ID   GGT7_HUMAN              Reviewed;         662 AA.
AC   Q9UJ14; Q8N899; Q8NF66; Q9BYP5; Q9BYP6;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   11-NOV-2015, entry version 129.
DE   RecName: Full=Gamma-glutamyltransferase 7;
DE            Short=GGT 7;
DE            EC=2.3.2.2;
DE   AltName: Full=Gamma-glutamyltransferase-like 3;
DE   AltName: Full=Gamma-glutamyltransferase-like 5;
DE   AltName: Full=Gamma-glutamyltranspeptidase 7;
DE   AltName: Full=Glutathione hydrolase 7;
DE            EC=3.4.19.13;
DE   Contains:
DE     RecName: Full=Gamma-glutamyltransferase 7 heavy chain;
DE   Contains:
DE     RecName: Full=Gamma-glutamyltransferase 7 light chain;
DE   Flags: Precursor;
GN   Name=GGT7; Synonyms=GGTL3, GGTL5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INTERACTION WITH FAM57A.
RX   PubMed=12270127; DOI=10.1016/S0006-291X(02)02227-1;
RA   He X.H., Di Y., Li J., Xie Y., Tang Y., Zhang F., Wei L., Zhang Y.,
RA   Qin W.X., Huo K., Li Y., Wan D.F., Gu J.R.;
RT   "Molecular cloning and characterization of CT120, a novel membrane-
RT   associated gene involved in amino acid transport and glutathione
RT   metabolism.";
RL   Biochem. Biophys. Res. Commun. 297:528-536(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Spleen;
RX   PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA   Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA   Ohara O.;
RT   "Characterization of long cDNA clones from human adult spleen. II. The
RT   complete sequences of 81 cDNA clones.";
RL   DNA Res. 10:49-57(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [5]
RP   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).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
CC   -!- FUNCTION: Cleaves glutathione conjugates. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a
CC       peptide + a 5-L-glutamyl amino acid.
CC   -!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L-
CC       glutamate.
CC   -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC   -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The
CC       active site is located in the light chain (By similarity). Isoform
CC       3 interacts with FAM57A. {ECO:0000250,
CC       ECO:0000269|PubMed:12270127}.
CC   -!- INTERACTION:
CC       O00155:GPR25; NbExp=3; IntAct=EBI-1058791, EBI-10178951;
CC       Q8TAF8:LHFPL5; NbExp=3; IntAct=EBI-1058791, EBI-2820517;
CC       Q13021:MALL; NbExp=3; IntAct=EBI-1058791, EBI-750078;
CC       Q9NWH2:TMEM242; NbExp=3; IntAct=EBI-1058791, EBI-10315004;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC       membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=a;
CC         IsoId=Q9UJ14-1; Sequence=Displayed;
CC         Note=Gene prediction confirmed by EST data.;
CC       Name=2;
CC         IsoId=Q9UJ14-4; Sequence=VSP_008134, VSP_008138, VSP_008139;
CC         Note=No experimental confirmation available.;
CC       Name=3; Synonyms=GGTL3B, B;
CC         IsoId=Q9UJ14-5; Sequence=VSP_008136, VSP_008137;
CC       Name=4;
CC         IsoId=Q9UJ14-6; Sequence=VSP_008133, VSP_008140, VSP_008141;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed, but at low level, except in
CC       the airway epithelial cells. Detected in brain, heart, kidney,
CC       liver, lung, spleen, testis and trachea.
CC   -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC03394.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AY138815; AAN15928.1; -; mRNA.
DR   EMBL; AK097100; BAC04950.1; -; mRNA.
DR   EMBL; AK090413; BAC03394.1; ALT_INIT; mRNA.
DR   EMBL; AL049709; CAB61787.2; -; Genomic_DNA.
DR   CCDS; CCDS13242.2; -. [Q9UJ14-1]
DR   RefSeq; NP_821158.2; NM_178026.2. [Q9UJ14-1]
DR   UniGene; Hs.433738; -.
DR   ProteinModelPortal; Q9UJ14; -.
DR   SMR; Q9UJ14; 133-655.
DR   BioGrid; 108953; 25.
DR   IntAct; Q9UJ14; 5.
DR   STRING; 9606.ENSP00000338964; -.
DR   MEROPS; T03.017; -.
DR   PhosphoSite; Q9UJ14; -.
DR   BioMuta; GGT7; -.
DR   DMDM; 152031612; -.
DR   MaxQB; Q9UJ14; -.
DR   PaxDb; Q9UJ14; -.
DR   PRIDE; Q9UJ14; -.
DR   Ensembl; ENST00000336431; ENSP00000338964; ENSG00000131067. [Q9UJ14-1]
DR   GeneID; 2686; -.
DR   KEGG; hsa:2686; -.
DR   UCSC; uc002xay.3; human. [Q9UJ14-1]
DR   UCSC; uc002xba.1; human. [Q9UJ14-5]
DR   CTD; 2686; -.
DR   GeneCards; GGT7; -.
DR   H-InvDB; HIX0203047; -.
DR   HGNC; HGNC:4259; GGT7.
DR   HPA; HPA013204; -.
