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Glutathione hydrolase 1 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (GGT 1) (EC 2.3.2.2) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) (CD antigen CD224) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain]

 GGT1_RAT                Reviewed;         568 AA.
P07314; Q63217; Q63218; Q6AZ32;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 4.
22-NOV-2017, entry version 145.
RecName: Full=Glutathione hydrolase 1 proenzyme;
EC=3.4.19.13 {ECO:0000269|PubMed:6122208};
AltName: Full=Gamma-glutamyltransferase 1;
AltName: Full=Gamma-glutamyltranspeptidase 1;
Short=GGT 1;
EC=2.3.2.2 {ECO:0000269|PubMed:6122208};
AltName: Full=Leukotriene-C4 hydrolase;
EC=3.4.19.14 {ECO:0000269|PubMed:6122208};
AltName: CD_antigen=CD224;
Contains:
RecName: Full=Glutathione hydrolase 1 heavy chain;
Contains:
RecName: Full=Glutathione hydrolase 1 light chain;
Flags: Precursor;
Name=Ggt1; Synonyms=Ggt;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2567622; DOI=10.1016/0304-3835(89)90217-6;
Griffiths S.A., Manson M.M.;
"Rat liver gamma glutamyl transpeptidase mRNA differs in the 5'
untranslated sequence from the corresponding kidney mRNA.";
Cancer Lett. 46:69-74(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 31-43 AND 380-388.
TISSUE=Kidney;
PubMed=2869484; DOI=10.1073/pnas.83.4.937;
Laperche Y., Bulle F., Aissani T., Chobert M.-N., Aggerbeck M.,
Hanoune J., Guellaen G.;
"Molecular cloning and nucleotide sequence of rat kidney gamma-
glutamyl transpeptidase cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 83:937-941(1986).
[3]
ERRATUM, AND SEQUENCE REVISION TO 66-135.
Laperche Y., Bulle F., Aissani T., Chobert M.-N., Aggerbeck M.,
Hanoune J., Guellaen G.;
Proc. Natl. Acad. Sci. U.S.A. 86:3159-3159(1989).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 1-21.
PubMed=6136502;
Matsuda Y., Tsuji A., Katunuma N.;
"Studies on the structure of gamma-glutamyltranspeptidase. III.
Evidence that the amino terminus of the heavy subunit is the membrane
binding segment.";
J. Biochem. 93:1427-1433(1983).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-18.
STRAIN=Wistar; TISSUE=Liver;
PubMed=7910821;
Brouillet A., Darbouy M., Okamoto T., Chobert M.-N., Lahuna O.,
Garlatti M., Goodspeed D.C., Laperche Y.;
"Functional characterization of the rat gamma-glutamyl transpeptidase
promoter that is expressed and regulated in the liver and hepatoma
cells.";
J. Biol. Chem. 269:14878-14884(1994).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
TISSUE=Kidney;
PubMed=1671556; DOI=10.1021/bi00220a025;
Kurauchi O., Lahuna O., Darbouy M., Aggerbeck M., Chobert M.-N.,
Laperche Y.;
"Organization of the 5' end of the rat gamma-glutamyl transpeptidase
gene: structure of a promoter active in the kidney.";
Biochemistry 30:1618-1623(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-568.
TISSUE=Kidney;
PubMed=2869471; DOI=10.1093/nar/14.3.1393;
Coloma J., Pitot H.C.;
"Characterization and sequence of a cDNA clone of gamma-
glutamyltranspeptidase.";
Nucleic Acids Res. 14:1393-1403(1986).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 64-136.
PubMed=2907498; DOI=10.1016/0378-1119(88)90307-1;
Sakamuro D., Yamazoe M., Matsuda Y., Kangawa K., Taniguchi N.,
Matsuo H., Yoshikawa H., Ogasawara N.;
"The primary structure of human gamma-glutamyl transpeptidase.";
Gene 73:1-9(1988).
[10]
PROTEIN SEQUENCE OF 30-47 AND 380-402.
TISSUE=Kidney;
PubMed=2896486; DOI=10.1016/0003-9861(88)90390-6;
Tate S.S., Khadse V., Wellner D.;
"Renal gamma-glutamyl transpeptidases: structural and immunological
studies.";
Arch. Biochem. Biophys. 262:397-408(1988).
[11]
CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Kidney;
PubMed=6122208; DOI=10.1073/pnas.79.4.1088;
Anderson M.E., Allison R.D., Meister A.;
"Interconversion of leukotrienes catalyzed by purified gamma-glutamyl
transpeptidase: concomitant formation of leukotriene D4 and gamma-
glutamyl amino acids.";
Proc. Natl. Acad. Sci. U.S.A. 79:1088-1091(1982).
[12]
GENE ORGANIZATION, AND ALTERNATIVE PROMOTER USAGE.
