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Q5R5L3

- DJC10_PONAB

UniProt

Q5R5L3 - DJC10_PONAB

Protein

DnaJ homolog subfamily C member 10

Gene

DNAJC10

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (21 Dec 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, 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. 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
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    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 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 793761DnaJ homolog subfamily C member 10PRO_0000281485Add
    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

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R5L3.
    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 – 662106Thioredoxin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini671 – 778108Thioredoxin 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

    HOVERGENiHBG057048.
    InParanoidiQ5R5L3.
    KOiK09530.

    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.

    Q5R5L3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVWLSKDDY IRDLKRIILC FLIVYMAILV GTEQDFYSLL GVSKTASSRE    50
    IRQAFKKLAL KLHPDKNPNN PNAHGNFLKI NRAYEVLKDE DLRKKYDKYG 100
    EKGLEDNQGG QYESWNYYRY DFGIYDDDPE IITLERREFD AAVNSGELWF 150
    VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR IGAVNCGDDR MLCRMKGVNS 200
    YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL WTGNFVNSIQ 250
    TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL 300
    CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF 350
    ELLSAHTLED RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR 400
    FDCSSAPDIC SNLYVFQPSL AVFKGQGTKE YEIHHGKKIL YDILAFAKES 450
    VNSHVTTLGP QNFPANDKEP WLVDFFAPWC PPCRALLPEL RRASNLLYGQ 500
    LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH HSAEQILEFI 550
    EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR 600
    MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYQYHSY 650
    NGWNRDAYSL RIWGLGFLPQ VSTGLTPQTF SEKVLQGKNH WVIDFYAPWC 700
    GPCQNFAPEF ELLARMIKGK VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF 750
    YESAKRTFQE EQINIRDAKA IAALINEKLE TLQNQGKRNK DEL 793
    Length:793
    Mass (Da):90,951
    Last modified:December 21, 2004 - v1
    Checksum:iFADC1167FC65121E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860844 mRNA. Translation: CAH92953.1.
    RefSeqiNP_001126740.1. NM_001133268.1.
    UniGeneiPab.5348.

    Genome annotation databases

    GeneIDi100173742.
    KEGGipon:100173742.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR860844 mRNA. Translation: CAH92953.1 .
    RefSeqi NP_001126740.1. NM_001133268.1.
    UniGenei Pab.5348.

    3D structure databases

    ProteinModelPortali Q5R5L3.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100173742.
    KEGGi pon:100173742.

    Organism-specific databases

    CTDi 54431.

    Phylogenomic databases

    HOVERGENi HBG057048.
    InParanoidi Q5R5L3.
    KOi K09530.

    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. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiDJC10_PONAB
    AccessioniPrimary (citable) accession number: Q5R5L3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 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