P15105 (GLNA_MOUSE) 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

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

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. Ref.7
Subcellular location	Cytoplasm. Mitochondrion By similarity.
Post-translational modification	Ubiquitinated by ZNRF1. Ref.10
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	cell proliferation Inferred from electronic annotation. Source: Compara glutamate metabolic process Inferred from electronic annotation. Source: Compara glutamine biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of insulin secretion Inferred from electronic annotation. Source: Compara positive regulation of synaptic transmission, glutamatergic Inferred from electronic annotation. Source: Compara protein homooligomerization Inferred from electronic annotation. Source: Compara response to glucose stimulus Inferred from mutant phenotype PubMed 17854388. Source: MGI
Cellular_component	axon terminus Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay PubMed 14651853. Source: MGI perikaryon Inferred from electronic annotation. Source: Compara protein complex Inferred from electronic annotation. Source: Compara rough endoplasmic reticulum Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate binding Inferred from electronic annotation. Source: Compara glutamate decarboxylase activity Inferred from electronic annotation. Source: EC glutamate-ammonia ligase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: Compara manganese ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6
	Chain	2 – 373	372	Glutamine synthetase		PRO_0000153141
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.6
	Modified residue	104	1	Phosphotyrosine Ref.9
	Modified residue	180	1	Phosphotyrosine Ref.9
Experimental info
	Sequence conflict	91	1	K → R in CAA34381. Ref.1
	Sequence conflict	111	1	T → S in AAA17989. Ref.2
	Sequence conflict	133	1	M → L in BAE37022. Ref.4
	Sequence conflict	249	1	G → V in CAA34381. Ref.1
	Sequence conflict	269	1	C → W in AAA17989. Ref.2
	Sequence conflict	299	1	R → A in CAA34381. Ref.1
	Sequence conflict	342 – 343	2	PS → LR in CAA34381. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P15105 [UniParc]. Last modified April 17, 2007. Version 6. Checksum: 1EC9CDC5D81DE63F	FASTA	373	42,120
	10 20 30 40 50 60 MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE PKCVEELPEW 70 80 90 100 110 120 NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR KDPNKLVLCE VFKYNRKPAE TNLRHICKRI 130 140 150 160 170 180 MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY 190 200 210 220 230 240 RACLYAGVKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWI ARFILHRVCE DFGVIATFDP 250 260 270 280 290 300 KPIPGNWNGA GCHTNFSTKA MREENGLKCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL 310 320 330 340 350 360 TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPYA VTEAIVRTCL 370 LNETGDEPFQ YKN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mouse glutamine synthetase is encoded by a single gene that can be expressed in a localized fashion." Kuo C.F., Darnell J.E. Jr. J. Mol. Biol. 208:45-56(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence of a mouse glutamine synthetase cDNA." Lindemann A.E., Tempest P.R. Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymus.
[3]	"Glutamine synthetase mRNA in rodents." Labruyere W.T., van Hemert F.J., Lamers W.H. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: FVB. Tissue: Liver.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Amnion, Hippocampus and Vagina.
[5]	"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: FVB/N. Tissue: Colon.
[6]	Bienvenut W.V. Submitted (JUL-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-11; 15-25; 96-103; 174-181; 292-298 AND 341-357, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Liver.
[7]	"Molecular characterization and immunohistochemical localization of palmdelphin, a cytosolic isoform of the paralemmin protein family implicated in membrane dynamics." Hu B., Petrasch-Parwez E., Laue M.M., Kilimann M.W. Eur. J. Cell Biol. 84:853-866(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PALMD.
[8]	Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 26-41; 46-52; 174-222 AND 341-357, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[9]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104 AND TYR-180, MASS SPECTROMETRY. Tissue: Brain.
[10]	"Proteasomal degradation of glutamine synthetase regulates schwann cell differentiation." Saitoh F., Araki T. J. Neurosci. 30:1204-1212(2010) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X16314 mRNA. Translation: CAA34381.1. U09114 mRNA. Translation: AAA17989.1. AY044241 mRNA. Translation: AAK95328.1. AK159106 mRNA. Translation: BAE34822.1. AK160670 mRNA. Translation: BAE35950.1. AK162685 mRNA. Translation: BAE37022.1. AK168493 mRNA. Translation: BAE40380.1. BC015086 mRNA. Translation: AAH15086.1.
IPI	IPI00626790.
PIR	AJMSQ. S04991.
RefSeq	NP_032157.2. NM_008131.3.
UniGene	Mm.210745.
3D structure databases
ProteinModelPortal	P15105.
SMR	P15105. Positions 10-365.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15105. 6 interactions.
PTM databases
PhosphoSite	P15105.
2D gel databases
REPRODUCTION-2DPAGE	IPI00626790. P15105.
SWISS-2DPAGE	P15105.
UCD-2DPAGE	P15105.
Proteomic databases
PaxDb	P15105.
PRIDE	P15105.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000086199; ENSMUSP00000083375; ENSMUSG00000026473.
GeneID	14645.
KEGG	mmu:14645.
UCSC	uc007daq.1. mouse.
Organism-specific databases
CTD	2752.
MGI	MGI:95739. Glul.
Phylogenomic databases
eggNOG	COG0174.
GeneTree	ENSGT00390000010047.
HOGENOM	HOG000061500.
HOVERGEN	HBG005847.
InParanoid	P15105.
KO	K01915.
OMA	YGIDIEF.
OrthoDB	EOG444KKD.
Gene expression databases
ArrayExpress	P15105.
Bgee	P15105.
CleanEx	MM_GLUL.
Genevestigator	P15105.
GermOnline	ENSMUSG00000026473. Mus musculus.
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	286500.
SOURCE	Search...

Entry information

Entry name

GLNA_MOUSE

Accession

Primary (citable) accession number: P15105
Secondary accession number(s): Q3TRK7, Q64432, Q91VC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 17, 2007
Last modified:	May 1, 2013
This is version 120 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program