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Glutathione hydrolase 5 proenzyme (EC 3.4.19.13) (Gamma-glutamyl leukotrienase) (GGL) (Gamma-glutamyltransferase 5) (GGT 5) (EC 2.3.2.2) (Gamma-glutamyltransferase-like activity 1) (Gamma-glutamyltranspeptidase 5) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) [Cleaved into: Glutathione hydrolase 5 heavy chain; Glutathione hydrolase 5 light chain]

 GGT5_MOUSE              Reviewed;         573 AA.
Q9Z2A9; Q8C7B4;
29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
18-SEP-2013, sequence version 2.
28-FEB-2018, entry version 136.
RecName: Full=Glutathione hydrolase 5 proenzyme;
EC=3.4.19.13;
AltName: Full=Gamma-glutamyl leukotrienase;
Short=GGL;
AltName: Full=Gamma-glutamyltransferase 5;
Short=GGT 5;
EC=2.3.2.2;
AltName: Full=Gamma-glutamyltransferase-like activity 1;
AltName: Full=Gamma-glutamyltranspeptidase 5;
AltName: Full=Leukotriene-C4 hydrolase;
EC=3.4.19.14;
Contains:
RecName: Full=Glutathione hydrolase 5 heavy chain;
Contains:
RecName: Full=Glutathione hydrolase 5 light chain;
Flags: Precursor;
Name=Ggt5; Synonyms=Ggtla1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6 X 129; TISSUE=Spleen;
PubMed=9774450; DOI=10.1074/jbc.273.43.28277;
Carter B.Z., Shi Z.-Z., Barrios R., Lieberman M.W.;
"Gamma-glutamyl leukotrienase, a gamma-glutamyl transpeptidase gene
family member, is expressed primarily in spleen.";
J. Biol. Chem. 273:28277-28285(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Heart;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Heart, Kidney, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione
conjugates, but maybe not glutathione itself. Converts leukotriene
C4 (LTC4) to leukotriene D4 (LTD4).
-!- 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.
-!- CATALYTIC ACTIVITY: Leukotriene C(4) + H(2)O = leukotriene D(4) +
L-glutamate.
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis.
-!- SUBUNIT: Heterodimer composed of the light and heavy chains. The
active site is located in the light chain (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Z2A9-1; Sequence=Displayed;
Name=2;
IsoId=Q9Z2A9-2; Sequence=VSP_008147, VSP_008148;
Note=Very low expression.;
-!- TISSUE SPECIFICITY: Very low level of expression. Detected in
spleen lymphocytes, medullary and paracortical thymic lymphocytes,
lung interstitial cells, bronchial epithelium, proximal tubules in
kidney, crypt cells in small intestine, neurons in brain stem and
cerebral cortex and in Purkinje cells.
-!- PTM: Cleaved by autocatalysis into a large and a small subunit.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF077765; AAC71001.1; -; mRNA.
EMBL; AK052183; BAC34873.1; -; mRNA.
EMBL; AK170326; BAE41720.1; -; mRNA.
EMBL; AC087540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466553; EDL31901.1; -; Genomic_DNA.
EMBL; BC113775; AAI13776.1; -; mRNA.
CCDS; CCDS23928.1; -. [Q9Z2A9-1]
RefSeq; NP_035950.2; NM_011820.4. [Q9Z2A9-1]
UniGene; Mm.257927; -.
ProteinModelPortal; Q9Z2A9; -.
SMR; Q9Z2A9; -.
STRING; 10090.ENSMUSP00000072074; -.
MEROPS; T03.002; -.
iPTMnet; Q9Z2A9; -.
PhosphoSitePlus; Q9Z2A9; -.
SwissPalm; Q9Z2A9; -.
PaxDb; Q9Z2A9; -.
PeptideAtlas; Q9Z2A9; -.
PRIDE; Q9Z2A9; -.
Ensembl; ENSMUST00000072217; ENSMUSP00000072074; ENSMUSG00000006344. [Q9Z2A9-1]
GeneID; 23887; -.
KEGG; mmu:23887; -.
UCSC; uc007fqq.1; mouse. [Q9Z2A9-1]
CTD; 2687; -.
MGI; MGI:1346063; Ggt5.
eggNOG; KOG2410; Eukaryota.
eggNOG; COG0405; LUCA.
GeneTree; ENSGT00550000074591; -.
