Gamma-glutamyltransferase 1

GGT1
Identifiers
Aliases	GGT1, CD224, D22S672, D22S732, GGT, GGT 1, GTG, gamma-glutamyltransferase 1, GGTD
External IDs	OMIM: 612346; MGI: 95706; GeneCards: GGT1
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4GDX, 4GG2, 4Z9O, 4ZBK, 4ZC6, 4ZCG
Enzyme activity
Gene location (Human)
Chr.	Chromosome 22 (human)
End	24,629,005 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	75,586,200 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; mucosa of transverse colon; ; gallbladder; ; right lung; ; body of pancreas; ; upper lobe of left lung; ; right lobe of thyroid gland; ; human kidney; ; left lobe of thyroid gland; ; gonad;
	Top expressed in
	right kidney; ; proximal tubule; ; human kidney; ; intestinal villus; ; duodenum; ; seminal vesicula; ; epithelium of small intestine; ; jejunum; ; decidua; ; efferent ductule;
	More reference expression data
	n/a
Gene ontology
Molecular function	transferase activity; peptidase activity; protein binding; acyltransferase activity; hydrolase activity; glutathione hydrolase activity; hypoglycin A gamma-glutamyl transpeptidase activity; peptidyltransferase activity; leukotriene-C(4) hydrolase; leukotriene C4 gamma-glutamyl transferase activity;
Cellular component	integral component of membrane; membrane; plasma membrane; extracellular exosome; extracellular space;
Biological process	leukotriene metabolic process; zymogen activation; glutathione biosynthetic process; regulation of immune system process; cysteine biosynthetic process; spermatogenesis; regulation of inflammatory response; xenobiotic metabolic process; glutamate metabolic process; glutathione catabolic process; proteolysis; cellular amino acid metabolic process; glutathione metabolic process; fatty acid metabolic process; leukotriene D4 biosynthetic process; protein biosynthesis; peptide modification; response to estradiol; response to lipopolysaccharide; response to tumor necrosis factor;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	2678
	14598
	ENSG00000100031
	ENSMUSG00000006345
	P19440
	Q60928
NM_013430; NM_001032364; NM_001032365; NM_001288833; NM_005265;
	NM_013421
	NM_008116; NM_001305992
	NP_001275762; NP_038265; NP_038347
NP_001292921; NP_032142; NP_001366466; NP_001366467; NP_001366468;
	NP_001366469; NP_001366470
	Wikidata
View/Edit Human	View/Edit Mouse

Gamma-glutamyltransferase 1 (GGT1), also known as CD224 (Cluster of Differentiation 224), is a human gene.^[5]

Function

Human gamma-glutamyltransferase catalyzes the transfer of the glutamyl moiety of glutathione to a variety of amino acids and dipeptide acceptors. This heteroduplex enzyme is composed of a heavy chain and a light chain, which are derived from a single precursor protein, and is present in tissues involved in absorption and secretion. This enzyme is a member of the gamma-glutamyltransferase protein family, of which many members have not yet been fully characterized. This gene encodes several transcript variants; studies suggest that many transcripts of this gene family may be non-functional or represent pseudogenes. The functional transcripts which have been fully characterized have been grouped and classified as type I gamma-glutamyltransferase. Complex splicing events may take place in a tissue-specific manner, resulting in marked dissimilarity in the 5' UTRs. Several 5' UTR transcript variants of the type I gene have been identified in different tissues and cancer cells.^[5]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000100031 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000006345 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: GGT1 gamma-glutamyltransferase 1".

