GGT3_HUMAN
ID GGT3_HUMAN Reviewed; 568 AA.
AC A6NGU5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Putative glutathione hydrolase 3 proenzyme {ECO:0000305};
DE EC=3.4.19.13 {ECO:0000250|UniProtKB:P19440};
DE AltName: Full=Gamma-glutamyltransferase 3;
DE AltName: Full=Putative gamma-glutamyltranspeptidase 3;
DE Short=GGT 3;
DE EC=2.3.2.2 {ECO:0000250|UniProtKB:P19440};
DE Contains:
DE RecName: Full=Putative glutathione hydrolase 3 heavy chain;
DE Contains:
DE RecName: Full=Putative glutathione hydrolase 3 light chain;
DE Flags: Precursor;
GN Name=GGT3P {ECO:0000312|HGNC:HGNC:4252}; Synonyms=GGT3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=18357469; DOI=10.1007/s00439-008-0487-7;
RA Heisterkamp N., Groffen J., Warburton D., Sneddon T.P.;
RT "The human gamma-glutamyltransferase gene family.";
RL Hum. Genet. 123:321-332(2008).
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 -!- 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 -!- 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 -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {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.
CC {ECO:0000250|UniProtKB:P19440}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; AC008132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A6NGU5; -.
DR SMR; A6NGU5; -.
DR IntAct; A6NGU5; 2.
DR GlyConnect; 1694; 4 N-Linked glycans (2 sites).
DR GlyGen; A6NGU5; 7 sites, 4 N-linked glycans (2 sites).
DR BioMuta; HGNC:4252; -.
DR jPOST; A6NGU5; -.
DR MassIVE; A6NGU5; -.
DR MaxQB; A6NGU5; -.
DR PeptideAtlas; A6NGU5; -.
DR PRIDE; A6NGU5; -.
DR GeneCards; GGT3P; -.
DR HGNC; HGNC:4252; GGT3P.
DR neXtProt; NX_A6NGU5; -.
DR InParanoid; A6NGU5; -.
DR PathwayCommons; A6NGU5; -.
DR Reactome; R-HSA-174403; Glutathione synthesis and recycling.
DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR UniPathway; UPA00204; -.
DR ChiTaRS; GGT3P; human.
DR Pharos; A6NGU5; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A6NGU5; protein.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:1901750; P:leukotriene D4 biosynthetic process; ISS:UniProtKB.
DR GO; GO:0031179; P:peptide modification; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0002682; P:regulation of immune system process; IBA:GO_Central.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
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.
DR TIGRFAMs; TIGR00066; g_glut_trans; 1.
DR PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 5: Uncertain;
KW Acyltransferase; Glutathione biosynthesis; Glycoprotein; Hydrolase;
KW Membrane; Protease; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..380
FT /note="Putative glutathione hydrolase 3 heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000334690"
FT CHAIN 381..568
FT /note="Putative glutathione hydrolase 3 light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000334691"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 5..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000305"
FT TOPO_DOM 27..568
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 381
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 399
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 450..451
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 568 AA; 61502 MW; 48BF7C2A2DFEF165 CRC64;
MKKKLVVLGL LAVVLVLVIV GLCLWLPSAS KEPDNHVYTR AAVAADAKQC LEIGRDTLRD
GGSAVDAAIA ALLCVGLMNA HSMGIGVGLF LTIYNSTTRK AEVINAREVA PRLAFASMFN
SSEQSQKGGL SVAVPGEIRG YELAHQRHGR LPWARLFQPS IQLARQGFPV GKGLAAVLEN
KRTVIEQQPV LCEVFCRDRK VLREGERLTL PRLADTYEML AIEGAQAFYN GSLMAQIVKD
IQAAGGIVTA EDLNNYCAEL IEHPLNISLG DAVLYMPSAR LSGPVLALIL NILKGYNFSR
ESVETPEQKG LTYHRIVEAF RFAYAKRTLL GDPKFVDVTE VVRNMTSEFF AAQLRSQISD
HTTHPISYYK PEFYTPDDGG TAHLSVVAED GSAVSATSTI NLYFGSKVCS PVSGILFNNM
DDFSSPSITN EFGAPPSPAN FIQPGKQPLL SMCPTIMVGQ DGQVRMVVGA AGGTQITTDT
ALAIIYNLWF GYDVKRAVEE PRLHNKLLPN VTTVERNIDQ AVTAALETRH HHTQIASTFI
AVVQAIVRTA GGWAAASDSR KGGEPAGY
