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Putative glutathione hydrolase 3 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 3) (Putative gamma-glutamyltranspeptidase 3) (GGT 3) (EC 2.3.2.2) [Cleaved into: Putative glutathione hydrolase 3 heavy chain; Putative glutathione hydrolase 3 light chain]

 GGT3_HUMAN              Reviewed;         568 AA.
A6NGU5;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 2.
27-SEP-2017, entry version 82.
RecName: Full=Putative glutathione hydrolase 3 proenzyme;
EC=3.4.19.13;
AltName: Full=Gamma-glutamyltransferase 3;
AltName: Full=Putative gamma-glutamyltranspeptidase 3;
Short=GGT 3;
EC=2.3.2.2;
Contains:
RecName: Full=Putative glutathione hydrolase 3 heavy chain;
Contains:
RecName: Full=Putative glutathione hydrolase 3 light chain;
Flags: Precursor;
Name=GGT3P; Synonyms=GGT3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[2]
INVOLVEMENT IN EPILEPSY.
PubMed=14642999; DOI=10.1016/j.eplepsyres.2003.08.008;
Tutor-Crespo M.J., Hermida J., Tutor J.C.;
"Assessment of copper status in epileptic patients treated with
anticonvulsant drugs by measuring the specific oxidase activity of
ceruloplasmin.";
Epilepsy Res. 56:147-153(2003).
[3]
IDENTIFICATION, AND NOMENCLATURE.
PubMed=18357469; DOI=10.1007/s00439-008-0487-7;
Heisterkamp N., Groffen J., Warburton D., Sneddon T.P.;
"The human gamma-glutamyltransferase gene family.";
Hum. Genet. 123:321-332(2008).
-!- FUNCTION: Initiates extracellular glutathione (GSH) breakdown;
catalyzes the transfer of the glutamyl moiety of glutathione to
amino acids and dipeptide acceptors. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a
peptide + a 5-L-glutamyl amino acid.
-!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L-
glutamate.
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
membrane protein {ECO:0000250}.
-!- PTM: Cleaved by autocatalysis into a large and a small subunit.
{ECO:0000250}.
-!- MISCELLANEOUS: In some epileptic patients treated with phenytoin,
phenobarbital and carbamazepin, GGT3 is found, as an additional
form of GGT. This group of patients has levels of ceruloplasmin
and oxidase activity that were significantly higher than in the
group of patients without GGT3. However, levels of ceruloplasmin
and oxidase activity are significantly higher in this group of
patients without GGT3 than those of the control group.
-!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
{ECO:0000305}.
-!- CAUTION: Could be the product of a pseudogene. According to
PubMed:18357469, it is not functional. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AC008132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
UniGene; Hs.595809; -.
ProteinModelPortal; A6NGU5; -.
SMR; A6NGU5; -.
EPD; A6NGU5; -.
MaxQB; A6NGU5; -.
PaxDb; A6NGU5; -.
PRIDE; A6NGU5; -.
GeneCards; GGT3P; -.
HGNC; HGNC:4252; GGT3P.
HPA; HPA045635; -.
HPA; HPA047534; -.
HPA; HPA065444; -.
neXtProt; NX_A6NGU5; -.
eggNOG; KOG2410; Eukaryota.
eggNOG; COG0405; LUCA.
HOVERGEN; HBG005835; -.
InParanoid; A6NGU5; -.
Reactome; R-HSA-174403; Glutathione synthesis and recycling.
Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
UniPathway; UPA00204; -.
Proteomes; UP000005640; Unplaced.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0036374; F:glutathione hydrolase activity; IEA:UniProtKB-EC.
GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006751; P:glutathione catabolic process; IEA:InterPro.
GO; GO:1901750; P:leukotriene D4 biosynthetic process; ISS:UniProtKB.
InterPro; IPR000101; GGT_peptidase.
InterPro; IPR029055; Ntn_hydrolases_N.
PANTHER; PTHR11686; PTHR11686; 1.
Pfam; PF01019; G_glu_transpept; 1.
PRINTS; PR01210; GGTRANSPTASE.
SUPFAM; SSF56235; SSF56235; 1.
TIGRFAMs; TIGR00066; g_glut_trans; 1.
PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
5: Uncertain;
Acyltransferase; Complete proteome; Glutathione biosynthesis;
Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix;
Zymogen.
CHAIN 1 380 Putative glutathione hydrolase 3 heavy
chain. {ECO:0000250}.
/FTId=PRO_0000334690.
CHAIN 381 568 Putative glutathione hydrolase 3 light
chain. {ECO:0000250}.
/FTId=PRO_0000334691.
TOPO_DOM 1 4 Cytoplasmic. {ECO:0000255}.
TRANSMEM 5 26 Helical; Signal-anchor for type II
membrane protein. {ECO:0000305}.
TOPO_DOM 27 568 Extracellular. {ECO:0000255}.
REGION 450 451 Glutamate binding. {ECO:0000250}.
ACT_SITE 381 381 Nucleophile. {ECO:0000250}.
BINDING 107 107 Glutamate. {ECO:0000250}.
BINDING 399 399 Glutamate. {ECO:0000250}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 344 344 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 510 510 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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


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