ID GSH1_MOUSE Reviewed; 637 AA. AC P97494; O09166; Q8VCS5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 16-JUN-2009, entry version 70. DE RecName: Full=Glutamate--cysteine ligase catalytic subunit; DE EC=6.3.2.2; DE AltName: Full=Gamma-glutamylcysteine synthetase; DE AltName: Full=Gamma-ECS; DE AltName: Full=GCS heavy chain; GN Name=Gclc; Synonyms=Glclc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Liver; RX MEDLINE=97366291; PubMed=9223101; RA Kang Y., Oiao X., Jurma O., Knusel B., Andersen J.K.; RT "Cloning/brain localization of mouse glutamylcysteine synthetase heavy RT chain mRNA."; RL NeuroReport 8:2053-2060(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C57BL/6; TISSUE=Kidney; RX MEDLINE=97368178; PubMed=9224945; DOI=10.1016/S0167-4781(97)00058-4; RA Reid L.L., Botta D., Lu Y., Gallagher E.P., Kavanagh T.J.; RT "Molecular cloning and sequencing of the cDNA encoding the catalytic RT subunit of mouse glutamate-cysteine ligase."; RL Biochim. Biophys. Acta 1352:233-237(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Liver; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + L-cysteine = ADP + CC phosphate + gamma-L-glutamyl-L-cysteine. CC -!- ENZYME REGULATION: Feedback inhibition by glutathione. CC -!- PATHWAY: Sulfur metabolism; glutathione biosynthesis; glutathione CC from L-cysteine and L-glutamate: step 1/2. CC -!- SUBUNIT: Heterodimer of a catalytic heavy chain and a regulatory CC light chain. CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3 CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U85414; AAB42020.1; -; mRNA. DR EMBL; U85498; AAB52542.1; -; mRNA. DR EMBL; BC019374; AAH19374.1; -; mRNA. DR IPI; IPI00125658; -. DR RefSeq; NP_034425.1; -. DR UniGene; Mm.89888; -. DR PRIDE; P97494; -. DR Ensembl; ENSMUSG00000032350; Mus musculus. DR GeneID; 14629; -. DR KEGG; mmu:14629; -. DR MGI; MGI:104990; Gclc. DR HOGENOM; P97494; -. DR HOVERGEN; P97494; -. DR OMA; P97494; FNTVEDN. DR BRENDA; 6.3.2.2; 244. DR NextBio; 286474; -. DR ArrayExpress; P97494; -. DR Bgee; P97494; -. DR CleanEx; MM_GCLC; -. DR GermOnline; ENSMUSG00000032350; Mus musculus. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0017109; C:glutamate-cysteine ligase complex; IDA:MGI. DR GO; GO:0043531; F:ADP binding; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050662; F:coenzyme binding; ISS:UniProtKB. DR GO; GO:0016595; F:glutamate binding; ISS:UniProtKB. DR GO; GO:0004357; F:glutamate-cysteine ligase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI. DR GO; GO:0006916; P:anti-apoptosis; ISS:UniProtKB. DR GO; GO:0045454; P:cell redox homeostasis; ISS:UniProtKB. DR GO; GO:0006534; P:cysteine metabolic process; ISS:UniProtKB. DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB. DR GO; GO:0006750; P:glutathione biosynthetic process; ISS:UniProtKB. DR GO; GO:0019852; P:L-ascorbic acid metabolic process; IMP:MGI. DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:MGI. DR GO; GO:0016481; P:negative regulation of transcription; ISS:UniProtKB. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquiti...; IMP:MGI. DR GO; GO:0050880; P:regulation of blood vessel size; ISS:UniProtKB. DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IGI:MGI. DR GO; GO:0046685; P:response to arsenic; IMP:MGI. DR GO; GO:0009408; P:response to heat; ISS:UniProtKB. DR GO; GO:0009725; P:response to hormone stimulus; ISS:UniProtKB. DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI. DR InterPro; IPR004308; GCS. DR PANTHER; PTHR11164; GCS; 1. DR Pfam; PF03074; GCS; 1. PE 2: Evidence at transcript level; KW ATP-binding; Glutathione biosynthesis; Ligase; Nucleotide-binding. FT INIT_MET 1 1 Removed (Probable). FT CHAIN 2 637 Glutamate--cysteine ligase catalytic FT subunit. FT /FTId=PRO_0000192564. FT CONFLICT 6 6 Q -> H (in Ref. 1; AAB42020). FT CONFLICT 25 26 HG -> RD (in Ref. 1; AAB42020). FT CONFLICT 32 32 H -> Q (in Ref. 3; AAH19374). FT CONFLICT 500 500 G -> E (in Ref. 1; AAB42020). SQ SEQUENCE 637 AA; 72571 MW; 8A176CD1DE49094C CRC64; MGLLSQGSPL SWEETQRHAD HVRRHGILQF LHIYHAVKDR HKDVLKWGDE VEYMLVSFDH ENRKVQLLLN GGDVLETLQE KGERTNPNHP TLWRPEYGSY MIEGTPGQPY GGTMSEFNTV EANMRKRRKE ATSVLGEHQA LCTITSFPRL GCPGFTLPEH RPNPEEGGAS KSLFFPDEAI NKHPRFGTLT RNIRHRRGEK VVINVPIFKD KNTPSPFVET FPEDAEASKA SQPDHIYMDA MGFGMGNCCL QVTFQACSIS EARYLYDQLA TICPIVMALS AASPFYRGYV SDIDCRWGVI SASVDDRTRE ERGLEPLKNN RFRISKSRYD SIDSYLSKCG EKYNDIDLTI DKEIYEQLLE EGIDHLLAQH VAHLFIRDPL TLFEEKIHLD DANESDHFEN IQSTNWQTMR FKPPPPNSDI GWRVEFRPME VQLTDFENSA YVVFVVLLTR VILSYKLDFL IPLSKVDENM KVAQKRDAVL QGMFYFRKDI CKGGNAVVDG CSKAQSSSEP AAEEYTLMSI DTIINGKEGV FPGLIPILNS YLENMEVDVD TRCSILNYLK LIKKRASGEL MTVARWMREF IANHPDYKQD SVITDEINYS LIWKCNQIAD ELCECPELLG SGFRKAKYSG GKSDPSA //