GSH0_MOUSE
ID GSH0_MOUSE Reviewed; 274 AA.
AC O09172;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Glutamate--cysteine ligase regulatory subunit;
DE AltName: Full=GCS light chain;
DE AltName: Full=Gamma-ECS regulatory subunit;
DE AltName: Full=Gamma-glutamylcysteine synthetase regulatory subunit;
DE AltName: Full=Glutamate--cysteine ligase modifier subunit;
GN Name=Gclm; Synonyms=Glclr;
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=9294003; DOI=10.1016/s0167-4781(97)00092-4;
RA Reid L.L., Botta D., Shao J., Hudson F.N., Kavanagh T.J.;
RT "Molecular cloning and sequencing of the cDNA encoding mouse glutamate-
RT cysteine ligase regulatory subunit.";
RL Biochim. Biophys. Acta 1353:107-110(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ;
RA Dalton T.P., Solis W.A., Dieter M.Z., Freshwater S., Harrer J.,
RA Shertzer H.G., Nebert D.W.;
RT "Mouse glutamate-cysteine ligase regulatory subunit: gene structure and
RT regulation by agents that cause oxidative stress.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and 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 -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione from
CC L-cysteine and L-glutamate: step 1/2.
CC -!- SUBUNIT: Heterodimer of a catalytic heavy chain and a regulatory light
CC chain.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Glutamate--
CC cysteine ligase light chain subfamily. {ECO:0000305}.
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DR EMBL; U95053; AAB96893.1; -; mRNA.
DR EMBL; AF149060; AAG15424.1; -; Genomic_DNA.
DR EMBL; AF149054; AAG15424.1; JOINED; Genomic_DNA.
DR EMBL; AF149055; AAG15424.1; JOINED; Genomic_DNA.
DR EMBL; AF149056; AAG15424.1; JOINED; Genomic_DNA.
DR EMBL; AF149057; AAG15424.1; JOINED; Genomic_DNA.
DR EMBL; AF149058; AAG15424.1; JOINED; Genomic_DNA.
DR EMBL; AF149059; AAG15424.1; JOINED; Genomic_DNA.
DR EMBL; AK028236; BAC25831.1; -; mRNA.
DR CCDS; CCDS17808.1; -.
DR RefSeq; NP_032155.1; NM_008129.4.
DR AlphaFoldDB; O09172; -.
DR SMR; O09172; -.
DR BioGRID; 199941; 4.
DR IntAct; O09172; 1.
DR STRING; 10090.ENSMUSP00000029769; -.
DR iPTMnet; O09172; -.
DR PhosphoSitePlus; O09172; -.
DR SwissPalm; O09172; -.
DR EPD; O09172; -.
DR jPOST; O09172; -.
DR PaxDb; O09172; -.
DR PeptideAtlas; O09172; -.
DR PRIDE; O09172; -.
DR ProteomicsDB; 271178; -.
DR Antibodypedia; 4034; 448 antibodies from 36 providers.
DR DNASU; 14630; -.
DR Ensembl; ENSMUST00000029769; ENSMUSP00000029769; ENSMUSG00000028124.
DR Ensembl; ENSMUST00000178826; ENSMUSP00000136987; ENSMUSG00000028124.
DR GeneID; 14630; -.
DR KEGG; mmu:14630; -.
DR UCSC; uc008reo.2; mouse.
DR CTD; 2730; -.
DR MGI; MGI:104995; Gclm.
DR VEuPathDB; HostDB:ENSMUSG00000028124; -.
DR eggNOG; KOG3023; Eukaryota.
DR GeneTree; ENSGT00510000047658; -.
DR HOGENOM; CLU_055657_1_0_1; -.
DR InParanoid; O09172; -.
DR OMA; NWGCLRK; -.
DR OrthoDB; 1516283at2759; -.
DR PhylomeDB; O09172; -.
DR TreeFam; TF105986; -.
DR BRENDA; 6.3.2.2; 3474.
DR Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR UniPathway; UPA00142; UER00209.
DR BioGRID-ORCS; 14630; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Gclm; mouse.
DR PRO; PR:O09172; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O09172; protein.
DR Bgee; ENSMUSG00000028124; Expressed in right kidney and 253 other tissues.
DR ExpressionAtlas; O09172; baseline and differential.
DR Genevisible; O09172; MM.
DR GO; GO:0017109; C:glutamate-cysteine ligase complex; IDA:MGI.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; ISO:MGI.
DR GO; GO:0035226; F:glutamate-cysteine ligase catalytic subunit binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IGI:MGI.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0097069; P:cellular response to thyroxine stimulus; IEA:Ensembl.
DR GO; GO:0006534; P:cysteine metabolic process; IMP:MGI.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; IDA:MGI.
DR GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR GO; GO:0035733; P:hepatic stellate cell activation; IEA:Ensembl.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IGI:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0035229; P:positive regulation of glutamate-cysteine ligase activity; IDA:MGI.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IGI:MGI.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEA:Ensembl.
DR GO; GO:0051409; P:response to nitrosative stress; ISO:MGI.
DR GO; GO:0007584; P:response to nutrient; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR032963; Gclm.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR13295; PTHR13295; 1.
DR SUPFAM; SSF51430; SSF51430; 1.
PE 1: Evidence at protein level;
KW Acetylation; Glutathione biosynthesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..274
FT /note="Glutamate--cysteine ligase regulatory subunit"
FT /id="PRO_0000192574"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48507"
SQ SEQUENCE 274 AA; 30535 MW; E1D591CAB71CEA11 CRC64;
MGTDSRAAGA LLARASTLHL QTGNLLNWGR LRKKCPSTHS EELRDCIQKT LNEWSSQISP
DLVREFPDVL ECTMSHAVEK INPDEREEMK VSAKLFIVGS NSSSSTRSAV DMACSVLGVA
QLDSVIMASP PIEDGVNLSL EHLQPYWEEL ENLVQSKKIV AIGTSDLDKT QLEQLYQWAQ
VKPNSNQVNL ASCCVMPPDL TAFAKQFDIQ LLTHNDPKEL LSEASFQEAL QESIPDIEAQ
DWVPLWLLRY SVIVKSRGII KSKGYILQAK RRGS
