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Q8HZM5 (GLNA_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 By similarity. Mitochondrion By similarity.

Post-translational modification

Ubiquitinated by ZNRF1 By similarity.

Sequence similarities

Belongs to the glutamine synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 373372Glutamine synthetase
PRO_0000153137

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1041Phosphotyrosine By similarity

Secondary structure

..................................................................... 373
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8HZM5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E5AD18AEED3F0C52

FASTA37342,028
        10         20         30         40         50         60 
MATSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKGVEELPEW 

        70         80         90        100        110        120 
NFDGSSTFQS EGSNSDMYLV PAAMFRDPFR KDPNKLVFCE VFKYNRKPAE TNLRHTCKRI 

       130        140        150        160        170        180 
MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY 

       190        200        210        220        230        240 
RACLYAGIKI AGTNAEVMPA QWEFQIGPCE GIDMGDHLWV ARFILHRVCE DFGVIATFDP 

       250        260        270        280        290        300 
KPIPGNWNGA GCHTNFSTKA MREENGLKYI EESIEKLSKR HQYHIRAYDP KGGLDNARRL 

       310        320        330        340        350        360 
TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL 

       370 
LNETGDEPFQ YKN 

« Hide

References

[1]"A splice variant acquiring an extra transcript leader region decreases the translation of glutamine synthetase gene."
Shin D., Park S., Park C.
Biochem. J. 374:175-184(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF544242 mRNA. Translation: AAN41001.1.
AF544243 Genomic DNA. Translation: AAN41002.1.
RefSeqNP_001002965.1. NM_001002965.1.
XP_005622277.1. XM_005622220.1.
UniGeneCfa.1407.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2UU7X-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O2-373[»]
ProteinModelPortalQ8HZM5.
SMRQ8HZM5. Positions 3-372.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ8HZM5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000020795; ENSCAFP00000019307; ENSCAFG00000013102.
GeneID403443.
KEGGcfa:403443.

Organism-specific databases

CTD2752.

Phylogenomic databases

eggNOGCOG0174.
GeneTreeENSGT00390000010047.
HOGENOMHOG000061500.
HOVERGENHBG005847.
InParanoidQ8HZM5.
KOK01915.
OrthoDBEOG7CZK5G.

Enzyme and pathway databases

SABIO-RKQ8HZM5.

Family and domain databases

Gene3D3.30.590.10. 1 hit.
InterProIPR008147. 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]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ8HZM5.
NextBio20816961.

Entry information

Entry nameGLNA_CANFA
AccessionPrimary (citable) accession number: Q8HZM5
Secondary accession number(s): Q8HZM4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 75 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references