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Protein

DnaJ homolog subfamily C member 10

Gene

Dnajc10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  • ATPase activator activity Source: UniProtKB
  • ATPase binding Source: UniProtKB
  • chaperone binding Source: UniProtKB
  • disulfide oxidoreductase activity Source: UniProtKB
  • Hsp70 protein binding Source: MGI
  • misfolded protein binding Source: UniProtKB
  • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
  • protein disulfide oxidoreductase activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase

Enzyme and pathway databases

BRENDAi1.8.1.8 3474

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Dnajc10
Synonyms:Erdj5, Jpdi
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914111 Dnajc10

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Mice are viable and healthy but show enhanced endoplasmic reticulum stress response in the salivary gland.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi158C → A: Abolishes disulfide reductase activity; when associated with A-161; A-480; A-483; A-588; A-591; A-700 and A-703. 2 Publications1
Mutagenesisi161C → A: Abolishes disulfide reductase activity; when associated with A-158; A-480; A-483; A-588; A-591; A-700 and A-703. 2 Publications1
Mutagenesisi480C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-483; A-588; A-591; A-700 and A-703. 2 Publications1
Mutagenesisi483C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-588; A-591; A-700 and A-703. 2 Publications1
Mutagenesisi588C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-591; A-700 and A-703. 2 Publications1
Mutagenesisi591C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-700 and A-703. 2 Publications1
Mutagenesisi700C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-703. 2 Publications1
Mutagenesisi703C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-700. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000028148433 – 793DnaJ homolog subfamily C member 10Add BLAST761

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi158 ↔ 161Redox-active
Disulfide bondi480 ↔ 483Redox-active
Glycosylationi530N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi588 ↔ 591Redox-active
Disulfide bondi700 ↔ 703Redox-active

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9DC23
MaxQBiQ9DC23
PaxDbiQ9DC23
PeptideAtlasiQ9DC23
PRIDEiQ9DC23

PTM databases

iPTMnetiQ9DC23
PhosphoSitePlusiQ9DC23

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiENSMUSG00000027006 Expressed in 287 organ(s), highest expression level in prostate gland
CleanExiMM_DNAJC10
GenevisibleiQ9DC23 MM

Interactioni

Subunit structurei

Interacts with HSPA5 (via its J domain). Interacts with EDEM1.3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi211769, 2 interactors
IntActiQ9DC23, 1 interactor
STRINGi10090.ENSMUSP00000028392

Structurei

Secondary structure

1793
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9DC23
SMRiQ9DC23
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9DC23

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 100JPROSITE-ProRule annotationAdd BLAST66
Domaini130 – 232Thioredoxin 1PROSITE-ProRule annotationAdd BLAST103
Domaini454 – 553Thioredoxin 2PROSITE-ProRule annotationAdd BLAST100
Domaini557 – 665Thioredoxin 3PROSITE-ProRule annotationAdd BLAST109
Domaini671 – 776Thioredoxin 4PROSITE-ProRule annotationAdd BLAST106

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni235 – 350Trxb 1Add BLAST116
Regioni348 – 463Trxb 2Add BLAST116

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi790 – 793Prevents secretion from ERPROSITE-ProRule annotation4

Domaini

Thioredoxin domains 3 and 4 are the primary reductase domains.1 Publication
The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CXXC motif.1 Publication

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IMZF Eukaryota
KOG0191 Eukaryota
COG0526 LUCA
COG2214 LUCA
GeneTreeiENSGT00930000150840
HOGENOMiHOG000231882
HOVERGENiHBG057048
InParanoidiQ9DC23
KOiK09530
OMAiAVNCGDN
OrthoDBiEOG091G0BFU
TreeFamiTF105169

