Reviewed,
UniProtKB/Swiss-Prot Q99MZ4 (GGT7_RAT)
Last modified
February 9, 2010.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Gamma-glutamyltransferase 7 Short name=GGT 7 EC=2.3.2.2 Alternative name(s): Gamma-glutamyltranspeptidase 7 Gamma-glutamyltransferase-like 3 Cleaved into the following 2 chains: 1- Recommended name: Gamma-glutamyltransferase 7 heavy chain 2- Recommended name: Gamma-glutamyltransferase 7 light chain | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 662 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Cleaves glutathione conjugates By similarity. |
| Catalytic activity | (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid. |
| Pathway | |
| Subunit structure | Heterodimer composed of the light and heavy chains. The active site is located in the light chain. Interacts with FAM57A By similarity. |
| Subcellular location | Membrane; Single-pass type II membrane protein By similarity. |
| Sequence similarities | Belongs to the gamma-glutamyltransferase family. |
| Caution | The N-terminus was extended based on the genomic sequence, in analogy to ortholog sequences. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glutathione biosynthesis |
| Cellular component | Membrane |
| Domain | Signal-anchor Transmembrane |
| Molecular function | Acyltransferase Transferase |
| PTM | Glycoprotein Phosphoprotein Zymogen |
| 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 – 472 | 472 | Gamma-glutamyltransferase 7 heavy chain By similarity | PRO_0000011070 | |||||
| Chain | 473 – 662 | 190 | Gamma-glutamyltransferase 7 light chain By similarity | PRO_0000011071 | |||||
Regions | |||||||||
| Topological domain | 1 – 106 | 106 | Cytoplasmic Potential | ||||||
| Transmembrane | 107 – 127 | 21 | Signal-anchor for type II membrane protein Potential | ||||||
| Topological domain | 128 – 662 | 535 | Extracellular Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 72 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 83 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 198 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 267 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 283 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 330 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 353 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 394 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 519 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 523 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 586 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Rattus norvegicus gamma-glutamyltranspeptidase homolog mRNA complete code." Yamaguchi T., Araki K., Nawa H. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-662. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF244973 mRNA. Translation: AAK27971.1. Different initiation. |
| IPI | IPI00325117. |
| PIR | JC7331. |
| RefSeq | NP_569107.2. |
| UniGene | Rn.15462 |
3D structure databases | |
| SMR | Q99MZ4. Positions 134-461. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q99MZ4. |
Protein family/group databases | |
| MEROPS | T03.017. |
PTM databases | |
| PhosphoSite | Q99MZ4. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000025315; ENSRNOP00000025315; ENSRNOG00000018441; Rattus norvegicus. [Genome view] |
| GeneID | 156275. |
| KEGG | rno:156275. |
| UCSC | NM_130423. rat. |
Organism-specific databases | |
| CTD | 156275. |
| RGD | 619870. Ggt7. |
Phylogenomic databases | |
| HOVERGEN | Q99MZ4. |
| InParanoid | Q99MZ4. |
| OMA | THDLARA. |
| OrthoDB | EOG9D55HK. |
| PhylomeDB | Q99MZ4. |
Enzyme and pathway databases | |
| BRENDA | 2.3.2.2. 248. |
Gene expression databases | |
| ArrayExpress | Q99MZ4. |
| Genevestigator | Q99MZ4. |
| GermOnline | ENSRNOG00000018441. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR000101. GGT_peptidase. [Graphical view] |
| PANTHER | PTHR11686. GGT_peptidase. 1 hit. |
| Pfam | PF01019. G_glu_transpept. 1 hit. [Graphical view] |
| PRINTS | PR01210. GGTRANSPTASE. |
| PROSITE | PS00462. G_GLU_TRANSPEPTIDASE. False negative. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 620939. |
Entry information
| Entry name | GGT7_RAT | ||||||||
| Accession | Primary (citable) accession number: Q99MZ4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


