Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8LCE1 (GLN12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine synthetase cytosolic isozyme 1-2

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase GLN1;2
Short name=GLN1;2
Gene names
Name:GLN1-2
Synonyms:GSR2
Ordered Locus Names:At1g66200
ORF Names:F15E12.14
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Low-affinity glutamine synthetase. May contribute to the homeostatic control of glutamine synthesis in roots.

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

Subunit structure

Homooctamer By similarity.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in the pericycle of all root tissues. Ref.7

Induction

By ammonium supply under nitrogen-limited condition. Induced by sucrose, glucose, fructose, and during leaf senescence. Ref.5 Ref.6 Ref.7

Sequence similarities

Belongs to the glutamine synthetase family.

Biophysicochemical properties

Kinetic parameters:

Measured at pH 7.8 and 30 degrees Celsius for all experiments.

KM=3.8 mM for glutamate Ref.7

KM=2450 µM for ammonium

KM=1100 µM for ATP

Vmax=65.7 nmol/sec/mg enzyme with glutamate as substrate

Vmax=65.7 nmol/sec/mg enzyme with ammonium as substrate

Vmax=66.6 nmol/sec/mg enzyme with ATP as substrate

Ontologies

Keywords
   Biological processNitrogen fixation
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

nitrogen fixation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q8LCE1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 356355Glutamine synthetase cytosolic isozyme 1-2
PRO_0000239819

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue21Phosphoserine Ref.8
Modified residue481Phosphoserine By similarity

Experimental info

Sequence conflict2901R → L in AAM63710. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: 19D19BF1388E5192

FASTA35639,207
        10         20         30         40         50         60 
MSLLADLVNL DISDNSEKII AEYIWVGGSG MDMRSKARTL PGPVTDPSKL PKWNYDGSST 

        70         80         90        100        110        120 
GQAPGQDSEV ILYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AEIFANPDVI 

       130        140        150        160        170        180 
AEVPWYGIEQ EYTLLQKDVN WPLGWPIGGF PGPQGPYYCS IGADKSFGRD IVDAHYKASL 

       190        200        210        220        230        240 
YAGINISGIN GEVMPGQWEF QVGPSVGISA ADEIWIARYI LERITEIAGV VVSFDPKPIP 

       250        260        270        280        290        300 
GDWNGAGAHT NYSTKSMREE GGYEIIKKAI EKLGLRHKEH ISAYGEGNER RLTGHHETAD 

       310        320        330        340        350 
INTFLWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAET TLLWNP 

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Senescence-associated gene expression during ozone-induced leaf senescence in Arabidopsis."
Miller J.D., Arteca R.N., Pell E.J.
Plant Physiol. 120:1015-1024(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[6]"Carbon and amino acids reciprocally modulate the expression of glutamine synthetase in Arabidopsis."
Oliveira I.C., Coruzzi G.M.
Plant Physiol. 121:301-310(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Kinetic properties and ammonium-dependent regulation of cytosolic isoenzymes of glutamine synthetase in Arabidopsis."
Ishiyama K., Inoue E., Watanabe-Takahashi A., Obara M., Yamaya T., Takahashi H.
J. Biol. Chem. 279:16598-16605(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, INDUCTION.
[8]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC026480 Genomic DNA. Translation: AAG51310.1.
CP002684 Genomic DNA. Translation: AEE34474.1.
AY091101 mRNA. Translation: AAM14052.1.
AY122962 mRNA. Translation: AAM67495.1.
AY086653 mRNA. Translation: AAM63710.1.
PIRH96686.
S18602.
RefSeqNP_176794.1. NM_105291.3. [Q8LCE1-1]
UniGeneAt.47484.
At.74857.

3D structure databases

ProteinModelPortalQ8LCE1.
SMRQ8LCE1. Positions 4-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid28156. 1 interaction.
IntActQ8LCE1. 1 interaction.

Proteomic databases

PaxDbQ8LCE1.
PRIDEQ8LCE1.

Protocols and materials databases

DNASU842935.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G66200.1; AT1G66200.1; AT1G66200. [Q8LCE1-1]
GeneID842935.
KEGGath:AT1G66200.

Organism-specific databases

TAIRAT1G66200.

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000061500.
InParanoidQ8LCE1.
PhylomeDBQ8LCE1.

Enzyme and pathway databases

BioCycARA:GQT-852-MONOMER.
ARA:GQT-853-MONOMER.
SABIO-RKQ8LCE1.

Gene expression databases

ArrayExpressQ8LCE1.
GenevestigatorQ8LCE1.

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...

Entry information

Entry nameGLN12_ARATH
AccessionPrimary (citable) accession number: Q8LCE1
Secondary accession number(s): Q9C8C7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: May 14, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names