Chikhi N, Holic N, Guellaen G, Laperche Y (April 1999). "Gamma-glutamyl transpeptidase gene organization and expression: a comparative analysis in rat, mouse, pig and human species". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 122 (4): 367–80. doi:10.1016/S0305-0491(99)00013-9. PMID 10392451.
Indirani N, Hill PG (July 1977). "Partial purification and some properties of gamma-glutamyl transpeptidase from human bile". Biochimica et Biophysica Acta (BBA) - Enzymology. 483 (1): 57–62. doi:10.1016/0005-2744(77)90007-9. PMID 18198.
Tate SS, Ross ME (September 1977). "Human kidney gamma-glutamyl transpeptidase. Catalytic properties, subunit structure, and localization of the gamma-glutamyl binding site on the light subunit". The Journal of Biological Chemistry. 252 (17): 6042–5. doi:10.1016/S0021-9258(17)40026-3. PMID 19463.
Welbourne TC (1978). "Cytoplasmic gamma-glutamyltransferase: isolation, product formation and physiological role". Current Problems in Clinical Biochemistry. 8: 201–15. PMID 28899.
Courtay C, Oster T, Michelet F, Visvikis A, Diederich M, Wellman M, Siest G (June 1992). "Gamma-glutamyltransferase: nucleotide sequence of the human pancreatic cDNA. Evidence for a ubiquitous gamma-glutamyltransferase polypeptide in human tissues". Biochemical Pharmacology. 43 (12): 2527–33. doi:10.1016/0006-2952(92)90140-E. PMID 1378736.
Pawlak A, Cohen EH, Octave JN, Schweickhardt R, Wu SJ, Bulle F, Chikhi N, Baik JH, Siegrist S, Guellaën G (February 1990). "An alternatively processed mRNA specific for gamma-glutamyl transpeptidase in human tissues". The Journal of Biological Chemistry. 265 (6): 3256–62. doi:10.1016/S0021-9258(19)39761-3. PMID 1968061.
Pitot HC, Goodspeed D, Dunn T, Hendrich S, Maronpot RR, Moran S (January 1989). "Regulation of the expression of some genes for enzymes of glutathione metabolism in hepatotoxicity and hepatocarcinogenesis". Toxicology and Applied Pharmacology. 97 (1): 23–34. Bibcode:1989ToxAP..97...23P. doi:10.1016/0041-008X(89)90052-5. PMID 2563599.
Goodspeed DC, Dunn TJ, Miller CD, Pitot HC (March 1989). "Human gamma-glutamyl transpeptidase cDNA: comparison of hepatoma and kidney mRNA in the human and rat". Gene. 76 (1): 1–9. doi:10.1016/0378-1119(89)90002-4. PMID 2568315.
Pawlak A, Wu SJ, Bulle F, Suzuki A, Chikhi N, Ferry N, Baik JH, Siegrist S, Guellaën G (October 1989). "Different gamma-glutamyl transpeptidase mRNAs are expressed in human liver and kidney". Biochemical and Biophysical Research Communications. 164 (2): 912–8. Bibcode:1989BBRC..164..912P. doi:10.1016/0006-291X(89)91545-3. PMID 2573352.
Laperche Y, Bulle F, Aissani T, Chobert MN, Aggerbeck M, Hanoune J, Guellaën G (February 1986). "Molecular cloning and nucleotide sequence of rat kidney gamma-glutamyl transpeptidase cDNA". Proceedings of the National Academy of Sciences of the United States of America. 83 (4): 937–41. Bibcode:1986PNAS...83..937L. doi:10.1073/pnas.83.4.937. PMC 322985. PMID 2869484.
Bulle F, Mattei MG, Siegrist S, Pawlak A, Passage E, Chobert MN, Laperche Y, Guellaën G (July 1987). "Assignment of the human gamma-glutamyl transferase gene to the long arm of chromosome 22". Human Genetics. 76 (3): 283–6. doi:10.1007/BF00283624. PMID 2885259. S2CID 32375892.
Tate SS, Khadse V, Wellner D (May 1988). "Renal gamma-glutamyl transpeptidases: structural and immunological studies". Archives of Biochemistry and Biophysics. 262 (2): 397–408. doi:10.1016/0003-9861(88)90390-6. PMID 2896486.
Tate SS, Galbraith RA (August 1988). "In vitro translation and processing of human hepatoma cell (Hep G2) gamma-glutamyl transpeptidase". Biochemical and Biophysical Research Communications. 154 (3): 1167–73. Bibcode:1988BBRC..154.1167T. doi:10.1016/0006-291X(88)90263-X. PMID 2900635.
Rajpert-De Meyts E, Heisterkamp N, Groffen J (December 1988). "Cloning and nucleotide sequence of human gamma-glutamyl transpeptidase". Proceedings of the National Academy of Sciences of the United States of America. 85 (23): 8840–4. Bibcode:1988PNAS...85.8840R. doi:10.1073/pnas.85.23.8840. PMC 282602. PMID 2904146.
Sakamuro D, Yamazoe M, Matsuda Y, Kangawa K, Taniguchi N, Matsuo H, Yoshikawa H, Ogasawara N (December 1988). "The primary structure of human gamma-glutamyl transpeptidase". Gene. 73 (1): 1–9. doi:10.1016/0378-1119(88)90307-1. PMID 2907498.
Ikeda Y, Fujii J, Anderson ME, Taniguchi N, Meister A (September 1995). "Involvement of Ser-451 and Ser-452 in the catalysis of human gamma-glutamyl transpeptidase". The Journal of Biological Chemistry. 270 (38): 22223–8. doi:10.1074/jbc.270.38.22223. PMID 7673200.
Wetmore LA, Gerard C, Drazen JM (August 1993). "Human lung expresses unique gamma-glutamyl transpeptidase transcripts". Proceedings of the National Academy of Sciences of the United States of America. 90 (16): 7461–5. Bibcode:1993PNAS...90.7461W. doi:10.1073/pnas.90.16.7461. PMC 47161. PMID 7689219.
Ikeda Y, Fujii J, Taniguchi N, Meister A (May 1995). "Human gamma-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit". The Journal of Biological Chemistry. 270 (21): 12471–5. doi:10.1074/jbc.270.21.12471. PMID 7759490.
Courtay C, Heisterkamp N, Siest G, Groffen J (February 1994). "Expression of multiple gamma-glutamyltransferase genes in man". The Biochemical Journal. 297 (Pt 3): 503–8. doi:10.1042/bj2970503. PMC 1137862. PMID 7906515.
Ikeda Y, Fujii J, Taniguchi N (February 1993). "Significance of Arg-107 and Glu-108 in the catalytic mechanism of human gamma-glutamyl transpeptidase. Identification by site-directed mutagenesis". The Journal of Biological Chemistry. 268 (6): 3980–5. doi:10.1016/S0021-9258(18)53567-5. PMID 8095045.

External links

GGT1 +protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This membrane protein–related article is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000100031 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000006345 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] 1 2 "Entrez Gene: GGT1 gamma-glutamyltransferase 1".

[1]

[2]

[3]

[4]

[5]

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)
1–50	CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50
51–100	CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100
101–150	CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150
151–200	CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200
201–250	CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 CD248 CD249
251–300	CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299
301–350	CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350
351–371	CD351 CD352 CD353 CD354 CD355 CD357 CD358 CD360 CD361 CD362 CD363 CD364 CD365 CD366 CD367 CD368 CD369 CD370 CD371
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Gamma-glutamyltransferase 1

Function

See also

References

Further reading

External links