Q6PKC3 · TXD11_HUMAN
- ProteinThioredoxin domain-containing protein 11
- GeneTXNDC11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids985 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May act as a redox regulator involved in DUOX proteins folding. The interaction with DUOX1 and DUOX2 suggest that it belongs to a multiprotein complex constituting the thyroid H2O2 generating system. It is however not sufficient to assist DUOX1 and DUOX2 in H2O2 generation.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameThioredoxin domain-containing protein 11
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6PKC3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Single-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 65-85 | Helical | ||||
Sequence: LLCGAVALGCALLLALKFTCS |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_022767 | 783 | in dbSNP:rs3190321 | |||
Sequence: V → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,279 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000120173 | 1-985 | Thioredoxin domain-containing protein 11 | |||
Sequence: MSECGGRGGGSSSSEDAEDEGGGGGGPAGSDCLSSSPTLATASSAGRLRRGLRGAFLMARQRPELLCGAVALGCALLLALKFTCSRAKDVIIPAKPPVSFFSLRSPVLDLFQGQLDYAEYVRRDSEVVLLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGKCRKQKHFFYFPVIYLYHRSFGPIEYKGPMSAVYIEKFVRRVMKPLLYIPSQSELLDFLSNYEPGVLGYFEFSGSPQPPGYLTFFTSALHSLKKALESTSSPRALVSFTGEWHLETKIYVLDYLGTVRFGVITNKHLAKLVSLVHSGSVYLHRHFNTSLVFPREVLNYTAENICKWALENQETLFRWLRPHGGKSLLLNNELKKGPALFLFIPFNPLAESHPLIDEITEVALEYNNCHGDQVVERLLQHLRRVDAPVLESLALEVPAQLPDPPTITASPCCNTVVLPQWHSFSRTHNVCELCVNQTSGGMKPSSVSVPQCSFFEMAAALDSFYLKEQTFYHVASDSIECSNFLTSYSPFSYYTACCRTISRGVSGFIDSEQGVFEAPTVAFSSLEKKCEVDAPSSVPHIEENRYLFPEVDMTSTNFTGLSCRTNKTLNIYLLDSNLFWLYAERLGAPSSTQVKEFAAIVDVKEESHYILDPKQALMKLTLESFIQNFSVLYSPLKRHLIGSGSAQFPSQHLITEVTTDTFWEVVLQKQDVLLLYYAPWCGFCPSLNHIFIQLARNLPMDTFTVARIDVSQNDLPWEFMVDRLPTVLFFPCNRKDLSVKYPEDVPITLPNLLRFILHHSDPASSPQNVANSPTKECLQSEAVLQRGHISHLEREIQKLRAEISSLQRAQVQVESQLSSARRDEHRLRQQQRALEEQHSLLHAHSEQLQALYEQKTRELQELARKLQELADASENLLTENTWLKILVATMERKLEGRDGAESLAAQREVHPKQPEPSATPQLPGSSPPPANVSATLVSERNKENRTD | ||||||
Disulfide bond | 469↔472 | Redox-active | ||||
Sequence: CELC | ||||||
Disulfide bond | 719↔722 | Redox-active | ||||
Sequence: CGFC | ||||||
Modified residue | 828 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed at low level. Expressed at higher level in thyroid and prostate.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with the cytoplasmic part of DUOX1 and DUOX2. Interacts with TPO and CYBA.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6PKC3 | HTT P42858 | 7 | EBI-749812, EBI-466029 | |
BINARY | Q6PKC3 | KLHL38 Q2WGJ6 | 3 | EBI-749812, EBI-6426443 | |
BINARY | Q6PKC3 | MKRN3 Q13064 | 3 | EBI-749812, EBI-2340269 | |
BINARY | Q6PKC3 | PRPF18 Q99633 | 3 | EBI-749812, EBI-2798416 | |
XENO | Q6PKC3 | PRO_0000037551 Q9WMX2 | 2 | EBI-749812, EBI-6863748 | |
BINARY | Q6PKC3 | RAB2B Q8WUD1 | 3 | EBI-749812, EBI-5542466 | |
BINARY | Q6PKC3 | ZNF417 Q8TAU3 | 3 | EBI-749812, EBI-740727 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-38 | Disordered | ||||
Sequence: MSECGGRGGGSSSSEDAEDEGGGGGGPAGSDCLSSSPT | ||||||
Domain | 92-214 | Thioredoxin 1 | ||||
Sequence: IPAKPPVSFFSLRSPVLDLFQGQLDYAEYVRRDSEVVLLFFYAPWCGQSIAARAEIEQAASRLSDQVLFVAINCWWNQGKCRKQKHFFYFPVIYLYHRSFGPIEYKGPMSAVYIEKFVRRVMK | ||||||
Domain | 649-799 | Thioredoxin 2 | ||||
Sequence: LDPKQALMKLTLESFIQNFSVLYSPLKRHLIGSGSAQFPSQHLITEVTTDTFWEVVLQKQDVLLLYYAPWCGFCPSLNHIFIQLARNLPMDTFTVARIDVSQNDLPWEFMVDRLPTVLFFPCNRKDLSVKYPEDVPITLPNLLRFILHHSD | ||||||
Coiled coil | 821-919 | |||||
Sequence: VLQRGHISHLEREIQKLRAEISSLQRAQVQVESQLSSARRDEHRLRQQQRALEEQHSLLHAHSEQLQALYEQKTRELQELARKLQELADASENLLTENT | ||||||
Region | 935-985 | Disordered | ||||
Sequence: RDGAESLAAQREVHPKQPEPSATPQLPGSSPPPANVSATLVSERNKENRTD |
Sequence similarities
Belongs to the protein disulfide isomerase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6PKC3-1
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.
- Name1
- Length985
- Mass (Da)110,529
- Last updated2005-07-05 v2
- Checksum4A8C852F8E81B8BC
Q6PKC3-2
- Name2
- Differences from canonical
- 265-291: Missing
Q6PKC3-3
- Name3
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK027464 EMBL· GenBank· DDBJ | BAB55129.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK027646 EMBL· GenBank· DDBJ | BAB55262.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074534 EMBL· GenBank· DDBJ | BAC11044.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC002856 EMBL· GenBank· DDBJ | AAH02856.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013727 EMBL· GenBank· DDBJ | AAH13727.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC018635 EMBL· GenBank· DDBJ | AAH18635.1 EMBL· GenBank· DDBJ | mRNA | ||
AF131780 EMBL· GenBank· DDBJ | AAD20043.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
CR457152 EMBL· GenBank· DDBJ | CAG33433.1 EMBL· GenBank· DDBJ | mRNA |