GLNA_MOUSE
ID GLNA_MOUSE Reviewed; 373 AA.
AC P15105; Q3TRK7; Q64432; Q91VC6;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 6.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:30158707};
DE Short=GS {ECO:0000303|PubMed:30158707};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P15104};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
DE AltName: Full=Palmitoyltransferase GLUL {ECO:0000305};
DE EC=2.3.1.225 {ECO:0000250|UniProtKB:P15104};
GN Name=Glul {ECO:0000303|PubMed:30158707, ECO:0000312|MGI:MGI:95739};
GN Synonyms=Glns;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2475638; DOI=10.1016/0022-2836(89)90086-7;
RA Kuo C.F., Darnell J.E. Jr.;
RT "Mouse glutamine synthetase is encoded by a single gene that can be
RT expressed in a localized fashion.";
RL J. Mol. Biol. 208:45-56(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RA Lindemann A.E., Tempest P.R.;
RT "Sequence of a mouse glutamine synthetase cDNA.";
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/NJ; TISSUE=Liver;
RA Labruyere W.T., van Hemert F.J., Lamers W.H.;
RT "Glutamine synthetase mRNA in rodents.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Hippocampus, and Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 2-11; 15-25; 96-103; 174-181; 292-298 AND 341-357,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [7]
RP INTERACTION WITH PALMD.
RX PubMed=16323283; DOI=10.1016/j.ejcb.2005.07.002;
RA Hu B., Petrasch-Parwez E., Laue M.M., Kilimann M.W.;
RT "Molecular characterization and immunohistochemical localization of
RT palmdelphin, a cytosolic isoform of the paralemmin protein family
RT implicated in membrane dynamics.";
RL Eur. J. Cell Biol. 84:853-866(2005).
RN [8]
RP PROTEIN SEQUENCE OF 26-41; 46-52; 174-222 AND 341-357, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=17557305; DOI=10.1002/dvdy.21185;
RA He Y., Hakvoort T.B., Vermeulen J.L., Lamers W.H., Van Roon M.A.;
RT "Glutamine synthetase is essential in early mouse embryogenesis.";
RL Dev. Dyn. 236:1865-1875(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP UBIQUITINATION.
RX PubMed=20107048; DOI=10.1523/jneurosci.3591-09.2010;
RA Saitoh F., Araki T.;
RT "Proteasomal degradation of glutamine synthetase regulates schwann cell
RT differentiation.";
RL J. Neurosci. 30:1204-1212(2010).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25870278; DOI=10.1073/pnas.1423968112;
RA Qvartskhava N., Lang P.A., Goerg B., Pozdeev V.I., Ortiz M.P., Lang K.S.,
RA Bidmon H.J., Lang E., Leibrock C.B., Herebian D., Bode J.G., Lang F.,
RA Haeussinger D.;
RT "Hyperammonemia in gene-targeted mice lacking functional hepatic glutamine
RT synthetase.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:5521-5526(2015).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30158707; DOI=10.1038/s41586-018-0466-7;
RA Eelen G., Dubois C., Cantelmo A.R., Goveia J., Bruening U., DeRan M.,
RA Jarugumilli G., van Rijssel J., Saladino G., Comitani F., Zecchin A.,
RA Rocha S., Chen R., Huang H., Vandekeere S., Kalucka J., Lange C.,
RA Morales-Rodriguez F., Cruys B., Treps L., Ramer L., Vinckier S.,
RA Brepoels K., Wyns S., Souffreau J., Schoonjans L., Lamers W.H., Wu Y.,
RA Haustraete J., Hofkens J., Liekens S., Cubbon R., Ghesquiere B.,
RA Dewerchin M., Gervasio F.L., Li X., van Buul J.D., Wu X., Carmeliet P.;
RT "Role of glutamine synthetase in angiogenesis beyond glutamine synthesis.";
RL Nature 561:63-69(2018).
