Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P97494 (GSH1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate--cysteine ligase catalytic subunit

EC=6.3.2.2
Alternative name(s):
GCS heavy chain
Gamma-ECS
Gamma-glutamylcysteine synthetase
Gene names
Name:Gclc
Synonyms:Glclc
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Feedback inhibition by glutathione.

Pathway

Sulfur metabolism; glutathione biosynthesis; glutathione from L-cysteine and L-glutamate: step 1/2.

Subunit structure

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

Sequence similarities

Belongs to the glutamate--cysteine ligase type 3 family.

Ontologies

Keywords
   Biological processGlutathione biosynthesis
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-ascorbic acid metabolic process

Inferred from mutant phenotype PubMed 11118286. Source: MGI

apoptotic mitochondrial changes

Inferred from genetic interaction PubMed 15288121. Source: MGI

cell redox homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

cysteine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione metabolic process

Inferred from mutant phenotype PubMed 11118286. Source: MGI

negative regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of extrinsic apoptotic signaling pathway

Inferred from genetic interaction PubMed 15288121. Source: MGI

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein ubiquitination

Inferred from mutant phenotype PubMed 17189825. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 17189825. Source: MGI

regulation of blood vessel size

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mitochondrial depolarization

Inferred from genetic interaction PubMed 15288121. Source: MGI

response to arsenic-containing substance

Inferred from mutant phenotype PubMed 17189825. Source: MGI

response to heat

Inferred from sequence or structural similarity. Source: UniProtKB

response to hormone

Inferred from sequence or structural similarity. Source: UniProtKB

response to nitrosative stress

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

response to xenobiotic stimulus

Inferred from mutant phenotype PubMed 17189825. Source: MGI

   Cellular_componentcytosol

Inferred from direct assay PubMed 12384496. Source: MGI

glutamate-cysteine ligase complex

Inferred from direct assay PubMed 12384496. Source: MGI

   Molecular_functionADP binding

Inferred from sequence or structural similarity. Source: UniProtKB

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

coenzyme binding

Inferred from sequence or structural similarity. Source: UniProtKB

glutamate binding

Inferred from sequence or structural similarity. Source: UniProtKB

glutamate-cysteine ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

magnesium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein heterodimerization activity

Inferred from physical interaction PubMed 12384496PubMed 16081425. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637Glutamate--cysteine ligase catalytic subunit
PRO_0000192564

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue51Phosphoserine By similarity
Modified residue81Phosphoserine By similarity

Experimental info

Sequence conflict61Q → H in AAB42020. Ref.1
Sequence conflict25 – 262HG → RD in AAB42020. Ref.1
Sequence conflict321H → Q in AAH19374. Ref.3
Sequence conflict5001G → E in AAB42020. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P97494 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 8A176CD1DE49094C

FASTA63772,571
        10         20         30         40         50         60 
MGLLSQGSPL SWEETQRHAD HVRRHGILQF LHIYHAVKDR HKDVLKWGDE VEYMLVSFDH 

        70         80         90        100        110        120 
ENRKVQLLLN GGDVLETLQE KGERTNPNHP TLWRPEYGSY MIEGTPGQPY GGTMSEFNTV 

       130        140        150        160        170        180 
EANMRKRRKE ATSVLGEHQA LCTITSFPRL GCPGFTLPEH RPNPEEGGAS KSLFFPDEAI 

       190        200        210        220        230        240 
NKHPRFGTLT RNIRHRRGEK VVINVPIFKD KNTPSPFVET FPEDAEASKA SQPDHIYMDA 

       250        260        270        280        290        300 
MGFGMGNCCL QVTFQACSIS EARYLYDQLA TICPIVMALS AASPFYRGYV SDIDCRWGVI 

       310        320        330        340        350        360 
SASVDDRTRE ERGLEPLKNN RFRISKSRYD SIDSYLSKCG EKYNDIDLTI DKEIYEQLLE 

       370        380        390        400        410        420 
EGIDHLLAQH VAHLFIRDPL TLFEEKIHLD DANESDHFEN IQSTNWQTMR FKPPPPNSDI 

       430        440        450        460        470        480 
GWRVEFRPME VQLTDFENSA YVVFVVLLTR VILSYKLDFL IPLSKVDENM KVAQKRDAVL 

       490        500        510        520        530        540 
QGMFYFRKDI CKGGNAVVDG CSKAQSSSEP AAEEYTLMSI DTIINGKEGV FPGLIPILNS 

       550        560        570        580        590        600 
YLENMEVDVD TRCSILNYLK LIKKRASGEL MTVARWMREF IANHPDYKQD SVITDEINYS 

       610        620        630 
LIWKCNQIAD ELCECPELLG SGFRKAKYSG GKSDPSA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning/brain localization of mouse glutamylcysteine synthetase heavy chain mRNA."
Kang Y., Oiao X., Jurma O., Knusel B., Andersen J.K.
NeuroReport 8:2053-2060(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Molecular cloning and sequencing of the cDNA encoding the catalytic subunit of mouse glutamate-cysteine ligase."
Reid L.L., Botta D., Lu Y., Gallagher E.P., Kavanagh T.J.
Biochim. Biophys. Acta 1352:233-237(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Kidney.
[3]"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: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85414 mRNA. Translation: AAB42020.1.
U85498 mRNA. Translation: AAB52542.1.
BC019374 mRNA. Translation: AAH19374.1.
CCDSCCDS23354.1.
RefSeqNP_034425.1. NM_010295.2.
UniGeneMm.89888.

3D structure databases

ProteinModelPortalP97494.
SMRP97494. Positions 2-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199940. 1 interaction.
IntActP97494. 2 interactions.
MINTMINT-1869507.

PTM databases

PhosphoSiteP97494.

Proteomic databases

MaxQBP97494.
PaxDbP97494.
PRIDEP97494.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034905; ENSMUSP00000034905; ENSMUSG00000032350.
GeneID14629.
KEGGmmu:14629.
UCSCuc009qtm.2. mouse.

Organism-specific databases

CTD2729.
MGIMGI:104990. Gclc.

Phylogenomic databases

eggNOGNOG269969.
HOGENOMHOG000199354.
HOVERGENHBG005924.
InParanoidP97494.
KOK11204.
OMARWMREFI.
OrthoDBEOG7B8S3B.
PhylomeDBP97494.
TreeFamTF105644.

Enzyme and pathway databases

BRENDA6.3.2.2. 3474.
SABIO-RKP97494.
UniPathwayUPA00142; UER00209.

Gene expression databases

ArrayExpressP97494.
BgeeP97494.
CleanExMM_GCLC.
GenevestigatorP97494.

Family and domain databases

InterProIPR004308. GCS.
[Graphical view]
PANTHERPTHR11164. PTHR11164. 1 hit.
PfamPF03074. GCS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio286474.
PROP97494.
SOURCESearch...

Entry information

Entry nameGSH1_MOUSE
AccessionPrimary (citable) accession number: P97494
Secondary accession number(s): O09166, Q8VCS5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 116 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot