Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9DC23 (DJC10_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily C member 10

EC=1.8.4.-
Alternative name(s):
Endoplasmic reticulum DNA J domain-containing protein 5
Short name=ER-resident protein ERdj5
Short name=ERdj5
Endoplasmic reticulum DnaJ-PDI fusion protein 1
J domain-containing protein disulfide isomerase-like protein
Short name=J domain-containing PDI-like protein
Short name=JPDI
Gene names
Name:Dnajc10
Synonyms:Erdj5, Jpdi
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length793 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.7 Ref.9

Subunit structure

Interacts with HSPA5 (via its J domain). Interacts with EDEM1. Ref.6 Ref.7 Ref.9

Subcellular location

Endoplasmic reticulum lumen Ref.6.

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. Ref.1 Ref.6

Domain

Thioredoxin domains 3 and 4 are the primary reductase domains (Ref.9).

The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CXXC motif (Ref.9).

Disruption phenotype

Mice are viable and healthy but show enhanced endoplasmic reticulum stress response in the salivary gland. Ref.8

Sequence similarities

Contains 1 J domain.

Contains 4 thioredoxin domains.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainRedox-active center
Repeat
Signal
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from direct assay Ref.7Ref.9. Source: UniProtKB

cell redox homeostasis

Inferred from electronic annotation. Source: InterPro

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ATPase activity

Inferred from mutant phenotype Ref.6. Source: UniProtKB

protein folding in endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.6. Source: UniProtKB

endoplasmic reticulum chaperone complex

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum lumen

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATPase activator activity

Inferred from mutant phenotype Ref.6. Source: UniProtKB

ATPase binding

Inferred from physical interaction Ref.6. Source: UniProtKB

chaperone binding

Inferred from direct assay Ref.7. Source: UniProtKB

disulfide oxidoreductase activity

Inferred from direct assay Ref.7. Source: UniProtKB

misfolded protein binding

Inferred from sequence or structural similarity. Source: UniProtKB

oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor

Inferred from direct assay Ref.9. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9. Source: UniProtKB

protein disulfide oxidoreductase activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 793761DnaJ homolog subfamily C member 10
PRO_0000281484

Regions

Domain35 – 10066J
Domain130 – 232103Thioredoxin 1
Domain454 – 553100Thioredoxin 2
Domain557 – 665109Thioredoxin 3
Domain671 – 776106Thioredoxin 4
Region235 – 350116Trxb 1
Region348 – 463116Trxb 2
Motif790 – 7934Prevents secretion from ER Potential

Amino acid modifications

Glycosylation5301N-linked (GlcNAc...) Potential
Disulfide bond158 ↔ 161Redox-active
Disulfide bond480 ↔ 483Redox-active
Disulfide bond588 ↔ 591Redox-active
Disulfide bond700 ↔ 703Redox-active

Experimental info

Mutagenesis1581C → A: Abolishes disulfide reductase activity; when associated with A-161; A-480; A-483; A-588; A-591; A-700 and A-703. Ref.7 Ref.9
Mutagenesis1611C → A: Abolishes disulfide reductase activity; when associated with A-158; A-480; A-483; A-588; A-591; A-700 and A-703. Ref.7 Ref.9
Mutagenesis4801C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-483; A-588; A-591; A-700 and A-703. Ref.7 Ref.9
Mutagenesis4831C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-588; A-591; A-700 and A-703. Ref.7 Ref.9
Mutagenesis5881C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-591; A-700 and A-703. Ref.7 Ref.9
Mutagenesis5911C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-700 and A-703. Ref.7 Ref.9
Mutagenesis7001C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-703. Ref.7 Ref.9
Mutagenesis7031C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-700. Ref.7 Ref.9
Sequence conflict911D → H in BAB23413. Ref.3
Sequence conflict3101T → A in AAQ14555. Ref.2
Sequence conflict3241E → G in AAH33461. Ref.4
Sequence conflict4331I → T in AAH33461. Ref.4
Sequence conflict5381E → G in AAQ14555. Ref.2
Sequence conflict651 – 6522NG → RP in AAQ14555. Ref.2
Sequence conflict6541N → NS in AAN73273. Ref.1
Sequence conflict6801F → FR in AAN73273. Ref.1
Sequence conflict7671D → M in AAQ14555. Ref.2

Secondary structure

...................................................................................................................................... 793
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9DC23 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 00C88EF3F5497BE1

FASTA79390,583
        10         20         30         40         50         60 
MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE IRQAFKKLAL 

        70         80         90        100        110        120 
KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWSYYRY 

       130        140        150        160        170        180 
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR 

       190        200        210        220        230        240 
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAAVKYNGDR SKESLVAFAM QHVRSTVTEL 

       250        260        270        280        290        300 
STGNFVNAIE TAFAAGVGWL ITFCSKGEDC LTSQTRLRLS GMLDGLVNVG WVDCDAQDSL 