CC -!- FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent
CC conversion of glutamate and ammonia to glutamine (By similarity). Its
CC role depends on tissue localization: in the brain, it regulates the
CC levels of toxic ammonia and converts neurotoxic glutamate to harmless
CC glutamine, whereas in the liver, it is one of the enzymes responsible
CC for the removal of ammonia (PubMed:25870278). Essential for
CC proliferation of fetal skin fibroblasts (By similarity). Independently
CC of its glutamine synthetase activity, required for endothelial cell
CC migration during vascular development (PubMed:30158707). Involved in
CC angiogenesis by regulating membrane localization and activation of the
CC GTPase RHOJ, possibly by promoting RHOJ palmitoylation (By similarity).
CC May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate
CC and then transfer the palmitoyl group to RHOJ (By similarity). Plays a
CC role in ribosomal 40S subunit biogenesis (By similarity).
CC {ECO:0000250|UniProtKB:P15104, ECO:0000269|PubMed:25870278,
CC ECO:0000269|PubMed:30158707}.
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 Evidence={ECO:0000250|UniProtKB:P15104};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000250|UniProtKB:P15104};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P09606};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P15104};
CC -!- ACTIVITY REGULATION: Glutamine synthetase activity is inhibited by
CC methionine sulfoximine (MSO). {ECO:0000250|UniProtKB:P15104}.
CC -!- SUBUNIT: Decamer; composed of two pentamers (By similarity). Interacts
CC with PALMD (PubMed:16323283). Interacts with RHOJ (By similarity).
CC {ECO:0000250|UniProtKB:P15104, ECO:0000269|PubMed:16323283}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P15104}. Microsome
CC {ECO:0000250|UniProtKB:P09606}. Mitochondrion
CC {ECO:0000250|UniProtKB:P09606}. Cell membrane
CC {ECO:0000250|UniProtKB:P15104}; Lipid-anchor
CC {ECO:0000250|UniProtKB:P15104}. Note=Mainly localizes in the cytosol,
CC with a fraction associated with the cell membrane.
CC {ECO:0000250|UniProtKB:P15104}.
CC -!- TISSUE SPECIFICITY: Expressed in microvascular endothelial cells.
CC {ECO:0000269|PubMed:30158707}.
CC -!- PTM: Palmitoylated; undergoes autopalmitoylation.
CC {ECO:0000250|UniProtKB:P15104}.
CC -!- PTM: Ubiquitinated by ZNRF1. {ECO:0000269|PubMed:20107048}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality when embryos move from the
CC uterine tube to the uterine environment (PubMed:17557305). Conditional
CC deletion in the liver leads to a marked increase of plasma ammonia
CC levels, causing increased locomotion, impaired fear memory and a
CC slightly reduced life span (PubMed:25870278). Conditional deletion in
CC endothelial cells impairs vessel sprouting during vascular development
CC due to defects in endothelial cell migration (PubMed:30158707).
CC {ECO:0000269|PubMed:17557305, ECO:0000269|PubMed:25870278,
CC ECO:0000269|PubMed:30158707}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; X16314; CAA34381.1; -; mRNA.
DR EMBL; U09114; AAA17989.1; -; mRNA.
DR EMBL; AY044241; AAK95328.1; -; mRNA.
DR EMBL; AK159106; BAE34822.1; -; mRNA.
DR EMBL; AK160670; BAE35950.1; -; mRNA.
DR EMBL; AK162685; BAE37022.1; -; mRNA.
DR EMBL; AK168493; BAE40380.1; -; mRNA.
DR EMBL; BC015086; AAH15086.1; -; mRNA.
DR CCDS; CCDS15381.1; -.
DR PIR; S04991; AJMSQ.
DR RefSeq; NP_032157.2; NM_008131.4.
DR AlphaFoldDB; P15105; -.
DR SMR; P15105; -.
DR BioGRID; 199947; 16.
DR IntAct; P15105; 14.
DR MINT; P15105; -.
DR STRING; 10090.ENSMUSP00000083375; -.
DR iPTMnet; P15105; -.
DR PhosphoSitePlus; P15105; -.
DR SwissPalm; P15105; -.
DR REPRODUCTION-2DPAGE; IPI00626790; -.
DR REPRODUCTION-2DPAGE; P15105; -.
DR SWISS-2DPAGE; P15105; -.
DR UCD-2DPAGE; P15105; -.
