Q9ESH6 (GLRX1_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 78.
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: Glutaredoxin-1 Alternative name(s): Thioltransferase-1 Short name=TTase-1 | ||||
| Gene names |
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| 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 | 107 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 | Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. |
| Subcellular location | |
| Sequence similarities | Belongs to the glutaredoxin family. Contains 1 glutaredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Electron transport Transport |
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| PTM | Acetylation Disulfide bond |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chainInferred from electronic annotation. Source: UniProtKB-KW transportInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activityInferred from electronic annotation. Source: InterPro |
| 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 – 107 | 106 | Glutaredoxin-1 | PRO_0000141604 | |||||||
Regions | |||||||||||
| Domain | 3 – 106 | 104 | Glutaredoxin | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||||
| Disulfide bond | 23 ↔ 26 | Redox-active By similarity | |||||||||
| Disulfide bond | 79 ↔ 83 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 9 | 1 | K → R in AAK07419. Ref.2 | ||||||||
Sequences
References
| « Hide 'large scale' references | |
| [1] | "Cloning of rat glutaredoxin." Miranda-Vizuete A. Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "Cloning and expression of glutaredoxin cDNA gene from PC12 cell line in E.coli." Liu C.Z., Xie Z.H., He Y.H., Wang A.M., Ma C. Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pituitary. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF167981 mRNA. Translation: AAF89637.3. AF319950 mRNA. Translation: AAK07419.1. BC061555 mRNA. Translation: AAH61555.1. |
| IPI | IPI00231191. |
| RefSeq | NP_071614.1. NM_022278.1. |
| UniGene | Rn.1484. |
3D structure databases | |
| ProteinModelPortal | Q9ESH6. |
| SMR | Q9ESH6. Positions 2-106. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q9ESH6. |
Proteomic databases | |
| PRIDE | Q9ESH6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000016372; ENSRNOP00000016372; ENSRNOG00000012183. |
| GeneID | 64045. |
| KEGG | rno:64045. |
| UCSC | NM_022278. rat. |
Organism-specific databases | |
| CTD | 64045. |
| RGD | 70951. Glrx1. |
Phylogenomic databases | |
| eggNOG | roNOG16576. |
| GeneTree | ENSGT00390000003677. |
| HOVERGEN | HBG000283. |
| InParanoid | Q9ESH6. |
| OMA | TNAIQDY. |
| OrthoDB | EOG4N8R6D. |
| PhylomeDB | Q9ESH6. |
Gene expression databases | |
| ArrayExpress | Q9ESH6. |
| Genevestigator | Q9ESH6. |
| GermOnline | ENSRNOG00000012183. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR011767. GLR_AS. IPR002109. Glutaredoxin. IPR011899. Glutaredoxin_euk/vir. IPR014025. Glutaredoxin_subgr. IPR012336. Thioredoxin-like_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| KO | K03676. |
| Pfam | PF00462. Glutaredoxin. 1 hit. [Graphical view] |
| PRINTS | PR00160. GLUTAREDOXIN. |
| SUPFAM | SSF52833. Thiordxn-like_fd. 1 hit. |
| TIGRFAMs | TIGR02180. GRX_euk. 1 hit. |
| PROSITE | PS00195. GLUTAREDOXIN_1. 1 hit. PS51354. GLUTAREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 612705. |
Entry information
| Entry name | GLRX1_RAT | ||||||||
| Accession | Primary (citable) accession number: Q9ESH6 Secondary accession number(s): Q99PB7 | ||||||||
| 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