Reviewed,
UniProtKB/Swiss-Prot O95881 (TXD12_HUMAN)
Last modified
June 16, 2009.
Version 78.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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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 ERp18 hTLP19 | ||||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||||
| Taxonomic identifier | 9606 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 172 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 | Possesses significant protein thiol-disulfide oxidase activity. Ref.7 |
| Catalytic activity | 2 glutathione + protein-disulfide = glutathione disulfide + protein-dithiol. |
| Subcellular location | |
| Tissue specificity | Widely expressed. Ref.1 |
| Sequence similarities | Contains 1 thioredoxin domain. |
| biophysicochemical properties | Kinetic parameters: KM=25 µM for Asn-Arg-Cys-Ser-Gln-Gly-Ser-Cys-Trp-Asn pH dependence: Optimum pH is 6.5. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Domain | Redox-active center Signal |
| Molecular function | Oxidoreductase |
| PTM | Disulfide bond |
| Technical term | 3D-structure Direct protein sequencing |
| 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 – 26 | 26 | Ref.6 | ||||||||||||||||||||||||
| Chain | 27 – 172 | 146 | Thioredoxin domain-containing protein 12 | PRO_0000034189 | |||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||
| Motif | 169 – 172 | 4 | Prevents secretion from ER Potential | ||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||
| Disulfide bond | 66 ↔ 69 | Redox-active Ref.7 | |||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||
| Mutagenesis | 66 | 1 | C → S: Loss of oxidase activity. Ref.7 | ||||||||||||||||||||||||
| Mutagenesis | 69 | 1 | C → S: Loss of oxidase activity. Ref.7 | ||||||||||||||||||||||||
| Sequence conflict | 102 | 1 | D → H in AAH08913. Ref.5 | ||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||
| Helix | 43 – 53 | 11 | |||||||||||||||||||||||||
| Beta strand | 57 – 62 | 6 | |||||||||||||||||||||||||
| Helix | 67 – 77 | 11 | |||||||||||||||||||||||||
| Helix | 80 – 86 | 7 | |||||||||||||||||||||||||
| Beta strand | 89 – 95 | 7 | |||||||||||||||||||||||||
| Helix | 96 – 98 | 3 | |||||||||||||||||||||||||
| Helix | 103 – 105 | 3 | |||||||||||||||||||||||||
| Beta strand | 112 – 118 | 7 | |||||||||||||||||||||||||
| Helix | 144 – 158 | 15 | |||||||||||||||||||||||||
| Helix | 159 – 161 | 3 | |||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and characterization of a novel human thioredoxin-like gene hTLP19 encoding a secretory protein." Liu F., Rong Y.P., Zeng L.C., Zhang X., Han Z.G. Gene 315:71-78(2003) [PubMed: 14557066] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. |
| [2] | Mei G., Yu W., Gibbs R.A. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [3] | "The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. Gray A.M.Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [4] | "The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. Bentley D.R.Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "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: Colon, Kidney and Ovary. |
| [6] | "Signal peptide prediction based on analysis of experimentally verified cleavage sites." Zhang Z., Henzel W.J. Protein Sci. 13:2819-2824(2004) [PubMed: 15340161] [Abstract] Cited for: PROTEIN SEQUENCE OF 27-41. |
| [7] | "Functional characterization of ERp18, a new endoplasmic reticulum-located thioredoxin superfamily member." Alanen H.I., Williamson R.A., Howard M.J., Lappi A.-K., Jaentti H.P., Rautio S.M., Kellokumpu S., Ruddock L.W. J. Biol. Chem. 278:28912-28920(2003) [PubMed: 12761212] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, MUTAGENESIS OF CYS-66 AND CYS-69. |
| [8] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF543416 mRNA. Translation: AAN34781.1. AF131758 mRNA. Translation: AAD20035.1. AY358982 mRNA. Translation: AAQ89341.1. AL445685 Genomic DNA. Translation: CAI17031.1. BC001493 mRNA. Translation: AAH01493.1. BC008953 mRNA. Translation: AAH08953.1. BC008913 mRNA. Translation: AAH08913.1. | |||||||||||||
| IPI | IPI00026328. | ||||||||||||
| RefSeq | NP_056997.1. | ||||||||||||
| UniGene | Hs.476033 | ||||||||||||
3D structure databases | |||||||||||||
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| SMR | O95881. Positions 30-163. | ||||||||||||
| ModBase | Search... | ||||||||||||
Proteomic databases | |||||||||||||
| PeptideAtlas | O95881. | ||||||||||||
| PRIDE | O95881. | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENSG00000117862. Homo sapiens. [Contig view] | ||||||||||||
| GeneID | 51060. | ||||||||||||
| KEGG | hsa:51060. | ||||||||||||
Organism-specific databases | |||||||||||||
| GeneCards | GC01M052199. | ||||||||||||
| H-InvDB | HIX0000579. HIX0029114. | ||||||||||||
| HGNC | HGNC:24626. TXNDC12. | ||||||||||||
| MIM | 609448. gene. | ||||||||||||
| PharmGKB | PA142670665. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | O95881. | ||||||||||||
| HOVERGEN | O95881. | ||||||||||||
| OMA | O95881. CHACKAL. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BRENDA | 1.8.4.2. 247. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | O95881. | ||||||||||||
| Bgee | O95881. | ||||||||||||
| CleanEx | HS_TXNDC12. | ||||||||||||
| GermOnline | ENSG00000117862. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR017936. Thioredoxin-like. IPR017937. Thioredoxin_CS. IPR012335. Thioredoxin_fold. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit. | ||||||||||||
| PROSITE | PS00194. THIOREDOXIN_1. 1 hit. PS51352. THIOREDOXIN_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other Resources | |||||||||||||
| DrugBank | DB00143. Glutathione. | ||||||||||||
| NextBio | 53641. | ||||||||||||
| SOURCE | Search... | ||||||||||||
Entry information
| Entry name | TXD12_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O95881 Secondary accession number(s): Q5T1T4, Q96H50 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 1 Human chromosome 1: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


