A2TIL1 (GSHR_CALJA) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 46.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutathione reductase, mitochondrial Short name=GR Short name=GRase EC=1.8.1.7 | ||
| Gene names |
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| Organism | Callithrix jacchus (White-tufted-ear marmoset) [Reference proteome] | ||
| Taxonomic identifier | 9483 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Platyrrhini › Cebidae › Callitrichinae › Callithrix |
Protein attributes
| Sequence length | 522 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 | Maintains high levels of reduced glutathione in the cytosol By similarity. |
| Catalytic activity | 2 glutathione + NADP+ = glutathione disulfide + NADPH. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer; disulfide-linked By similarity. |
| Subcellular location | Isoform Mitochondrial: Mitochondrion By similarity. Isoform Cytoplasmic: Cytoplasm By similarity. |
| Sequence similarities | Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Mitochondrion |
| Coding sequence diversity | Alternative initiation |
| Domain | Redox-active center Transit peptide |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Disulfide bond |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | NADP binding Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide bindingInferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform Mitochondrial (identifier: A2TIL1-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform Cytoplasmic (identifier: A2TIL1-2) The sequence of this isoform differs from the canonical sequence as follows: 1-43: Missing. | ||||||
| Note: Initiator Met-1 is removed. Contains a N-acetylalanine at position 2 (By similarity). |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 43 | 43 | Mitochondrion Potential | ||||||||
| Chain | 44 – 522 | 479 | Glutathione reductase, mitochondrial | PRO_0000314948 | |||||||
Regions | |||||||||||
| Nucleotide binding | 94 – 102 | 9 | FAD By similarity | ||||||||
Sites | |||||||||||
| Active site | 511 | 1 | Proton acceptor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 102 ↔ 107 | Redox-active By similarity | |||||||||
| Disulfide bond | 134 | Interchain By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 1 – 43 | 43 | Missing in isoform Cytoplasmic. | VSP_030441 | |||||||
Sequences
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References
| [1] | "Free radical scavenging enzymes in Callithrix jacchus." Atanasova S., von Ahsen N., Schlumbohm C., Wieland E., Oellerich M., Armstrong V. Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | EF203010 mRNA. Translation: ABN05297.1. |
| RefSeq | NP_001171974.1. NM_001185045.1. |
3D structure databases | |
| ProteinModelPortal | A2TIL1. |
| SMR | A2TIL1. Positions 61-522. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | A2TIL1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100393824. |
Organism-specific databases | |
| CTD | 2936. |
Phylogenomic databases | |
| HOGENOM | HOG000276712. |
| HOVERGEN | HBG004959. |
| OrthoDB | EOG42BX8H. |
Family and domain databases | |
| Gene3D | 3.30.390.30. 1 hit. |
| InterPro | IPR016156. FAD/NAD-linked_Rdtase_dimer. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glutathione_Rdtase_euk/bac. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD-bd_dom. [Graphical view] |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. |
| SUPFAM | SSF55424. FAD/NAD-linked_reductase_dimer. 1 hit. |
| TIGRFAMs | TIGR01421. gluta_reduc_1. 1 hit. |
| PROSITE | PS00076. PYRIDINE_REDOX_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSHR_CALJA | ||||||||
| Accession | Primary (citable) accession number: A2TIL1 | ||||||||
| 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 |