Q9DC23 · DJC10_MOUSE
- ProteinDnaJ homolog subfamily C member 10
- GeneDnajc10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids793 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Endoplasmic reticulum disulfide reductase involved both in the correct folding of proteins and degradation of misfolded proteins. Required for efficient folding of proteins in the endoplasmic reticulum by catalyzing the removal of non-native disulfide bonds formed during the folding of proteins, such as LDLR. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins recognized by EDEM1. Interaction with HSPA5 is required its activity, not for the disulfide reductase activity, but to facilitate the release of DNAJC10 from its substrate. Promotes apoptotic signaling pathway in response to endoplasmic reticulum stress.
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 | |
Cellular Component | endoplasmic reticulum chaperone complex | |
Cellular Component | endoplasmic reticulum lumen | |
Molecular Function | ATPase activator activity | |
Molecular Function | ATPase binding | |
Molecular Function | disulfide oxidoreductase activity | |
Molecular Function | Hsp70 protein binding | |
Molecular Function | misfolded protein binding | |
Molecular Function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor | |
Molecular Function | protein-disulfide reductase activity | |
Molecular Function | protein-folding chaperone binding | |
Biological Process | ERAD pathway | |
Biological Process | intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress | |
Biological Process | IRE1-mediated unfolded protein response | |
Biological Process | negative regulation of protein phosphorylation | |
Biological Process | positive regulation of ATP-dependent activity | |
Biological Process | protein folding in endoplasmic reticulum | |
Biological Process | response to endoplasmic reticulum stress |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDnaJ homolog subfamily C member 10
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9DC23
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Mice are viable and healthy but show enhanced endoplasmic reticulum stress response in the salivary gland.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 158 | Abolishes disulfide reductase activity; when associated with A-161; A-480; A-483; A-588; A-591; A-700 and A-703. | ||||
Sequence: C → A | ||||||
Mutagenesis | 161 | Abolishes disulfide reductase activity; when associated with A-158; A-480; A-483; A-588; A-591; A-700 and A-703. | ||||
Sequence: C → A | ||||||
Mutagenesis | 480 | Abolishes disulfide reductase activity; when associated with A-158; A-161; A-483; A-588; A-591; A-700 and A-703. | ||||
Sequence: C → A | ||||||
Mutagenesis | 483 | Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-588; A-591; A-700 and A-703. | ||||
Sequence: C → A | ||||||
Mutagenesis | 588 | Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-591; A-700 and A-703. | ||||
Sequence: C → A | ||||||
Mutagenesis | 591 | Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-700 and A-703. | ||||
Sequence: C → A | ||||||
Mutagenesis | 700 | Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-703. | ||||
Sequence: C → A | ||||||
Mutagenesis | 703 | Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-700. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 32 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-32 | |||||
Sequence: MGVWLNKDDFIRDLKRISLCLLILYVVVVVGT | ||||||
Chain | PRO_0000281484 | 33-793 | DnaJ homolog subfamily C member 10 | |||