Family and domain databases

CDDicd06257 DnaJ, 1 hit
cd03004 PDI_a_ERdj5_C, 3 hits
cd03003 PDI_a_ERdj5_N, 1 hit
Gene3Di1.10.287.110, 1 hit
InterProiView protein in InterPro
IPR001623 DnaJ_domain
IPR021170 ERdj5
IPR035674 ERdj5_TRX_C
IPR035673 ERdj5_TRX_N
IPR036869 J_dom_sf
IPR036249 Thioredoxin-like_sf
IPR017937 Thioredoxin_CS
IPR013766 Thioredoxin_domain
PfamiView protein in Pfam
PF00226 DnaJ, 1 hit
PF00085 Thioredoxin, 4 hits
PIRSFiPIRSF037293 DnaJ_homolog_subfam-C, 1 hit
PRINTSiPR00625 JDOMAIN
SMARTiView protein in SMART
SM00271 DnaJ, 1 hit
SUPFAMiSSF46565 SSF46565, 1 hit
SSF52833 SSF52833, 6 hits
PROSITEiView protein in PROSITE
PS50076 DNAJ_2, 1 hit
PS00014 ER_TARGET, 1 hit
PS00194 THIOREDOXIN_1, 2 hits
PS51352 THIOREDOXIN_2, 3 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DC23-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE
60 70 80 90 100
IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG
110 120 130 140 150
EKGLEDNQGG QYESWSYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF
160 170 180 190 200
VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS
210 220 230 240 250
YPSLFIFRSG MAAVKYNGDR SKESLVAFAM QHVRSTVTEL STGNFVNAIE
260 270 280 290 300
TAFAAGVGWL ITFCSKGEDC LTSQTRLRLS GMLDGLVNVG WVDCDAQDSL
310 320 330 340 350
CKSLDTTAST TAYFPPGATL NDREKSSVLF LNSLDAKEIY MEIIHNLPDF
360 370 380 390 400
ELLSANQLED RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR
410 420 430 440 450
FDCSSAPGIC SDLYVFQPCL AVFKGQGTKE YEIHHGKKIL YDILAFAKES
460 470 480 490 500
VNSHVTTLGP QNFPASDKEP WLVDFFAPWC PPCRALLPEL RKASTLLYGQ
510 520 530 540 550
LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSIHEYEGH HSAEQILEFI
560 570 580 590 600
EDLRNPSVVS LTPSTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR
610 620 630 640 650
MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSKAYQYHSY
660 670 680 690 700
NGWNRDAYSL RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVVDFYAPWC
710 720 730 740 750
GPCQNFAPEF ELLARMIKGK VRAGKVDCQA YPQTCQKAGI KAYPSVKLYQ
760 770 780 790
YERAKKSIWE EQINSRDAKT IAALIYGKLE TLQSQVKRNK DEL
Length:793
Mass (Da):90,583
Last modified:July 27, 2011 - v2
Checksum:i00C88EF3F5497BE1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti91D → H in BAB23413 (PubMed:16141072).Curated1
Sequence conflicti310T → A in AAQ14555 (Ref. 2) Curated1
Sequence conflicti324E → G in AAH33461 (PubMed:19468303).Curated1
Sequence conflicti433I → T in AAH33461 (PubMed:19468303).Curated1
Sequence conflicti538E → G in AAQ14555 (Ref. 2) Curated1
Sequence conflicti651 – 652NG → RP in AAQ14555 (Ref. 2) Curated2
Sequence conflicti654N → NS in AAN73273 (PubMed:12411443).Curated1
Sequence conflicti680F → FR in AAN73273 (PubMed:12411443).Curated1
Sequence conflicti767D → M in AAQ14555 (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255459 mRNA Translation: AAN73273.1
AF314002 mRNA Translation: AAQ14555.1
AK004617 mRNA Translation: BAB23413.1
AL928587 Genomic DNA No translation available.
BC002207 mRNA Translation: AAH02207.1
BC033461 mRNA Translation: AAH33461.1
CCDSiCCDS38159.1
RefSeqiNP_077143.2, NM_024181.2
UniGeneiMm.21762

