ID   GLN12_ARATH             Reviewed;         356 AA.
AC   Q8LCE1; Q9C8C7;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Glutamine synthetase cytosolic isozyme 1-2;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate--ammonia ligase GLN1;2;
DE            Short=GLN1;2;
GN   Name=GLN1-2; Synonyms=GSR2; OrderedLocusNames=At1g66200;
GN   ORFNames=F15E12.14;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R., Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INDUCTION.
RX   PubMed=10444084; DOI=10.1104/pp.120.4.1015;
RA   Miller J.D., Arteca R.N., Pell E.J.;
RT   "Senescence-associated gene expression during ozone-induced leaf senescence
RT   in Arabidopsis.";
RL   Plant Physiol. 120:1015-1024(1999).
RN   [6]
RP   INDUCTION.
RX   PubMed=10482686; DOI=10.1104/pp.121.1.301;
RA   Oliveira I.C., Coruzzi G.M.;
RT   "Carbon and amino acids reciprocally modulate the expression of glutamine
RT   synthetase in Arabidopsis.";
RL   Plant Physiol. 121:301-310(1999).
RN   [7]
RP   BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14757761; DOI=10.1074/jbc.m313710200;
RA   Ishiyama K., Inoue E., Watanabe-Takahashi A., Obara M., Yamaya T.,
RA   Takahashi H.;
RT   "Kinetic properties and ammonium-dependent regulation of cytosolic
RT   isoenzymes of glutamine synthetase in Arabidopsis.";
RL   J. Biol. Chem. 279:16598-16605(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
RN   [9]
RP   INTERACTION WITH GRF3.
RX   PubMed=21094157; DOI=10.1016/j.febslet.2010.11.025;
RA   Shin R., Jez J.M., Basra A., Zhang B., Schachtman D.P.;
RT   "14-3-3 proteins fine-tune plant nutrient metabolism.";
RL   FEBS Lett. 585:143-147(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Low-affinity glutamine synthetase. May contribute to the
CC       homeostatic control of glutamine synthesis in roots.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC         phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=3.8 mM for glutamate {ECO:0000269|PubMed:14757761};
CC         KM=2450 uM for ammonium {ECO:0000269|PubMed:14757761};
CC         KM=1100 uM for ATP {ECO:0000269|PubMed:14757761};
CC         Vmax=65.7 nmol/sec/mg enzyme with glutamate as substrate
CC         {ECO:0000269|PubMed:14757761};
CC         Vmax=65.7 nmol/sec/mg enzyme with ammonium as substrate
CC         {ECO:0000269|PubMed:14757761};
CC         Vmax=66.6 nmol/sec/mg enzyme with ATP as substrate
CC         {ECO:0000269|PubMed:14757761};
CC         Note=Measured at pH 7.8 and 30 degrees Celsius for all experiments.;
CC   -!- SUBUNIT: Homooctamer (By similarity). Interacts with GRF3.
CC       {ECO:0000250|UniProtKB:P16580, ECO:0000269|PubMed:21094157}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q8LCE1-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Expressed in the pericycle of all root tissues.
CC       {ECO:0000269|PubMed:14757761}.
CC   -!- INDUCTION: By ammonium supply under nitrogen-limited condition. Induced
CC       by sucrose, glucose, fructose, and during leaf senescence.
CC       {ECO:0000269|PubMed:10444084, ECO:0000269|PubMed:10482686,
CC       ECO:0000269|PubMed:14757761}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR   EMBL; AC026480; AAG51310.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE34474.1; -; Genomic_DNA.
DR   EMBL; AY091101; AAM14052.1; -; mRNA.
DR   EMBL; AY122962; AAM67495.1; -; mRNA.
DR   EMBL; AY086653; AAM63710.1; -; mRNA.
DR   PIR; H96686; H96686.
DR   PIR; S18602; S18602.
DR   RefSeq; NP_176794.1; NM_105291.4. [Q8LCE1-1]
DR   AlphaFoldDB; Q8LCE1; -.
DR   SMR; Q8LCE1; -.
DR   BioGRID; 28156; 3.
DR   IntAct; Q8LCE1; 1.
DR   STRING; 3702.Q8LCE1; -.
DR   iPTMnet; Q8LCE1; -.
DR   MetOSite; Q8LCE1; -.
DR   PaxDb; 3702-AT1G66200-3; -.
DR   DNASU; 842935; -.
DR   EnsemblPlants; AT1G66200.1; AT1G66200.1; AT1G66200. [Q8LCE1-1]
DR   GeneID; 842935; -.
DR   Gramene; AT1G66200.1; AT1G66200.1; AT1G66200. [Q8LCE1-1]
DR   KEGG; ath:AT1G66200; -.
DR   Araport; AT1G66200; -.
DR   TAIR; AT1G66200; GSR2.
DR   eggNOG; KOG0683; Eukaryota.
DR   HOGENOM; CLU_036762_0_1_1; -.
DR   InParanoid; Q8LCE1; -.
DR   OMA; CAIGANK; -.
DR   PhylomeDB; Q8LCE1; -.
DR   BRENDA; 6.3.1.2; 399.
DR   SABIO-RK; Q8LCE1; -.
DR   PRO; PR:Q8LCE1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q8LCE1; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IBA:GO_Central.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR008147; Gln_synt_N.
DR   InterPro; IPR036651; Gln_synt_N_sf.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR027302; Gln_synth_N_conserv_site.
DR   PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF110; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-2; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
DR   Genevisible; Q8LCE1; AT.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Ligase;
KW   Nitrogen fixation; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..356
FT                   /note="Glutamine synthetase cytosolic isozyme 1-2"
FT                   /id="PRO_0000239819"
FT   DOMAIN          19..99
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          106..356
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
FT   MOD_RES         48
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q43127"
FT   CONFLICT        290
FT                   /note="R -> L (in Ref. 4; AAM63710)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   356 AA;  39207 MW;  19D19BF1388E5192 CRC64;
     MSLLADLVNL DISDNSEKII AEYIWVGGSG MDMRSKARTL PGPVTDPSKL PKWNYDGSST
     GQAPGQDSEV ILYPQAIFKD PFRRGNNILV MCDAYTPAGE PIPTNKRHAA AEIFANPDVI
     AEVPWYGIEQ EYTLLQKDVN WPLGWPIGGF PGPQGPYYCS IGADKSFGRD IVDAHYKASL
     YAGINISGIN GEVMPGQWEF QVGPSVGISA ADEIWIARYI LERITEIAGV VVSFDPKPIP
     GDWNGAGAHT NYSTKSMREE GGYEIIKKAI EKLGLRHKEH ISAYGEGNER RLTGHHETAD
     INTFLWGVAN RGASIRVGRD TEKEGKGYFE DRRPASNMDP YVVTSMIAET TLLWNP
//