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Protein

Glutamine synthetase

Gene

Glul

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential for proliferation of fetal skin fibroblasts. This enzyme has 2 functions: it catalyzes the production of glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA), the latter in a pyridoxal phosphate-independent manner (By similarity).By similarity

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Protein has several cofactor binding sites:

GO - Molecular functioni

  • ATP binding Source: RGD
  • dynein light chain binding Source: RGD
  • glutamate-ammonia ligase activity Source: RGD
  • glutamate binding Source: RGD
  • glutamate decarboxylase activity Source: UniProtKB-EC
  • identical protein binding Source: Ensembl
  • magnesium ion binding Source: RGD
  • manganese ion binding Source: RGD

GO - Biological processi

  • ammonia assimilation cycle Source: RGD
  • cell proliferation Source: Ensembl
  • cellular response to starvation Source: Ensembl
  • glutamate metabolic process Source: RGD
  • glutamine biosynthetic process Source: RGD
  • neurotransmitter metabolic process Source: RGD
  • positive regulation of epithelial cell proliferation Source: RGD
  • positive regulation of insulin secretion Source: RGD
  • positive regulation of synaptic transmission, glutamatergic Source: RGD
  • protein homooligomerization Source: RGD
  • response to glucose Source: Ensembl

Keywordsi

Molecular functionLigase, Lyase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.3.1.2. 5301.
ReactomeiR-RNO-210455. Astrocytic Glutamate-Glutamine Uptake And Metabolism.
R-RNO-70614. Amino acid synthesis and interconversion (transamination).

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate decarboxylase (EC:4.1.1.15)
Glutamate--ammonia ligase
Gene namesi
Name:Glul
Synonyms:Glns
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi2710. Glul.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001531432 – 373Glutamine synthetaseAdd BLAST372

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei104PhosphotyrosineBy similarity1
Modified residuei343PhosphoserineBy similarity1

Post-translational modificationi

Ubiquitinated by ZNRF1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP09606.
PRIDEiP09606.

2D gel databases

World-2DPAGEi0004:P09606.

PTM databases

iPTMnetiP09606.
PhosphoSitePlusiP09606.
SwissPalmiP09606.

Expressioni

Inductioni

By glucocorticoids. Stimulated by the N-methyl-D-aspartate (NMDA) type glutamate receptor antagonist MK801. Vitamin D and the Wnt signaling pathway inhibit its expression and activity. Down-regulated during osteoblast mineralization.1 Publication

Gene expression databases

BgeeiENSRNOG00000049560.
GenevisibleiP09606. RN.

Interactioni

Subunit structurei

Homooctamer and homotetramer. Interacts with PALMD (By similarity).By similarity

GO - Molecular functioni

  • dynein light chain binding Source: RGD
  • identical protein binding Source: Ensembl

Protein-protein interaction databases

BioGridi247058. 2 interactors.
IntActiP09606. 1 interactor.
MINTiMINT-4578083.
STRINGi10116.ENSRNOP00000065890.

Structurei

3D structure databases

ProteinModelPortaliP09606.
SMRiP09606.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

eggNOGiKOG0683. Eukaryota.
COG0174. LUCA.
GeneTreeiENSGT00390000010047.
HOVERGENiHBG005847.
InParanoidiP09606.
KOiK01915.
OMAiMMPDGVT.
OrthoDBiEOG091G07E9.
PhylomeDBiP09606.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiView protein in InterPro
IPR008147. Gln_synt_b-grasp.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
PfamiView protein in Pfam
PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
SMARTiView protein in SMART
SM01230. Gln-synt_C. 1 hit.
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiView protein in PROSITE
PS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P09606-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATSASSHLN KGIKQMYMNL PQGEKIQLMY IWVDGTGEGL RCKTRTLDCD
60 70 80 90 100
PKCVEELPEW NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR RDPNKLVFCE
110 120 130 140 150
VFKYNRKPAE TNLRHSCKRI MDMVSSQHPW FGMEQEYTLM GTDGHPFGWP
160 170 180 190 200
SNGFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGIKI TGTNAEVMPA
210 220 230 240 250
QWEFQIGPCE GIRMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA
260 270 280 290 300
GCHTNFSTKA MREENGLRCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL
310 320 330 340 350
TGFHETSNIN DFSAGVANRS ASIRIPRIVG QEKKGYFEDR RPSANCDPYA
360 370
VTEAIVRTCL LNETGDEPFQ YKN
Length:373
Mass (Da):42,268
Last modified:January 23, 2007 - v3
Checksum:iA7C12D9C5959BCA1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti74N → D in AAH61559 (PubMed:15489334).Curated1
Sequence conflicti128H → R in AAC42038 (PubMed:1674354).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07921 mRNA. Translation: CAA30754.1.
M29599
, M29595, M29596, M29597, M29598 Genomic DNA. Translation: AAA65096.1.
M29579 mRNA. Translation: AAA65095.1.
M91652 mRNA. Translation: AAC42038.1.
BC061559 mRNA. Translation: AAH61559.1.
BC072694 mRNA. Translation: AAH72694.1.
PIRiS01242. AJRTQ.
RefSeqiNP_058769.4. NM_017073.3.
UniGeneiRn.2204.

Genome annotation databases

EnsembliENSRNOT00000075480; ENSRNOP00000065890; ENSRNOG00000049560.
GeneIDi24957.
KEGGirno:24957.

Similar proteinsi

Entry informationi

Entry nameiGLNA_RAT
AccessioniPrimary (citable) accession number: P09606
Secondary accession number(s): Q6P7Q9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: August 30, 2017
This is version 148 of the entry and version 3 of the sequence. See 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