Genome annotation databases

EnsembliENSMUST00000028392; ENSMUSP00000028392; ENSMUSG00000027006
GeneIDi66861
KEGGimmu:66861
UCSCiuc008khj.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF255459 mRNA Translation: AAN73273.1
AF314002 mRNA Translation: AAQ14555.1
AK004617 mRNA Translation: BAB23413.1
AL928587 Genomic DNA No translation available.
BC002207 mRNA Translation: AAH02207.1
BC033461 mRNA Translation: AAH33461.1
CCDSiCCDS38159.1
RefSeqiNP_077143.2, NM_024181.2
UniGeneiMm.21762

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3APOX-ray2.40A33-793[»]
3APQX-ray1.84A/B34-242[»]
3APSX-ray1.90A/B668-789[»]
5AYKX-ray2.25A32-793[»]
5AYLX-ray2.40A32-793[»]
ProteinModelPortaliQ9DC23
SMRiQ9DC23
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211769, 2 interactors
IntActiQ9DC23, 1 interactor
STRINGi10090.ENSMUSP00000028392

PTM databases

iPTMnetiQ9DC23
PhosphoSitePlusiQ9DC23

Proteomic databases

EPDiQ9DC23
MaxQBiQ9DC23
PaxDbiQ9DC23
PeptideAtlasiQ9DC23
PRIDEiQ9DC23

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028392; ENSMUSP00000028392; ENSMUSG00000027006
GeneIDi66861
KEGGimmu:66861
UCSCiuc008khj.1 mouse

Organism-specific databases

CTDi54431
MGIiMGI:1914111 Dnajc10

Phylogenomic databases

eggNOGiENOG410IMZF Eukaryota
KOG0191 Eukaryota
COG0526 LUCA
COG2214 LUCA
GeneTreeiENSGT00930000150840
HOGENOMiHOG000231882
HOVERGENiHBG057048
InParanoidiQ9DC23
KOiK09530
OMAiAVNCGDN
OrthoDBiEOG091G0BFU
TreeFamiTF105169

Enzyme and pathway databases

BRENDAi1.8.1.8 3474

Miscellaneous databases

EvolutionaryTraceiQ9DC23
PROiPR:Q9DC23
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027006 Expressed in 287 organ(s), highest expression level in prostate gland
CleanExiMM_DNAJC10
GenevisibleiQ9DC23 MM

Family and domain databases

CDDicd06257 DnaJ, 1 hit
cd03004 PDI_a_ERdj5_C, 3 hits
cd03003 PDI_a_ERdj5_N, 1 hit
Gene3Di1.10.287.110, 1 hit
InterProiView protein in InterPro
IPR001623 DnaJ_domain
IPR021170 ERdj5
IPR035674 ERdj5_TRX_C
IPR035673 ERdj5_TRX_N
IPR036869 J_dom_sf
IPR036249 Thioredoxin-like_sf
IPR017937 Thioredoxin_CS
IPR013766 Thioredoxin_domain
PfamiView protein in Pfam
PF00226 DnaJ, 1 hit
PF00085 Thioredoxin, 4 hits
PIRSFiPIRSF037293 DnaJ_homolog_subfam-C, 1 hit
PRINTSiPR00625 JDOMAIN
SMARTiView protein in SMART
SM00271 DnaJ, 1 hit
SUPFAMiSSF46565 SSF46565, 1 hit
SSF52833 SSF52833, 6 hits
PROSITEiView protein in PROSITE
PS50076 DNAJ_2, 1 hit
PS00014 ER_TARGET, 1 hit
PS00194 THIOREDOXIN_1, 2 hits
PS51352 THIOREDOXIN_2, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiDJC10_MOUSE
AccessioniPrimary (citable) accession number: Q9DC23
Secondary accession number(s): A2ASA2
, Q71S84, Q8CH78, Q8CIB0, Q99LV4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: November 7, 2018
This is version 134 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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Main funding by: National Institutes of Health

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