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Q6NRT6

- DJC10_XENLA

UniProt

Q6NRT6 - DJC10_XENLA

Protein

DnaJ homolog subfamily C member 10

Gene

dnajc10

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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. Also involved in endoplasmic reticulum-associated degradation (ERAD) by reducing incorrect disulfide bonds in misfolded glycoproteins By similarity.By similarity

    GO - Molecular functioni

    1. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: UniProtKB
    2. 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. 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
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-981000. dnajc10.

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 796763DnaJ homolog subfamily C member 10PRO_0000281487Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi159 ↔ 162Redox-activePROSITE-ProRule annotation
    Disulfide bondi481 ↔ 484Redox-activePROSITE-ProRule annotation
    Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi589 ↔ 592Redox-activePROSITE-ProRule annotation
    Disulfide bondi701 ↔ 704Redox-activePROSITE-ProRule annotation
    Glycosylationi753 – 7531N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliQ6NRT6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 10065JPROSITE-ProRule annotationAdd
    BLAST
    Domaini131 – 233103Thioredoxin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini455 – 554100Thioredoxin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini558 – 668111Thioredoxin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini672 – 780109Thioredoxin 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni236 – 351116Trxb 1Add
    BLAST
    Regioni349 – 464116Trxb 2Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi793 – 7964Prevents 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

    HOVERGENiHBG057048.
    KOiK09530.

    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. 3 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q6NRT6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKHSLNTATS SSSVLKRTIL YLVLISLAAL VYCDDDYYDL LGVSKAATNR    50
    EIRQAFKKLA LKLHPDKNKD PDAHNKFLKI NRAYEVLKDE DLRKKYDKYG 100
    EKGLDEQNQG GGYQSWSYYR YDFGIYDDDL EIITLDRGEF DGAVNSGELW 150
    FINFYSPGCS HCHDLAPTWR QFAKEMDGLL RIGAVNCGDN RMLCRSQGIN 200
    SYPNLYIFKS GMNPVKYYGE RSKERLVNFA MPYISSTVTE LWAGNFRSSI 250
    EDAFSSGVGW LITFCSDTGD CLNSQTRSKL AGLLEGLVKV GWMDCATQGD 300
    LCDNLEITSS ATVYFPPGST LTDKENGDVL FLNSLDAREI YKEVLNHLPD 350
    LETISPESLQ GKLSHHRWLL FFTFGTDEQS SLPEFKKLTV HLRSEHVQVG 400
    KFDCYSSPSI CSELYIHKPC VAAFKGKGIS AYEIHHGKVQ LYDLVSFAKE 450
    SVNSHVITLG PTNFPGKDRD TWLVDFFAPW CPPCRALLPE LRIASKRLFG 500
    QIKFGTLDCT IHEGLCNMHN IRAYPTTVVF NHSNIHEYAG HNNAEEILEF 550
    IEDLRNPSVV TLTPETFQSL VRNRRGDEMW MVDFYAPWCG PCQALMPEWK 600
    RMARHINGLI SVGSIDCQKY SLFCTQERVN GYPEIRLYPA NINPQHTYYR 650
    YTGWHRDSQS LRNWALMYLP KASFDLTPES FHEHVINGKD NWVLDFYAPW 700
    CGPCQNFNPE FEILARAVKG KIKAGKVNCQ AYEHLCNSAS IRSYPTVRLY 750
    PYNGSKKKDY FGEQIDSRDA KEIAQIITKR IEAIKRVKEA YNKDEL 796
    Length:796
    Mass (Da):90,984
    Last modified:July 5, 2004 - v1
    Checksum:iF3AB8453C8397F37
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC070632 mRNA. Translation: AAH70632.1.
    RefSeqiNP_001084933.1. NM_001091464.1.
    UniGeneiXl.47147.

    Genome annotation databases

    GeneIDi431990.
    KEGGixla:431990.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC070632 mRNA. Translation: AAH70632.1 .
    RefSeqi NP_001084933.1. NM_001091464.1.
    UniGenei Xl.47147.

    3D structure databases

    ProteinModelPortali Q6NRT6.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 431990.
    KEGGi xla:431990.

    Organism-specific databases

    CTDi 54431.
    Xenbasei XB-GENE-981000. dnajc10.

    Phylogenomic databases

    HOVERGENi HBG057048.
    KOi K09530.

    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. 3 hits.
    PS51352. THIOREDOXIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. NIH - Xenopus Gene Collection (XGC) project
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryo.

    Entry informationi

    Entry nameiDJC10_XENLA
    AccessioniPrimary (citable) accession number: Q6NRT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3