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P04773

- GLNA_CRIGR

UniProt

P04773 - GLNA_CRIGR

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Protein

Glutamine synthetase

Gene

GLUL

Organism
Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

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.By similarity

Catalytic activityi

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.
L-glutamate = 4-aminobutanoate + CO2.

Cofactori

Biotin.By similarity
Magnesium or manganese.By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. glutamate-ammonia ligase activity Source: UniProtKB-EC
  3. glutamate decarboxylase activity Source: UniProtKB-EC

GO - Biological processi

  1. glutamine biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Lyase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate decarboxylase (EC:4.1.1.15)
Glutamate--ammonia ligase
Gene namesi
Name:GLUL
OrganismiCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifieri10029 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Subcellular locationi

Cytoplasm By similarity. Mitochondrion By similarity

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 373372Glutamine synthetasePRO_0000153138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei104 – 1041PhosphotyrosineBy similarity

Post-translational modificationi

Ubiquitinated by ZNRF1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Interactioni

Subunit structurei

Homooctamer and homotetramer. Interacts with PALMD By similarity.By similarity

Structurei

3D structure databases

ProteinModelPortaliP04773.
SMRiP04773. Positions 3-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

HOVERGENiHBG005847.
KOiK01915.

Family and domain databases

Gene3Di3.30.590.10. 1 hit.
InterProiIPR008147. 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]
PfamiPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMiSSF54368. SSF54368. 1 hit.
PROSITEiPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04773-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE
60 70 80 90 100
PKCVEELPEW NFDGSSTFQS ESSNSDMYLS PVAMFRDPFR KEPNKLVFCE
110 120 130 140 150
VFKYNQKPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLL GTDGHPFGWP
160 170 180 190 200
SDGFPGPQGL YYCGVGADKA YRRDIMEAHY RACLYAGVKI TGTYAEVKHA
210 220 230 240 250
QWEFQIGPCE GIRMGDHLWV ARFILHRVCK DFGVIATFDS KPIPGNWNGA
260 270 280 290 300
GCHTNFSTKT MREENGLKHI KEAIEKLSKR HRYHIRAYDP KGGLDNARRL
310 320 330 340 350
TGFHKTSNIN DFSAGVADRS ASIRIPRTVG QEKKGYFEAR CPSANCDPFA
360 370
VTEAIVRTCL LNETGDQPFQ YKN
Length:373
Mass (Da):42,320
Last modified:January 23, 2007 - v4
Checksum:i611D58CE20FB16CF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121G → N in CAA27211. 1 PublicationCurated
Sequence conflicti18 – 192MS → LC in CAA27211. 1 PublicationCurated
Sequence conflicti72 – 721S → G in CAA27211. 1 PublicationCurated
Sequence conflicti91 – 922KE → RD in CAA27211. 1 PublicationCurated
Sequence conflicti106 – 1061Q → R in CAA27211. 1 PublicationCurated
Sequence conflicti116 – 1161T → S in CAA27211. 1 PublicationCurated
Sequence conflicti140 – 1401L → M in CAA27211. 1 PublicationCurated
Sequence conflicti152 – 1521D → N in CAA27211. 1 PublicationCurated
Sequence conflicti160 – 1601L → P in CAA27211. 1 PublicationCurated
Sequence conflicti172 – 1721R → G in CAA27211. 1 PublicationCurated
Sequence conflicti176 – 1761M → V in CAA27211. 1 PublicationCurated
Sequence conflicti194 – 1941Y → N in CAA27211. 1 PublicationCurated
Sequence conflicti198 – 1992KH → MP in CAA27211. 1 PublicationCurated
Sequence conflicti230 – 2301K → E in CAA27211. 1 PublicationCurated
Sequence conflicti240 – 2401S → P in CAA27211. 1 PublicationCurated
Sequence conflicti260 – 2601T → A in CAA27211. 1 PublicationCurated
Sequence conflicti271 – 2711K → E in CAA27211. 1 PublicationCurated
Sequence conflicti299 – 2991R → G in CAA27211. 1 PublicationCurated
Sequence conflicti305 – 3051K → E in CAA27211. 1 PublicationCurated
Sequence conflicti318 – 3181D → N in CAA27211. 1 PublicationCurated
Sequence conflicti339 – 3413ARC → DRR in CAA27211. 1 PublicationCurated
Sequence conflicti367 – 3671Q → E in CAA27211. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03495 mRNA. Translation: CAA27211.1.
AF150961 mRNA. Translation: AAG43362.1.
RefSeqiNP_001233699.1. NM_001246770.1.

Genome annotation databases

GeneIDi100689337.
KEGGicge:100689337.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X03495 mRNA. Translation: CAA27211.1 .
AF150961 mRNA. Translation: AAG43362.1 .
RefSeqi NP_001233699.1. NM_001246770.1.

3D structure databases

ProteinModelPortali P04773.
SMRi P04773. Positions 3-372.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100689337.
KEGGi cge:100689337.

Organism-specific databases

CTDi 2752.

Phylogenomic databases

HOVERGENi HBG005847.
KOi K01915.

Family and domain databases

Gene3Di 3.30.590.10. 1 hit.
InterProi 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 ]
Pfami PF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view ]
SUPFAMi SSF54368. SSF54368. 1 hit.
PROSITEi PS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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].

Entry informationi

Entry nameiGLNA_CRIGR
AccessioniPrimary (citable) accession number: P04773
Secondary accession number(s): Q9EQP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 89 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3