ID GLNA_BOVIN Reviewed; 373 AA. AC P15103; O02850; Q3ZBU6; Q866Q7; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 24-JAN-2024, entry version 161. DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:9321487}; DE Short=GS {ECO:0000303|PubMed:9321487}; 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:9321487}; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Hypothalamus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-267. RX PubMed=9321487; DOI=10.1007/s003359900577; RA Masabanda J., Wigger G., Eggen A., Stranzinger G., Fries R.; RT "The bovine glutamine synthase gene (GLUL) maps to 10q33 and a pseudogene RT (GLULP) to 16q21."; RL Mamm. Genome 8:794-795(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 258-352. RC TISSUE=Kidney; RA Matthews J.C., Etienne N.M.P.; RT "The pattern of EAAC1 and GLT-1 glutamate transporter expression by RT skeletal and adipose tissues of fattening cattle differs from that of RT glutamine synthetase."; RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 267-373. RC TISSUE=Liver; RX PubMed=2893372; DOI=10.1073/pnas.85.1.160; RA Smith D.D. Jr., Campbell J.W.; RT "Distribution of glutamine synthetase and carbamoyl-phosphate synthetase I RT in vertebrate liver."; RL Proc. Natl. Acad. Sci. U.S.A. 85:160-164(1988). 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 (By similarity). Essential for proliferation CC of fetal skin fibroblasts. Independently of its glutamine synthetase CC activity, required for endothelial cell migration during vascular CC development: acts by regulating membrane localization and activation of CC the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as CC a palmitoyltransferase for RHOJ: able to autopalmitoylate and then CC transfer the palmitoyl group to RHOJ (By similarity). Plays a role in CC ribosomal 40S subunit biogenesis (By similarity). CC {ECO:0000250|UniProtKB:P15104, ECO:0000250|UniProtKB:P15105}. 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 (By similarity). Interacts with RHOJ (By similarity). CC {ECO:0000250|UniProtKB:P15104, ECO:0000250|UniProtKB:P15105}. 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 -!- PTM: Palmitoylated; undergoes autopalmitoylation. CC {ECO:0000250|UniProtKB:P15104}. CC -!- PTM: Ubiquitinated by ZNRF1. {ECO:0000250|UniProtKB:P15105}. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC103099; AAI03100.1; -; mRNA. DR EMBL; Y10347; CAA71373.1; ALT_SEQ; Genomic_DNA. DR EMBL; AY186585; AAO27470.1; -; mRNA. DR EMBL; J03604; AAA87357.1; -; mRNA. DR PIR; A34006; A34006. DR RefSeq; NP_001035564.1; NM_001040474.2. DR RefSeq; XP_005217320.1; XM_005217263.3. DR PDB; 7U5N; EM; 2.58 A; A/B/C/D/E/F/G/H/I/J=1-373. DR PDB; 8ECY; EM; 2.00 A; A/B/D/F/H/I/J/L/M/Q=1-373. DR PDBsum; 7U5N; -. DR PDBsum; 8ECY; -. DR AlphaFoldDB; P15103; -. DR EMDB; EMD-26356; -. DR EMDB; EMD-28025; -. DR SMR; P15103; -. DR STRING; 9913.ENSBTAP00000057244; -. DR PaxDb; 9913-ENSBTAP00000038301; -. DR Ensembl; ENSBTAT00000038488.5; ENSBTAP00000038301.4; ENSBTAG00000013631.6. DR Ensembl; ENSBTAT00000074216.1; ENSBTAP00000057244.1; ENSBTAG00000013631.6. DR GeneID; 281199; -. DR KEGG; bta:281199; -. DR CTD; 2752; -. DR VEuPathDB; HostDB:ENSBTAG00000013631; -. DR VGNC; VGNC:29426; GLUL. DR eggNOG; KOG0683; Eukaryota. DR GeneTree; ENSGT00390000010047; -. DR HOGENOM; CLU_036762_1_1_1; -. DR InParanoid; P15103; -. DR OMA; DRRPNAN; -. DR OrthoDB; 1115057at2759; -. DR TreeFam; TF300491; -. DR Reactome; R-BTA-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism. DR Reactome; R-BTA-8964539; Glutamate and glutamine metabolism. DR Proteomes; UP000009136; Chromosome 16. DR Bgee; ENSBTAG00000013631; Expressed in prefrontal cortex and 104 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamine synthetase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central. DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB. DR GO; GO:0010594; P:regulation of endothelial cell migration; ISS:UniProtKB. DR GO; GO:1903670; P:regulation of sprouting angiogenesis; ISS:UniProtKB. DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1. DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 2. 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:SF45; GLUTAMINE SYNTHETASE; 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. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Angiogenesis; ATP-binding; Cell membrane; KW Cytoplasm; Endoplasmic reticulum; Ligase; Lipoprotein; Magnesium; KW 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:0000250|UniProtKB:P15105" FT CHAIN 2..373 FT /note="Glutamine synthetase" FT /id="PRO_0000153136" FT DOMAIN 26..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:0000250|UniProtKB:P15105" FT MOD_RES 104 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P15105" FT MOD_RES 343 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15104" FT HELIX 6..8 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 11..18 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 26..33 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 40..49 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 60..63 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 76..86 FT /evidence="ECO:0007829|PDB:8ECY" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 95..102 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 114..123 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 130..140 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 158..160 FT /evidence="ECO:0007829|PDB:8ECY" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 173..186 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 190..195 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 201..210 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 213..232 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 245..247 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 251..257 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:8ECY" FT TURN 264..266 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 267..278 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 281..287 FT /evidence="ECO:0007829|PDB:8ECY" FT TURN 290..293 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 301..305 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 314..316 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 321..325 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 327..332 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 337..339 FT /evidence="ECO:0007829|PDB:8ECY" FT HELIX 348..359 FT /evidence="ECO:0007829|PDB:8ECY" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:8ECY" SQ SEQUENCE 373 AA; 42031 MW; BBCC6A953FD7DAD5 CRC64; MATSASSHLN KGIKQVYMAL PQGDKVQAMY IWIDGTGEGL RCKTRTLDSE PKCIEELPEW NFDGSSTFQS EGSNSDMYLV PAAMFRDPFR KDPNKLVFCE VFKYNRKPAE TNLRHTCKRI MDMVSNQRPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY RACLYAGIKI GGTNAEVMPA QWEFQIGPCE GIDMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPFA VTEALIRTCL LNETGDEPFQ YKN //