PubMed=10392451; DOI=10.1016/S0305-0491(99)00013-9;
Chikhi N., Holic N., Guellaen G., Laperche Y.;
"Gamma-glutamyl transpeptidase gene organization and expression: a
comparative analysis in rat, mouse, pig and human species.";
Comp. Biochem. Physiol. 122B:367-380(1999).
[13]
GLYCOSYLATION, AND SIALIC ACID CONTENT.
PubMed=8776; DOI=10.1073/pnas.73.8.2599;
Tate S.S., Meister A.;
"Subunit structure and isozymic forms of gamma-glutamyl
transpeptidase.";
Proc. Natl. Acad. Sci. U.S.A. 73:2599-2603(1976).
[14]
GLYCOSYLATION.
PubMed=6142889;
Nash B., Tate S.S.;
"In vitro translation and processing of rat kidney gamma-glutamyl
transpeptidase.";
J. Biol. Chem. 259:678-685(1984).
[15]
GLYCOSYLATION.
PubMed=2573604;
Blochberger T.C., Sabatine J.M., Lee Y.C., Hughey R.P.;
"O-linked glycosylation of rat renal gamma-glutamyltranspeptidase
adjacent to its membrane anchor domain.";
J. Biol. Chem. 264:20718-20722(1989).
-!- FUNCTION: Cleaves the gamma-glutamyl bond of extracellular
glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other
gamma-glutamyl compounds. The metabolism of glutathione releases
free glutamate and the dipeptide cysteinyl-glycine, which is
hydrolyzed to cysteine and glycine by dipeptidases. In the
presence of high concentrations of dipeptides and some amino
acids, can also catalyze a transpeptidation reaction, transferring
the gamma-glutamyl moiety to an acceptor amino acid to form a new
gamma-glutamyl compound. Initiates extracellular glutathione (GSH)
breakdown, provides cells with a local cysteine supply and
contributes to maintain intracellular GSH level. It is part of the
cell antioxidant defense mechanism.
{ECO:0000250|UniProtKB:P19440}.
-!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a
peptide + a 5-L-glutamyl amino acid. {ECO:0000269|PubMed:6122208}.
-!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L-
glutamate. {ECO:0000269|PubMed:6122208}.
-!- CATALYTIC ACTIVITY: Leukotriene C(4) + H(2)O = leukotriene D(4) +
L-glutamate. {ECO:0000269|PubMed:6122208}.
-!- ENZYME REGULATION: Activated by autocatalytic cleavage.
{ECO:0000250|UniProtKB:P19440}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=5.9 uM for leukotriene C(4) {ECO:0000269|PubMed:6122208};
KM=5.7 uM for glutathione {ECO:0000269|PubMed:6122208};
KM=5.8 uM for gamma-glutamyl-p-anilide
{ECO:0000269|PubMed:6122208};
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- SUBUNIT: Heterodimer composed of the light and heavy chains. The
active site is located in the light chain.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P19440}.
-!- TISSUE SPECIFICITY: Detected in adult kidney and mammary gland,
and in fetal liver.
-!- PTM: N-glycosylated on both chains; contains sialic acid residues.
It is not known if the sialic acid residues are present on N-
linked or on O-linked glycans. {ECO:0000269|PubMed:6142889}.
-!- PTM: O-glycosylated; close to the membrane anchor on the heavy
chain and on the light chain. The sugar moieties are localized to
the stretch Thr-28 to Ser-30. Contains sialic acid residues. It is
not known if the sialic acid residues are present on N-linked or
on O-linked glycans. {ECO:0000269|PubMed:2573604}.
-!- PTM: Cleaved by autocatalysis into a large and a small subunit and
the autocatalytic cleavage is essential to the functional
activation of the enzyme. {ECO:0000250|UniProtKB:P19440}.
-!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA27224.1; Type=Frameshift; Positions=66, 134; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X15443; CAA33483.1; -; mRNA.
EMBL; M33821; AAA57295.1; ALT_SEQ; mRNA.
EMBL; M33822; AAB59698.1; -; mRNA.
EMBL; BC078768; AAH78768.1; -; mRNA.
EMBL; L29167; AAA41218.1; -; mRNA.
EMBL; M57672; AAA41217.1; -; Genomic_DNA.
EMBL; X03518; CAA27224.1; ALT_FRAME; mRNA.
PIR; A05225; A05225.
RefSeq; NP_446292.2; NM_053840.2.
UniGene; Rn.10010; -.
ProteinModelPortal; P07314; -.
SMR; P07314; -.
BindingDB; P07314; -.
ChEMBL; CHEMBL2943; -.
iPTMnet; P07314; -.
PhosphoSitePlus; P07314; -.
UniCarbKB; P07314; -.
