ID   GLNA_ACOCA              Reviewed;         373 AA.
AC   Q9QY94;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-NOV-2023, entry version 94.
DE   RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P15104};
DE            Short=GS {ECO:0000250|UniProtKB:P15104};
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:0000250|UniProtKB:P15104};
OS   Acomys cahirinus (Cairo spiny mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Deomyinae; Acomys.
OX   NCBI_TaxID=10068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   PubMed=10411642; DOI=10.1046/j.1432-1327.1999.00436.x;
RA   Lamers W.H., Boon L., Van Hemert F.J., Labruyere W.T., De Jong P.,
RA   Ruijter J.M., Moorman A.F.;
RT   "Glutamine synthetase expression in perinatal spiny mouse liver.";
RL   Eur. J. Biochem. 262:803-809(1999).
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).
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}.
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DR   EMBL; AF110381; AAF14691.1; -; mRNA.
DR   AlphaFoldDB; Q9QY94; -.
DR   SMR; Q9QY94; -.
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; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Angiogenesis; ATP-binding; Cell membrane; Cytoplasm;
KW   Endoplasmic reticulum; Ligase; Lipoprotein; Magnesium; Manganese; Membrane;
KW   Metal-binding; Microsome; Mitochondrion; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; 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_0000153135"
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: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"
SQ   SEQUENCE   373 AA;  42165 MW;  51BAD0B2EBA18AB6 CRC64;
     MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE PKCVEELPEW
     NFDGSSTFQS EGSNSDMYLS PVAMFRDPFR KEPNKLVFCE VFKYNRKPAE TNLRHSCKRI
     MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY
     RACLYAGVKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWV ARFILHRVCE DFGVIATFDP
     KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL
     TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKRGYFEDR RPSANCDPYA VTEAIVRTCL
     LNETGNEPFQ YKN
//