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Protein

Glutamate--cysteine ligase regulatory subunit

Gene

Gclm

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

Functioni

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

  • glutamate-cysteine ligase activity Source: RGD
  • glutamate-cysteine ligase catalytic subunit binding Source: UniProtKB
  • protein heterodimerization activity Source: RGD

GO - Biological processi

  • aging Source: RGD
  • apoptotic mitochondrial changes Source: Ensembl
  • 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 thyroxine stimulus Source: RGD
  • cysteine metabolic process Source: Ensembl
  • glutamate metabolic process Source: UniProtKB
  • glutathione biosynthetic process Source: UniProtKB
  • negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  • negative regulation of neuron apoptotic process Source: RGD
  • positive regulation of glutamate-cysteine ligase activity Source: RGD
  • regulation of blood vessel size Source: UniProtKB
  • regulation of mitochondrial depolarization Source: Ensembl
  • response to activity Source: RGD
  • response to drug Source: UniProtKB
  • response to human chorionic gonadotropin Source: RGD
  • response to nitrosative stress Source: RGD
  • response to oxidative stress Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Glutathione biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10025.
BRENDAi6.3.2.2. 5301.
ReactomeiR-RNO-1614635. Sulfur amino acid metabolism.
R-RNO-174403. Glutathione synthesis and recycling.
SABIO-RKP48508.
UniPathwayiUPA00142; UER00209.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate--cysteine ligase regulatory subunit
Alternative name(s):
GCS light chain
Gamma-ECS regulatory subunit
Gamma-glutamylcysteine synthetase regulatory subunit
Glutamate--cysteine ligase modifier subunit
Gene namesi
Name:Gclm
Synonyms:Glclr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi619871. Gclm.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 274274Glutamate--cysteine ligase regulatory subunitPRO_0000192575Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591PhosphoserineCombined sources
Modified residuei263 – 2631N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP48508.
PRIDEiP48508.

PTM databases

iPTMnetiP48508.
PhosphoSiteiP48508.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevisibleiP48508. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248351. 1 interaction.
STRINGi10116.ENSRNOP00000018343.

Structurei

3D structure databases

ProteinModelPortaliP48508.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3023. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00510000047658.
HOGENOMiHOG000007111.
HOVERGENiHBG005923.
InParanoidiP48508.
KOiK11205.
OMAiEYLQPYW.
OrthoDBiEOG7B5WWG.
PhylomeDBiP48508.
TreeFamiTF105986.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR032963. Gclm.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR13295. PTHR13295. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
SUPFAMiSSF51430. SSF51430. 1 hit.

Sequencei

Sequence statusi: Complete.

P48508-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTDSRAAGA LLARASTLHL QTGNLLNWGR LRKKCPSTHS EELRDCIQKT
60 70 80 90 100
LNEWSSQISP DLVREFPDVL ECTMSHAVEK INPDEREEMK VSAKLFIVGS
110 120 130 140 150
NSSSSTRNAV DMACSVLGVA QLDSVIMASP PIEDGVNLSL EHLQPYWEEL
160 170 180 190 200
ENLVQSKKIV AIGTSDLDKT QLEQLYQWAQ VKPNSNQVNL ASCCVMPPDL
210 220 230 240 250
TAFAKQFDIQ LLTHNDPKEL LSEASFQEAL QESIPDIEAQ EWVPLWLLRY
260 270
SVIVKSRGII KSKGYILQAK RKGS
Length:274
Mass (Da):30,548
Last modified:February 1, 1996 - v1
Checksum:iC99E35591C96C9CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S65555 mRNA. Translation: AAB28225.1.
L22191 mRNA. Translation: AAA41543.1.
BC078867 mRNA. Translation: AAH78867.1.
PIRiA48019.
RefSeqiNP_059001.1. NM_017305.2.
UniGeneiRn.2460.

Genome annotation databases

EnsembliENSRNOT00000018343; ENSRNOP00000018343; ENSRNOG00000013409.
GeneIDi29739.
KEGGirno:29739.
UCSCiRGD:619871. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S65555 mRNA. Translation: AAB28225.1.
L22191 mRNA. Translation: AAA41543.1.
BC078867 mRNA. Translation: AAH78867.1.
PIRiA48019.
RefSeqiNP_059001.1. NM_017305.2.
UniGeneiRn.2460.

3D structure databases

ProteinModelPortaliP48508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248351. 1 interaction.
STRINGi10116.ENSRNOP00000018343.

PTM databases

iPTMnetiP48508.
PhosphoSiteiP48508.

Proteomic databases

PaxDbiP48508.
PRIDEiP48508.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000018343; ENSRNOP00000018343; ENSRNOG00000013409.
GeneIDi29739.
KEGGirno:29739.
UCSCiRGD:619871. rat.

Organism-specific databases

CTDi2730.
RGDi619871. Gclm.

Phylogenomic databases

eggNOGiKOG3023. Eukaryota.
COG0656. LUCA.
GeneTreeiENSGT00510000047658.
HOGENOMiHOG000007111.
HOVERGENiHBG005923.
InParanoidiP48508.
KOiK11205.
OMAiEYLQPYW.
OrthoDBiEOG7B5WWG.
PhylomeDBiP48508.
TreeFamiTF105986.

Enzyme and pathway databases

UniPathwayiUPA00142; UER00209.
BioCyciMetaCyc:MONOMER-10025.
BRENDAi6.3.2.2. 5301.
ReactomeiR-RNO-1614635. Sulfur amino acid metabolism.
R-RNO-174403. Glutathione synthesis and recycling.
SABIO-RKP48508.

Miscellaneous databases

NextBioi610240.
PROiP48508.

Gene expression databases

GenevisibleiP48508. RN.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR032963. Gclm.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR13295. PTHR13295. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
SUPFAMiSSF51430. SSF51430. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Amino acid sequence and function of the light subunit of rat kidney gamma-glutamylcysteine synthetase."
    Huang C.-S., Anderson M.E., Meister A.
    J. Biol. Chem. 268:20578-20583(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 139-156 AND 219-241.
    Tissue: Kidney.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGSH0_RAT
AccessioniPrimary (citable) accession number: P48508
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: May 11, 2016
This is version 113 of the entry and version 1 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.