Glutamine synthetase - Cricetulus griseus (Chinese hamster)

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P04773 (GLNA_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)

Taxonomic identifier

10029 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus

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

Removed By similarity

Chain

2 – 373

372

Glutamine synthetase

PRO_0000153138

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

104

Phosphotyrosine By similarity

Modified residue

180

Phosphotyrosine By similarity

Experimental info

Sequence conflict

G → N in CAA27211. Ref.2

Sequence conflict

18 – 19

MS → LC in CAA27211. Ref.2

Sequence conflict

S → G in CAA27211. Ref.2

Sequence conflict

91 – 92

KE → RD in CAA27211. Ref.2

Sequence conflict

106

Q → R in CAA27211. Ref.2

Sequence conflict

116

T → S in CAA27211. Ref.2

Sequence conflict

140

L → M in CAA27211. Ref.2

Sequence conflict

152

D → N in CAA27211. Ref.2

Sequence conflict

160

L → P in CAA27211. Ref.2

Sequence conflict

172

R → G in CAA27211. Ref.2

Sequence conflict

176

M → V in CAA27211. Ref.2

Sequence conflict

194

Y → N in CAA27211. Ref.2

Sequence conflict

198 – 199

KH → MP in CAA27211. Ref.2

Sequence conflict

230

K → E in CAA27211. Ref.2

Sequence conflict

240

S → P in CAA27211. Ref.2

Sequence conflict

260

T → A in CAA27211. Ref.2

Sequence conflict

271

K → E in CAA27211. Ref.2

Sequence conflict

299

R → G in CAA27211. Ref.2

Sequence conflict

305

K → E in CAA27211. Ref.2

Sequence conflict

318

D → N in CAA27211. Ref.2

Sequence conflict

339 – 341

ARC → DRR in CAA27211. Ref.2

Sequence conflict

367

Q → E in CAA27211. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P04773 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 611D58CE20FB16CF
Show »

FASTA

373

42,320

        10         20         30         40         50         60 
MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE PKCVEELPEW 

        70         80         90        100        110        120 
NFDGSSTFQS ESSNSDMYLS PVAMFRDPFR KEPNKLVFCE VFKYNQKPAE TNLRHTCKRI 

       130        140        150        160        170        180 
MDMVSNQHPW FGMEQEYTLL GTDGHPFGWP SDGFPGPQGL YYCGVGADKA YRRDIMEAHY 

       190        200        210        220        230        240 
RACLYAGVKI TGTYAEVKHA QWEFQIGPCE GIRMGDHLWV ARFILHRVCK DFGVIATFDS 

       250        260        270        280        290        300 
KPIPGNWNGA GCHTNFSTKT MREENGLKHI KEAIEKLSKR HRYHIRAYDP KGGLDNARRL 

       310        320        330        340        350        360 
TGFHKTSNIN DFSAGVADRS ASIRIPRTVG QEKKGYFEAR CPSANCDPFA VTEAIVRTCL 

       370 
LNETGDQPFQ YKN

« Hide

References

[1]	"The cloning and nucleotide sequence of cDNA for an amplified glutamine synthetase gene from the Chinese hamster." Hayward B.E., Hussain A., Wilson R.H., Lyons A., Woodcock V., McIntosh B., Harris T.J.R. Nucleic Acids Res. 14:999-1008(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Ovary.
[2]	Tong Y., Wang H. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X03495 mRNA. Translation: CAA27211.1. AF150961 mRNA. Translation: AAG43362.1.
RefSeq	NP_001233699.1. NM_001246770.1.
3D structure databases
ProteinModelPortal	P04773.
SMR	P04773. Positions 3-372.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100689337.
Organism-specific databases
CTD	2752.
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_CRIGR

Accession

Primary (citable) accession number: P04773
Secondary accession number(s): Q9EQP8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 84 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents