GGT1
entrez
2678
canonical
uniprot
P19440
canonical
ensembl
ENSG00000100031
resolver
ensp
ENSP00000383231
resolver
ensp
ENSP00000383232
resolver
ensp
ENSP00000620747
resolver
genesymbol
GGT1
resolver
genesymbol_syn
GGT
resolver
hgnc
HGNC:4250
resolver
uniprot
A0A140VJJ9
resolver
uniprot
Q08247
resolver
uniprot
Q14404
resolver
uniprot
Q8TBS1
resolver
uniprot
Q9UMK1
resolver
uniprot_entry
A0A140VJJ9_HUMAN
resolver
uniprot_entry
GGT1_HUMAN
resolver
uniprot_sec
Q08247
resolver
uniprot_sec
Q14404
resolver
uniprot_sec
Q8TBS1
resolver
uniprot_sec
Q9UMK1
resolver
activity_regulation
ACTIVITY REGULATION: Activated by autocatalytic cleavage (PubMed:23682772). Inhibited by serine-borate (PubMed:21447318). {ECO:0000269|PubMed:21447318, ECO:0000269|PubMed:23682772}.
uniprot
proteins
amino_acid_sequence
MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY
uniprot
proteins
disease_involvement
DISEASE: Glutathionuria (GLUTH) [MIM:231950]: A very rare, autosomal recessive metabolic disorder characterized by the presence of glutathione in the urine, due to generalized gamma-glutamyl transpeptidase deficiency. Most patients manifest mild to moderate intellectual disability, and behavioral disturbance. Seizures, tremor, marfanoid features and strabismus are observed in some patients. {ECO:0000269|PubMed:29483667}. Note=The disease is caused by variants affecting the gene represented in this entry. A large homozygous deletion that removes several exons of all isoforms of GGT1 has been found in one family affected by glutathionuria. {ECO:0000269|PubMed:29483667}.
uniprot
proteins
ec_number
2.3.2.2
uniprot
proteins
ec_number
3.4.19.13
uniprot
proteins
ec_number
3.4.19.14
uniprot
proteins
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) (PubMed:17924658, PubMed:21447318, PubMed:27791009). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases (PubMed:27791009). 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:17924658, PubMed:21447318, PubMed:7673200, PubMed:7759490, PubMed:8095045, PubMed:8827453). Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4. {ECO:0000269|PubMed:17924658, ECO:0000269|PubMed:20622017, ECO:0000269|PubMed:21447318, ECO:0000269|PubMed:24047895, ECO:0000269|PubMed:27791009, ECO:0000269|PubMed:7673200, ECO:0000269|PubMed:7759490, ECO:0000269|PubMed:8095045, ECO:0000269|PubMed:8827453}.; FUNCTION: [Isoform 3]: Seems to be catalytically inactive. {ECO:0000269|PubMed:7689219}.
uniprot
proteins
mass_dalton
61410
uniprot
proteins
mutagenesis
MUTAGEN 100; /note="K->N: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 102; /note="E->Q: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 107; /note="R->K: Reduces enzyme gamma-glutamyltranspeptidase activity by 99%."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 107; /note="R->Q,H: Abolishes gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 108; /note="E->Q: Reduces gamma-glutamyltranspeptidase activity by 98%."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 112; /note="R->Q: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 139; /note="R->Q: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 147; /note="R->Q: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 150; /note="R->Q: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:8095045"; MUTAGEN 192; /note="C->W: Loss of autocatalytic cleavage, cell membrane localization and decrease in gamma-glutamyltranspeptidase activity; when associated with Y-193."; /evidence="ECO:0000269|PubMed:23682772"; MUTAGEN 193; /note="E->Y: Loss of autocatalytic cleavage, cell membrane localization and decrease in gamma-glutamyltranspeptidase activity; when associated with W-192."; /evidence="ECO:0000269|PubMed:23682772"; MUTAGEN 383; /note="H->A: Reduces gamma-glutamyltranspeptidase activity by 66%."; /evidence="ECO:0000269|PubMed:8827453"; MUTAGEN 385; /note="S->A: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:7673200"; MUTAGEN 413; /note="S->A: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:7673200"; MUTAGEN 422; /note="D->A: Reduces enzyme gamma-glutamyltranspeptidase activity by 90%."; /evidence="ECO:0000269|PubMed:7759490"; MUTAGEN 423; /note="D->A: Abolishes gamma-glutamyltranspeptidase activity. Increases KM for D-gamma-glutamyl-p-nitroanalide by over 1000-fold."; /evidence="ECO:0000269|PubMed:7759490"; MUTAGEN 425; /note="S->A: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:7673200"; MUTAGEN 451; /note="S->A: Reduces gamma-glutamyltranspeptidase activity by 99%. Abolishes activity; when associated with A-452."; /evidence="ECO:0000269|PubMed:7673200"; MUTAGEN 452; /note="S->A: Reduces gamma-glutamyltranspeptidase activity by 99%. Abolishes activity; when associated with A-451."; /evidence="ECO:0000269|PubMed:7673200"; MUTAGEN 454; /note="C->A: No effect on gamma-glutamyltranspeptidase activity."; /evidence="ECO:0000269|PubMed:7759490"; MUTAGEN 505; /note="H->A: Reduces gamma-glutamyltranspeptidase activity by 90%."; /evidence="ECO:0000269|PubMed:8827453"; MUTAGEN 545; /note="Q->K: Reduces enzyme activity by 97%."; /evidence="ECO:0000269|PubMed:24047895
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis. {ECO:0000269|PubMed:21447318}.; PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000269|PubMed:21447318}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated on both chains. Contains hexoses, hexosamines and sialic acid residues. Glycosylation profiles tested in kidney and liver tissues reveal the presence of tissue-specific and site-specific glycan composition, despite the overlap in composition among the N-glycans. A total of 36 glycan compositions, with 40 unique structures are observed. Up to 15 different glycans are observed at a single site, with site-specific variation in glycan composition. The difference in glycosylation profiles in the 2 tissues do not affect the enzyme activity. {ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:17924658, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19463, ECO:0000269|PubMed:20622017, ECO:0000269|PubMed:23682772, ECO:0000269|PubMed:24047895, ECO:0000269|PubMed:2900635}.; PTM: Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme. {ECO:0000269|PubMed:23682772}.
uniprot
proteins
protein_family
Gamma-glutamyltransferase family
uniprot
proteins
pubmed
10392451
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
1378736
uniprot
proteins
pubmed
15084671
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17924658
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19463
uniprot
proteins
pubmed
1968061
uniprot
proteins
pubmed
20622017
uniprot
proteins
pubmed
21447318
uniprot
proteins
pubmed
23682772
uniprot
proteins
pubmed
24047895
uniprot
proteins
pubmed
2563599
uniprot
proteins
pubmed
2568315
uniprot
proteins
pubmed
26013825
uniprot
proteins
pubmed
27791009
uniprot
proteins
pubmed
2896486
uniprot
proteins
pubmed
2900635
uniprot
proteins
pubmed
2904146
uniprot
proteins
pubmed
2907498
uniprot
proteins
pubmed
29483667
uniprot
proteins
pubmed
7673200
uniprot
proteins
pubmed
7689219
uniprot
proteins
pubmed
7759490
uniprot
proteins
pubmed
8095045
uniprot
proteins
pubmed
8827453
uniprot
proteins
pubmed
9738450
uniprot
proteins
sequence_length
569
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23682772, ECO:0000269|PubMed:8095045}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
uniprot
proteins
transmembrane_region
TRANSMEM 5..26; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000250|UniProtKB:P07314
uniprot
proteins