Reviewed,
UniProtKB/Swiss-Prot Q11067 (PDIA6_CAEEL)
Last modified
June 16, 2009.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable protein disulfide-isomerase A6 EC=5.3.4.1 | ||||
| Gene names |
| ||||
| Organism | Caenorhabditis elegans [Complete proteome] | ||||
| Taxonomic identifier | 6239 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 440 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)
| Catalytic activity | Catalyzes the rearrangement of -S-S- bonds in proteins. |
| Subcellular location | Endoplasmic reticulum lumen By similarity. |
| Sequence similarities | Belongs to the protein disulfide isomerase family. Contains 2 thioredoxin domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Endoplasmic reticulum |
| Domain | Redox-active center Repeat Signal |
| Molecular function | Isomerase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro growthInferred from mutant phenotype. Source: WormBase locomotionInferred from mutant phenotype. Source: WormBase nematode larval developmentInferred from mutant phenotype. Source: WormBase |
| Cellular component | endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum lumenInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | protein disulfide isomerase 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 – 18 | 18 | Potential | ||||||||
| Chain | 19 – 440 | 422 | Probable protein disulfide-isomerase A6 | PRO_0000034241 | |||||||
Regions | |||||||||||
| Domain | 19 – 131 | 113 | Thioredoxin 1 | ||||||||
| Domain | 127 – 273 | 147 | Thioredoxin 2 | ||||||||
| Motif | 437 – 440 | 4 | Prevents secretion from ER By similarity | ||||||||
| Compositional bias | 142 – 152 | 11 | Poly-Ser | ||||||||
| Compositional bias | 158 – 163 | 6 | Poly-Gly | ||||||||
| Compositional bias | 425 – 436 | 12 | Asp/Glu-rich (acidic) | ||||||||
Sites | |||||||||||
| Active site | 54 | 1 | Nucleophile By similarity | ||||||||
| Active site | 57 | 1 | Nucleophile By similarity | ||||||||
| Active site | 194 | 1 | Nucleophile By similarity | ||||||||
| Active site | 197 | 1 | Nucleophile By similarity | ||||||||
| Site | 55 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 56 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 117 | 1 | Lowers pKa of C-terminal Cys of first active site By similarity | ||||||||
| Site | 195 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 196 | 1 | Contributes to redox potential value By similarity | ||||||||
| Site | 259 | 1 | Lowers pKa of C-terminal Cys of second active site By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 54 ↔ 57 | Redox-active By similarity | |||||||||
| Disulfide bond | 194 ↔ 197 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2. |
Cross-references
Sequence databases | |
|---|---|
| U40411 Genomic DNA. Translation: AAC47065.1. | |
| PIR | T15352. |
| RefSeq | NP_509190.1. |
| UniGene | Cel.6685 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1MEK based on UniProtKB P07237. |
| ModBase | Search... |
Genome annotation databases | |
| Ensembl | B0403.4. Caenorhabditis elegans. [Contig view] |
| GeneID | 180974. |
| KEGG | cel:B0403.4. |
| NMPDR | fig|6239.3.peg.23679. |
Organism-specific databases | |
| WormBase | WBGene00015168. tag-320. |
| WormPep | B0403.4. CE03880. [WorfDB] |
Phylogenomic databases | |
| OMA | Q11067. LEPEWAA. |
Enzyme and pathway databases | |
| BRENDA | 5.3.4.1. 672. |
Gene expression databases | |
| ArrayExpress | Q11067. |
Family and domain databases | |
| InterPro | IPR005788. Disulphide_isomerase. IPR017936. Thioredoxin-like. IPR006662. Thioredoxin-like_subdom. IPR017937. Thioredoxin_CS. IPR013766. Thioredoxin_domain. IPR012335. Thioredoxin_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.30.10. Thioredoxin_fold. 2 hits. |
| Pfam | PF00085. Thioredoxin. 2 hits. [Graphical view] |
| PRINTS | PR00421. THIOREDOXIN. |
| TIGRFAMs | TIGR01126. pdi_dom. 2 hits. |
| PROSITE | PS00194. THIOREDOXIN_1. 2 hits. PS51352. THIOREDOXIN_2. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 911804. |
Entry information
| Entry name | PDIA6_CAEEL | ||||||||
| Accession | Primary (citable) accession number: Q11067 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Caenorhabditis annotation project | ||||||||
Relevant documents
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormPep |
| SIMILARITY comments Index of protein domains and families |

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