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Q9DC23

- DJC10_MOUSE

UniProt

Q9DC23 - DJC10_MOUSE

Protein

DnaJ homolog subfamily C member 10

Gene

Dnajc10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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

    1. ATPase activator activity Source: UniProtKB
    2. ATPase binding Source: UniProtKB
    3. chaperone binding Source: UniProtKB
    4. disulfide oxidoreductase activity Source: UniProtKB
    5. misfolded protein binding Source: UniProtKB
    6. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. protein disulfide oxidoreductase activity Source: UniProtKB

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
    3. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
    4. negative regulation of protein phosphorylation Source: UniProtKB
    5. positive regulation of ATPase activity Source: UniProtKB
    6. protein folding in endoplasmic reticulum Source: UniProtKB
    7. response to endoplasmic reticulum stress Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    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
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1914111. Dnajc10.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum chaperone complex Source: UniProtKB
    3. endoplasmic reticulum lumen Source: UniProtKB

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi158 – 1581C → A: Abolishes disulfide reductase activity; when associated with A-161; A-480; A-483; A-588; A-591; A-700 and A-703. 2 Publications
    Mutagenesisi161 – 1611C → A: Abolishes disulfide reductase activity; when associated with A-158; A-480; A-483; A-588; A-591; A-700 and A-703. 2 Publications
    Mutagenesisi480 – 4801C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-483; A-588; A-591; A-700 and A-703. 2 Publications
    Mutagenesisi483 – 4831C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-588; A-591; A-700 and A-703. 2 Publications
    Mutagenesisi588 – 5881C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-591; A-700 and A-703. 2 Publications
    Mutagenesisi591 – 5911C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-700 and A-703. 2 Publications
    Mutagenesisi700 – 7001C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-703. 2 Publications
    Mutagenesisi703 – 7031C → A: Abolishes disulfide reductase activity; when associated with A-158; A-161; A-480; A-483; A-588; A-591 and A-700. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 793761DnaJ homolog subfamily C member 10PRO_0000281484Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi158 ↔ 161Redox-active
    Disulfide bondi480 ↔ 483Redox-active
    Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi588 ↔ 591Redox-active
    Disulfide bondi700 ↔ 703Redox-active

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9DC23.
    PaxDbiQ9DC23.
    PRIDEiQ9DC23.

    PTM databases

    PhosphoSiteiQ9DC23.

    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

    ArrayExpressiQ9DC23.
    BgeeiQ9DC23.
    CleanExiMM_DNAJC10.
    GenevestigatoriQ9DC23.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi211769. 2 interactions.

    Structurei

    Secondary structure

    1
    793
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 405
    Helixi48 – 6215
    Helixi64 – 663
    Helixi73 – 8715
    Helixi90 – 9910
    Turni100 – 1034
    Helixi115 – 1206
    Beta strandi121 – 1233
    Turni124 – 1274
    Beta strandi131 – 1333
    Helixi136 – 14510
    Beta strandi149 – 1546
    Helixi159 – 17416
    Turni175 – 1784
    Beta strandi179 – 1857
    Turni186 – 1883
    Helixi190 – 1956
    Beta strandi200 – 2078
    Helixi222 – 23413
    Beta strandi237 – 2393
    Helixi242 – 25514
    Beta strandi258 – 2647
    Helixi273 – 28210
    Turni283 – 2864
    Beta strandi287 – 2937
    Turni294 – 2963
    Helixi298 – 3014
    Beta strandi311 – 3144
    Turni322 – 3243
    Helixi325 – 3273
    Beta strandi328 – 3314
    Helixi336 – 34611
    Helixi355 – 3628
    Beta strandi365 – 3728
    Helixi382 – 3865
    Helixi387 – 3915
    Helixi392 – 3943
    Beta strandi396 – 4027
    Helixi403 – 4053
    Helixi407 – 4126
    Beta strandi419 – 4268
    Beta strandi429 – 4335
    Helixi440 – 45112
    Beta strandi455 – 4573
    Turni460 – 4623
    Beta strandi471 – 4766
    Helixi481 – 49616
    Turni497 – 5004
    Beta strandi502 – 5076
    Turni508 – 5103
    Helixi512 – 5176
    Beta strandi522 – 5309
    Beta strandi533 – 5375
    Helixi543 – 55412
    Beta strandi557 – 5604
    Helixi563 – 5697
    Turni570 – 5723
    Beta strandi579 – 5846
    Helixi589 – 60517
    Turni606 – 6083
    Beta strandi609 – 6157
    Turni616 – 6194
    Helixi620 – 6256
    Beta strandi630 – 6378
    Beta strandi641 – 6433
    Helixi657 – 6659
    Beta strandi672 – 6743
    Helixi677 – 6837
    Turni684 – 6863
    Beta strandi691 – 6966
    Helixi701 – 71717
    Turni718 – 7203
    Beta strandi722 – 7276
    Turni728 – 7303
    Helixi732 – 7376
    Beta strandi742 – 75211
    Helixi753 – 7553
    Beta strandi757 – 7637
    Helixi768 – 78013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3APOX-ray2.40A33-793[»]
    3APQX-ray1.84A/B34-242[»]
    3APSX-ray1.90A/B668-789[»]
    ProteinModelPortaliQ9DC23.
    SMRiQ9DC23. Positions 34-782.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9DC23.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 10066JPROSITE-ProRule annotationAdd
    BLAST
    Domaini130 – 232103Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini454 – 553100Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini557 – 665109Thioredoxin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini671 – 776106Thioredoxin 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni235 – 350116Trxb 1Add
    BLAST
    Regioni348 – 463116Trxb 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi790 – 7934Prevents secretion from ERPROSITE-ProRule annotation