DR CPTAC; non-CPTAC-3816; -.
DR EPD; P15105; -.
DR jPOST; P15105; -.
DR MaxQB; P15105; -.
DR PaxDb; P15105; -.
DR PeptideAtlas; P15105; -.
DR PRIDE; P15105; -.
DR ProteomicsDB; 266809; -.
DR Antibodypedia; 1536; 686 antibodies from 42 providers.
DR DNASU; 14645; -.
DR Ensembl; ENSMUST00000086199; ENSMUSP00000083375; ENSMUSG00000026473.
DR Ensembl; ENSMUST00000140685; ENSMUSP00000123157; ENSMUSG00000026473.
DR GeneID; 14645; -.
DR KEGG; mmu:14645; -.
DR UCSC; uc007daq.2; mouse.
DR CTD; 2752; -.
DR MGI; MGI:95739; Glul.
DR VEuPathDB; HostDB:ENSMUSG00000026473; -.
DR eggNOG; KOG0683; Eukaryota.
DR GeneTree; ENSGT00390000010047; -.
DR HOGENOM; CLU_036762_1_1_1; -.
DR InParanoid; P15105; -.
DR OMA; DRRPNAN; -.
DR OrthoDB; 784869at2759; -.
DR PhylomeDB; P15105; -.
DR TreeFam; TF300491; -.
DR BRENDA; 6.3.1.2; 3474.
DR Reactome; R-MMU-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR BioGRID-ORCS; 14645; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Glul; mouse.
DR PRO; PR:P15105; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P15105; protein.
DR Bgee; ENSMUSG00000026473; Expressed in efferent duct and 260 other tissues.
DR ExpressionAtlas; P15105; baseline and differential.
DR Genevisible; P15105; MM.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097386; C:glial cell projection; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0045503; F:dynein light chain binding; ISO:MGI.
DR GO; GO:0016595; F:glutamate binding; ISO:MGI.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0030145; F:manganese ion binding; ISO:MGI.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019676; P:ammonia assimilation cycle; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0008283; P:cell population proliferation; ISO:MGI.
DR GO; GO:0009267; P:cellular response to starvation; IEP:MGI.
DR GO; GO:0006536; P:glutamate metabolic process; ISO:MGI.
DR GO; GO:0006542; P:glutamine biosynthetic process; ISO:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR GO; GO:0010594; P:regulation of endothelial cell migration; IMP:UniProtKB.
DR GO; GO:1904749; P:regulation of protein localization to nucleolus; ISO:MGI.
DR GO; GO:1903670; P:regulation of sprouting angiogenesis; IMP:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IMP:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; ISO:MGI.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
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 Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 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.
PE 1: Evidence at protein level;
KW Acetylation; Angiogenesis; ATP-binding; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; Ligase; Lipoprotein;
KW Magnesium; Manganese; Membrane; Metal-binding; Microsome; Mitochondrion;
KW Nucleotide-binding; Palmitate; Phosphoprotein; Reference proteome;
KW Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..373
FT /note="Glutamine synthetase"
FT /id="PRO_0000153141"
FT DOMAIN 24..106
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 113..373
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 134
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 196
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 203..208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 246..247
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 253
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 255..257
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 319
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 336..338
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 338
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 340
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 104
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 91
FT /note="K -> R (in Ref. 1; CAA34381)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="T -> S (in Ref. 2; AAA17989)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="M -> L (in Ref. 4; BAE37022)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="G -> V (in Ref. 1; CAA34381)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="C -> W (in Ref. 2; AAA17989)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="R -> A (in Ref. 1; CAA34381)"
FT /evidence="ECO:0000305"
FT CONFLICT 342..343
FT /note="PS -> LR (in Ref. 1; CAA34381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42120 MW; 1EC9CDC5D81DE63F CRC64;
MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE PKCVEELPEW
NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR KDPNKLVLCE VFKYNRKPAE TNLRHICKRI
MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY
RACLYAGVKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWI ARFILHRVCE DFGVIATFDP
KPIPGNWNGA GCHTNFSTKA MREENGLKCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL
TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPYA VTEAIVRTCL
LNETGDEPFQ YKN
