GSHB_MOUSE
ID GSHB_MOUSE Reviewed; 474 AA.
AC P51855;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Glutathione synthetase {ECO:0000303|PubMed:8660701};
DE Short=GSH synthetase;
DE Short=GSH-S;
DE EC=6.3.2.3 {ECO:0000250|UniProtKB:P48637};
DE AltName: Full=Glutathione synthase;
GN Name=Gss;
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].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=8660701; DOI=10.1006/abbi.1996.0301;
RA Shi Z.Z., Carter B.Z., Habib G.M., He X., Sazer S., Lebovitz R.M.,
RA Lieberman M.W.;
RT "A single mouse glutathione synthetase gene encodes six mRNAs with
RT different 5' ends.";
RL Arch. Biochem. Biophys. 331:215-224(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC 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).
CC -!- FUNCTION: Catalyzes the production of glutathione from gamma-
CC glutamylcysteine and glycine in an ATP-dependent manner. Glutathione
CC (gamma-glutamylcysteinylglycine, GSH) is the most abundant
CC intracellular thiol in living aerobic cells and is required for
CC numerous processes including the protection of cells against oxidative
CC damage, amino acid transport, the detoxification of foreign compounds,
CC the maintenance of protein sulfhydryl groups in a reduced state and
CC acts as a cofactor for a number of enzymes.
CC {ECO:0000250|UniProtKB:P48637}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP +
CC glutathione + H(+) + phosphate; Xref=Rhea:RHEA:13557,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:57925, ChEBI:CHEBI:58173,
CC ChEBI:CHEBI:456216; EC=6.3.2.3;
CC Evidence={ECO:0000250|UniProtKB:P48637};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13558;
CC Evidence={ECO:0000250|UniProtKB:P48637};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P48637};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P48637};
CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 2/2. {ECO:0000250|UniProtKB:P48637}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P48637}.
CC -!- SIMILARITY: Belongs to the eukaryotic GSH synthase family.
CC {ECO:0000305}.
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DR EMBL; U35456; AAB09730.1; -; mRNA.
DR EMBL; BC003784; AAH03784.1; -; mRNA.
DR CCDS; CCDS16951.1; -.
DR PIR; S71322; S71322.
DR RefSeq; NP_032206.1; NM_008180.2.
DR RefSeq; XP_006498844.1; XM_006498781.2.
DR AlphaFoldDB; P51855; -.
DR SMR; P51855; -.
DR BioGRID; 200089; 8.
DR STRING; 10090.ENSMUSP00000078630; -.
DR iPTMnet; P51855; -.
DR PhosphoSitePlus; P51855; -.
DR EPD; P51855; -.
DR jPOST; P51855; -.
DR PaxDb; P51855; -.
DR PeptideAtlas; P51855; -.
DR PRIDE; P51855; -.
DR ProteomicsDB; 271446; -.
DR Antibodypedia; 25920; 439 antibodies from 34 providers.
DR DNASU; 14854; -.
DR Ensembl; ENSMUST00000079691; ENSMUSP00000078630; ENSMUSG00000027610.
DR GeneID; 14854; -.
DR KEGG; mmu:14854; -.
DR UCSC; uc008nkx.2; mouse.
DR CTD; 2937; -.
DR MGI; MGI:95852; Gss.
DR VEuPathDB; HostDB:ENSMUSG00000027610; -.
DR eggNOG; KOG0021; Eukaryota.
DR GeneTree; ENSGT00390000013764; -.
DR InParanoid; P51855; -.
DR OMA; NGLVMYP; -.
DR OrthoDB; 1189955at2759; -.
DR PhylomeDB; P51855; -.
DR TreeFam; TF105187; -.
DR Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR SABIO-RK; P51855; -.
DR UniPathway; UPA00142; UER00210.
DR BioGRID-ORCS; 14854; 12 hits in 76 CRISPR screens.
DR ChiTaRS; Gss; mouse.
DR PRO; PR:P51855; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P51855; protein.
DR Bgee; ENSMUSG00000027610; Expressed in right kidney and 205 other tissues.
DR ExpressionAtlas; P51855; baseline and differential.
DR Genevisible; P51855; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0043295; F:glutathione binding; ISS:UniProtKB.
DR GO; GO:0004363; F:glutathione synthase activity; IDA:MGI.
DR GO; GO:0016594; F:glycine binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; ISO:MGI.
DR GO; GO:0046686; P:response to cadmium ion; IDA:MGI.
DR CDD; cd00228; eu-GS; 1.
DR Gene3D; 1.10.1080.10; -; 1.
DR Gene3D; 3.30.1490.50; -; 1.
DR Gene3D; 3.30.1490.80; -; 1.
DR Gene3D; 3.40.50.1760; -; 1.
DR InterPro; IPR005615; Glutathione_synthase.
DR InterPro; IPR014042; Glutathione_synthase_a-hlx.
DR InterPro; IPR014709; Glutathione_synthase_C_euk.
DR InterPro; IPR014049; Glutathione_synthase_N_euk.
DR InterPro; IPR037013; GSH-S_sub-bd_sf.
DR InterPro; IPR004887; GSH_synth_subst-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR11130; PTHR11130; 1.
DR Pfam; PF03917; GSH_synth_ATP; 1.
DR Pfam; PF03199; GSH_synthase; 1.
DR PIRSF; PIRSF001558; GSHase; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR TIGRFAMs; TIGR01986; glut_syn_euk; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Glutathione biosynthesis; Ligase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P48637"
FT CHAIN 2..474
FT /note="Glutathione synthetase"
FT /id="PRO_0000211262"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 148..151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214..216
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267..270
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 305
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 364..373
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 398..401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 452
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 461..462
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P48637"
FT MOD_RES 415
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P48637"
SQ SEQUENCE 474 AA; 52247 MW; E1302C5B2C28A43A CRC64;
MATSWGSILQ DEKQLEELAK QAIDRALAEG VLLRSAQHPS SSDVVTYAPF TLFPSPVPSA
LLEQAYAVQM DFNILVDAVS QNPAFLEQTL SSTIKKDDYT ARLFDIYKQV LKEGIAQTVF
LGLNRSDYMF QCGADGSKAL KQIEINTISA SFGGLASRTP AVHRHVLNVL NKTKEASKIL
SNNPSKGLAL GIAKAWELYG SANAVVLLIA QEKERNIFDQ RAVENELLDR KIHVIRGRFE
DVSERGSLDQ NRRLFMDDQE VAVVYFRDGY MPSQYNSQNW EARLMLERSR AAKCPDIAIQ
LAGTKKVQQE LSRVGLLEAL LPGQPEAVAR LRATFAGLYS LDMGEEGDQA IAEALAAPSH
FVLKPQREGG GNNLYGEEMV QALEQLKDSE ERASYILMEK IEPEPFRNCL LRPGSPAQVV
QCISELGIFG VYVRQGTTLV MNKHVGHLLR TKAVEHADGG VAAGVAVLDN PYPV