Sequence: DQNFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYESWSYYRYDFGIYDDDPEIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWREFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAAVKYNGDRSKESLVAFAMQHVRSTVTELSTGNFVNAIETAFAAGVGWLITFCSKGEDCLTSQTRLRLSGMLDGLVNVGWVDCDAQDSLCKSLDTTASTTAYFPPGATLNDREKSSVLFLNSLDAKEIYMEIIHNLPDFELLSANQLEDRLAHHRWLVFFHFGKNENANDPELKKLKTLLKNEHIQVGRFDCSSAPGICSDLYVFQPCLAVFKGQGTKEYEIHHGKKILYDILAFAKESVNSHVTTLGPQNFPASDKEPWLVDFFAPWCPPCRALLPELRKASTLLYGQLKVGTLDCTIHEGLCNMYNIQAYPTTVVFNQSSIHEYEGHHSAEQILEFIEDLRNPSVVSLTPSTFNELVKQRKHDEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSVDCQQYHSFCTQENVQRYPEIRFYPQKSSKAYQYHSYNGWNRDAYSLRSWGLGFLPQASIDLTPQTFNEKVLQGKTHWVVDFYAPWCGPCQNFAPEFELLARMIKGKVRAGKVDCQAYPQTCQKAGIKAYPSVKLYQYERAKKSIWEEQINSRDAKTIAALIYGKLETLQSQVKRNKDEL | ||||||
Disulfide bond | 158↔161 | Redox-active | ||||
Sequence: CSHC | ||||||
Disulfide bond | 480↔483 | Redox-active | ||||
Sequence: CPPC | ||||||
Glycosylation | 530 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 588↔591 | Redox-active | ||||
Sequence: CHPC | ||||||
Disulfide bond | 700↔703 | Redox-active | ||||
Sequence: CGPC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous. Particularly abundant in secretory tissues. Ubiquitous in fetal tissues and tumor tissues. Higher expression in fetal tissues than in adult tissues. Expressed in testis, pancreas, fetal thymus and fetal kidney. High expression in heart, liver, kidney, and testis. Low expression in spleen and skeletal muscle.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 35-100 | J | ||||
Sequence: NFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNNPNAHGDFLKINRAYEVLKDEDLRKKYDKYG | ||||||
Domain | 130-232 | Thioredoxin 1 | ||||
Sequence: EIITLERREFDAAVNSGELWFVNFYSPGCSHCHDLAPTWREFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSGMAAVKYNGDRSKESLVAFAMQH | ||||||
Region | 235-350 | Trxb 1 | ||||
Sequence: STVTELSTGNFVNAIETAFAAGVGWLITFCSKGEDCLTSQTRLRLSGMLDGLVNVGWVDCDAQDSLCKSLDTTASTTAYFPPGATLNDREKSSVLFLNSLDAKEIYMEIIHNLPDF | ||||||
Region | 348-463 | Trxb 2 | ||||
Sequence: PDFELLSANQLEDRLAHHRWLVFFHFGKNENANDPELKKLKTLLKNEHIQVGRFDCSSAPGICSDLYVFQPCLAVFKGQGTKEYEIHHGKKILYDILAFAKESVNSHVTTLGPQNF | ||||||
Domain | 454-553 | Thioredoxin 2 | ||||
Sequence: HVTTLGPQNFPASDKEPWLVDFFAPWCPPCRALLPELRKASTLLYGQLKVGTLDCTIHEGLCNMYNIQAYPTTVVFNQSSIHEYEGHHSAEQILEFIEDL | ||||||
Domain | 557-665 | Thioredoxin 3 | ||||
Sequence: SVVSLTPSTFNELVKQRKHDEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSVDCQQYHSFCTQENVQRYPEIRFYPQKSSKAYQYHSYNGWNRDAYSLRSWGL | ||||||
Domain | 671-776 | Thioredoxin 4 | ||||
Sequence: ASIDLTPQTFNEKVLQGKTHWVVDFYAPWCGPCQNFAPEFELLARMIKGKVRAGKVDCQAYPQTCQKAGIKAYPSVKLYQYERAKKSIWEEQINSRDAKTIAALIY | ||||||
Motif | 790-793 | Prevents secretion from ER | ||||
Sequence: KDEL |
Domain
Thioredoxin domains 3 and 4 are the primary reductase domains.
The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CXXC motif.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length793
- Mass (Da)90,583
- Last updated2011-07-27 v2
- Checksum00C88EF3F5497BE1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 91 | in Ref. 3; BAB23413 | ||||
Sequence: D → H | ||||||
Sequence conflict | 310 | in Ref. 2; AAQ14555 | ||||
Sequence: T → A | ||||||
Sequence conflict | 324 | in Ref. 4; AAH33461 | ||||
Sequence: E → G | ||||||
Sequence conflict | 433 | in Ref. 4; AAH33461 | ||||
Sequence: I → T | ||||||
Sequence conflict | 538 | in Ref. 2; AAQ14555 | ||||
Sequence: E → G | ||||||
Sequence conflict | 651-652 | in Ref. 2; AAQ14555 | ||||
Sequence: NG → RP | ||||||
Sequence conflict | 654 | in Ref. 1; AAN73273 | ||||
Sequence: N → NS | ||||||
Sequence conflict | 680 | in Ref. 1; AAN73273 | ||||
Sequence: F → FR | ||||||
Sequence conflict | 767 | in Ref. 2; AAQ14555 | ||||
Sequence: D → M |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF255459 EMBL· GenBank· DDBJ | AAN73273.1 EMBL· GenBank· DDBJ | mRNA | ||
AF314002 EMBL· GenBank· DDBJ | AAQ14555.1 EMBL· GenBank· DDBJ | mRNA | ||
AK004617 EMBL· GenBank· DDBJ | BAB23413.1 EMBL· GenBank· DDBJ | mRNA | ||
AL928587 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC002207 EMBL· GenBank· DDBJ | AAH02207.1 EMBL· GenBank· DDBJ | mRNA | ||
BC033461 EMBL· GenBank· DDBJ | AAH33461.1 EMBL· GenBank· DDBJ | mRNA |