Q0V8L2 (GGT7_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 42.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Gamma-glutamyltransferase 7 Short name=GGT 7 EC=2.3.2.2 Alternative name(s): Gamma-glutamyltransferase-like 3 Gamma-glutamyltranspeptidase 7 Cleaved into the following 2 chains: | ||||
| Gene names |
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| Organism | Bos taurus (Bovine) | ||||
| Taxonomic identifier | 9913 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
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. Glutathione + H2O = L-cysteinylglycine + L-glutamate. |
| Pathway | |
| Subunit structure | Heterodimer composed of the light and heavy chains. The active site is located in the light chain By similarity. |
| Subcellular location | Membrane; Single-pass type II membrane protein By similarity. |
| Sequence similarities | Belongs to the gamma-glutamyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glutathione biosynthesis |
| Cellular component | Membrane |
| Domain | Signal-anchor Transmembrane Transmembrane helix |
| Molecular function | Acyltransferase Transferase |
| PTM | Glycoprotein Phosphoprotein Zymogen |
| Technical term | Complete proteome Reference 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-KW |
| Molecular function | gamma-glutamyltransferase activity Inferred 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_0000260258 | |||||
| Chain | 473 – 662 | 190 | Gamma-glutamyltransferase 7 light chain By similarity | PRO_0000260259 | |||||
Regions | |||||||||
| Topological domain | 1 – 106 | 106 | Cytoplasmic Potential | ||||||
| Transmembrane | 107 – 127 | 21 | Helical; 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 | 452 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 519 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 586 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [2] | NIH - Mammalian Gene Collection (MGC) project Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Basal ganglia. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BT026206 mRNA. Translation: ABG67045.1. BC150107 mRNA. Translation: AAI50108.1. |
| IPI | IPI00724222. |
| RefSeq | NP_001069869.1. NM_001076401.1. |
| UniGene | Bt.26555. |
3D structure databases | |
| ProteinModelPortal | Q0V8L2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0V8L2. |
Protein family/group databases | |
| MEROPS | T03.017. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000017688; ENSBTAP00000017688; ENSBTAG00000013301. |
| GeneID | 615929. |
| KEGG | bta:615929. |
Organism-specific databases | |
| CTD | 2686. |
Phylogenomic databases | |
| HOVERGEN | HBG039468. |
| InParanoid | Q0V8L2. |
| OMA | VTHDLAR. |
| OrthoDB | EOG483D48. |
| PhylomeDB | Q0V8L2. |
Family and domain databases | |
| InterPro | IPR000101. GGT_peptidase. [Graphical view] |
| KO | K00681. |
| 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... |
Entry information
| Entry name | GGT7_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q0V8L2 Secondary accession number(s): A6QR42 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with