| Tbio | DnaJ homolog subfamily C member 10 |
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.
This gene encodes an endoplasmic reticulum co-chaperone which is part of the endoplasmic reticulum-associated degradation complex involved in recognizing and degrading misfolded proteins. The encoded protein reduces incorrect disulfide bonds in misfolded glycoproteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Oct 2012]
This gene encodes an endoplasmic reticulum co-chaperone which is part of the endoplasmic reticulum-associated degradation complex involved in recognizing and degrading misfolded proteins. The encoded protein reduces incorrect disulfide bonds in misfolded glycoproteins. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Oct 2012]
Comments
| Disease | Target Count |
|---|---|
| IGA Glomerulonephritis | 454 |
| Prostatic Neoplasms | 471 |
| Disease | Target Count | Z-score | Confidence |
|---|---|---|---|
| Trichinosis | 7 | 3.084 | 1.5 |
| Species | Source |
|---|---|
| Chimp | OMA EggNOG |
| Macaque | OMA EggNOG Inparanoid |
| Mouse | OMA EggNOG Inparanoid |
| Rat | OMA EggNOG Inparanoid |
| Dog | OMA EggNOG Inparanoid |
| Horse | OMA EggNOG Inparanoid |
| Cow | OMA EggNOG Inparanoid |
| Pig | OMA EggNOG Inparanoid |
| Opossum | OMA EggNOG Inparanoid |
| Platypus | OMA EggNOG Inparanoid |
| Chicken | OMA EggNOG Inparanoid |
| Anole lizard | OMA EggNOG Inparanoid |
| Xenopus | OMA EggNOG |
| Zebrafish | OMA EggNOG Inparanoid |
| C. elegans | OMA EggNOG Inparanoid |
| PMID | Text |
|---|---|
| 25055872 | ERdj5 is a member of the proteostasis network that regulates rod opsin biogenesis and supports a role for disulfide bond formation/reduction in rod opsin biogenesis and disease. |
| 23769672 | ERdj5 acts as the endoplasmic reticulum reductase, both preparing misfolded proteins for degradation and catalyzing the folding of proteins that form obligatory non-native disulfides. |
| 23363602 | ERdj5, by binding to Sel1L, triggers BiP-Cholera toxin interaction proximal to the Hrd1 complex; postulate this scenario enables the Hrd1-associated retrotranslocation machinery to capture the toxin efficiently once the toxin is released from BiP |
| 19122239 | ERdj5 decreases neuroblastoma cell survival by down-regulating the UPR, raising the possibility that this protein could be a target for anti-tumor approaches. |
| 18653895 | study found that an endoplasmic reticulum (ER) protein ERdj5 had a reductase activity, cleaved the disulfide bonds of misfolded proteins & accelerated ER-associated degradation through its physical and functional associations with EDEM & BiP |
| 18400946 | ERdj4 and ERdj5 promote turnover of misfolded SP-C and this activity is dependent on their ability to stimulate BiP ATPase activity. |
| 14587667 | The organization of the functional motifs of hMTHr suggests that the protein might be a member of a molecular chaperone family. |
| 12446677 | JPDI may have roles in folding of some proteins in the ER, chaperoning by BiP and formation of proper disulfide bonds |
| 12411443 | ERdj5 is a ubiquitous protein localized in the ER and is particularly abundant in secretory cells. Its transcription is induced during ER stress, suggesting potential roles for ERdj5 in protein folding and translocation across the ER membrane. |
MGVWLNKDDYIRDLKRIILCFLIVYMAILVGTDQDFYSLLGVSKTASSREIRQAFKKLALKLHPDKNPNN 1 - 70 PNAHGDFLKINRAYEVLKDEDLRKKYDKYGEKGLEDNQGGQYESWNYYRYDFGIYDDDPEIITLERREFD 71 - 140 AAVNSGELWFVNFYSPGCSHCHDLAPTWRDFAKEVDGLLRIGAVNCGDDRMLCRMKGVNSYPSLFIFRSG 141 - 210 MAPVKYHGDRSKESLVSFAMQHVRSTVTELWTGNFVNSIQTAFAAGIGWLITFCSKGGDCLTSQTRLRLS 211 - 280 GMLDGLVNVGWMDCATQDNLCKSLDITTSTTAYFPPGATLNNKEKNSILFLNSLDAKEIYLEVIHNLPDF 281 - 350 ELLSANTLEDRLAHHRWLLFFHFGKNENSNDPELKKLKTLLKNDHIQVGRFDCSSAPDICSNLYVFQPSL 351 - 420 AVFKGQGTKEYEIHHGKKILYDILAFAKESVNSHVTTLGPQNFPANDKEPWLVDFFAPWCPPCRALLPEL 421 - 490 RRASNLLYGQLKFGTLDCTVHEGLCNMYNIQAYPTTVVFNQSNIHEYEGHHSAEQILEFIEDLMNPSVVS 491 - 560 LTPTTFNELVTQRKHNEVWMVDFYSPWCHPCQVLMPEWKRMARTLTGLINVGSIDCQQYHSFCAQENVQR 561 - 630 YPEIRFFPPKSNKAYHYHSYNGWNRDAYSLRIWGLGFLPQVSTDLTPQTFSEKVLQGKNHWVIDFYAPWC 631 - 700 GPCQNFAPEFELLARMIKGKVKAGKVDCQAYAQTCQKAGIRAYPTVKFYFYERAKRNFQEEQINTRDAKA 701 - 770 IAALISEKLETLRNQGKRNKDEL 771 - 793 //
| PMID | Year | Title |
|---|---|---|
| 25944712 | 2015 | N-terminome analysis of the human mitochondrial proteome. |
| 25416956 | 2014 | A proteome-scale map of the human interactome network. |
| 25055872 | 2014 | The co-chaperone and reductase ERdj5 facilitates rod opsin biogenesis and quality control. |
| 23769672 | 2013 | ERdj5 is the ER reductase that catalyzes the removal of non-native disulfides and correct folding of the LDL receptor. |
| 23363602 | 2013 | The ERdj5-Sel1L complex facilitates cholera toxin retrotranslocation. |
| 23192594 | 2013 | Gene-environment interactions and obesity traits among postmenopausal African-American and Hispanic women in the Women's Health Initiative SHARe Study. |
| 22229892 | 2012 | Redox-dependent protein quality control in the endoplasmic reticulum: folding to degradation. |
| 21632540 | 2011 | Characterization of early EDEM1 protein maturation events and their functional implications. |
| 21329881 | 2011 | Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5. |
| 21269460 | 2011 | Initial characterization of the human central proteome. |
| More... |