PRIDE; P07314; -.
GeneID; 116568; -.
KEGG; rno:116568; -.
CTD; 2678; -.
RGD; 2683; Ggt1.
HOVERGEN; HBG005835; -.
InParanoid; P07314; -.
KO; K18592; -.
PhylomeDB; P07314; -.
BRENDA; 2.3.2.2; 5301.
UniPathway; UPA00204; -.
PRO; PR:P07314; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0031982; C:vesicle; ISO:RGD.
GO; GO:0036374; F:glutathione hydrolase activity; ISS:UniProtKB.
GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
GO; GO:0002951; F:leukotriene-C(4) hydrolase; ISO:RGD.
GO; GO:0000048; F:peptidyltransferase activity; ISO:RGD.
GO; GO:0016755; F:transferase activity, transferring amino-acyl groups; IDA:RGD.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006520; P:cellular amino acid metabolic process; ISO:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
GO; GO:0019344; P:cysteine biosynthetic process; ISO:RGD.
GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
GO; GO:0006750; P:glutathione biosynthetic process; ISO:RGD.
GO; GO:0006751; P:glutathione catabolic process; ISS:UniProtKB.
GO; GO:1901750; P:leukotriene D4 biosynthetic process; ISO:RGD.
GO; GO:0031179; P:peptide modification; IDA:RGD.
GO; GO:0006508; P:proteolysis; ISO:RGD.
GO; GO:0002682; P:regulation of immune system process; ISO:RGD.
GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IEP:RGD.
GO; GO:0007283; P:spermatogenesis; ISO:RGD.
GO; GO:0031638; P:zymogen activation; 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.
1: Evidence at protein level;
Acyltransferase; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glutathione biosynthesis;
Glycoprotein; Hydrolase; Membrane; Protease; Reference proteome;
Sialic acid; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix; Zymogen.
CHAIN 1 379 Glutathione hydrolase 1 heavy chain.
/FTId=PRO_0000011064.
CHAIN 380 568 Glutathione hydrolase 1 light chain.
/FTId=PRO_0000011065.
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 380 380 Nucleophile. {ECO:0000250}.
BINDING 106 106 Glutamate. {ECO:0000250}.
BINDING 398 398 Glutamate. {ECO:0000250}.
BINDING 419 419 Glutamate. {ECO:0000250}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 114 114 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 119 119 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 343 343 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 427 427 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 510 510 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 49 73 {ECO:0000250}.
DISULFID 191 195 {ECO:0000250}.
CONFLICT 9 9 G -> A (in Ref. 7; AAA41217).
{ECO:0000305}.
CONFLICT 39 39 R -> K (in Ref. 2; AAA57295/AAB59698).
{ECO:0000305}.
CONFLICT 111 111 R -> K (in Ref. 2; AAB59698).
{ECO:0000305}.
CONFLICT 370 370 P -> A (in Ref. 2; AAA57295/AAB59698 and
8; CAA27224). {ECO:0000305}.
CONFLICT 397 397 S -> M (in Ref. 8; CAA27224).
{ECO:0000305}.
CONFLICT 416 416 F -> V (in Ref. 8; CAA27224).
{ECO:0000305}.
CONFLICT 444 444 P -> L (in Ref. 2; AAA57295/AAB59698).
{ECO:0000305}.
SEQUENCE 568 AA; 61610 MW; 24DC62A1DEEEA38C CRC64;
MKNRFLVLGL VAVVLVFVII GLCIWLPTTS GKPDHVYSRA AVATDAKRCS EIGRDMLQEG
GSVVDAAIAS LLCMGLINAH SMGIGGGLFF TIYNSTTRKA EVINAREMAP RLANTSMFNN
SKDSEEGGLS VAVPGEIRGY ELAHQRHGRL PWARLFQPSI QLARHGFPVG KGLARALDKK
RDIIEKTPAL CEVFCRQGKV LQEGETVTMP KLADTLQILA QEGARAFYNG SLTAQIVKDI
QEAGGIMTVE DLNNYRAEVI EHPMSIGLGD STLYVPSAPL SGPVLILILN ILKGYNFSPK
SVATPEQKAL TYHRIVEAFR FAYAKRTMLG DPKFVDVSQV IRNMSSEFYA TQLRARITDE
TTHPTAYYEP EFYLPDDGGT AHLSVVSEDG SAVAATSTIN LYFGSKVLSR VSGILFNDEM
DDFSSPNFTN QFGVAPSPAN FIKPGKQPLS SMCPSIIVDK DGKVRMVVGA SGGTQITTSV
ALAIINSLWF GYDVKRAVEE PRLHNQLLPN TTTVEKNIDQ VVTAGLKTRH HHTEVTPDFI
AVVQAVVRTS GGWAAASDSR KGGEPAGY


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