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P09606 (GLNA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine synthetase

Short name=GS
EC=6.3.1.2
Alternative name(s):
Glutamate decarboxylase
EC=4.1.1.15
Glutamate--ammonia ligase
Gene names
Name:Glul
Synonyms:Glns
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

L-glutamate = 4-aminobutanoate + CO2.

Cofactor

Biotin By similarity.

Magnesium or manganese By similarity.

Subunit structure

Homooctamer and homotetramer. Interacts with PALMD By similarity.

Subcellular location

Cytoplasm. Mitochondrion By similarity.

Induction

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. Ref.6

Post-translational modification

Ubiquitinated by ZNRF1 By similarity.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Lyase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processammonia assimilation cycle

Inferred from direct assay PubMed 28323. Source: RGD

cell proliferation

Inferred from electronic annotation. Source: Ensembl

glutamate metabolic process

Inferred from direct assay PubMed 4403443. Source: RGD

glutamine biosynthetic process

Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD

neurotransmitter metabolic process

Traceable author statement Ref.3. Source: RGD

positive regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 9915876. Source: RGD

positive regulation of insulin secretion

Inferred from mutant phenotype PubMed 12575909. Source: RGD

positive regulation of synaptic transmission, glutamatergic

Inferred from mutant phenotype PubMed 10696145. Source: RGD

protein homooligomerization

Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD

response to glucose

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentaxon terminus

Inferred from direct assay PubMed 6105901. Source: RGD

cell projection

Inferred from direct assay PubMed 31966. Source: RGD

cytoplasm

Inferred from direct assay PubMed 9219972. Source: RGD

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 28323PubMed 37288. Source: RGD

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from direct assay PubMed 37288PubMed 6105901. Source: RGD

perikaryon

Inferred from direct assay PubMed 1363168PubMed 31966. Source: RGD

protein complex

Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD

rough endoplasmic reticulum

Inferred from direct assay PubMed 1363168PubMed 31966. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD

dynein light chain binding

Inferred from physical interaction PubMed 14760703. Source: RGD

glutamate binding

Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD

glutamate decarboxylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glutamate-ammonia ligase activity

Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD

magnesium ion binding

Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD

manganese ion binding

Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 373372Glutamine synthetase
PRO_0000153143

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1041Phosphotyrosine By similarity

Experimental info

Sequence conflict741N → D in AAH61559. Ref.4
Sequence conflict1281H → R in AAC42038. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P09606 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A7C12D9C5959BCA1

FASTA37342,268
        10         20         30         40         50         60 
MATSASSHLN KGIKQMYMNL PQGEKIQLMY IWVDGTGEGL RCKTRTLDCD PKCVEELPEW 

        70         80         90        100        110        120 
NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR RDPNKLVFCE VFKYNRKPAE TNLRHSCKRI 

       130        140        150        160        170        180 
MDMVSSQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY 

       190        200        210        220        230        240 
RACLYAGIKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWV ARFILHRVCE DFGVIATFDP 

       250        260        270        280        290        300 
KPIPGNWNGA GCHTNFSTKA MREENGLRCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL 

       310        320        330        340        350        360 
TGFHETSNIN DFSAGVANRS ASIRIPRIVG QEKKGYFEDR RPSANCDPYA VTEAIVRTCL 

       370 
LNETGDEPFQ YKN 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of rat glutamine synthetase mRNA."
van de Zande L., Labruyere W., Smaling M., Moorman A., Wilson R.H., Charles R., Lamers W.H.
Nucleic Acids Res. 16:7726-7726(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Liver.
[2]"Isolation and characterization of the rat glutamine synthetase-encoding gene."
van de Zande L., Labruyere W.T., Arnberg A.C., Wilson R.H., van de Bogaert A.J.W., Das A.T., van Oorschot D.A.J., Frijters C., Charles R., Moorman A.F.M., Lamers W.H.
Gene 87:225-232(1990) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X07921 mRNA. Translation: CAA30754.1.
M29599 expand/collapse EMBL AC list , 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.
PIRAJRTQ. S01242.
RefSeqNP_058769.4. NM_017073.3.
UniGeneRn.2204.

3D structure databases

ProteinModelPortalP09606.
SMRP09606. Positions 3-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247058. 2 interactions.
IntActP09606. 1 interaction.
MINTMINT-4578083.

PTM databases

PhosphoSiteP09606.

2D gel databases

World-2DPAGE0004:P09606.

Proteomic databases

PRIDEP09606.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000075480; ENSRNOP00000065890; ENSRNOG00000049560.
GeneID24957.
KEGGrno:24957.

Organism-specific databases

CTD2752.
RGD2710. Glul.

Phylogenomic databases

GeneTreeENSGT00390000010047.
HOVERGENHBG005847.
KOK01915.
OMARIPRNVG.
OrthoDBEOG7CZK5G.
PhylomeDBP09606.

Gene expression databases

GenevestigatorP09606.

Family and domain databases

Gene3D3.30.590.10. 1 hit.
InterProIPR008147. 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]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604985.
PROP09606.

Entry information

Entry nameGLNA_RAT
AccessionPrimary (citable) accession number: P09606
Secondary accession number(s): Q6P7Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families