Q8LCE1 (GLN12_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Mesangiospermae › eudicotyledons › Gunneridae › Pentapetalae › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Nitrogen fixation
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glutamine biosynthetic process Inferred from electronic annotation. Source: InterPro nitrogen fixation Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Glutamine synthetase cytosolic isozyme 1-2		PRO_0000239819
Amino acid modifications
	Modified residue	2	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	290	1	R → L in AAM63710. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 13, 2006. Version 2. Checksum: 19D19BF1388E5192	FASTA	356	39,207
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. Strain: cv. Columbia. Tissue: Seedling.
+	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.
PIR	H96686. S18602.
RefSeq	NP_176794.1. NM_105291.3.
UniGene	At.47484. At.74857.
3D structure databases
ProteinModelPortal	Q8LCE1.
SMR	Q8LCE1. Positions 4-354.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	28156. 1 interaction.
IntAct	Q8LCE1. 1 interaction.
Proteomic databases
PaxDb	Q8LCE1.
PRIDE	Q8LCE1.
Protocols and materials databases
DNASU	842935.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G66200.1; AT1G66200.1; AT1G66200.
GeneID	842935.
KEGG	ath:AT1G66200.
Organism-specific databases
TAIR	AT1G66200.
Phylogenomic databases
eggNOG	COG0174.
HOGENOM	HOG000061500.
InParanoid	Q8LCE1.
PhylomeDB	Q8LCE1.
ProtClustDB	PLN02284.
Enzyme and pathway databases
BioCyc	ARA:GQT-852-MONOMER. ARA:GQT-853-MONOMER.
SABIO-RK	Q8LCE1.
Gene expression databases
ArrayExpress	Q8LCE1.
Genevestigator	Q8LCE1.
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. SSF54368. 1 hit.
PROSITE	PS00180. GLNA_1. 1 hit. PS00181. GLNA_ATP. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLN12_ARATH

Accession

Primary (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:	February 19, 2014
This is version 78 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program