GGT7_RAT
ID GGT7_RAT Reviewed; 662 AA.
AC Q99MZ4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Glutathione hydrolase 7 {ECO:0000305};
DE EC=3.4.19.13 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltransferase 7;
DE Short=GGT 7;
DE EC=2.3.2.2 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltransferase-like 3;
DE AltName: Full=Gamma-glutamyltranspeptidase 7;
DE Contains:
DE RecName: Full=Glutathione hydrolase 7 heavy chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase 7 light chain;
DE Flags: Precursor;
GN Name=Ggt7 {ECO:0000312|RGD:619870}; Synonyms=Ggtl3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-662.
RA Yamaguchi T., Araki K., Nawa H.;
RT "Rattus norvegicus gamma-glutamyltranspeptidase homolog mRNA complete
RT code.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-79 AND SER-83, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-523 AND ASN-586, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Hydrolyzes and transfers gamma-glutamyl moieties from
CC glutathione and other gamma-glutamyl compounds to acceptors.
CC {ECO:0000250|UniProtKB:P19440}.
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:0000250|UniProtKB:P19440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905;
CC Evidence={ECO:0000250|UniProtKB:P19440};
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:0000250|UniProtKB:P19440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC Evidence={ECO:0000250|UniProtKB:P19440};
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:0000250|UniProtKB:P19440};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC Evidence={ECO:0000250|UniProtKB:P19440};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000250|UniProtKB:P19440}.
CC -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The active
CC site is located in the light chain. {ECO:0000250|UniProtKB:P19440}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P19440}; Single-
CC pass type II membrane protein {ECO:0000250|UniProtKB:P07314}.
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit and the
CC autocatalytic cleavage is essential to the functional activation of the
CC enzyme. {ECO:0000250|UniProtKB:P19440}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK27971.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF244973; AAK27971.1; ALT_INIT; mRNA.
DR PIR; JC7331; JC7331.
DR RefSeq; NP_569107.2; NM_130423.2.
DR AlphaFoldDB; Q99MZ4; -.
DR SMR; Q99MZ4; -.
DR BioGRID; 250899; 1.
DR STRING; 10116.ENSRNOP00000025315; -.
DR MEROPS; T03.017; -.
DR GlyGen; Q99MZ4; 9 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; Q99MZ4; -.
DR PhosphoSitePlus; Q99MZ4; -.
DR SwissPalm; Q99MZ4; -.
DR jPOST; Q99MZ4; -.
DR PaxDb; Q99MZ4; -.
DR PRIDE; Q99MZ4; -.
DR Ensembl; ENSRNOT00000025315; ENSRNOP00000025315; ENSRNOG00000018441.
DR GeneID; 156275; -.
DR KEGG; rno:156275; -.
DR UCSC; RGD:619870; rat.
DR CTD; 2686; -.
DR RGD; 619870; Ggt7.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000156917; -.
DR HOGENOM; CLU_014813_4_1_1; -.
DR InParanoid; Q99MZ4; -.
DR OMA; FMVIGSP; -.
DR OrthoDB; 1419292at2759; -.
DR PhylomeDB; Q99MZ4; -.
DR TreeFam; TF333329; -.
DR Reactome; R-RNO-174403; Glutathione synthesis and recycling.
DR Reactome; R-RNO-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR UniPathway; UPA00204; -.
DR PRO; PR:Q99MZ4; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000018441; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; Q99MZ4; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0036374; F:glutathione hydrolase activity; IBA:GO_Central.
DR GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IBA:GO_Central.
DR GO; GO:1902883; P:negative regulation of response to oxidative stress; ISO:RGD.
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; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Glutathione biosynthesis; Glycoprotein; Hydrolase;
KW Membrane; Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..472
FT /note="Glutathione hydrolase 7 heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000011070"
FT CHAIN 473..662
FT /note="Glutathione hydrolase 7 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000011071"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P07314"
FT TRANSMEM 107..127
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..662
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P07314"
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"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ14"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
SQ SEQUENCE 662 AA; 70383 MW; FB8B7643700BB03A CRC64;
MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS
FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG
VTVALVMQIY FGDPQIFQQG AVVTDASCCT ALGMEVLSKQ GSSVDAAVAA ALCLGIVAPH
SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREEALQR SWDTKPGLLV GVPGMVKGLY
EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLAHALAEQL PPNASDRFLE TFLPLGHPPL
PGSLLRRPDL AEVLDILGIS GPAAFYNGGN LTLEMVAEVQ HAGGVMTEED FSNYSALTEK
PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS
RLGDPVYDST ISESMDDMLS KVEAANFRGH ISDSQAAPAP LLPVYELDGA PTAAQVLVMG
PDDFIVAMVS SLNRPFGSGL LTPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL
SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL
QSNVLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNNFIIGVKD PRSLDATGAS
IL
