GLNA_MACFA
ID GLNA_MACFA Reviewed; 374 AA.
AC Q4R7U3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Glutamine synthetase {ECO:0000250|UniProtKB:P15104};
DE Short=GS {ECO:0000250|UniProtKB:P09606};
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};
GN ORFNames=QtsA-14381 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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; AB168719; BAE00829.1; -; mRNA.
DR RefSeq; NP_001270340.1; NM_001283411.1.
DR AlphaFoldDB; Q4R7U3; -.
DR SMR; Q4R7U3; -.
DR STRING; 9541.XP_005540218.1; -.
DR GeneID; 101926704; -.
DR CTD; 2752; -.
DR eggNOG; KOG0683; Eukaryota.
DR OrthoDB; 784869at2759; -.
DR Proteomes; UP000233100; Unplaced.
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 Angiogenesis; ATP-binding; Cell membrane; Cytoplasm; Endoplasmic reticulum;
KW Ligase; Lipoprotein; Magnesium; Manganese; Membrane; Metal-binding;
KW Microsome; Mitochondrion; Nucleotide-binding; Palmitate; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation.
FT CHAIN 1..374
FT /note="Glutamine synthetase"
FT /id="PRO_0000153140"
FT DOMAIN 24..106
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 114..374
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 135
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 137
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 197
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 204..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 204
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 247..248
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 254
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 256..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 320
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 337..339
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 341
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15104"
SQ SEQUENCE 374 AA; 42023 MW; 6F2A0035CA38C68A CRC64;
MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW
NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE SFQVQFEGPA ETNLRHTCKR
IMDMVSNQHP WFGMEQEYTL MGTDGHPFGW PSNGFPGPQG PYYCGVGADR AYGRDIVEAH
YRACLYAGVK IAGTNAEVMP AQWEFQIGPC EGISMGDHLW VARFILHRVC EDFGVIATFD
PKPIPGNWNG AGCHTNFSTK AMREENGLKY IEEAIEKLSK RHQYHIRAYD PKGGLDNARR
LTGFHETSNI NDFSAGVANR SASIRIPRTV GQEKKGYFED RRPSANCDPF SVTEALIRTC
LLNETGDEPF QYKN
