Gene Details:
- Gene ID: AT5G35630
- Gene Symbol: ATGSL1, GLN2, GS2
- Gene Name: GLUTAMINE SYNTHETASE LIKE 1, GLUTAMINE SYNTHETASE 2, glutamine synthetase 2
- Description: glutamine synthetase 2;(source:Araport11)
- TAIR Accession: locus:2165897
- Genome: Araport11_genome_release
- Species: Arabidopsis thaliana
Transcripts:
Plant Ontology Annotations:
- PO:0009005 — root — raíz (Spanish, exact), radices (exact, plural), radix (exact), 根 (Japanese, exact), aerial root (narrow), climbing root (narrow)
- PO:0009025 — vascular leaf — foliage leaf (exact), hoja vascular (Spanish, exact), leaf, vascular (exact), vascular leaves (exact, plural), 維管束のある葉, または維管束植物の葉 (Japanese, exact), crozier (related), macrophyll (related), megaphyll (related), ascidia (narrow), ascidium (narrow), fiddlehead (narrow), frond (narrow), needle-like leaf (narrow), pitcher (narrow), pitcher blade (narrow), pitcher-blade (narrow), scale-like leaf (narrow), sterile frond (narrow), trophophyll (narrow)
- PO:0000293 — guard cell — célula guardiana (Spanish, exact), occlusive cell (exact), 孔辺細胞 (Japanese, exact)
Gene Ontology:
- GO:0022626 — located in — cytosolic ribosome
- GO:0009941 — located in — chloroplast envelope
- GO:0009535 — located in — chloroplast thylakoid membrane
- GO:0019676 — acts upstream of or within — ammonia assimilation cycle
- GO:0004356 — enables — glutamine synthetase activity
- GO:0048046 — located in — apoplast
- GO:0009507 — located in — chloroplast
- GO:0046686 — acts upstream of or within — response to cadmium ion
- GO:0006542 — involved in — glutamine biosynthetic process
- GO:0009570 — located in — chloroplast stroma
- GO:0009536 — located in — plastid
- GO:1901149 — enables — salicylic acid binding
- GO:0005739 — located in — mitochondrion
- GO:0003729 — enables — mRNA binding
- GO:0005737 — is active in — cytoplasm
- GO:0009579 — located in — thylakoid
Function-related keywords:
Literature:
- Carbon and amino acids reciprocally modulate the expression of glutamine synthetase in Arabidopsis. DOI: 10.1104/pp.121.1.301 ; PMID: 10482686
- Senescence-associated gene expression during ozone-induced leaf senescence in Arabidopsis. DOI: 10.1104/pp.120.4.1015 ; PMID: 10444084
- The glutamine synthetase gene family of Arabidopsis thaliana: light-regulation and differential expression in leaves, roots and seeds. DOI: 10.1007/BF00290662 ; PMID: 1684022
- New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy. DOI: 10.1074/jbc.M406763200 ; PMID: 15322131
- Gln49 and Ser174 residues play critical roles in determining the catalytic efficiencies of plant glutamine synthetase. DOI: 10.1093/pcp/pci238 ; PMID: 16338958
- The Arabidopsis halophytic relative Thellungiella halophila tolerates nitrogen-limiting conditions by maintaining growth, nitrogen uptake, and assimilation. DOI: 10.1104/pp.108.118125 ; PMID: 18467466
