GLNA_CRIGR
ID GLNA_CRIGR Reviewed; 373 AA.
AC P04773; Q9EQP8;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:2868445};
DE Short=GS {ECO:0000303|PubMed:2868445};
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 Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=2868445; DOI=10.1093/nar/14.2.999;
RA Hayward B.E., Hussain A., Wilson R.H., Lyons A., Woodcock V., McIntosh B.,
RA Harris T.J.R.;
RT "The cloning and nucleotide sequence of cDNA for an amplified glutamine
RT synthetase gene from the Chinese hamster.";
RL Nucleic Acids Res. 14:999-1008(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tong Y., Wang H.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; X03495; CAA27211.1; -; mRNA.
DR EMBL; AF150961; AAG43362.1; -; mRNA.
DR RefSeq; NP_001233699.1; NM_001246770.1.
DR AlphaFoldDB; P04773; -.
DR SMR; P04773; -.
DR STRING; 10029.NP_001233699.1; -.
DR GeneID; 100689337; -.
DR KEGG; cge:100689337; -.
DR eggNOG; KOG0683; Eukaryota.
DR OrthoDB; 784869at2759; -.
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:glutamate-ammonia ligase 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; -; 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 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_0000153138"
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"
FT CONFLICT 12
FT /note="G -> N (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 18..19
FT /note="MS -> LC (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="S -> G (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 91..92
FT /note="KE -> RD (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="Q -> R (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 116
FT /note="T -> S (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="L -> M (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="D -> N (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="L -> P (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="R -> G (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="M -> V (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="Y -> N (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..199
FT /note="KH -> MP (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> E (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="S -> P (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="T -> A (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="K -> E (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="R -> G (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="K -> E (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="D -> N (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..341
FT /note="ARC -> DRR (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="Q -> E (in Ref. 2; CAA27211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 373 AA; 42320 MW; 611D58CE20FB16CF CRC64;
MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE PKCVEELPEW
NFDGSSTFQS ESSNSDMYLS PVAMFRDPFR KEPNKLVFCE VFKYNQKPAE TNLRHTCKRI
MDMVSNQHPW FGMEQEYTLL GTDGHPFGWP SDGFPGPQGL YYCGVGADKA YRRDIMEAHY
RACLYAGVKI TGTYAEVKHA QWEFQIGPCE GIRMGDHLWV ARFILHRVCK DFGVIATFDS
KPIPGNWNGA GCHTNFSTKT MREENGLKHI KEAIEKLSKR HRYHIRAYDP KGGLDNARRL
TGFHKTSNIN DFSAGVADRS ASIRIPRTVG QEKKGYFEAR CPSANCDPFA VTEAIVRTCL
LNETGDQPFQ YKN
