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Protein

Glutamate--cysteine ligase catalytic subunit

Gene

Gclc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.

Enzyme regulationi

Feedback inhibition by glutathione.

Pathwayi: glutathione biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes glutathione from L-cysteine and L-glutamate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamate--cysteine ligase regulatory subunit (Gclm), Glutamate--cysteine ligase catalytic subunit (Gclc)
  2. Glutathione synthetase (Gss)
This subpathway is part of the pathway glutathione biosynthesis, which is itself part of Sulfur metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes glutathione from L-cysteine and L-glutamate, the pathway glutathione biosynthesis and in Sulfur metabolism.

GO - Molecular functioni

GO - Biological processi

  • aging Source: RGD
  • apoptotic mitochondrial changes Source: Ensembl
  • cell redox homeostasis Source: UniProtKB
  • cellular response to fibroblast growth factor stimulus Source: RGD
  • cellular response to follicle-stimulating hormone stimulus Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to hepatocyte growth factor stimulus Source: RGD
  • cellular response to insulin stimulus Source: RGD
  • cellular response to mechanical stimulus Source: RGD
  • cellular response to thyroxine stimulus Source: RGD
  • cysteine metabolic process Source: UniProtKB
  • glutamate metabolic process Source: UniProtKB
  • glutathione biosynthetic process Source: UniProtKB
  • L-ascorbic acid metabolic process Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  • negative regulation of hepatic stellate cell activation Source: RGD
  • negative regulation of neuron apoptotic process Source: RGD
  • negative regulation of protein ubiquitination Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  • regulation of blood vessel size Source: UniProtKB
  • regulation of mitochondrial depolarization Source: Ensembl
  • response to activity Source: RGD
  • response to arsenic-containing substance Source: Ensembl
  • response to cadmium ion Source: RGD
  • response to heat Source: UniProtKB
  • response to hormone Source: UniProtKB
  • response to human chorionic gonadotropin Source: RGD
  • response to interleukin-1 Source: RGD
  • response to nitrosative stress Source: RGD
  • response to nutrient Source: RGD
  • response to oxidative stress Source: UniProtKB
  • response to xenobiotic stimulus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10024.
BRENDAi6.3.2.2. 5301.
ReactomeiR-RNO-1614635. Sulfur amino acid metabolism.
R-RNO-174403. Glutathione synthesis and recycling.
SABIO-RKP19468.
UniPathwayiUPA00142; UER00209.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--cysteine ligase catalytic subunit (EC:6.3.2.2)
Alternative name(s):
GCS heavy chain
Gamma-ECS
Gamma-glutamylcysteine synthetase
Gene namesi
Name:Gclc
Synonyms:Glclc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 8

Organism-specific databases

RGDi619868. Gclc.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Ensembl
  • glutamate-cysteine ligase complex Source: RGD
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2366469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 637637Glutamate--cysteine ligase catalytic subunitPRO_0000192565Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei5 – 51PhosphoserineCombined sources
Modified residuei8 – 81PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP19468.
PRIDEiP19468.

PTM databases

iPTMnetiP19468.
PhosphoSiteiP19468.

Expressioni

Tissue specificityi

Most abundant in kidney. Also found in liver and testis.

Gene expression databases

BgeeiENSRNOG00000006302.
GenevisibleiP19468. RN.

Interactioni

Subunit structurei

Heterodimer of a catalytic heavy chain and a regulatory light chain.

GO - Molecular functioni

  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi247323. 1 interaction.
STRINGi10116.ENSRNOP00000035540.

Structurei

3D structure databases

ProteinModelPortaliP19468.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3754. Eukaryota.
ENOG410XQIG. LUCA.
GeneTreeiENSGT00390000011908.
HOGENOMiHOG000199354.
HOVERGENiHBG005924.
InParanoidiP19468.
KOiK11204.
OMAiPIQRTTE.
OrthoDBiEOG091G03DC.
PhylomeDBiP19468.
TreeFamiTF105644.