- Global analysis of Arabidopsis gene expression uncovers a complex array of changes impacting pathogen response and cell cycle during geminivirus infection. DOI: 10.1104/pp.108.121038 ; PMID: 18650403
- Leaf proteome responses of Arabidopsis thaliana exposed to mild cadmium stress. DOI: 10.1016/j.jplph.2009.09.015 ; PMID: 20005002
- Unique status of NIA2 in nitrate assimilation: NIA2 expression is promoted by HY5/HYH and inhibited by PIF4. DOI: 10.4161/psb.4.11.9795 ; PMID: 20009559
- The ACR11 encodes a novel type of chloroplastic ACT domain repeat protein that is coordinately expressed with GLN2 in Arabidopsis. DOI: 10.1186/1471-2229-11-118 ; PMID: 21861936
- The amino-terminal domain of chloroplast Hsp93 is important for its membrane association and functions in vivo. DOI: 10.1104/pp.112.193300 ; PMID: 22353577
- Expression pattern of genes encoding nitrate and ammonium assimilating enzymes in Arabidopsis thaliana exposed to short term NaCl stress. DOI: 10.1016/j.jplph.2012.09.011 ; PMID: 23122335
- Physiological and metabolic consequences of autophagy deficiency for the management of nitrogen and protein resources in Arabidopsis leaves depending on nitrate availability. DOI: 10.1111/nph.12307 ; PMID: 23647084
- A proteomics approach identifies novel proteins involved in gravitropic signal transduction. DOI: 10.3732/ajb.1200339 ; PMID: 23281391
- Proteome and metabolome profiling of cytokinin action in Arabidopsis identifying and up-regulation. DOI: 10.1093/jxb/ert227 ; PMID: 24064926
- Identification of multiple salicylic acid-binding proteins using two high throughput screens. DOI: 10.3389/fpls.2014.00777 ; PMID: 25628632
- Endogenous Arabidopsis messenger RNAs transported to distant tissues. DOI: 10.1038/nplants.2015.25 ; PMID: 27247031
- Cytosolic Glutamine Synthetase Gln1;2 Is the Main Isozyme Contributing to GS1 Activity and Can Be Up-Regulated to Relieve Ammonium Toxicity. DOI: 10.1104/pp.16.01195 ; PMID: 27231101
- Nitrogen remobilization during leaf senescence: lessons from Arabidopsis to crops. DOI: 10.1093/jxb/erw365 ; PMID: 27707774
- ACR11 is an Activator of Plastid-Type Glutamine Synthetase GS2 in Arabidopsis thaliana. DOI: 10.1093/pcp/pcx033 ; PMID: 28339983
- Three cytosolic glutamine synthetase isoforms localized in different-order veins act together for N remobilization and seed filling in Arabidopsis. DOI: 10.1093/jxb/ery217 ; PMID: 29873769
- Roles of Cytosolic Glutamine Synthetases in Arabidopsis Development and Stress Responses. DOI: 10.1093/pcp/pcy235 ; PMID: 30649517
- Arabidopsis thaliana mutants devoid of chloroplast glutamine synthetase (GS2) have non-lethal phenotype under photorespiratory conditions. DOI: 10.1016/j.plaphy.2019.10.009 ; PMID: 31622939
- Discovering the RNA-Binding Proteome of Plant Leaves with an Improved RNA Interactome Capture Method. DOI: 10.3390/biom10040661 ; PMID: 32344669
- Transcriptome Profile Analysis of Arabidopsis Reveals the Drought Stress-Induced Long Non-coding RNAs Associated With Photosynthesis, Chlorophyll Synthesis, Fatty Acid Synthesis and Degradation. DOI: 10.3389/fpls.2021.643182 ; PMID: 34113361
- Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis. DOI: 10.1021/pr034025j ; PMID: 12938931
- The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions. DOI: 10.1016/j.cub.2004.02.039 ; PMID: 15028209
- New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast, and versatile fractionation strategy. DOI: 10.1074/jbc.M406763200 ; PMID: 15322131
- High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome. DOI: 10.1007/s11103-005-0699-3 ; PMID: 15821981
- High light response of the thylakoid proteome in arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study. DOI: 10.1104/pp.106.080150 ; PMID: 16648217
- Membrane proteomic analysis of Arabidopsis thaliana using alternative solubilization techniques. DOI: 10.1021/pr060525b ; PMID: 17432890
- Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots. DOI: 10.1093/jxb/erm207 ; PMID: 17916636
- Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. DOI: 10.1371/journal.pone.0001994 ; PMID: 18431481
- Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study. DOI: 10.1016/j.phytochem.2008.04.007 ; PMID: 18538804
- Quantitative proteomics of a chloroplast SRP54 sorting mutant and its genetic interactions with CLPC1 in Arabidopsis. DOI: 10.1104/pp.108.124545 ; PMID: 18633119
- The oligomeric stromal proteome of Arabidopsis thaliana chloroplasts. DOI: 10.1074/mcp.M500180-MCP200 ; PMID: 16207701
- High heterogeneity within the ribosomal proteins of the Arabidopsis thaliana 80S ribosome. DOI: 10.1007/s11103-005-0699-3 ; PMID: 15821981
- High light response of the thylakoid proteome in arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study. DOI: 10.1104/pp.106.080150 ; PMID: 16648217
- Membrane proteomic analysis of Arabidopsis thaliana using alternative solubilization techniques. DOI: 10.1021/pr060525b ; PMID: 17432890
- Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots. DOI: 10.1093/jxb/erm207 ; PMID: 17916636
- Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. DOI: 10.1371/journal.pone.0001994 ; PMID: 18431481
- Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study. DOI: 10.1016/j.phytochem.2008.04.007 ; PMID: 18538804
- High light response of the thylakoid proteome in arabidopsis wild type and the ascorbate-deficient mutant vtc2-2. A comparative proteomics study. DOI: 10.1104/pp.106.080150 ; PMID: 16648217
- Membrane proteomic analysis of Arabidopsis thaliana using alternative solubilization techniques. DOI: 10.1021/pr060525b ; PMID: 17432890
- Comparative proteomic analysis of NaCl stress-responsive proteins in Arabidopsis roots. DOI: 10.1093/jxb/erm207 ; PMID: 17916636
- Sorting signals, N-terminal modifications and abundance of the chloroplast proteome. DOI: 10.1371/journal.pone.0001994 ; PMID: 18431481
- Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study. DOI: 10.1016/j.phytochem.2008.04.007 ; PMID: 18538804
