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Q498R3

- DJC10_RAT

UniProt

Q498R3 - DJC10_RAT

Protein

DnaJ homolog subfamily C member 10

Gene

Dnajc10

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 2 (20 Mar 2007)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. ATPase activator activity Source: Ensembl
    2. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
    3. 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: Ensembl
    4. negative regulation of protein phosphorylation Source: Ensembl
    5. protein folding in endoplasmic reticulum Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DnaJ homolog subfamily C member 10 (EC:1.8.4.-)
    Gene namesi
    Name:Dnajc10
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 3

    Organism-specific databases

    RGDi1307813. Dnajc10.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 793761DnaJ homolog subfamily C member 10PRO_0000281486Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ498R3.
    PRIDEiQ498R3.

    PTM databases

    PhosphoSiteiQ498R3.

    Expressioni

    Gene expression databases

    GenevestigatoriQ498R3.

    Interactioni

    Subunit structurei

    Interacts with HSPA5 (via its J domain). Interacts with EDEM1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ498R3. 5 interactions.
    MINTiMINT-4572149.
    STRINGi10116.ENSRNOP00000009839.

    Structurei

    3D structure databases

    ProteinModelPortaliQ498R3.
    ModBaseiSearch...
    MobiDBiSearch...

    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.By similarity
    The thioredoxin-like regions Trxb 1 and 2 lack a redox-active CXXC motif.By similarity

    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.
    InParanoidiQ498R3.
    KOiK09530.
    OMAiYPSLFIF.
    OrthoDBiEOG7RZ5QH.
    PhylomeDBiQ498R3.
    TreeFamiTF105169.

    Family and domain databases

    Gene3Di1.10.287.110. 1 hit.
    3.40.30.10. 4 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.

    Q498R3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVWLNRDEF IRDVKRISLC LLVLYVVIVV GTDQNFYSLL GVSKTASSRE    50
    IRQAFKKLAL KLHPDKNPNN PNAHGDFLKI NRAYEVLKDE DLRKKYDKYG 100
    EKGLEDNQGG QYESWSYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF 150
    VNFYSPGCSH CHDLAPTWRE FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS 200
    YPSLFIFRSG MAAVKYNGDR SKESLVSFAM QHVRTTVTEL STGNFVNAIE 250
    TAFAAGIGWL ITFCFKGEDC LTPQTRLRLS GMLDGLVNVG WVDCDTQDSL 300
    CKSLDATAST TAYFPPGATL NNKEKSSVLF LNSLDAKEIY MEIIHNLPDF 350
    ELLSANKLED RLAHHRWLVF FHFGKNENAN DPELKKLKTL LKNEHIQVGR 400
    FDCSSAPGIC SDLYVFQSCL AVFKGQGTKE YEIHHGKKIL YDILAFAKES 450
    VNSHVTTLGP QNFPASDKEP WLVDFFAPWC PPCRALLPEL RKASTLLYGQ 500
    LKVGTLDCTI HEGLCNMYNI QAYPTTVVFN QSSVHEYEGH HSAEQILEFI 550
    EDLRNPSVVS LTPTTFNELV KQRKHDEVWM VDFYSPWCHP CQVLMPEWKR 600
    MARTLTGLIN VGSVDCQQYH SFCTQENVQR YPEIRFYPQK SSRAYQYHSY 650
    NGWNRDAYSL RSWGLGFLPQ ASIDLTPQTF NEKVLQGKTH WVIDFYAPWC 700
    GPCQNFAPEF ELLARMIKGK VKAGKVDCQA YPQTCQKAGI RAYPSVKLYL 750
    YERAKKSIWE EQINSRDAKT IAALIYGKLE TFQSQVKRNK DEL 793
    Length:793
    Mass (Da):90,747
    Last modified:March 20, 2007 - v2
    Checksum:i9578A69C36C858C9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03024291 Genomic DNA. No translation available.
    BC100105 mRNA. Translation: AAI00106.1.
    RefSeqiNP_001099956.2. NM_001106486.2.
    UniGeneiRn.8642.

    Genome annotation databases

    EnsembliENSRNOT00000009839; ENSRNOP00000009839; ENSRNOG00000006803.
    GeneIDi295690.
    KEGGirno:295690.
    UCSCiRGD:1307813. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AABR03024291 Genomic DNA. No translation available.
    BC100105 mRNA. Translation: AAI00106.1 .
    RefSeqi NP_001099956.2. NM_001106486.2.
    UniGenei Rn.8642.

    3D structure databases

    ProteinModelPortali Q498R3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q498R3. 5 interactions.
    MINTi MINT-4572149.
    STRINGi 10116.ENSRNOP00000009839.

    PTM databases

    PhosphoSitei Q498R3.

    Proteomic databases

    PaxDbi Q498R3.
    PRIDEi Q498R3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000009839 ; ENSRNOP00000009839 ; ENSRNOG00000006803 .
    GeneIDi 295690.
    KEGGi rno:295690.
    UCSCi RGD:1307813. rat.

    Organism-specific databases

    CTDi 54431.
    RGDi 1307813. Dnajc10.

    Phylogenomic databases

    eggNOGi COG0526.
    GeneTreei ENSGT00730000110455.
    HOGENOMi HOG000231882.
    HOVERGENi HBG057048.
    InParanoidi Q498R3.
    KOi K09530.
    OMAi YPSLFIF.
    OrthoDBi EOG7RZ5QH.
    PhylomeDBi Q498R3.
    TreeFami TF105169.

    Miscellaneous databases

    NextBioi 639891.
    PROi Q498R3.

    Gene expression databases

    Genevestigatori Q498R3.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    3.40.30.10. 4 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. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "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] OF 262-793.
      Tissue: Spleen.

    Entry informationi

    Entry nameiDJC10_RAT
    AccessioniPrimary (citable) accession number: Q498R3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 88 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3