P46409 (GSTMU_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 82.
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: Glutathione S-transferase Mu 1 EC=2.5.1.18 Alternative name(s): GST Mu I GST class-mu |
| Organism | Oryctolagus cuniculus (Rabbit) [Reference proteome] |
| Taxonomic identifier | 9986 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus![]() |
Protein attributes
| Sequence length | 218 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. |
| Catalytic activity | RX + glutathione = HX + R-S-glutathione. |
| Subunit structure | Homodimer. |
| Subcellular location | |
| Tissue specificity | Well expressed in rabbit liver, brain and kidney. |
| Sequence similarities | Belongs to the GST superfamily. Mu family. Contains 1 GST C-terminal domain. Contains 1 GST N-terminal domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Molecular function | Transferase |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | glutathione transferase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 218 | 217 | Glutathione S-transferase Mu 1 | PRO_0000185837 | |||||
Regions | |||||||||
| Domain | 2 – 88 | 87 | GST N-terminal | ||||||
| Domain | 90 – 208 | 119 | GST C-terminal | ||||||
| Region | 7 – 8 | 2 | Glutathione binding By similarity | ||||||
| Region | 46 – 50 | 5 | Glutathione binding By similarity | ||||||
| Region | 59 – 60 | 2 | Glutathione binding By similarity | ||||||
| Region | 72 – 73 | 2 | Glutathione binding By similarity | ||||||
Sites | |||||||||
| Binding site | 116 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Cloning and expression of a cDNA for mu-class glutathione S-transferase from rabbit liver." Lee S.H., Lee S.H., Han J.S., Kim Y.S., Koh J.K. Arch. Biochem. Biophys. 318:424-429(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Purification and characterization of class mu glutathione S-transferase isozymes from rabbit hepatic tissue." Primiano T., Novak R.F. Arch. Biochem. Biophys. 301:404-410(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L23766 mRNA. Translation: AAA69665.1. |
| PIR | S65674. |
| RefSeq | NP_001075721.1. NM_001082252.1. |
| UniGene | Ocu.2029. |
3D structure databases | |
| ProteinModelPortal | P46409. |
| SMR | P46409. Positions 1-215. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 9986.ENSOCUP00000021965. |
Proteomic databases | |
| PRIDE | P46409. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100009073. |
Organism-specific databases | |
| CTD | 2946. |
Phylogenomic databases | |
| eggNOG | NOG300089. |
| HOGENOM | HOG000115735. |
| HOVERGEN | HBG106842. |
| OrthoDB | EOG47D9H2. |
Family and domain databases | |
| Gene3D | 1.20.1050.10. 1 hit. 3.40.30.10. 1 hit. |
| InterPro | IPR010987. Glutathione-S-Trfase_C-like. IPR004045. Glutathione_S-Trfase_N. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR003081. GST_mu. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Pfam | PF00043. GST_C. 1 hit. PF02798. GST_N. 1 hit. [Graphical view] |
| PRINTS | PR01267. GSTRNSFRASEM. |
| SUPFAM | SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit. |
| PROSITE | PS50405. GST_CTER. 1 hit. PS50404. GST_NTER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSTMU_RABIT | ||||||||
| Accession | Primary (citable) accession number: P46409 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
