P09606 (GLNA_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	373 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cytoplasm Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase Lyase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ammonia assimilation cycle Inferred from direct assay PubMed 28323. Source: RGD cell proliferation Inferred from electronic annotation. Source: Compara 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 stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	axon terminus Inferred from direct assay PubMed 6105901. Source: RGD mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell 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_function	ATP binding Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD glutamate binding Inferred from direct assay PubMed 28323PubMed 4403443. Source: RGD glutamate decarboxylase activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 373	372	Glutamine synthetase		PRO_0000153143
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	104	1	Phosphotyrosine By similarity
	Modified residue	180	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	74	1	N → D in AAH61559. Ref.4
	Sequence conflict	128	1	H → R in AAC42038. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P09606 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A7C12D9C5959BCA1	FASTA	373	42,268
	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

References

	« Hide 'large scale' referencesShow '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, 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 , 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.
IPI	IPI00324020.
PIR	AJRTQ. S01242.
RefSeq	NP_058769.4. NM_017073.3.
UniGene	Rn.2204.
3D structure databases
ProteinModelPortal	P09606.
SMR	P09606. Positions 3-372.
ModBase	Search...
Protein-protein interaction databases
IntAct	P09606. 1 interaction.
PTM databases
PhosphoSite	P09606.
2D gel databases
World-2DPAGE	0004:P09606.
Proteomic databases
PRIDE	P09606.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000075480; ENSRNOP00000065890; ENSRNOG00000049560.
GeneID	24957.
KEGG	rno:24957.
Organism-specific databases
CTD	2752.
RGD	2710. Glul.
Phylogenomic databases
GeneTree	ENSGT00390000010047.
HOVERGEN	HBG005847.
KO	K01915.
Gene expression databases
Genevestigator	P09606.
Family and domain databases
Gene3D	3.30.590.10. 1 hit.
InterPro	IPR008147. 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]
Pfam	PF00120. Gln-synt_C. 1 hit. PF03951. Gln-synt_N. 1 hit. [Graphical view]
SUPFAM	SSF54368. Gln_synt_beta. 1 hit.
PROSITE	PS00180. GLNA_1. 1 hit. PS00181. GLNA_ATP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	604985.

Entry information

Entry name

GLNA_RAT

Accession

Primary (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 1, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program