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Protein

DnaJ homolog subfamily C member 10

Gene

Dnajc10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914111. Dnajc10.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

Complete GO annotation...

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...)Sequence 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.
CleanExiMM_DNAJC10.
GenevisibleiQ9DC23. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • ATPase binding Source: UniProtKB
  • chaperone binding Source: UniProtKB
  • Hsp70 protein binding Source: MGI
  • misfolded protein binding Source: UniProtKB

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi36 – 40Combined sources5
Helixi48 – 62Combined sources15
Helixi64 – 66Combined sources3
Helixi73 – 87Combined sources15
Helixi90 – 99Combined sources10
Turni100 – 103Combined sources4
Helixi115 – 120Combined sources6
Beta strandi121 – 123Combined sources3
Turni124 – 127Combined sources4
Beta strandi131 – 133Combined sources3
Helixi136 – 145Combined sources10
Beta strandi149 – 154Combined sources6
Helixi159 – 174Combined sources16
Turni175 – 178Combined sources4
Beta strandi179 – 185Combined sources7
Turni186 – 188Combined sources3
Helixi190 – 195Combined sources6
Beta strandi200 – 207Combined sources8
Helixi222 – 234Combined sources13
Beta strandi237 – 239Combined sources3
Helixi242 – 255Combined sources14
Beta strandi258 – 264Combined sources7
Helixi273 – 282Combined sources10
Turni283 – 286Combined sources4
Beta strandi287 – 293Combined sources7
Turni294 – 296Combined sources3
Helixi298 – 301Combined sources4
Beta strandi311 – 314Combined sources4
Turni322 – 324Combined sources3
Helixi325 – 327Combined sources3
Beta strandi328 – 331Combined sources4
Helixi336 – 346Combined sources11
Helixi355 – 362Combined sources8
Beta strandi365 – 372Combined sources8
Helixi382 – 386Combined sources5
Helixi387 – 391Combined sources5
Helixi392 – 394Combined sources3
Beta strandi396 – 402Combined sources7
Helixi403 – 405Combined sources3
Helixi407 – 412Combined sources6
Beta strandi419 – 426Combined sources8
Beta strandi429 – 433Combined sources5
Helixi440 – 451Combined sources12
Beta strandi455 – 457Combined sources3
Turni460 – 462Combined sources3
Beta strandi471 – 476Combined sources6
Helixi481 – 496Combined sources16
Turni497 – 500Combined sources4
Beta strandi502 – 507Combined sources6
Turni508 – 510Combined sources3
Helixi512 – 517Combined sources6
Beta strandi522 – 530Combined sources9
Beta strandi533 – 537Combined sources5
Helixi543 – 554Combined sources12
Beta strandi557 – 560Combined sources4
Helixi563 – 569Combined sources7
Turni570 – 572Combined sources3
Beta strandi579 – 584Combined sources6
Helixi589 – 605Combined sources17
Turni606 – 608Combined sources3
Beta strandi609 – 615Combined sources7
Turni616 – 619Combined sources4
Helixi620 – 625Combined sources6
Beta strandi630 – 637Combined sources8
Beta strandi641 – 643Combined sources3
Helixi657 – 665Combined sources9
Beta strandi672 – 674Combined sources3
Helixi677 – 683Combined sources7
Turni684 – 686Combined sources3
Beta strandi691 – 696Combined sources6
Helixi701 – 717Combined sources17
Turni718 – 720Combined sources3
Beta strandi722 – 727Combined sources6
Turni728 – 730Combined sources3
Helixi732 – 737Combined sources6
Beta strandi742 – 752Combined sources11
Helixi753 – 755Combined sources3
Beta strandi757 – 763Combined sources7
Helixi768 – 780Combined sources13

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[»]
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

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation
Contains 4 thioredoxin domains.PROSITE-ProRule annotation

Keywords - Domaini

Redox-active center, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IMZF. Eukaryota.
KOG0191. Eukaryota.
COG0526. LUCA.
COG2214. LUCA.
GeneTreeiENSGT00860000133723.
HOGENOMiHOG000231882.
HOVERGENiHBG057048.
InParanoidiQ9DC23.
KOiK09530.
OMAiTELWTGN.
OrthoDBiEOG091G0BFU.
TreeFamiTF105169.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
3.40.30.10. 5 hits.
InterProiIPR001623. DnaJ_domain.
IPR021170. ERdj5.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view]
PIRSFiPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF52833. SSF52833. 6 hits.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]

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. Translation: CAM19646.1.
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.

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. Translation: CAM19646.1.
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[»]
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.
GeneTreeiENSGT00860000133723.
HOGENOMiHOG000231882.
HOVERGENiHBG057048.
InParanoidiQ9DC23.
KOiK09530.
OMAiTELWTGN.
OrthoDBiEOG091G0BFU.
TreeFamiTF105169.

Enzyme and pathway databases

BRENDAi1.8.1.8. 3474.

Miscellaneous databases

EvolutionaryTraceiQ9DC23.
PROiQ9DC23.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027006.
CleanExiMM_DNAJC10.
GenevisibleiQ9DC23. MM.

Family and domain databases

CDDicd06257. DnaJ. 1 hit.
Gene3Di1.10.287.110. 1 hit.
3.40.30.10. 5 hits.
InterProiIPR001623. DnaJ_domain.
IPR021170. ERdj5.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view]
PIRSFiPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF52833. SSF52833. 6 hits.
PROSITEiPS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDJC10_MOUSE
AccessioniPrimary (citable) accession number: Q9DC23
Secondary accession number(s): A2ASA2
, Q71S84, Q8CH78, Q8CIB0, Q99LV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 123 of the entry and version 2 of the sequence. [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
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.