- Analysis of protein complexes in Arabidopsis leaves using size exclusion chromatography and label-free protein correlation profiling. DOI: 10.1016/j.jprot.2017.06.004 ; PMID: 28627464
Sequences:
cDNA Sequence
- >AT5G35630.1
TACCACAATCACTTATGAGTATTGAAGTTGAGATAGAGGAGGTACAAGGAGACCTTATCTGCAGAAGACAAAAAGCCATTTTTAGCAAAACTAAAGAAAGAAAAAAGATTGAAACACAAATATGCGCCACTCGTAGTCCACCCCTATCTCTTTGGCAAAAGCCACTTCACTCTTTTTCCCTTTTTATATATTAAAAATAAAGATTCTTAAGGCTCTTCATATTTTGCTTTTTGTCAACTCTTTCTTTGCCATCTGTTACAAACACCAAACTCTCCTGATTCATCAGTTTTAAGTCTTCTTCAAGTCCCAGGGATCATCAATCCAATGGCTCAGATCTTAGCAGCTTCTCCAACATGTCAGATGAGAGTGCCTAAACACTCATCAGTCATTGCATCATCATCCAAGTTATGGAGCTCTGTTGTGTTGAAACAGAAGAAGCAGAGCAACAACAAAGTCAGAGGCTTTAGAGTTCTTGCTCTCCAATCTGATAACAGTACTGTCAATAGAGTTGAGACTCTTCTCAATTTAGACACCAAACCTTACTCTGACAGGATCATTGCTGAATACATTTGGATCGGAGGATCTGGAATTGACCTTAGAAGCAAGTCAAGGACTATCGAAAAGCCGGTGGAGGATCCTTCTGAGCTACCTAAGTGGAACTATGATGGTTCGAGTACCGGTCAAGCACCTGGTGAAGATAGTGAAGTGATTCTATACCCGCAAGCTATCTTCAGAGATCCTTTCCGTGGAGGCAATAACATCTTGGTTATCTGTGATACTTGGACACCAGCTGGTGAGCCAATTCCAACAAACAAACGTGCTAAAGCTGCTGAGATCTTCAGTAACAAGAAGGTCTCTGGCGAGGTTCCATGGTTCGGCATTGAACAAGAGTACACTTTACTTCAGCAAAACGTCAAATGGCCTTTAGGTTGGCCTGTTGGAGCGTTCCCTGGTCCTCAGGGTCCTTACTACTGTGGAGTTGGAGCTGACAAGATTTGGGGGCGTGACATTTCAGATGCTCATTACAAAGCTTGTTTATATGCTGGAATTAACATTAGTGGTACTAATGGTGAAGTTATGCCTGGACAGTGGGAGTTCCAAGTTGGCCCGAGCGTAGGAATTGATGCAGGTGATCATGTTTGGTGTGCTAGATACCTTCTTGAGAGAATCACAGAACAAGCTGGTGTTGTCCTAACACTTGATCCCAAACCGATAGAGGGTGACTGGAACGGTGCTGGTTGCCACACCAATTACAGTACCAAGAGCATGAGAGAGGAAGGAGGATTTGAAGTGATCAAGAAGGCTATCTTGAACCTCTCGCTTCGCCACAAGGAGCACATCAGTGCCTACGGTGAAGGAAACGAGAGAAGGTTGACCGGAAAGCACGAGACAGCTAGTATTGACCAGTTCTCATGGGGCGTGGCTAACCGTGGATGCTCTATTCGTGTGGGACGTGACACCGAGGCGAAAGGAAAAGGTTACTTAGAAGATCGCCGTCCAGCATCTAACATGGACCCATACATTGTGACCTCACTTTTGGCAGAGACCACACTCCTGTGGGAGCCAACTCTTGAGGCTGAAGCCCTTGCAGCTCAAAAGCTTTCTTTGAATGTTTAAAATTAGTCGAAACTTTCATGAATCTGATGAACACACGTGTCTATGTGGTCTCTCAAGTTGTTTAAACATTCGGATTAAGACATTGTTTGTTGTCTTTTCATTTGCATTTTTAAAACTCAGAATTGTATGGACAATGTTCATCCTTTTATATTGGTTCTTTTGACTGTTAGAGCATGTCCAATGGTTGAATTTAAGCTGGTTCTTAACTGTTGAAAGATTTAATGTGTAATTGTGTATTTAAGTGTAACATCCTCAATCTCAAAGGTTG - >AT5G35630.2
TACCACAATCACTTATGAGTATTGAAGTTGAGATAGAGGAGGTACAAGGAGACCTTATCTGCAGAAGACAAAAAGCCATTTTTAGCAAAACTAAAGAAAGAAAAAAGATTGAAACACAAATATGCGCCACTCGTAGTCCACCCCTATCTCTTTGGCAAAAGCCACTTCACTCTTTTTCCCTTTTTATATATTAAAAATAAAGATTCTTAAGGCTCTTCATATTTTGCTTTTTGTCAACTCTTTCTTTGCCATCTGTTACAAACACCAAACTCTCCTGATTCATCAGTTTTAAGTCTTCTTCAAGTCCCAGGGATCATCAATCCAATGGCTCAGATCTTAGCAGCTTCTCCAACATGTCAGATGAGAGTGCCTAAACACTCATCAGTCATTGCATCATCATCCAAGTTATGGAGCTCTGTTGTGTTGAAACAGAAGAAGCAGAGCAACAACAAAGTCAGAGGCTTTAGAGTTCTTGCTCTCCAATCTGATAACAGTACTGTCAATAGAGTTGAGACTCTTCTCAATTTAGACACCAAACCTTACTCTGACAGGATCATTGCTGAATACATTTGGATCGGAGGATCTGGAATTGACCTTAGAAGCAAGTCAAGGACTATCGAAAAGCCGGTGGAGGATCCTTCTGAGCTACCTAAGTGGAACTATGATGGTTCGAGTACCGGTCAAGCACCTGGTGAAGATAGTGAAGTGATTCTATACCCGCAAGCTATCTTCAGAGATCCTTTCCGTGGAGGCAATAACATCTTGGTTATCTGTGATACTTGGACACCAGCTGGTGAGCCAATTCCAACAAACAAACGTGCTAAAGCTGCTGAGATCTTCAGTAACAAGAAGGTCTCTGGCGAGGTTCCATGGTTCGGCATTGAACAAGAGTACACTTTACTTCAGCAAAACGTCAAATGGCCTTTAGGTTGGCCTGTTGGAGCGTTCCCTGGTCCTCAGGGTCCTTACTACTGTGGAGTTGGAGCTGACAAGATTTGGGGGCGTGACATTTCAGATGCTCATTACAAAGCTTGTTTATATGCTGGAATTAACATTAGTGGTACTAATGGTGAAGTTATGCCTGGACAGTGGGAGTTCCAAGTTGGCCCGAGCGTAGGAATTGATGCAGGTGATCATGTTTGGTGTGCTAGATACCTTCTTGAGAGAATCACAGAACAAGCTGGTGTTGTCCTAACACTTGATCCCAAACCGATAGAGGGTGACTGGAACGGTGCTGGTTGCCACACCAATTACAGTACCAAGAGCATGAGAGAGGAAGGAGGATTTGAAGTGATCAAGAAGGCTATCTTGAACCTCTCGCTTCGCCACAAGGAGCACATCAGTGCCTACGGTGAAGGAAACGAGAGAAGGTTGACCGGAAAGCACGAGACAGCTAGTATTGACCAGTTCTCATGGGGCGTGGCTAACCGTGGATGCTCTATTCGTGTGGGACGTGACACCGAGGCGAAAGGAAAAGGTTACTTAGAAGATCGCCGTCCAGCATCTAACATGGACCCATACATTGTGACCTCACTTTTGGCAGAGACCACACTCCTGTGGGAGCCAACTCTTGAGGCTGAAGCCCTTGCAGCTCAAAAGCTTTCTTTGAATGTTTAAAATTAGTCGAAACTTTCATGAATCTGATGAACACACGTGTCTATGTGGTCTCTCAAGTTGTTTAAACATTCGGATTAAGACATTGTTTGTTGTCTTTTCATTTGCATTTTTAAAACTCAGAATTGTATGGACAATGTTCATCCTTTTATATTGGTTCTTTTGACTGTTAGAGCATGTCCAATGGTTGAATTTAAGCTGGTTCTTAACTGTTGAAAGATTTAATGTGTAATTGTGTATTTAAGTGTAACATCCTCAATCTCAAAGGTTG - >AT5G35630.3
TACCACAATCACTTATGAGTATTGAAGTTGAGATAGAGGAGGTACAAGGAGACCTTATCTGCAGAAGACAAAAAGCCATTTTTAGCAAAACTAAAGAAAGAAAAAAGATTGAAACACAAATATGCGCCACTCGTAGTCCACCCCTATCTCTTTGGCAAAAGCCACTTCACTCTTTTTCCCTTTTTATATATTAAAAATAAAGATTCTTAAGGCTCTTCATATTTTGCTTTTTGTCAACTCTTTCTTTGCCATCTGTTACAAACACCAAACTCTCCTGATTCATCAGTTTTAAGTCTTCTTCAAGTCCCAGGGATCATCAATCCAATGGCTCAGATCTTAGCAGCTTCTCCAACATGTCAGATGAGAGTGCCTAAACACTCATCAGTCATTGCATCATCATCCAAGTTATGGAGCTCTGTTGTGTTGAAACAGAAGAAGCAGAGCAACAACAAAGTCAGAGGCTTTAGAGTTCTTGCTCTCCAATCTGATAACAGTACTGTCAATAGAGTTGAGACTCTTCTCAATTTAGACACCAAACCTTACTCTGACAGGATCATTGCTGAATACATTTGGATCGGAGGATCTGGAATTGACCTTAGAAGCAAGTCAAGGACTATCGAAAAGCCGGTGGAGGATCCTTCTGAGCTACCTAAGTGGAACTATGATGGTTCGAGTACCGGTCAAGCACCTGGTGAAGATAGTGAAGTGATTCTATACCCGCAAGCTATCTTCAGAGATCCTTTCCGTGGAGGCAATAACATCTTGGTTATCTGTGATACTTGGACACCAGCTGGTGAGCCAATTCCAACAAACAAACGTGCTAAAGCTGCTGAGATCTTCAGTAACAAGAAGGTCTCTGGCGAGGTTCCATGGTTCGGCATTGAACAAGAGTACACTTTACTTCAGCAAAACGTCAAATGGCCTTTAGGTTGGCCTGTTGGAGCGTTCCCTGGTCCTCAGGGTCCTTACTACTGTGGAGTTGGAGCTGACAAGATTTGGGGGCGTGACATTTCAGATGCTCATTACAAAGCTTGTTTATATGCTGGAATTAACATTAGTGGTACTAATGGTGAAGTTATGCCTGGACAGTGGGAGTTCCAAGTTGGCCCGAGCGTAGGAATTGATGCAGGTGATCATGTTTGGTGTGCTAGATACCTTCTTGAGAGAATCACAGAACAAGCTGGTGTTGTCCTAACACTTGATCCCAAACCGATAGAGGGTGACTGGAACGGTGCTGGTTGCCACACCAATTACAGTACCAAGAGCATGAGAGAGGAAGGAGGATTTGAAGTGATCAAGAAGGCTATCTTGAACCTCTCGCTTCGCCACAAGGAGCACATCAGTGCCTACGGTGAAGGAAACGAGAGAAGGTTGACCGGAAAGCACGAGACAGCTAGTATTGACCAGTTCTCATGGGGCGTGGCTAACCGTGGATGCTCTATTCGTGTGGGACGTGACACCGAGGCGAAAGGAAAAGGTTACTTAGAAGATCGCCGTCCAGCATCTAACATGGACCCATACATTGTGACCTCACTTTTGGCAGAGACCACACTCCTGTGGGAGCCAACTCTTGAGGCTGAAGCCCTTGCAGCTCAAAAGCTTTCTTTGAATGTTTAAAATTAGTCGAAACTTTCATGAATCTGATGAACACACGTGTCTATGTGGTCTCTCAAGTTGTTTAAACATTCGGATTAAGACATTGTTTGTTGTCTTTTCATTTGCATTTTTAAAACTCAGAATTGTATGGACAATGTTCATCCTTTTATATTGGTTCTTTTGACTGTTAGAGCATGTCCAATGGTTGAATTTAAGCTGGTTCTTAACTGTTGAAAGATTTAATGTGTAATTGTGTATTTAAGTGTAACATCCTCAATCTCAAAGGTTG
CDS Sequence
Protein Sequence