HOGENOM; HOG000175620; -.
HOVERGEN; HBG005835; -.
InParanoid; Q9Z2A9; -.
KO; K18592; -.
OMA; NNGIMWF; -.
OrthoDB; EOG091G03Y3; -.
TreeFam; TF313608; -.
BRENDA; 3.4.19.14; 3474.
Reactome; R-MMU-174403; Glutathione synthesis and recycling.
Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-MMU-5423646; Aflatoxin activation and detoxification.
SABIO-RK; Q9Z2A9; -.
UniPathway; UPA00204; -.
UniPathway; UPA00880; -.
PRO; PR:Q9Z2A9; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000006344; -.
CleanEx; MM_GGT5; -.
ExpressionAtlas; Q9Z2A9; baseline and differential.
Genevisible; Q9Z2A9; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0036374; F:glutathione hydrolase activity; ISO:MGI.
GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0002951; F:leukotriene-C(4) hydrolase; ISO:MGI.
GO; GO:0000048; F:peptidyltransferase activity; ISO:MGI.
GO; GO:0006520; P:cellular amino acid metabolic process; ISO:MGI.
GO; GO:0006631; P:fatty acid metabolic process; ISO:MGI.
GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006751; P:glutathione catabolic process; ISO:MGI.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:1901750; P:leukotriene D4 biosynthetic process; IDA:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
InterPro; IPR000101; GGT_peptidase.
InterPro; IPR029055; Ntn_hydrolases_N.
PANTHER; PTHR11686; PTHR11686; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome;
Glutathione biosynthesis; Glycoprotein; Hydrolase;
Leukotriene biosynthesis; Membrane; Protease; Reference proteome;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix;
Zymogen.
CHAIN 1 388 Glutathione hydrolase 5 heavy chain.
{ECO:0000250}.
/FTId=PRO_0000011074.
CHAIN 389 573 Glutathione hydrolase 5 light chain.
{ECO:0000250}.
/FTId=PRO_0000011075.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 573 Extracellular. {ECO:0000255}.
REGION 454 455 Glutamate binding. {ECO:0000250}.
ACT_SITE 389 389 Nucleophile. {ECO:0000250}.
BINDING 110 110 Glutamate. {ECO:0000250}.
BINDING 407 407 Glutamate. {ECO:0000250}.
BINDING 428 428 Glutamate. {ECO:0000250}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 185 185 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 447 456 VPGERPPSSM -> DYHEQAVAWL (in isoform 2).
{ECO:0000303|PubMed:9774450}.
/FTId=VSP_008147.
VAR_SEQ 457 573 Missing (in isoform 2).
{ECO:0000303|PubMed:9774450}.
/FTId=VSP_008148.
CONFLICT 479 479 L -> P (in Ref. 1; AAC71001).
{ECO:0000305}.
SEQUENCE 573 AA; 61674 MW; CB00F377DA1BE83E CRC64;
MAWGHRATVC LVLLGVGLGL VIVVLAAVLS PRQASCGPGA FTRAAVAADS KICSDIGRAI
LQQRGSPVDA AIAALVCTGV VNPQSMGLGG GVVFTIYNAS TGKVEIINAR ETVPASYDQG
LLNQCKNVLP LGTGAQWIGV PGELRGYAEA HRRHGRLPWA QLFQPTIALL REGFRVPFIL
SQFLNNSILR PHLSASTLRQ LFFNGTETLR SQDPFPWPAL ANTLETVAKE GAEVLYTGRL
GRMLVEDIAK QGSLLTVQDL AAFQPEVVEP LEMPLGNYTL YSPPPPAGGA ILSFILNVLK
GFNFSAETVA RPGGEVNMYH HLVETLKFAV GQRWRLWDPS SHPGIQNISR DLLREDLAQR
IRQQIDGRGD HHQLSHYNLT GVRGNRMGTS HVSVLGEDGS AVAATSTINT PFGAMVYSPR
TGILLNNELL DLCWRHMPTS PITPPPVPGE RPPSSMVPSI LVNKGQGSKL VIGGAGGELI
ISAVAQTIMN KLWLGFDLTE AIASPILHVN SKGHVEYEPK FNQEVQKGLQ DRGQIQSQSQ
RPVFLNAVQA VFQEGPCVYA ASDLRKAGKA SGY


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