Reviewed,
UniProtKB/Swiss-Prot A6NGU5 (GGT3_HUMAN)
Last modified
November 3, 2009.
Version 22.
History...
Clusters with 100%,
90%,
50% identity |
 Documents (3) |
 Third-party data |
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Names and origin
| Protein names | Recommended name: Putative gamma-glutamyltranspeptidase 3 EC=2.3.2.2 Alternative name(s): Gamma-glutamyltransferase 3 Cleaved into the following 2 chains: 1- Recommended name: Putative gamma-glutamyltranspeptidase 3 heavy chain 2- Recommended name: Putative gamma-glutamyltranspeptidase 3 light chain | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Complete proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 568 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Uncertain. |
General annotation (Comments)
| Function | Initiates extracellular glutathione (GSH) breakdown; catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors By similarity. |
| Catalytic activity | (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid. |
| Pathway | |
| Subcellular location | Membrane; Single-pass type II membrane protein By similarity. |
| 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. |
| Sequence similarities | Belongs to the gamma-glutamyltransferase family. |
| Caution | Could be the product of a pseudogene. According to Ref.3, it is not functional. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glutathione biosynthesis |
| Cellular component | Membrane |
| Domain | Signal-anchor Transmembrane |
| Molecular function | Acyltransferase Transferase |
| PTM | Glycoprotein Zymogen |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glutathione biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW gamma-glutamyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 380 | 380 | Putative gamma-glutamyltranspeptidase 3 heavy chain By similarity | PRO_0000334690 | |||||
| Chain | 381 – 568 | 188 | Putative gamma-glutamyltranspeptidase 3 light chain By similarity | PRO_0000334691 | |||||
Regions | |||||||||
| Topological domain | 1 – 4 | 4 | Cytoplasmic Potential | ||||||
| Transmembrane | 5 – 26 | 22 | Signal-anchor for type II membrane protein Probable | ||||||
| Topological domain | 27 – 568 | 542 | Extracellular Potential | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 95 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 120 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 230 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 266 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 297 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 344 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 510 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The DNA sequence of human chromosome 22." 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.  Wright H.Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [2] | "Assessment of copper status in epileptic patients treated with anticonvulsant drugs by measuring the specific oxidase activity of ceruloplasmin." Tutor-Crespo M.J., Hermida J., Tutor J.C. Epilepsy Res. 56:147-153(2003) [PubMed: 14642999] [Abstract] Cited for: INVOLVEMENT IN EPILEPSY. |
| [3] | "The human gamma-glutamyltransferase gene family." Heisterkamp N., Groffen J., Warburton D., Sneddon T.P. Hum. Genet. 123:321-332(2008) [PubMed: 18357469] [Abstract] Cited for: IDENTIFICATION, NOMENCLATURE. |
Cross-references
Entry information
| Entry name | GGT3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: A6NGU5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 22 Human chromosome 22: entries, gene names and cross-references to MIM |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
