ID G1SH53_RABIT Unreviewed; 662 AA.
AC G1SH53;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:ENSOCUP00000001945.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001945.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000001945.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000001945.2,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000001945.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001945.2};
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|ARBA:ARBA00033643};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC Evidence={ECO:0000256|ARBA:ARBA00033643};
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|ARBA:ARBA00033701};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC Evidence={ECO:0000256|ARBA:ARBA00033701};
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 EMBL; AAGW02060181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002710839.1; XM_002710793.3.
DR AlphaFoldDB; G1SH53; -.
DR SMR; G1SH53; -.
DR STRING; 9986.ENSOCUP00000001945; -.
DR MEROPS; T03.017; -.
DR PaxDb; 9986-ENSOCUP00000001945; -.
DR Ensembl; ENSOCUT00000002254.4; ENSOCUP00000001945.2; ENSOCUG00000002250.4.
DR GeneID; 100346442; -.
DR KEGG; ocu:100346442; -.
DR CTD; 2686; -.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000156917; -.
DR HOGENOM; CLU_014813_4_1_1; -.
DR InParanoid; G1SH53; -.
DR OMA; ICGMGPP; -.
DR OrthoDB; 2910309at2759; -.
DR TreeFam; TF333329; -.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000001811; Chromosome 4.
DR Bgee; ENSOCUG00000002250; Expressed in brain and 17 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU368068};
KW Glutathione biosynthesis {ECO:0000256|ARBA:ARBA00022684};
KW Hydrolase {ECO:0000256|RuleBase:RU368068};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
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; 70360 MW; 29C7489B015F2717 CRC64;
MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS
FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG
VTVALVMQIY FGDPQIFQQG AVVTDAARCT SLGIEVLSKQ GSSVDAAVAA ALCLGIVAPH
SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREEALQR SWETKPGLLV GVPGMVKGLH
EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLARALAEQV PPNASERFLE MFLPSGHPPL
PGALLRRPDL AEVLDALGAS GPAAFYAGGN LTLEMVAEAQ HAGGVIMEED FSNYSALVEK
PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVP REQALHWVAE TLKIALALAS
RLGDPVYDST ITESMDDMLS KLEATYLRGH INDSQAAPAP LLPVYELDGA PTAAQVLVMG
PDDFIVAMVS SLNRPFGSGL ITPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL
SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL
QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNNFLIGVKD PRSPDAAGAT
LL
//
