1. NM_001162421.1. [Q2LL38-4]
UniGeneiBt.42124.

3D structure databases

ProteinModelPortaliQ2LL38.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000017940.

Proteomic databases

PaxDbiQ2LL38.
PRIDEiQ2LL38.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000017940; ENSBTAP00000017940; ENSBTAG00000013492. [Q2LL38-1]
GeneIDi511961.
KEGGibta:511961.

Organism-specific databases

CTDi53632.

Phylogenomic databases

eggNOGiKOG1764. Eukaryota.
COG0517. LUCA.
GeneTreeiENSGT00390000009849.
HOVERGENiHBG050431.
InParanoidiQ2LL38.
KOiK07200.
OMAiAKASRWT.
OrthoDBiEOG091G0CZV.
TreeFamiTF313247.

Enzyme and pathway databases

ReactomeiR-BTA-1632852. Macroautophagy.
R-BTA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-BTA-5628897. TP53 Regulates Metabolic Genes.
R-BTA-6804756. Regulation of TP53 Activity through Phosphorylation.

Gene expression databases

BgeeiENSBTAG00000013492.

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 nameiAAKG3_BOVIN
AccessioniPrimary (citable) accession number: Q2LL38
Secondary accession number(s): Q2LL34
, Q2LL35, Q2LL36, Q2LL37, Q2LL39, Q2LL40, Q2LL41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: October 5, 2016
This is version 62 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, 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.