GGT7_MOUSE
ID GGT7_MOUSE Reviewed; 662 AA.
AC Q99JP7; A2AQN1; Q91V91;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
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|MGI:MGI:1913385}; Synonyms=Ggtl3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary cancer;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 552-662.
RC STRAIN=ILS, and ISS;
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-83, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK032051; BAC27672.1; -; mRNA.
DR EMBL; AL844852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005772; AAH05772.1; -; mRNA.
DR EMBL; AF332053; AAK56082.1; -; mRNA.
DR EMBL; AF332054; AAK56083.1; -; mRNA.
DR CCDS; CCDS16949.1; -.
DR RefSeq; NP_659035.2; NM_144786.2.
DR AlphaFoldDB; Q99JP7; -.
DR SMR; Q99JP7; -.
DR BioGRID; 228881; 1.
DR IntAct; Q99JP7; 1.
DR MINT; Q99JP7; -.
DR STRING; 10090.ENSMUSP00000029131; -.
DR MEROPS; T03.017; -.
DR GlyConnect; 2332; 13 N-Linked glycans (3 sites).
DR GlyGen; Q99JP7; 9 sites, 12 N-linked glycans (3 sites).
DR iPTMnet; Q99JP7; -.
DR PhosphoSitePlus; Q99JP7; -.
DR SwissPalm; Q99JP7; -.
DR jPOST; Q99JP7; -.
DR MaxQB; Q99JP7; -.
DR PaxDb; Q99JP7; -.
DR PeptideAtlas; Q99JP7; -.
DR PRIDE; Q99JP7; -.
DR ProteomicsDB; 267792; -.
DR Antibodypedia; 2429; 144 antibodies from 24 providers.
DR DNASU; 207182; -.
DR Ensembl; ENSMUST00000029131; ENSMUSP00000029131; ENSMUSG00000027603.
DR GeneID; 207182; -.
DR KEGG; mmu:207182; -.
DR UCSC; uc012chc.1; mouse.
DR CTD; 2686; -.
DR MGI; MGI:1913385; Ggt7.
DR VEuPathDB; HostDB:ENSMUSG00000027603; -.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000156917; -.
DR HOGENOM; CLU_014813_4_1_1; -.
DR InParanoid; Q99JP7; -.
DR OMA; FMVIGSP; -.
DR OrthoDB; 1419292at2759; -.
DR PhylomeDB; Q99JP7; -.
DR TreeFam; TF333329; -.
DR Reactome; R-MMU-174403; Glutathione synthesis and recycling.
DR Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-MMU-9753281; Paracetamol ADME.
DR SABIO-RK; Q99JP7; -.
DR UniPathway; UPA00204; -.
DR BioGRID-ORCS; 207182; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Ggt7; mouse.
DR PRO; PR:Q99JP7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99JP7; protein.
DR Bgee; ENSMUSG00000027603; Expressed in nasal cavity epithelium and 140 other tissues.
DR ExpressionAtlas; Q99JP7; baseline and differential.
DR Genevisible; Q99JP7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
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:MGI.
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_0000011068"
FT CHAIN 473..662
FT /note="Glutathione hydrolase 7 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000011069"
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:0007744|PubMed:21183079"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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:0000255"
FT CARBOHYD 586
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 148
FT /note="S -> H (in Ref. 3; AAH05772)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 70251 MW; BA7F3413D694F381 CRC64;
MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS
FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG
VTVALVMQIY FGDPQIFQQG AVVTDASSCT ALGMEVLSKQ GSSVDAAVAA ALCLGIVAPH
SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREEALQR SWDTKPGLLV GVPGMVKGLH
EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLAHALAEQL PPNASDRFLD TFLPLGHPPL
PGSLLRRPDL AEVLDILGTS GPAAFYNGGN LTLEMVAEAQ HAGGVITEED FSNYSALTEK
PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS
RLGDPVYDST ITESMDDMLS KVEAANFRGH ISDSQAAPAP LLPVYELDGA PTAAQVLVMG
PDDFIVAMVS SLNRPFGSGL LTPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL
SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL
QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNTFIIGVKD PRSPDAAGAT
IL
