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Q6NRT6 (DJC10_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily C member 10

EC=1.8.4.-
Gene names
Name:dnajc10
OrganismXenopus laevis (African clawed frog)
Taxonomic identifier8355 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

Protein attributes

Sequence length796 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Domain

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 similarities

Contains 1 J domain.

Contains 4 thioredoxin domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Chain34 – 796763DnaJ homolog subfamily C member 10
PRO_0000281487

Regions

Domain36 – 10065J
Domain131 – 233103Thioredoxin 1
Domain455 – 554100Thioredoxin 2
Domain558 – 668111Thioredoxin 3
Domain672 – 780109Thioredoxin 4
Region236 – 351116Trxb 1
Region349 – 464116Trxb 2
Motif793 – 7964Prevents secretion from ER Potential

Amino acid modifications

Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation7531N-linked (GlcNAc...) Potential
Disulfide bond159 ↔ 162Redox-active By similarity
Disulfide bond481 ↔ 484Redox-active By similarity
Disulfide bond589 ↔ 592Redox-active By similarity
Disulfide bond701 ↔ 704Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NRT6 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F3AB8453C8397F37

FASTA79690,984
        10         20         30         40         50         60 
MKHSLNTATS SSSVLKRTIL YLVLISLAAL VYCDDDYYDL LGVSKAATNR EIRQAFKKLA 

        70         80         90        100        110        120 
LKLHPDKNKD PDAHNKFLKI NRAYEVLKDE DLRKKYDKYG EKGLDEQNQG GGYQSWSYYR 

       130        140        150        160        170        180 
YDFGIYDDDL EIITLDRGEF DGAVNSGELW FINFYSPGCS HCHDLAPTWR QFAKEMDGLL 

       190        200        210        220        230        240 
RIGAVNCGDN RMLCRSQGIN SYPNLYIFKS GMNPVKYYGE RSKERLVNFA MPYISSTVTE 

       250        260        270        280        290        300 
LWAGNFRSSI EDAFSSGVGW LITFCSDTGD CLNSQTRSKL AGLLEGLVKV GWMDCATQGD 

       310        320        330        340        350        360 
LCDNLEITSS ATVYFPPGST LTDKENGDVL FLNSLDAREI YKEVLNHLPD LETISPESLQ 

       370        380        390        400        410        420 
GKLSHHRWLL FFTFGTDEQS SLPEFKKLTV HLRSEHVQVG KFDCYSSPSI CSELYIHKPC 

       430        440        450        460        470        480 
VAAFKGKGIS AYEIHHGKVQ LYDLVSFAKE SVNSHVITLG PTNFPGKDRD TWLVDFFAPW 

       490        500        510        520        530        540 
CPPCRALLPE LRIASKRLFG QIKFGTLDCT IHEGLCNMHN IRAYPTTVVF NHSNIHEYAG 

       550        560        570        580        590        600 
HNNAEEILEF IEDLRNPSVV TLTPETFQSL VRNRRGDEMW MVDFYAPWCG PCQALMPEWK 

       610        620        630        640        650        660 
RMARHINGLI SVGSIDCQKY SLFCTQERVN GYPEIRLYPA NINPQHTYYR YTGWHRDSQS 

       670        680        690        700        710        720 
LRNWALMYLP KASFDLTPES FHEHVINGKD NWVLDFYAPW CGPCQNFNPE FEILARAVKG 

       730        740        750        760        770        780 
KIKAGKVNCQ AYEHLCNSAS IRSYPTVRLY PYNGSKKKDY FGEQIDSRDA KEIAQIITKR 

       790 
IEAIKRVKEA YNKDEL 

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC070632 mRNA. Translation: AAH70632.1.
RefSeqNP_001084933.1. NM_001091464.1.
UniGeneXl.47147.

3D structure databases

ProteinModelPortalQ6NRT6.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID431990.
KEGGxla:431990.

Organism-specific databases

CTD54431.
XenbaseXB-GENE-981000. dnajc10.

Phylogenomic databases

HOVERGENHBG057048.
KOK09530.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
3.40.30.10. 4 hits.
InterProIPR001623. DnaJ_domain.
IPR021170. DnaJ_homolog_subfam-C.
IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
PF00085. Thioredoxin. 4 hits.
[Graphical view]
PIRSFPIRSF037293. DnaJ_homolog_subfam-C. 1 hit.
PRINTSPR00625. JDOMAIN.
PR00421. THIOREDOXIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF52833. SSF52833. 6 hits.
PROSITEPS50076. DNAJ_2. 1 hit.
PS00014. ER_TARGET. 1 hit.
PS00194. THIOREDOXIN_1. 3 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDJC10_XENLA
AccessionPrimary (citable) accession number: Q6NRT6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families