ID GSH1_RAT Reviewed; 637 AA.
AC P19468;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-APR-2013, entry version 95.
DE RecName: Full=Glutamate--cysteine ligase catalytic subunit;
DE EC=6.3.2.2;
DE AltName: Full=GCS heavy chain;
DE AltName: Full=Gamma-ECS;
DE AltName: Full=Gamma-glutamylcysteine synthetase;
GN Name=Gclc; Synonyms=Glclc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Kidney;
RX PubMed=1967255;
RA Yan N., Meister A.;
RT "Amino acid sequence of rat kidney gamma-glutamylcysteine
RT synthetase.";
RL J. Biol. Chem. 265:1588-1593(1990).
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
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 -!- TISSUE SPECIFICITY: Most abundant in kidney. Also found in liver
CC and testis.
CC -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 3
CC family.
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DR EMBL; J05181; AAA41208.1; -; mRNA.
DR EMBL; BC081702; AAH81702.1; -; mRNA.
DR IPI; IPI00231862; -.
DR PIR; A35015; A35015.
DR RefSeq; NP_036947.1; NM_012815.2.
DR UniGene; Rn.8365; -.
DR ProteinModelPortal; P19468; -.
DR STRING; 10116.ENSRNOP00000035540; -.
DR PaxDb; P19468; -.
DR PRIDE; P19468; -.
DR Ensembl; ENSRNOT00000033196; ENSRNOP00000035540; ENSRNOG00000006302.
DR GeneID; 25283; -.
DR KEGG; rno:25283; -.
DR UCSC; RGD:619868; rat.
DR CTD; 2729; -.
DR RGD; 619868; Gclc.
DR eggNOG; NOG269969; -.
DR GeneTree; ENSGT00390000011908; -.
DR HOGENOM; HOG000199354; -.
DR HOVERGEN; HBG005924; -.
DR InParanoid; P19468; -.
DR KO; K11204; -.
DR OMA; GILQFLH; -.
DR OrthoDB; EOG47M1XB; -.
DR BioCyc; MetaCyc:MONOMER-10024; -.
DR BRENDA; 6.3.2.2; 5301.
DR SABIO-RK; P19468; -.
DR UniPathway; UPA00142; UER00209.
DR NextBio; 606009; -.
DR Genevestigator; P19468; -.
DR GermOnline; ENSRNOG00000006302; Rattus norvegicus.
DR GO; GO:0005829; C:cytosol; IEA:Compara.
DR GO; GO:0017109; C:glutamate-cysteine ligase complex; IDA:RGD.
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; IDA:RGD.
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; IEA:Compara.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Compara.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Compara.
DR GO; GO:0050880; P:regulation of blood vessel size; ISS:UniProtKB.
DR GO; GO:0051900; P:regulation of mitochondrial depolarization; IEA:Compara.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:Compara.
DR GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR GO; GO:0009725; P:response to hormone stimulus; ISS:UniProtKB.
DR GO; GO:0051409; P:response to nitrosative stress; IMP:RGD.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Compara.
DR InterPro; IPR004308; GCS.
DR PANTHER; PTHR11164; PTHR11164; 1.
DR Pfam; PF03074; GCS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Direct protein sequencing;
KW Glutathione biosynthesis; Ligase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed (Probable).
FT CHAIN 2 637 Glutamate--cysteine ligase catalytic
FT subunit.
FT /FTId=PRO_0000192565.
FT MOD_RES 5 5 Phosphoserine (By similarity).
FT MOD_RES 8 8 Phosphoserine (By similarity).
SQ SEQUENCE 637 AA; 72619 MW; 9F0AFA15684A5AE2 CRC64;
MGLLSQGSPL SWEETQRHAD HVRRHGILQF LHIYHAVKDR HKDVLKWGDE VEYMLVSFDH
ENRKVQLLLN GGDVLETLQE KGERTNPNHP TLWRPEYGSY MIEGTPGQPY GGTMSEFNTV
EDNMRKRRKE ATSVLGEHQA LCTITSFPRL GCPGFTLPEH RPNPEEGGAS KSLFFPDEAI
NKHPRFGTLT RNIRHRRGEK VVINVPIFKD KNTPSPFVET FPEDEEASKA SKPDHIYMDA
MGFGMGNCCL QVTFQACSIS EARYLYDQLA TICPIVMALS AASPFYRGYV SDIDCRWGVI
SASVDDRTRE ERGLEPLKNN RFKISKSRYD SIDSYLSKCG EKYNDIDLTI DTEIYEQLLE
EGIDHLLAQH VAHLFIRDPL TLFEEKIHLD DANESDHFEN IQSTNWQTMR FKPPPPNSDI
GWRVEFRPME VQLTDFENSA YVVFVVLLTR VILSYKLDFL IPLSKVDENM KVAQERDAVL
QGMFYFRKDI CKGGNAVVDG CSKAQTSSEP SAEEYTLMSI DTIINGKEGV FPGLIPILNS
YLENMEVDVD TRCSILNYLK LIKKRASGEL MTVARWMREF IANHPDYKQD SVITDEINYS
LILKCNQIAN ELCECPELLG SGFRKAKYSG GKSDPSD
//