       310        320        330        340        350        360 
CKSLDTTAST TAYFPPGATL NDREKSSVLF LNSLDAKEIY MEIIHNLPDF ELLSANQLED 

       370        380        390        400        410        420 
RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR FDCSSAPGIC SDLYVFQPCL 

       430        440        450        460        470        480 
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPASDKEP WLVDFFAPWC 

       490        500        510        520        530        540 
PPCRALLPEL RKASTLLYGQ LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSIHEYEGH 

       550        560        570        580        590        600 
HSAEQILEFI EDLRNPSVVS LTPSTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR 

       610        620        630        640        650        660 
MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSKAYQYHSY NGWNRDAYSL 

       670        680        690        700        710        720 
RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVVDFYAPWC GPCQNFAPEF ELLARMIKGK 

       730        740        750        760        770        780 
VRAGKVDCQA YPQTCQKAGI KAYPSVKLYQ YERAKKSIWE EQINSRDAKT IAALIYGKLE 

       790 
TLQSQVKRNK DEL 

« Hide

References

« Hide 'large scale' references
[1]"ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress."
Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P., Gustafsson J.-A., Sitia R., Spyrou G.
J. Biol. Chem. 278:1059-1066(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"ERDJPs, a novel family of ER chaperones."
Simmen T., Mezghrani A., Bertoli G., Sitia R.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Lung.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II and FVB/N x C57BL/6J.
Tissue: Mammary tumor.
[6]"JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs."
Hosoda A., Kimata Y., Tsuru A., Kohno K.
J. Biol. Chem. 278:2669-2676(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, INTERACTION WITH HSPA5.
[7]"ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER."
Ushioda R., Hoseki J., Araki K., Jansen G., Thomas D.Y., Nagata K.
Science 321:569-572(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EDEM1, MUTAGENESIS OF CYS-158; CYS-161; CYS-480; CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703.
[8]"Positive contribution of ERdj5/JPDI to endoplasmic reticulum protein quality control in the salivary gland."
Hosoda A., Tokuda M., Akai R., Kohno K., Iwawaki T.
Biochem. J. 425:117-125(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[9]"Structural basis of an ERAD pathway mediated by the ER-resident protein disulfide reductase ERdj5."
Hagiwara M., Maegawa K., Suzuki M., Ushioda R., Araki K., Matsumoto Y., Hoseki J., Nagata K., Inaba K.
Mol. Cell 41:432-444(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF 33-793, FUNCTION, INTERACTION WITH EDEM1, MUTAGENESIS OF CYS-158; CYS-161; CYS-480; CYS-483; CYS-588; CYS-591; CYS-700 AND CYS-703.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF255459 mRNA. Translation: AAN73273.1.
AF314002 mRNA. Translation: AAQ14555.1.
AK004617 mRNA. Translation: BAB23413.1.
AL928587 Genomic DNA. Translation: CAM19646.1.
BC002207 mRNA. Translation: AAH02207.1.
BC033461 mRNA. Translation: AAH33461.1.
CCDSCCDS38159.1.
RefSeqNP_077143.2. NM_024181.2.
UniGeneMm.21762.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3APOX-ray2.40A33-793[»]
3APQX-ray1.84A/B34-242[»]
3APSX-ray1.90A/B668-789[»]
ProteinModelPortalQ9DC23.
SMRQ9DC23. Positions 34-782.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid211769. 2 interactions.

PTM databases

PhosphoSiteQ9DC23.

Proteomic databases

MaxQBQ9DC23.
PaxDbQ9DC23.
PRIDEQ9DC23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028392; ENSMUSP00000028392; ENSMUSG00000027006.
GeneID66861.
KEGGmmu:66861.
UCSCuc008khj.1. mouse.

Organism-specific databases

CTD54431.
MGIMGI:1914111. Dnajc10.

Phylogenomic databases

eggNOGCOG0526.
GeneTreeENSGT00730000110455.
HOGENOMHOG000231882.
HOVERGENHBG057048.
InParanoidA2ASA2.
KOK09530.
OMAYPSLFIF.
OrthoDBEOG7RZ5QH.
TreeFamTF105169.

Gene expression databases

ArrayExpressQ9DC23.
BgeeQ9DC23.
CleanExMM_DNAJC10.
GenevestigatorQ9DC23.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
3.40.30.10. 5 hits.
InterProIPR001623. DnaJ_domain.
IPR021170. DnaJ_homolog_subfam-C.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view]
PIRSFPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF52833. SSF52833. 6 hits.
PROSITEPS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9DC23.
NextBio322847.
PROQ9DC23.
SOURCESearch...

Entry information

Entry nameDJC10_MOUSE
AccessionPrimary (citable) accession number: Q9DC23
Secondary accession number(s): A2ASA2 expand/collapse secondary AC list , Q71S84, Q8CH78, Q8CIB0, Q99LV4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 106 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot