GGT5_HUMAN
ID GGT5_HUMAN Reviewed; 586 AA.
AC P36269; Q53XM9; Q6GMP0; Q96FC1; Q9UFM5;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Glutathione hydrolase 5 proenzyme;
DE EC=3.4.19.13 {ECO:0000269|PubMed:1676842, ECO:0000269|PubMed:21447318, ECO:0000269|PubMed:30842656};
DE AltName: Full=Gamma-glutamyl transpeptidase-related enzyme {ECO:0000303|PubMed:1676842};
DE Short=GGT-rel {ECO:0000303|PubMed:1676842};
DE AltName: Full=Gamma-glutamyltransferase 5;
DE Short=GGT 5;
DE EC=2.3.2.2 {ECO:0000269|PubMed:21447318};
DE AltName: Full=Gamma-glutamyltransferase-like activity 1 {ECO:0000303|PubMed:1676842};
DE AltName: Full=Gamma-glutamyltranspeptidase 5;
DE AltName: Full=Leukotriene-C4 hydrolase;
DE EC=3.4.19.14 {ECO:0000269|PubMed:21447318};
DE Contains:
DE RecName: Full=Glutathione hydrolase 5 heavy chain;
DE Contains:
DE RecName: Full=Glutathione hydrolase 5 light chain;
DE Flags: Precursor;
GN Name=GGT5; Synonyms=GGTLA1;
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 [MRNA] (ISOFORM 1), VARIANT ARG-330, CATALYTIC
RP ACTIVITY, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=1676842; DOI=10.1073/pnas.88.14.6303;
RA Heisterkamp N., Rajpert-De Meyts E., Uribe L., Forman H.J., Groffen J.;
RT "Identification of a human gamma-glutamyl cleaving enzyme related to, but
RT distinct from, gamma-glutamyl transpeptidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:6303-6307(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-330.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and PNS;
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 [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-550.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [10]
RP CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=21447318; DOI=10.1016/j.ab.2011.03.026;
RA Wickham S., West M.B., Cook P.F., Hanigan M.H.;
RT "Gamma-glutamyl compounds: substrate specificity of gamma-glutamyl
RT transpeptidase enzymes.";
RL Anal. Biochem. 414:208-214(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=30842656; DOI=10.1038/s41586-019-1003-z;
RA Lu E., Wolfreys F.D., Muppidi J.R., Xu Y., Cyster J.G.;
RT "S-Geranylgeranyl-L-glutathione is a ligand for human B cell-confinement
RT receptor P2RY8.";
RL Nature 567:244-248(2019).
CC -!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione and
CC glutathione-S-conjugate such as leukotriene C4 (PubMed:21447318). Does
CC not cleaves gamma-glutamyl compounds such as gamma-glutamyl leucine
CC (PubMed:21447318). May also catalyze a transpeptidation reaction in
CC addition to the hydrolysis reaction, transferring the gamma-glutamyl
CC moiety to an acceptor amino acid to form a new gamma-glutamyl compound
CC (PubMed:21447318). Acts as a negative regulator of geranylgeranyl
CC glutathione bioactivity by cleaving off its gamma-glutamyl group,
CC playing a role in adaptive immune responses (PubMed:30842656).
CC {ECO:0000269|PubMed:21447318, ECO:0000269|PubMed:30842656}.
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:0000269|PubMed:21447318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23905;
CC Evidence={ECO:0000305};
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:0000269|PubMed:1676842, ECO:0000269|PubMed:21447318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28808;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + leukotriene C4 = L-glutamate + leukotriene D4;
CC Xref=Rhea:RHEA:31563, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:63166; EC=3.4.19.14;
CC Evidence={ECO:0000269|PubMed:21447318};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31564;
CC Evidence={ECO:0000305|PubMed:21447318};
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:0000269|PubMed:21447318, ECO:0000269|PubMed:30842656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59469;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-[(2E,6E,10E)-geranylgeranyl]-L-glutathione = L-
CC glutamate + S-[(2E,6E,10E)-geranylgeranyl]-L-cysteinylglycine;
CC Xref=Rhea:RHEA:65120, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:156326, ChEBI:CHEBI:156330;
CC Evidence={ECO:0000269|PubMed:30842656};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65121;
CC Evidence={ECO:0000305|PubMed:30842656};
CC -!- ACTIVITY REGULATION: Inhibited by serine-borate.
CC {ECO:0000269|PubMed:21447318}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.5 uM for glutathione {ECO:0000269|PubMed:21447318};
CC KM=10.2 uM for leukotriene C4 {ECO:0000269|PubMed:21447318};
CC KM=18.2 uM for S-methylglutathione {ECO:0000269|PubMed:21447318};
CC KM=14.8 uM for S-(4-nitro-benzyl)glutathione
CC {ECO:0000269|PubMed:21447318};
CC KM=43 uM for oxidized glutathione {ECO:0000269|PubMed:21447318};
CC -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC {ECO:0000269|PubMed:21447318}.
CC -!- PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis.
CC {ECO:0000269|PubMed:21447318}.
CC -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The active
CC site is located in the light chain. {ECO:0000250|UniProtKB:Q9Z2A9}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z2A9}; Single-
CC pass type II membrane protein {ECO:0000250|UniProtKB:Q9Z2A9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P36269-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P36269-2; Sequence=VSP_008146;
CC Name=3;
CC IsoId=P36269-3; Sequence=VSP_043470;
CC -!- PTM: Cleaved by autocatalysis into a large and a small subunit.
CC {ECO:0000250|UniProtKB:P19440}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q9Z2A9}.
CC -!- MISCELLANEOUS: A previous study reported that GSH and oxidized
CC glutathione (GSSG) are not substrates for murine GGT5 (By similarity).
CC However, this result contrasts with two studies reported that GSH is
CC indeed a substrate for GGT5 (PubMed:21447318, PubMed:1676842).
CC {ECO:0000250|UniProtKB:Q9Z2A9, ECO:0000269|PubMed:1676842,
CC ECO:0000269|PubMed:21447318}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB55910.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M64099; AAA58503.1; -; mRNA.
DR EMBL; AL117414; CAB55910.1; ALT_FRAME; mRNA.
DR EMBL; BT009808; AAP88810.1; -; mRNA.
DR EMBL; CT841518; CAJ86448.1; -; mRNA.
DR EMBL; AK292006; BAF84695.1; -; mRNA.
DR EMBL; AP000353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471095; EAW59643.1; -; Genomic_DNA.
DR EMBL; BC011362; AAH11362.1; -; mRNA.
DR EMBL; BC073999; AAH73999.1; -; mRNA.
DR CCDS; CCDS13825.1; -. [P36269-1]
DR CCDS; CCDS42989.1; -. [P36269-2]
DR CCDS; CCDS42990.1; -. [P36269-3]
DR PIR; A41125; A41125.
DR PIR; T17220; T17220.
DR RefSeq; NP_001093251.1; NM_001099781.2. [P36269-3]
DR RefSeq; NP_001093252.1; NM_001099782.2. [P36269-2]
DR RefSeq; NP_001289393.1; NM_001302464.1.
DR RefSeq; NP_001289394.1; NM_001302465.1.
DR RefSeq; NP_004112.2; NM_004121.3. [P36269-1]
DR AlphaFoldDB; P36269; -.
DR SMR; P36269; -.
DR BioGRID; 108954; 69.
DR IntAct; P36269; 5.
DR STRING; 9606.ENSP00000381340; -.
DR SwissLipids; SLP:000001455; -.
DR MEROPS; T03.002; -.
DR GlyGen; P36269; 8 sites, 4 O-linked glycans (2 sites).
DR iPTMnet; P36269; -.
DR PhosphoSitePlus; P36269; -.
DR BioMuta; GGT5; -.
DR DMDM; 116242493; -.
DR EPD; P36269; -.
DR jPOST; P36269; -.
DR MassIVE; P36269; -.
DR MaxQB; P36269; -.
DR PaxDb; P36269; -.
DR PeptideAtlas; P36269; -.
DR PRIDE; P36269; -.
DR ProteomicsDB; 55177; -. [P36269-1]
DR ProteomicsDB; 55178; -. [P36269-2]
DR ProteomicsDB; 55179; -. [P36269-3]
DR Antibodypedia; 285; 130 antibodies from 27 providers.
DR DNASU; 2687; -.
DR Ensembl; ENST00000263112.11; ENSP00000263112.7; ENSG00000099998.19. [P36269-2]
DR Ensembl; ENST00000327365.10; ENSP00000330080.4; ENSG00000099998.19. [P36269-1]
DR Ensembl; ENST00000398292.3; ENSP00000381340.3; ENSG00000099998.19. [P36269-3]
DR GeneID; 2687; -.
DR KEGG; hsa:2687; -.
DR MANE-Select; ENST00000327365.10; ENSP00000330080.4; NM_004121.5; NP_004112.2.
DR UCSC; uc002zzo.4; human. [P36269-1]
DR CTD; 2687; -.
DR DisGeNET; 2687; -.
DR GeneCards; GGT5; -.
DR HGNC; HGNC:4260; GGT5.
DR HPA; ENSG00000099998; Low tissue specificity.
DR MIM; 137168; gene.
DR neXtProt; NX_P36269; -.
DR OpenTargets; ENSG00000099998; -.
DR PharmGKB; PA162389442; -.
DR VEuPathDB; HostDB:ENSG00000099998; -.
DR eggNOG; KOG2410; Eukaryota.
DR GeneTree; ENSGT00940000155794; -.
DR HOGENOM; CLU_014813_4_1_1; -.
DR InParanoid; P36269; -.
DR OMA; VCGMGPP; -.
DR OrthoDB; 1419292at2759; -.
DR PhylomeDB; P36269; -.
DR TreeFam; TF313608; -.
DR BioCyc; MetaCyc:HS01949-MON; -.
DR BRENDA; 2.3.2.2; 2681.
DR BRENDA; 3.4.19.13; 2681.
DR PathwayCommons; P36269; -.
DR Reactome; R-HSA-174403; Glutathione synthesis and recycling.
DR Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-HSA-9664535; LTC4-CYSLTR mediated IL4 production.
DR Reactome; R-HSA-9753281; Paracetamol ADME.
DR SignaLink; P36269; -.
DR UniPathway; UPA00204; -.
DR UniPathway; UPA00880; -.
DR BioGRID-ORCS; 2687; 20 hits in 1076 CRISPR screens.
DR ChiTaRS; GGT5; human.
DR GeneWiki; GGTLA1; -.
DR GenomeRNAi; 2687; -.
DR Pharos; P36269; Tbio.
DR PRO; PR:P36269; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P36269; protein.
DR Bgee; ENSG00000099998; Expressed in right lobe of thyroid gland and 127 other tissues.
DR ExpressionAtlas; P36269; baseline and differential.
DR Genevisible; P36269; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0036374; F:glutathione hydrolase activity; IDA:UniProtKB.
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:0002951; F:leukotriene-C(4) hydrolase; IDA:UniProtKB.
DR GO; GO:0000048; F:peptidyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:BHF-UCL.
DR GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006751; P:glutathione catabolic process; IDA:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:1901750; P:leukotriene D4 biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
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 PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Glutathione biosynthesis;
KW Glycoprotein; Hydrolase; Leukotriene biosynthesis; Membrane; Protease;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix; Zymogen.
FT CHAIN 1..387
FT /note="Glutathione hydrolase 5 heavy chain"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT /id="PRO_0000011072"
FT CHAIN 388..586
FT /note="Glutathione hydrolase 5 light chain"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT /id="PRO_0000011073"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A9"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A9"
FT TOPO_DOM 30..586
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2A9"
FT ACT_SITE 388
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 110
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 406
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 427
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT BINDING 469..470
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P19440"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 101..132
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008146"
FT VAR_SEQ 445
FT /note="P -> PA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_043470"
FT VARIANT 11
FT /note="L -> I (in dbSNP:rs5760274)"
FT /id="VAR_028006"
FT VARIANT 330
FT /note="K -> R (in dbSNP:rs2275984)"
FT /evidence="ECO:0000269|PubMed:10591208,
FT ECO:0000269|PubMed:1676842"
FT /id="VAR_028007"
FT VARIANT 332
FT /note="Q -> H (in dbSNP:rs6004105)"
FT /id="VAR_028008"
FT VARIANT 475
FT /note="I -> V (in dbSNP:rs7288201)"
FT /id="VAR_024455"
FT CONFLICT 408
FT /note="N -> Y (in Ref. 5; CAB55910)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="R -> W (in Ref. 1; AAA58503)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 586 AA; 62261 MW; EE37B3CE516F5788 CRC64;
MARGYGATVS LVLLGLGLAL AVIVLAVVLS RHQAPCGPQA FAHAAVAADS KVCSDIGRAI
LQQQGSPVDA TIAALVCTSV VNPQSMGLGG GVIFTIYNVT TGKVEVINAR ETVPASHAPS
LLDQCAQALP LGTGAQWIGV PGELRGYAEA HRRHGRLPWA QLFQPTIALL RGGHVVAPVL
SRFLHNSILR PSLQASTLRQ LFFNGTEPLR PQDPLPWPAL ATTLETVATE GVEVFYTGRL
GQMLVEDIAK EGSQLTLQDL AKFQPEVVDA LEVPLGDYTL YSPPPPAGGA ILSFILNVLR
GFNFSTESMA RPEGRVNVYH HLVETLKFAK GQRWRLGDPR SHPKLQNASR DLLGETLAQL
IRQQIDGRGD HQLSHYSLAE AWGHGTGTSH VSVLGEDGSA VAATSTINTP FGAMVYSPRT
GIILNNELLD LCERCPRGSG TTPSPVSGDR VGGAPGRCWP PVPGERSPSS MVPSILINKA
QGSKLVIGGA GGELIISAVA QAIMSKLWLG FDLRAAIAAP ILHVNSKGCV EYEPNFSQEV
QRGLQDRGQN QTQRPFFLNV VQAVSQEGAC VYAVSDLRKS GEAAGY