Family and domain databases

InterProiIPR004308. GCS.
[Graphical view]
PANTHERiPTHR11164. PTHR11164. 1 hit.
PfamiPF03074. GCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19468-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLSQGSPL SWEETQRHAD HVRRHGILQF LHIYHAVKDR HKDVLKWGDE
60 70 80 90 100
VEYMLVSFDH ENRKVQLLLN GGDVLETLQE KGERTNPNHP TLWRPEYGSY
110 120 130 140 150
MIEGTPGQPY GGTMSEFNTV EDNMRKRRKE ATSVLGEHQA LCTITSFPRL
160 170 180 190 200
GCPGFTLPEH RPNPEEGGAS KSLFFPDEAI NKHPRFGTLT RNIRHRRGEK
210 220 230 240 250
VVINVPIFKD KNTPSPFVET FPEDEEASKA SKPDHIYMDA MGFGMGNCCL
260 270 280 290 300
QVTFQACSIS EARYLYDQLA TICPIVMALS AASPFYRGYV SDIDCRWGVI
310 320 330 340 350
SASVDDRTRE ERGLEPLKNN RFKISKSRYD SIDSYLSKCG EKYNDIDLTI
360 370 380 390 400
DTEIYEQLLE EGIDHLLAQH VAHLFIRDPL TLFEEKIHLD DANESDHFEN
410 420 430 440 450
IQSTNWQTMR FKPPPPNSDI GWRVEFRPME VQLTDFENSA YVVFVVLLTR
460 470 480 490 500
VILSYKLDFL IPLSKVDENM KVAQERDAVL QGMFYFRKDI CKGGNAVVDG
510 520 530 540 550
CSKAQTSSEP SAEEYTLMSI DTIINGKEGV FPGLIPILNS YLENMEVDVD
560 570 580 590 600
TRCSILNYLK LIKKRASGEL MTVARWMREF IANHPDYKQD SVITDEINYS
610 620 630
LILKCNQIAN ELCECPELLG SGFRKAKYSG GKSDPSD
Length:637
Mass (Da):72,619
Last modified:January 23, 2007 - v2
Checksum:i9F0AFA15684A5AE2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05181 mRNA. Translation: AAA41208.1.
BC081702 mRNA. Translation: AAH81702.1.
PIRiA35015.
RefSeqiNP_036947.1. NM_012815.2.
UniGeneiRn.8365.

Genome annotation databases

EnsembliENSRNOT00000033196; ENSRNOP00000035540; ENSRNOG00000006302.
GeneIDi25283.
KEGGirno:25283.
UCSCiRGD:619868. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J05181 mRNA. Translation: AAA41208.1.
BC081702 mRNA. Translation: AAH81702.1.
PIRiA35015.
RefSeqiNP_036947.1. NM_012815.2.
UniGeneiRn.8365.

3D structure databases

ProteinModelPortaliP19468.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247323. 1 interaction.
STRINGi10116.ENSRNOP00000035540.

Chemistry

ChEMBLiCHEMBL2366469.

PTM databases

iPTMnetiP19468.
PhosphoSiteiP19468.

Proteomic databases

PaxDbiP19468.
PRIDEiP19468.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000033196; ENSRNOP00000035540; ENSRNOG00000006302.
GeneIDi25283.
KEGGirno:25283.
UCSCiRGD:619868. rat.

Organism-specific databases

CTDi2729.
RGDi619868. Gclc.

Phylogenomic databases

eggNOGiKOG3754. Eukaryota.
ENOG410XQIG. LUCA.
GeneTreeiENSGT00390000011908.
HOGENOMiHOG000199354.
HOVERGENiHBG005924.
InParanoidiP19468.
KOiK11204.
OMAiPIQRTTE.
OrthoDBiEOG091G03DC.
PhylomeDBiP19468.
TreeFamiTF105644.

Enzyme and pathway databases

UniPathwayiUPA00142; UER00209.
BioCyciMetaCyc:MONOMER-10024.
BRENDAi6.3.2.2. 5301.
ReactomeiR-RNO-1614635. Sulfur amino acid metabolism.
R-RNO-174403. Glutathione synthesis and recycling.
SABIO-RKP19468.

Miscellaneous databases

PROiP19468.

Gene expression databases

BgeeiENSRNOG00000006302.
GenevisibleiP19468. RN.

Family and domain databases

InterProiIPR004308. GCS.
[Graphical view]
PANTHERiPTHR11164. PTHR11164. 1 hit.
PfamiPF03074. GCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGSH1_RAT
AccessioniPrimary (citable) accession number: P19468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.