GGT6_MOUSE
ID GGT6_MOUSE Reviewed; 497 AA.
AC Q6PDE7; Q5F245; Q9D347;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Glutathione hydrolase 6 {ECO:0000305};
DE EC=3.4.19.13 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltransferase 6;
DE Short=GGT 6;
DE EC=2.3.2.2 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltranspeptidase 6;
DE Contains:
DE RecName: Full=Glutathione hydrolase 6 heavy chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase 6 light chain;
DE Flags: Precursor;
GN Name=Ggt6 {ECO:0000312|MGI:MGI:1918772};
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Colon;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon;
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PDE7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PDE7-2; Sequence=VSP_030452;
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=BAB31233.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB31233.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK018485; BAB31233.1; ALT_SEQ; mRNA.
DR EMBL; AL662812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058747; AAH58747.1; -; mRNA.
DR CCDS; CCDS36216.1; -. [Q6PDE7-1]
DR RefSeq; NP_082095.2; NM_027819.2. [Q6PDE7-1]
DR RefSeq; XP_006534305.1; XM_006534242.3.
DR AlphaFoldDB; Q6PDE7; -.
DR SMR; Q6PDE7; -.
DR STRING; 10090.ENSMUSP00000075773; -.
DR MEROPS; T03.022; -.
DR GlyGen; Q6PDE7; 4 sites.
DR iPTMnet; Q6PDE7; -.
DR PhosphoSitePlus; Q6PDE7; -.
DR MaxQB; Q6PDE7; -.
DR PaxDb; Q6PDE7; -.
DR PeptideAtlas; Q6PDE7; -.
DR PRIDE; Q6PDE7; -.
DR ProteomicsDB; 266805; -. [Q6PDE7-1]
DR ProteomicsDB; 266806; -. [Q6PDE7-2]
DR Antibodypedia; 11242; 129 antibodies from 15 providers.
DR DNASU; 71522; -.
DR Ensembl; ENSMUST00000076443; ENSMUSP00000075773; ENSMUSG00000040471. [Q6PDE7-1]
DR Ensembl; ENSMUST00000100903; ENSMUSP00000098463; ENSMUSG00000040471. [Q6PDE7-2]
DR GeneID; 71522; -.
DR KEGG; mmu:71522; -.
DR UCSC; uc007jyw.1; mouse. [Q6PDE7-1]
DR CTD; 124975; -.
DR MGI; MGI:1918772; Ggt6.
DR VEuPathDB; HostDB:ENSMUSG00000040471; -.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000161883; -.
DR HOGENOM; CLU_049993_0_0_1; -.
DR InParanoid; Q6PDE7; -.
DR OMA; FWALFHN; -.
DR OrthoDB; 1209764at2759; -.
DR PhylomeDB; Q6PDE7; -.
DR TreeFam; TF338758; -.
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; Q6PDE7; -.
DR UniPathway; UPA00204; -.
DR BioGRID-ORCS; 71522; 4 hits in 73 CRISPR screens.
DR PRO; PR:Q6PDE7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PDE7; protein.
DR Bgee; ENSMUSG00000040471; Expressed in lip and 54 other tissues.
DR ExpressionAtlas; Q6PDE7; baseline and differential.
DR Genevisible; Q6PDE7; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Glutathione biosynthesis;
KW Glycoprotein; Hydrolase; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..?
FT /note="Glutathione hydrolase 6 heavy chain"
FT /id="PRO_0000314956"
FT CHAIN ?..497
FT /note="Glutathione hydrolase 6 light chain"
FT /id="PRO_0000314957"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P07314"
FT TRANSMEM 52..72
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..497
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P07314"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 117..154
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_030452"
FT CONFLICT 304
FT /note="E -> K (in Ref. 1; BAB31233)"
FT /evidence="ECO:0000305"
FT CONFLICT 315..319
FT /note="VLFTT -> GLLTN (in Ref. 1; BAB31233)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="V -> G (in Ref. 1; BAB31233)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="S -> F (in Ref. 1; BAB31233)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="R -> G (in Ref. 1; BAB31233)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="S -> F (in Ref. 1; BAB31233)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 51467 MW; 2E9C8CCD73F8AD42 CRC64;
MDATTGPVHY HKLQLWEPGV ESEEEEEEEE EEIAEPLVLS LRRLQNTPRN EVGGLPGAWA
RLLAGLLLLA VSSSLALRQL HSRDSPRGNL GSVAPPASRH SHRPGVYHHS AIISPAATCS
QLGQELLVAG GNVVDAGVGA ALCLAVVHPH ATGLGATFWG LFYNSSSGNS TALTAGPTQL
LAPGLGLPTG LPALHLLHAH FGRLPWPHLL TKPAMLAEKG FEVDAPLANA LAIQGTKGLC
PLFCHTNGTP LGLGARATNP NLAAVLRSAA LASSPDLAGK ALLNPLVRDL GLELPSAQPV
PSLEPALQLL LPRGVLFTTP GPSAGPELVE LLESTLHSRT PSSAPCPPFL QTAETPVSSA
LATVDSNGSM LLLISSINSS FGSGHLSPST GVLLSNLEAS PAPSAWACPL ILRDNLDDTE
ADMLGMVASG ISRGAKAMTC TLLNHLATPQ IPQQPQHQRP TESPGICGQG ALLQAVVHAE
HAHVSSVPSG CCPFQGY
