GGT7_BOVIN
ID GGT7_BOVIN Reviewed; 662 AA.
AC Q0V8L2; A6QR42;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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:0000250|UniProtKB:Q9UJ14}; Synonyms=GGTL3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; BT026206; ABG67045.1; -; mRNA.
DR EMBL; BC150107; AAI50108.1; -; mRNA.
DR RefSeq; NP_001069869.1; NM_001076401.1.
DR AlphaFoldDB; Q0V8L2; -.
DR SMR; Q0V8L2; -.
DR STRING; 9913.ENSBTAP00000017688; -.
DR MEROPS; T03.017; -.
DR PaxDb; Q0V8L2; -.
DR PRIDE; Q0V8L2; -.
DR Ensembl; ENSBTAT00000017688; ENSBTAP00000017688; ENSBTAG00000013301.
DR GeneID; 615929; -.
DR KEGG; bta:615929; -.
DR CTD; 2686; -.
DR VEuPathDB; HostDB:ENSBTAG00000013301; -.
DR VGNC; VGNC:29346; GGT7.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000156917; -.
DR HOGENOM; CLU_014813_4_1_1; -.
DR InParanoid; Q0V8L2; -.
DR OMA; FMVIGSP; -.
DR OrthoDB; 1419292at2759; -.
DR TreeFam; TF333329; -.
DR Reactome; R-BTA-174403; Glutathione synthesis and recycling.
DR Reactome; R-BTA-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-BTA-9753281; Paracetamol ADME.
DR UniPathway; UPA00204; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000013301; Expressed in olfactory segment of nasal mucosa and 99 other tissues.
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; 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; PTHR11686; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 2: Evidence at transcript 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_0000260258"
FT CHAIN 473..662
FT /note="Glutathione hydrolase 7 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000260259"
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:0000250|UniProtKB:Q99MZ4"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ14"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JP7"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99JP7"
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 452
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 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 662 AA; 70652 MW; 730D755DDB0B8433 CRC64;
MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAVP LRGRKDEDAF LGDPDTDPDS
FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAASEC SCRQDGLTVI VTACLTFATG
VTVALIMQIY FGDPQIFHQG AVVTDAARCT SLGIEVLSKQ GSSVDAAVAA ALCLGIVAPH
SSGLGGGGVM LVHDIRRNKS HLIDFRESAP GALREEALQR SWETKPGLLV GVPGMVKGLH
EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLAQALAEQP PPNASDRFRE TFLPMGHPPL
PGSLLRRPDL AAVLEVLGTY GPAAFYAGGN LTLEMVAEAQ HAGGVITEED FSNYSALLEK
PVCGVYRGHL VLSPRPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS
RLGDPIYDST ITESMDDMLS KVEAAYFRGQ INDSQAAPVP LLPIYELNGA PTAAQVLIMG
PDDFIVAMVS SLNRPFGSGL ITPSGILLNS QMLDFSWPNR TANHPAPSLE NSVQPGKRPL
SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL
QTNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNNFIIGVKD PRSPDAAGAT
IL
