Reviewed,
UniProtKB/Swiss-Prot A2TIL1 (GSHR_CALJA)
Last modified
November 25, 2008.
Version 14.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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Names and origin
| Protein names | Recommended name: Glutathione reductase, mitochondrial Short name=GRase Short name=GR EC=1.8.1.7 | ||
| Gene names |
| ||
| Organism | Callithrix jacchus (Common marmoset) | ||
| 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 | MitochondrionBy similarity. CytoplasmBy 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 Phosphoprotein |
Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro glutathione metabolic processInferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | FAD binding Inferred from electronic annotation. Source: InterPro NADP bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro glutathione-disulfide reductase activityInferred from electronic annotation. Source: InterPro |
| 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. | ||||||
| Notes: 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 | |||||||||||
| Modified residue | 65 | 1 | Phosphotyrosine By similarity | ||||||||
| 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 | |
|---|---|
| EF203010 mRNA. Translation: ABN05297.1. | |
3D structure databases | |
| SMR | A2TIL1. Positions 62-522. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | A2TIL1. |
Family and domain databases | |
| InterPro | IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR006322. Glut_reduct_1. IPR000815. Hg_reductase. IPR001100. Pyr_nuc-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR012999. Pyr_OxRdtase_I_AS. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00945. HGRDTASE. PR00411. PNDRDTASEI. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| 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 project | HPI (Human Proteome Initiative) | ||||||||

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