Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DnaJ homolog subfamily C member 10

Gene

dnajc10

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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. 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
Complete GO annotation...

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
Complete GO annotation...

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

        10         20         30         40         50
MKHSLNTATS SSSVLKRTIL YLVLISLAAL VYCDDDYYDL LGVSKAATNR
60 70 80 90 100
EIRQAFKKLA LKLHPDKNKD PDAHNKFLKI NRAYEVLKDE DLRKKYDKYG
110 120 130 140 150
EKGLDEQNQG GGYQSWSYYR YDFGIYDDDL EIITLDRGEF DGAVNSGELW
160 170 180 190 200
FINFYSPGCS HCHDLAPTWR QFAKEMDGLL RIGAVNCGDN RMLCRSQGIN
210 220 230 240 250
SYPNLYIFKS GMNPVKYYGE RSKERLVNFA MPYISSTVTE LWAGNFRSSI
260 270 280 290 300
EDAFSSGVGW LITFCSDTGD CLNSQTRSKL AGLLEGLVKV GWMDCATQGD
310 320 330 340 350
LCDNLEITSS ATVYFPPGST LTDKENGDVL FLNSLDAREI YKEVLNHLPD
360 370 380 390 400
LETISPESLQ GKLSHHRWLL FFTFGTDEQS SLPEFKKLTV HLRSEHVQVG
410 420 430 440 450
KFDCYSSPSI CSELYIHKPC VAAFKGKGIS AYEIHHGKVQ LYDLVSFAKE
460 470 480 490 500
SVNSHVITLG PTNFPGKDRD TWLVDFFAPW CPPCRALLPE LRIASKRLFG
510 520 530 540 550
QIKFGTLDCT IHEGLCNMHN IRAYPTTVVF NHSNIHEYAG HNNAEEILEF
560 570 580 590 600
IEDLRNPSVV TLTPETFQSL VRNRRGDEMW MVDFYAPWCG PCQALMPEWK
610 620 630 640 650
RMARHINGLI SVGSIDCQKY SLFCTQERVN GYPEIRLYPA NINPQHTYYR
660 670 680 690 700
YTGWHRDSQS LRNWALMYLP KASFDLTPES FHEHVINGKD NWVLDFYAPW
710 720 730 740 750
CGPCQNFNPE FEILARAVKG KIKAGKVNCQ AYEHLCNSAS IRSYPTVRLY
760 770 780 790
PYNGSKKKDY FGEQIDSRDA KEIAQIITKR IEAIKRVKEA YNKDEL
Length:796
Mass (Da):90,984
Last modified:July 5, 2004 - v1
Checksum:iF3AB8453C8397F37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
BC070632 mRNA. Translation: AAH70632.1.
RefSeqiNP_001084933.1. NM_001091464.1.
UniGeneiXl.47147.

3D structure databases

ProteinModelPortaliQ6NRT6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi431990.
KEGGixla:431990.

Organism-specific databases

CTDi54431.
XenbaseiXB-GENE-981000. dnajc10.

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]
ProtoNetiSearch...

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

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 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.