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Q5R5L3 (DJC10_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length793 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, 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.

Subunit structure

Interacts with HSPA5 (via its J domain). Interacts with EDEM1 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 – 3232 Potential
Chain33 – 793761DnaJ homolog subfamily C member 10
PRO_0000281485

Regions

Domain35 – 10066J
Domain130 – 232103Thioredoxin 1
Domain454 – 553100Thioredoxin 2
Domain557 – 662106Thioredoxin 3
Domain671 – 778108Thioredoxin 4
Region235 – 350116Trxb 1
Region348 – 463116Trxb 2
Motif790 – 7934Prevents secretion from ER Potential

Amino acid modifications

Glycosylation5301N-linked (GlcNAc...) Potential
Disulfide bond158 ↔ 161Redox-active By similarity
Disulfide bond480 ↔ 483Redox-active By similarity
Disulfide bond588 ↔ 591Redox-active By similarity
Disulfide bond700 ↔ 703Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R5L3 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: FADC1167FC65121E

FASTA79390,951
        10         20         30         40         50         60 
MGVWLSKDDY IRDLKRIILC FLIVYMAILV GTEQDFYSLL GVSKTASSRE IRQAFKKLAL 

        70         80         90        100        110        120 
KLHPDKNPNN PNAHGNFLKI NRAYEVLKDE DLRKKYDKYG EKGLEDNQGG QYESWNYYRY 

       130        140        150        160        170        180 
DFGIYDDDPE IITLERREFD AAVNSGELWF VNFYSPGCSH CHDLAPTWRD FAKEVDGLLR 

       190        200        210        220        230        240 
IGAVNCGDDR MLCRMKGVNS YPSLFIFRSG MAPVKYHGDR SKESLVSFAM QHVRSTVTEL 

       250        260        270        280        290        300 
WTGNFVNSIQ TAFAAGIGWL ITFCSKGGDC LTSQTRLRLS GMLDGLVNVG WMDCATQDNL 

       310        320        330        340        350        360 
CKSLDITTST TAYFPPGATL NNKEKNSILF LNSLDAKEIY LEVIHNLPDF ELLSAHTLED 

       370        380        390        400        410        420 
RLAHHRWLLF FHFGKNENSN DPELKKLKTL LKNDHIQVGR FDCSSAPDIC SNLYVFQPSL 

       430        440        450        460        470        480 
AVFKGQGTKE YEIHHGKKIL YDILAFAKES VNSHVTTLGP QNFPANDKEP WLVDFFAPWC 

       490        500        510        520        530        540 
PPCRALLPEL RRASNLLYGQ LKFGTLDCTV HEGLCNMYNI QAYPTTVVFN QSNIHEYEGH 

       550        560        570        580        590        600 
HSAEQILEFI EDLMNPSVVS LTPTTFNELV TQRKHNEVWM VDFYSPWCHP CQVLMPEWKR 

       610        620        630        640        650        660 
MARTLTGLIN VGSIDCQQYH SFCAQENVQR YPEIRFFPPK SNKAYQYHSY NGWNRDAYSL 

       670        680        690        700        710        720 
RIWGLGFLPQ VSTGLTPQTF SEKVLQGKNH WVIDFYAPWC GPCQNFAPEF ELLARMIKGK 

       730        740        750        760        770        780 
VKAGKVDCQA YAQTCQKAGI RAYPTVKFYF YESAKRTFQE EQINIRDAKA IAALINEKLE 

       790 
TLQNQGKRNK DEL 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860844 mRNA. Translation: CAH92953.1.
RefSeqNP_001126740.1. NM_001133268.1.
UniGenePab.5348.

3D structure databases

ProteinModelPortalQ5R5L3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173742.
KEGGpon:100173742.

Organism-specific databases

CTD54431.

Phylogenomic databases

HOVERGENHBG057048.
InParanoidQ5R5L3.
KOK09530.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
3.40.30.10. 5 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. 2 hits.
PS51352. THIOREDOXIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDJC10_PONAB
AccessionPrimary (citable) accession number: Q5R5L3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: December 21, 2004
Last modified: February 19, 2014
This is version 71 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