Reviewed,
UniProtKB/Swiss-Prot Q9CQU0 (TXD12_MOUSE)
Last modified
June 16, 2009.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Thioredoxin domain-containing protein 12 EC=1.8.4.2 Alternative name(s): Thioredoxin-like protein p19 Endoplasmic reticulum protein ERp19 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus |
Protein attributes
| Sequence length | 170 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 | Possesses significant protein thiol-disulfide oxidase activity By similarity. |
| Catalytic activity | 2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol. |
| Subcellular location | |
| Sequence similarities | Contains 1 thioredoxin domain. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Domain | Redox-active center Signal |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond Glycoprotein |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum lumenInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein-disulfide reductase (glutathione) 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | By similarity | ||||||||
| Chain | 25 – 170 | 146 | Thioredoxin domain-containing protein 12 | PRO_0000034190 | |||||||
Regions | |||||||||||
| Motif | 167 – 170 | 4 | Prevents secretion from ER Potential | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 128 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 64 ↔ 67 | Redox-active Potential | |||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins." Knoblach B., Keller B.O., Groenendyk J., Aldred S., Zheng J., Lemire B.D., Li L., Michalak M. Mol. Cell. Proteomics 2:1104-1119(2003) [PubMed: 12930873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Tissue: Embryo. |
| [2] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo and Kidney. |
| [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: Mammary gland. |
Cross-references
Sequence databases | |
|---|---|
| AY548113 mRNA. Translation: AAS55653.1. AK003481 mRNA. Translation: BAB22811.1. AK002862 mRNA. Translation: BAB22413.1. BC006857 mRNA. Translation: AAH06857.1. | |
| IPI | IPI00133110. |
| RefSeq | NP_079610.1. |
| UniGene | Mm.159965 |
3D structure databases | |
| SMR | Q9CQU0. Positions 28-161. |
| ModBase | Search... |
2-D gel databases | |
| REPRODUCTION-2DPAGE | Q9CQU0. |
Proteomic databases | |
| PRIDE | Q9CQU0. |
Genome annotation databases | |
| Ensembl | ENSMUSG00000028567. Mus musculus. [Contig view] |
| GeneID | 66073. |
| KEGG | mmu:66073. |
Organism-specific databases | |
| MGI | MGI:1913323. Txndc12. |
Phylogenomic databases | |
| HOGENOM | Q9CQU0. |
| HOVERGEN | Q9CQU0. |
| OMA | Q9CQU0. CHACKAL. |
Enzyme and pathway databases | |
| BRENDA | 1.8.4.2. 244. |
Gene expression databases | |
| ArrayExpress | Q9CQU0. |
| Bgee | Q9CQU0. |
Family and domain databases | |
| InterPro | IPR000886. ER_targeting_sequence. IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. |
| PROSITE | PS00014. ER_TARGET. 1 hit. PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 320548. |
| SOURCE | Search... |
Entry information
| Entry name | TXD12_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9CQU0 Secondary accession number(s): Q53YN1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


