ID   GSH0_BOVIN              Reviewed;         274 AA.
AC   Q2T9Y6;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the aldo/keto reductase family. Glutamate--
CC       cysteine ligase light chain subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC111206; AAI11207.1; -; mRNA.
DR   RefSeq; NP_001033232.1; NM_001038143.1.
DR   AlphaFoldDB; Q2T9Y6; -.
DR   SMR; Q2T9Y6; -.
DR   STRING; 9913.ENSBTAP00000026855; -.
DR   SwissPalm; Q2T9Y6; -.
DR   PaxDb; Q2T9Y6; -.
DR   PRIDE; Q2T9Y6; -.
DR   Ensembl; ENSBTAT00000026855; ENSBTAP00000026855; ENSBTAG00000007842.
DR   GeneID; 525659; -.
DR   KEGG; bta:525659; -.
DR   CTD; 2730; -.
DR   VEuPathDB; HostDB:ENSBTAG00000007842; -.
DR   VGNC; VGNC:29290; GCLM.
DR   eggNOG; KOG3023; Eukaryota.
DR   GeneTree; ENSGT00510000047658; -.
DR   HOGENOM; CLU_055657_1_0_1; -.
DR   InParanoid; Q2T9Y6; -.
DR   OMA; NWGCLRK; -.
DR   OrthoDB; 1516283at2759; -.
DR   TreeFam; TF105986; -.
DR   Reactome; R-BTA-174403; Glutathione synthesis and recycling.
DR   UniPathway; UPA00142; UER00209.
DR   Proteomes; UP000009136; Chromosome 3.
DR   Bgee; ENSBTAG00000007842; Expressed in liver and 104 other tissues.
DR   GO; GO:0017109; C:glutamate-cysteine ligase complex; ISS:UniProtKB.
DR   GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:Ensembl.
DR   GO; GO:0035226; F:glutamate-cysteine ligase catalytic subunit binding; ISS:UniProtKB.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; ISS:UniProtKB.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:Ensembl.
DR   GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006750; P:glutathione biosynthetic process; ISS:UniProtKB.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0035229; P:positive regulation of glutamate-cysteine ligase activity; IBA:GO_Central.
DR   GO; GO:0051900; P:regulation of mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Glutathione biosynthesis; Phosphoprotein; Reference proteome.
FT   CHAIN           1..274
FT                   /note="Glutamate--cysteine ligase regulatory subunit"
FT                   /id="PRO_0000253731"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O09172"
FT   MOD_RES         263
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P48507"
SQ   SEQUENCE   274 AA;  30533 MW;  D1E5B90BE45D6008 CRC64;
     MGTDSRAAGA LLARASTLHL QTGNLLNWGR LRKKCPSTHS EELRDCIQKT LNEWSSQISP
     DLIREFPDVL ECTVSHAVEK INPDEREEMK VSAKLFIVGS NSSSSTRNAV DMACSVLGVA
     QLDSVIIASP PVEDGVNLSL EHLQPYWEEL QNLVQSKKIV AIGTSDLDKT QLEQLYQWAQ
     VKPNSNQVNL ASCCVMPPDL TAFAKQFDIQ LLTHNDPKEL LSEASFQEAL QESIPDIRAH
     EWVPLWLLRY SVIVKSRGII KSKGYILQAK RKGS