DR   MIM; 612342; gene.
DR   neXtProt; NX_Q9UJ14; -.
DR   PharmGKB; PA28669; -.
DR   eggNOG; KOG2410; Eukaryota.
DR   eggNOG; COG0405; LUCA.
DR   GeneTree; ENSGT00550000074591; -.
DR   HOGENOM; HOG000231793; -.
DR   HOVERGEN; HBG039468; -.
DR   InParanoid; Q9UJ14; -.
DR   KO; K00681; -.
DR   OMA; MLVHDIR; -.
DR   OrthoDB; EOG7DNNTR; -.
DR   PhylomeDB; Q9UJ14; -.
DR   TreeFam; TF333329; -.
DR   Reactome; R-HSA-174403; Glutathione synthesis and recycling.
DR   Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR   UniPathway; UPA00204; -.
DR   ChiTaRS; GGT7; human.
DR   GeneWiki; GGTL3; -.
DR   GenomeRNAi; 2686; -.
DR   NextBio; 10602; -.
DR   PRO; PR:Q9UJ14; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   Bgee; Q9UJ14; -.
DR   CleanEx; HS_GGT7; -.
DR   ExpressionAtlas; Q9UJ14; baseline and differential.
DR   Genevisible; Q9UJ14; HS.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; TAS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003840; F:gamma-glutamyltransferase activity; TAS:UniProtKB.
DR   GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006749; P:glutathione metabolic process; TAS:UniProtKB.
DR   GO; GO:0019370; P:leukotriene biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR000101; GGT_peptidase.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   PANTHER; PTHR11686; PTHR11686; 1.
DR   Pfam; PF01019; G_glu_transpept; 1.
DR   PRINTS; PR01210; GGTRANSPTASE.
DR   SUPFAM; SSF56235; SSF56235; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Complete proteome;
KW   Glutathione biosynthesis; Glycoprotein; Hydrolase; Membrane;
KW   Phosphoprotein; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix; Zymogen.
FT   CHAIN         1    472       Gamma-glutamyltransferase 7 heavy chain.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000011066.
FT   CHAIN       473    662       Gamma-glutamyltransferase 7 light chain.
FT                                {ECO:0000250}.
FT                                /FTId=PRO_0000011067.
FT   TOPO_DOM      1    106       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    107    127       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM    128    662       Extracellular. {ECO:0000255}.
FT   MOD_RES      17     17       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q99MZ4}.
FT   MOD_RES      79     79       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q99JP7}.
FT   MOD_RES      83     83       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q99JP7}.
FT   CARBOHYD    198    198       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    267    267       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    283    283       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    353    353       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    394    394       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    452    452       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    519    519       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    523    523       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    586    586       N-linked (GlcNAc...). {ECO:0000255}.
FT   VAR_SEQ       1    283       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:12693554}.
FT                                /FTId=VSP_008133.
FT   VAR_SEQ       1     76       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_008134.
FT   VAR_SEQ     226    251       PGLLVGVPGMVKGLHEAHQLYGRLPW -> VGTLVRRESSG
FT                                ESLFIALLLTQALIC (in isoform 3).
FT                                {ECO:0000303|PubMed:12270127}.
FT                                /FTId=VSP_008136.
FT   VAR_SEQ     252    662       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:12270127}.
FT                                /FTId=VSP_008137.
FT   VAR_SEQ     273    289       ARALAEQLPPNMSERFR -> GQWGLGIWERHEVDGEG
FT                                (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_008138.
FT   VAR_SEQ     290    662       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_008139.
FT   VAR_SEQ     369    425       HLVLSPPPPHTGPALISALNILEGFNLTSLVSREQALHWVA
FT                                ETLKIALALASRLGDP -> DLSPGSQGPPSGEASQSMATS
FT                                FWPRDSSPFHRRETKAVSYLGSQLLKQTRVSPPSEK (in
FT                                isoform 4).
FT                                {ECO:0000303|PubMed:12693554}.
FT                                /FTId=VSP_008140.
FT   VAR_SEQ     426    662       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:12693554}.
FT                                /FTId=VSP_008141.
FT   CONFLICT      5      5       N -> K (in Ref. 1; AAN15928).
FT                                {ECO:0000305}.
SQ   SEQUENCE   662 AA;  70467 MW;  29DDBC719CADD195 CRC64;
     MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS
     FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG
     VTVALVMQIY FGDPQIFQQG AVVTDAARCT SLGIEVLSKQ GSSVDAAVAA ALCLGIVAPH
     SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREETLQR SWETKPGLLV GVPGMVKGLH
     EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLARALAEQL PPNMSERFRE TFLPSGRPPL
     PGSLLHRPDL AEVLDVLGTS GPAAFYAGGN LTLEMVAEAQ HAGGVITEED FSNYSALVEK
     PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS
     RLGDPVYDST ITESMDDMLS KVEAAYLRGH INDSQAAPAP LLPVYELDGA PTAAQVLIMG
     PDDFIVAMVS SLNQPFGSGL ITPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL
     SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL
     QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNNFIIAVKD PRSPDAAGAT
     IL
//