P07314 · GGT1_RAT

  • Protein
    Glutathione hydrolase 1 proenzyme
  • Gene
    Ggt1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4) (By similarity) (PubMed:6122208).
The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases (PubMed:6122208).
In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound (PubMed:6122208).
Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4 (PubMed:6122208).

Catalytic activity

Activity regulation

Activated by autocatalytic cleavage.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
5.9 μMleukotriene C4
5.7 μMglutathione
5.8 μMgamma-glutamyl-p-anilide

Pathway

Sulfur metabolism; glutathione metabolism.
Lipid metabolism; leukotriene D4 biosynthesis.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site106L-glutamate (UniProtKB | ChEBI)
Active site380Nucleophile
Binding site398-400L-glutamate (UniProtKB | ChEBI)
Binding site419L-glutamate (UniProtKB | ChEBI)
Binding site422L-glutamate (UniProtKB | ChEBI)
Binding site450-451L-glutamate (UniProtKB | ChEBI)
Binding site473L-glutamate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular space
Cellular Componentplasma membrane
Cellular Componentvesicle
Molecular Functionaminoacyltransferase activity
Molecular Functionglutathione hydrolase activity
Molecular Functionleukotriene C4 gamma-glutamyl transferase activity
Molecular Functionleukotriene-C(4) hydrolase
Molecular Functionpeptidyltransferase activity
Biological Processamino acid metabolic process
Biological Processcellular response to oxidative stress
Biological Processcysteine biosynthetic process
Biological Processfatty acid metabolic process
Biological Processglutamate metabolic process
Biological Processglutathione biosynthetic process
Biological Processglutathione catabolic process
Biological Processhepatoblast differentiation
Biological Processhepatocyte differentiation
Biological Processleukotriene D4 biosynthetic process
Biological Processleukotriene metabolic process
Biological Processliver regeneration
Biological Processpeptide modification
Biological Processproteolysis
Biological Processregulation of immune system process
Biological Processregulation of inflammatory response
Biological Processresponse to alcohol
Biological Processresponse to estradiol
Biological Processresponse to lipopolysaccharide
Biological Processresponse to tumor necrosis factor
Biological Processspermatogenesis
Biological Processzymogen activation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      Ggt1
    • Synonyms
      Ggt

Organism names

  • Taxonomic identifier
  • Strain
    • Wistar
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    P07314
  • Secondary accessions
    • Q63217
    • Q63218
    • Q6AZ32

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type II membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-4Cytoplasmic
Transmembrane5-26Helical; Signal-anchor for type II membrane protein
Topological domain27-568Extracellular

Keywords

Phenotypes & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 4 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Chemistry

PTM/Processing

Features

Showing features for chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00000110641-379Glutathione hydrolase 1 heavy chain
Disulfide bond49↔73
Glycosylation94N-linked (GlcNAc...) asparagine
Glycosylation114N-linked (GlcNAc...) asparagine
Glycosylation119N-linked (GlcNAc...) asparagine
Disulfide bond191↔195
Glycosylation229N-linked (GlcNAc...) asparagine
Glycosylation343N-linked (GlcNAc...) asparagine
ChainPRO_0000011065380-568Glutathione hydrolase 1 light chain
Glycosylation427N-linked (GlcNAc...) asparagine
Glycosylation510N-linked (GlcNAc...) asparagine

Post-translational modification

N-glycosylated on both chains; contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans.
O-glycosylated; close to the membrane anchor on the heavy chain and on the light chain. The sugar moieties are localized to the stretch Thr-28 to Ser-30. Contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans.
Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme.

Keywords

PTM databases

Expression

Tissue specificity

Detected in adult kidney and mammary gland, and in fetal liver.

Interaction

Subunit

Heterodimer composed of the light and heavy chains. The active site is located in the light chain.

Protein-protein interaction databases

Chemistry

Structure

Family & Domains

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    568
  • Mass (Da)
    61,610
  • Last updated
    2007-05-01 v4
  • Checksum
    24DC62A1DEEEA38C
MKNRFLVLGLVAVVLVFVIIGLCIWLPTTSGKPDHVYSRAAVATDAKRCSEIGRDMLQEGGSVVDAAIASLLCMGLINAHSMGIGGGLFFTIYNSTTRKAEVINAREMAPRLANTSMFNNSKDSEEGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARHGFPVGKGLARALDKKRDIIEKTPALCEVFCRQGKVLQEGETVTMPKLADTLQILAQEGARAFYNGSLTAQIVKDIQEAGGIMTVEDLNNYRAEVIEHPMSIGLGDSTLYVPSAPLSGPVLILILNILKGYNFSPKSVATPEQKALTYHRIVEAFRFAYAKRTMLGDPKFVDVSQVIRNMSSEFYATQLRARITDETTHPTAYYEPEFYLPDDGGTAHLSVVSEDGSAVAATSTINLYFGSKVLSRVSGILFNDEMDDFSSPNFTNQFGVAPSPANFIKPGKQPLSSMCPSIIVDKDGKVRMVVGASGGTQITTSVALAIINSLWFGYDVKRAVEEPRLHNQLLPNTTTVEKNIDQVVTAGLKTRHHHTEVTPDFIAVVQAVVRTSGGWAAASDSRKGGEPAGY

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
M0R8W8M0R8W8_RATGgt1447

Sequence caution

The sequence CAA27224.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict9in Ref. 7; AAA41217
Sequence conflict39in Ref. 2; AAA57295/AAB59698
Sequence conflict111in Ref. 2; AAB59698
Sequence conflict370in Ref. 2; AAA57295/AAB59698 and 8; CAA27224
Sequence conflict397in Ref. 8; CAA27224
Sequence conflict416in Ref. 8; CAA27224
Sequence conflict444in Ref. 2; AAA57295/AAB59698

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X15443
EMBL· GenBank· DDBJ
CAA33483.1
EMBL· GenBank· DDBJ
mRNA
M33821
EMBL· GenBank· DDBJ
AAA57295.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
M33822
EMBL· GenBank· DDBJ
AAB59698.1
EMBL· GenBank· DDBJ
mRNA
BC078768
EMBL· GenBank· DDBJ
AAH78768.1
EMBL· GenBank· DDBJ
mRNA
L29167
EMBL· GenBank· DDBJ
AAA41218.1
EMBL· GenBank· DDBJ
mRNA
M57672
EMBL· GenBank· DDBJ
AAA41217.1
EMBL· GenBank· DDBJ
Genomic DNA
X03518
EMBL· GenBank· DDBJ
CAA27224.1
EMBL· GenBank· DDBJ
mRNA Frameshift

Genome annotation databases

Similar Proteins

Disclaimer

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