Q9QY94 (GLNA_ACOCA) 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

Organism

Acomys cahirinus (Cairo spiny mouse)

Taxonomic identifier

10068 [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 › Deomyinae › Acomys

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 transcript 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 By similarity. Mitochondrion By similarity.
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
Gene Ontology (GO)
Biological_process	glutamine biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular_component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate decarboxylase activity Inferred from electronic annotation. Source: EC glutamate-ammonia ligase activity Inferred from electronic annotation. Source: EC
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_0000153135
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

Sequences

	Sequence		Length	Mass (Da)
	Q9QY94 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 51BAD0B2EBA18AB6	FASTA	373	42,165
	10 20 30 40 50 60 MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE PKCVEELPEW 70 80 90 100 110 120 NFDGSSTFQS EGSNSDMYLS PVAMFRDPFR KEPNKLVFCE VFKYNRKPAE TNLRHSCKRI 130 140 150 160 170 180 MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY 190 200 210 220 230 240 RACLYAGVKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWV ARFILHRVCE DFGVIATFDP 250 260 270 280 290 300 KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL 310 320 330 340 350 360 TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKRGYFEDR RPSANCDPYA VTEAIVRTCL 370 LNETGNEPFQ YKN

References

[1]	"Glutamine synthetase expression in perinatal spiny mouse liver." Lamers W.H., Boon L., Van Hemert F.J., Labruyere W.T., De Jong P., Ruijter J.M., Moorman A.F. Eur. J. Biochem. 262:803-809(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF110381 mRNA. Translation: AAF14691.1.
3D structure databases
ProteinModelPortal	Q9QY94.
SMR	Q9QY94. Positions 3-372.
ModBase	Search...
Proteomic databases
PRIDE	Q9QY94.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG005847.
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...

Entry information

Entry name

GLNA_ACOCA

Accession

Primary (citable) accession number: Q9QY94

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 60 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program