    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

    eggNOGiCOG0526.
    GeneTreeiENSGT00730000110455.
    HOGENOMiHOG000231882.
    HOVERGENiHBG057048.
    InParanoidiA2ASA2.
    KOiK09530.
    OMAiYPSLFIF.
    OrthoDBiEOG7RZ5QH.
    TreeFamiTF105169.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    3.40.30.10. 5 hits.
    InterProiIPR001623. DnaJ_domain.
    IPR021170. DnaJ_homolog_subfam-C.
    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

    MGVWLNKDDF IRDLKRISLC LLILYVVVVV GTDQNFYSLL GVSKTASSRE    50
    IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG 100
    EKGLEDNQGG QYESWSYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF 150
    VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS 200
    YPSLFIFRSG MAAVKYNGDR SKESLVAFAM QHVRSTVTEL STGNFVNAIE 250
    TAFAAGVGWL ITFCSKGEDC LTSQTRLRLS GMLDGLVNVG WVDCDAQDSL 300
    CKSLDTTAST TAYFPPGATL NDREKSSVLF LNSLDAKEIY MEIIHNLPDF 350
    ELLSANQLED RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR 400
    FDCSSAPGIC SDLYVFQPCL AVFKGQGTKE YEIHHGKKIL YDILAFAKES 450
    VNSHVTTLGP QNFPASDKEP WLVDFFAPWC PPCRALLPEL RKASTLLYGQ 500
    LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSIHEYEGH HSAEQILEFI 550
    EDLRNPSVVS LTPSTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR 600
    MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSKAYQYHSY 650
    NGWNRDAYSL RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVVDFYAPWC 700
    GPCQNFAPEF ELLARMIKGK VRAGKVDCQA YPQTCQKAGI KAYPSVKLYQ 750
    YERAKKSIWE EQINSRDAKT IAALIYGKLE TLQSQVKRNK DEL 793
    Length:793
    Mass (Da):90,583
    Last modified:July 27, 2011 - v2
    Checksum:i00C88EF3F5497BE1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti91 – 911D → H in BAB23413. (PubMed:16141072)Curated
    Sequence conflicti310 – 3101T → A in AAQ14555. 1 PublicationCurated
    Sequence conflicti324 – 3241E → G in AAH33461. (PubMed:19468303)Curated
    Sequence conflicti433 – 4331I → T in AAH33461. (PubMed:19468303)Curated
    Sequence conflicti538 – 5381E → G in AAQ14555. 1 PublicationCurated
    Sequence conflicti651 – 6522NG → RP in AAQ14555. 1 PublicationCurated
    Sequence conflicti654 – 6541N → NS in AAN73273. (PubMed:12411443)Curated
    Sequence conflicti680 – 6801F → FR in AAN73273. (PubMed:12411443)Curated
    Sequence conflicti767 – 7671D → M in AAQ14555. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS38159.1.
    RefSeqi NP_077143.2. NM_024181.2.
    UniGenei Mm.21762.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3APO X-ray 2.40 A 33-793 [» ]
    3APQ X-ray 1.84 A/B 34-242 [» ]
    3APS X-ray 1.90 A/B 668-789 [» ]
    ProteinModelPortali Q9DC23.
    SMRi Q9DC23. Positions 34-782.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211769. 2 interactions.

    PTM databases

    PhosphoSitei Q9DC23.

    Proteomic databases

    MaxQBi Q9DC23.
    PaxDbi Q9DC23.
    PRIDEi Q9DC23.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028392 ; ENSMUSP00000028392 ; ENSMUSG00000027006 .
    GeneIDi 66861.
    KEGGi mmu:66861.
    UCSCi uc008khj.1. mouse.

    Organism-specific databases

    CTDi 54431.
    MGIi MGI:1914111. Dnajc10.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00730000110455.
    HOGENOMi HOG000231882.
    HOVERGENi HBG057048.
    InParanoidi A2ASA2.
    KOi K09530.
    OMAi YPSLFIF.
    OrthoDBi EOG7RZ5QH.
    TreeFami TF105169.

    Miscellaneous databases

    EvolutionaryTracei Q9DC23.
    NextBioi 322847.
    PROi Q9DC23.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DC23.
    Bgeei Q9DC23.
    CleanExi MM_DNAJC10.
    Genevestigatori Q9DC23.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    3.40.30.10. 5 hits.
    InterProi IPR001623. DnaJ_domain.
    IPR021170. DnaJ_homolog_subfam-C.
    IPR012336. Thioredoxin-like_fold.
    IPR017937. Thioredoxin_CS.
    IPR013766. Thioredoxin_domain.
    [Graphical view ]
    Pfami PF00226. DnaJ. 1 hit.
    PF00085. Thioredoxin. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF52833. SSF52833. 6 hits.
    PROSITEi PS50076. DNAJ_2. 1 hit.
    PS00014. ER_TARGET. 1 hit.
    PS00194. THIOREDOXIN_1. 2 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    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: October 1, 2014
    This is version 107 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

    External Data

    Dasty 3