GSH0_RAT
ID GSH0_RAT Reviewed; 274 AA.
AC P48508;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 139-156 AND 219-241.
RC TISSUE=Kidney;
RX PubMed=8104188; DOI=10.1016/s0021-9258(20)80764-9;
RA Huang C.-S., Anderson M.E., Meister A.;
RT "Amino acid sequence and function of the light subunit of rat kidney gamma-
RT glutamylcysteine synthetase.";
RL J. Biol. Chem. 268:20578-20583(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Most abundant in kidney. Also found in liver and
CC testis.
CC -!- SIMILARITY: Belongs to the aldo/keto reductase family. Glutamate--
CC cysteine ligase light chain subfamily. {ECO:0000305}.
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DR EMBL; S65555; AAB28225.1; -; mRNA.
DR EMBL; L22191; AAA41543.1; -; mRNA.
DR EMBL; BC078867; AAH78867.1; -; mRNA.
DR PIR; A48019; A48019.
DR RefSeq; NP_059001.1; NM_017305.2.
DR AlphaFoldDB; P48508; -.
DR SMR; P48508; -.
DR BioGRID; 248351; 1.
DR CORUM; P48508; -.
DR STRING; 10116.ENSRNOP00000018343; -.
DR iPTMnet; P48508; -.
DR PhosphoSitePlus; P48508; -.
DR jPOST; P48508; -.
DR PaxDb; P48508; -.
DR PRIDE; P48508; -.
DR Ensembl; ENSRNOT00000018343; ENSRNOP00000018343; ENSRNOG00000013409.
DR GeneID; 29739; -.
DR KEGG; rno:29739; -.
DR UCSC; RGD:619871; rat.
DR CTD; 2730; -.
DR RGD; 619871; Gclm.
DR eggNOG; KOG3023; Eukaryota.
DR GeneTree; ENSGT00510000047658; -.
DR HOGENOM; CLU_055657_1_0_1; -.
DR InParanoid; P48508; -.
DR OMA; NWGCLRK; -.
DR OrthoDB; 1516283at2759; -.
DR PhylomeDB; P48508; -.
DR TreeFam; TF105986; -.
DR BioCyc; MetaCyc:MON-10025; -.
DR BRENDA; 6.3.2.2; 5301.
DR Reactome; R-RNO-174403; Glutathione synthesis and recycling.
DR SABIO-RK; P48508; -.
DR UniPathway; UPA00142; UER00209.
DR PRO; PR:P48508; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000013409; Expressed in kidney and 20 other tissues.
DR Genevisible; P48508; RN.
DR GO; GO:0017109; C:glutamate-cysteine ligase complex; IDA:RGD.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0004357; F:glutamate-cysteine ligase activity; IDA:RGD.
DR GO; GO:0035226; F:glutamate-cysteine ligase catalytic subunit binding; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; ISO:RGD.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISS:UniProtKB.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEP:RGD.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR GO; GO:0097069; P:cellular response to thyroxine stimulus; IEP:RGD.
DR GO; GO:0006534; P:cysteine metabolic process; ISO:RGD.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006750; P:glutathione biosynthetic process; IMP:RGD.
DR GO; GO:0006749; P:glutathione metabolic process; ISO:RGD.
DR GO; GO:0035733; P:hepatic stellate cell activation; IEP:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0035229; P:positive regulation of glutamate-cysteine ligase activity; IDA:RGD.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0044752; P:response to human chorionic gonadotropin; IEP:RGD.
DR GO; GO:0051409; P:response to nitrosative stress; IMP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
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; Direct protein sequencing; Glutathione biosynthesis;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..274
FT /note="Glutamate--cysteine ligase regulatory subunit"
FT /id="PRO_0000192575"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 263
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P48507"
SQ SEQUENCE 274 AA; 30548 MW; C99E35591C96C9CC CRC64;
MGTDSRAAGA LLARASTLHL QTGNLLNWGR LRKKCPSTHS EELRDCIQKT LNEWSSQISP
DLVREFPDVL ECTMSHAVEK INPDEREEMK VSAKLFIVGS NSSSSTRNAV DMACSVLGVA
QLDSVIMASP PIEDGVNLSL EHLQPYWEEL ENLVQSKKIV AIGTSDLDKT QLEQLYQWAQ
VKPNSNQVNL ASCCVMPPDL TAFAKQFDIQ LLTHNDPKEL LSEASFQEAL QESIPDIEAQ
EWVPLWLLRY SVIVKSRGII KSKGYILQAK RKGS
