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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:
  • biotinBy similarityNote: Biotin.By similarity
  • Mg2+By similarity, Mn2+By similarity

GO - Molecular functioni

  1. ATP binding Source: RGD
  2. dynein light chain binding Source: RGD
  3. glutamate-ammonia ligase activity Source: RGD
  4. glutamate binding Source: RGD
  5. glutamate decarboxylase activity Source: UniProtKB-EC
  6. magnesium ion binding Source: RGD
  7. manganese ion binding Source: RGD

GO - Biological processi

  1. ammonia assimilation cycle Source: RGD
  2. cell proliferation Source: Ensembl
  3. cellular response to starvation Source: Ensembl
  4. glutamate metabolic process Source: RGD
  5. glutamine biosynthetic process Source: RGD
  6. neurotransmitter metabolic process Source: RGD
  7. positive regulation of epithelial cell proliferation Source: RGD
  8. positive regulation of insulin secretion Source: RGD
  9. positive regulation of synaptic transmission, glutamatergic Source: RGD
  10. protein homooligomerization Source: RGD
  11. response to glucose Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Lyase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_214662. Amino acid synthesis and interconversion (transamination).
REACT_219617. Astrocytic Glutamate-Glutamine Uptake And Metabolism.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 13

Organism-specific databases

RGDi2710. Glul.

Subcellular locationi

Cytoplasm. Mitochondrion By similarity

GO - Cellular componenti

  1. axon terminus Source: RGD
  2. cell projection Source: RGD
  3. cytoplasm Source: RGD
  4. extracellular vesicular exosome Source: Ensembl
  5. glial cell projection Source: Ensembl
  6. intracellular membrane-bounded organelle Source: RGD
  7. mitochondrion Source: UniProtKB-SubCell
  8. neuron projection Source: RGD
  9. nucleus Source: Ensembl
  10. perikaryon Source: RGD
  11. protein complex Source: RGD
  12. rough endoplasmic reticulum Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 373372Glutamine synthetasePRO_0000153143Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei104 – 1041PhosphotyrosineBy similarity

Post-translational modificationi

Ubiquitinated by ZNRF1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP09606.

2D gel databases

World-2DPAGE0004:P09606.

PTM databases

PhosphoSiteiP09606.

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

GenevestigatoriP09606.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi247058. 2 interactions.
IntActiP09606. 1 interaction.
MINTiMINT-4578083.

Structurei

3D structure databases

ProteinModelPortaliP09606.
SMRiP09606. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000010047.
HOVERGENiHBG005847.
InParanoidiP09606.
KOiK01915.
OMAiRIPRNVG.
OrthoDBiEOG7CZK5G.
PhylomeDBiP09606.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741N → D in AAH61559. (PubMed:15489334)Curated
Sequence conflicti128 – 1281H → R in AAC42038. (PubMed:1674354)Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP09606.
SMRiP09606. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247058. 2 interactions.
IntActiP09606. 1 interaction.
MINTiMINT-4578083.

PTM databases

PhosphoSiteiP09606.

2D gel databases

World-2DPAGE0004:P09606.

Proteomic databases

PRIDEiP09606.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2752.
RGDi2710. Glul.

Phylogenomic databases

GeneTreeiENSGT00390000010047.
HOVERGENiHBG005847.
InParanoidiP09606.
KOiK01915.
OMAiRIPRNVG.
OrthoDBiEOG7CZK5G.
PhylomeDBiP09606.

Enzyme and pathway databases

ReactomeiREACT_214662. Amino acid synthesis and interconversion (transamination).
REACT_219617. Astrocytic Glutamate-Glutamine Uptake And Metabolism.

Miscellaneous databases

NextBioi604985.
PROiP09606.

Gene expression databases

GenevestigatoriP09606.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.
    Tissue: Liver.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  3. "Cloning and functional characterization of the rat glutamine synthetase gene."
    Mill J.F., Mearow K.M., Purohit H.J., Haleem-Smith H., King R., Freese E.
    Brain Res. Mol. Brain Res. 9:197-207(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Brown Norway.
    Tissue: Heart and Pituitary.
  5. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 15-41; 92-103; 190-213; 299-319 AND 341-357, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.
  6. "Wnt and steroid pathways control glutamate signalling by regulating glutamine synthetase activity in osteoblastic cells."
    Olkku A., Mahonen A.
    Bone 43:483-493(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.

Entry informationi

Entry nameiGLNA_RAT
AccessioniPrimary (citable) accession number: P09606
Secondary accession number(s): Q6P7Q9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 7, 2015
This is version 127 of the entry and version 3 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

External Data

Dasty 3

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 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.