ID F1S4Y1_PIG Unreviewed; 662 AA.
AC F1S4Y1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Glutathione hydrolase {ECO:0000256|RuleBase:RU368068};
DE EC=2.3.2.2 {ECO:0000256|RuleBase:RU368068};
DE EC=3.4.19.13 {ECO:0000256|RuleBase:RU368068};
DE AltName: Full=Gamma-glutamyltransferase {ECO:0000256|RuleBase:RU368068};
DE AltName: Full=Gamma-glutamyltranspeptidase {ECO:0000256|RuleBase:RU368068};
GN Name=GGT7 {ECO:0000313|Ensembl:ENSSSCP00000007757.2,
GN ECO:0000313|VGNC:VGNC:96321};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000007757.2, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000007757.2, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000007757.2,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000007757.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and
CC glutathione conjugates. {ECO:0000256|RuleBase:RU368068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione + H2O = an S-substituted L-
CC cysteinylglycine + L-glutamate; Xref=Rhea:RHEA:59468,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:29985, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:143103; EC=3.4.19.13;
CC Evidence={ECO:0000256|RuleBase:RU368068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] =
CC 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide];
CC Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795,
CC ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599,
CC ChEBI:CHEBI:78608; EC=2.3.2.2;
CC Evidence={ECO:0000256|RuleBase:RU368068};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + H2O = L-cysteinylglycine + L-glutamate;
CC Xref=Rhea:RHEA:28807, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:61694; EC=3.4.19.13;
CC Evidence={ECO:0000256|RuleBase:RU368068};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000256|ARBA:ARBA00005115, ECO:0000256|RuleBase:RU368068}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU368068}; Single-
CC pass type II membrane protein {ECO:0000256|RuleBase:RU368068}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000256|ARBA:ARBA00009381}.
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DR RefSeq; XP_003134453.3; XM_003134405.5.
DR AlphaFoldDB; F1S4Y1; -.
DR SMR; F1S4Y1; -.
DR STRING; 9823.ENSSSCP00000007757; -.
DR MEROPS; T03.017; -.
DR PaxDb; 9823-ENSSSCP00000007757; -.
DR PeptideAtlas; F1S4Y1; -.
DR Ensembl; ENSSSCT00000007970.5; ENSSSCP00000007757.2; ENSSSCG00000007285.5.
DR GeneID; 100519401; -.
DR KEGG; ssc:100519401; -.
DR CTD; 2686; -.
DR VGNC; VGNC:96321; GGT7.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000156917; -.
DR HOGENOM; CLU_014813_4_1_1; -.
DR InParanoid; F1S4Y1; -.
DR OMA; ICGMGPP; -.
DR OrthoDB; 2910309at2759; -.
DR TreeFam; TF333329; -.
DR Reactome; R-SSC-174403; Glutathione synthesis and recycling.
DR Reactome; R-SSC-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-SSC-9753281; Paracetamol ADME.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Bgee; ENSSSCG00000007285; Expressed in prefrontal cortex and 44 other cell types or tissues.
DR ExpressionAtlas; F1S4Y1; baseline and differential.
DR Genevisible; F1S4Y1; SS.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0036374; F:glutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR GO; GO:1902883; P:negative regulation of response to oxidative stress; IEA:Ensembl.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR000101; GGT_peptidase.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR PANTHER; PTHR11686; GAMMA GLUTAMYL TRANSPEPTIDASE; 1.
DR PANTHER; PTHR11686:SF9; GLUTATHIONE HYDROLASE 7; 1.
DR Pfam; PF01019; G_glu_transpept; 1.
DR PRINTS; PR01210; GGTRANSPTASE.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 1: Evidence at protein level;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU368068}; Hydrolase {ECO:0000256|RuleBase:RU368068};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1S4Y1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368068}.
FT REGION 26..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 70513 MW; AAEB47A189D6218A CRC64;
MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAVP LRGRKDEDAF LGDPDTDPDS
FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAASEC SCRQDGLTVI VTACLTFATG
VTVALIMQIY FGDPQIFHQG AVVTDAAHCT SLGIEVLSKQ GSSVDAAVAA ALCLGIVAPH
SSGLGGGGVM LVHDIRRNES RLIDFRESAP GALREEALQR SWETKPGLLV GVPGMVKGLH
EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLAQALAEQL PPNASEHFRE TFLPLGHVPL
PGSLLRRPDL AAVLDVLGTS GPAAFYAGGN LTLEMVAEAQ HAGGVITEED FSNYSALVEN
PVYGVYRGHL VLSPPAPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS
RLGDPVYDST ITESMDDMLS KVEAAYFRGQ INDSQTTTAP LLPIYELNGA PTAAQVLIMG
PDDFIVAMVS SLNRPFGSGL ITPSGILLNS QMLDFSWPNR TANHPAPSLE NSVQPGKRPL
SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL
QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNNFIIGVKD PRSPDAAGAT
IL
//
