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Q91YW3 (DNJC3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DnaJ homolog subfamily C member 3
Alternative name(s):
Interferon-induced, double-stranded RNA-activated protein kinase inhibitor
Protein kinase inhibitor of 58 kDa
Short name=Protein kinase inhibitor p58
Gene names
Name:Dnajc3
Synonyms:P58ipk
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity. Ref.3 Ref.4

Subunit structure

Interacts with EIF2AK2. Forms a trimeric complex with DNAJB1 and HSPA8. Interacts with PRKRIR/P52RIPK By similarity. Interacts with EIF2AK3. Ref.3

Subcellular location

Endoplasmic reticulum Ref.3.

Tissue specificity

Widely expressed, with high level in the liver. Ref.1

Induction

Up-regulated during an endoplasmic reticulum stress. Ref.3

Domain

The J domain mediates interaction with HSPA8 By similarity.

Binding to misfolded proteins is mediated by a hydrophobic patch forming a large groove within the first two TPR repeats.

Sequence similarities

Contains 1 J domain.

Contains 9 TPR repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSPA5P110212EBI-8381770,EBI-354921From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 504473DnaJ homolog subfamily C member 3
PRO_0000071046

Regions

Repeat37 – 7034TPR 1
Repeat72 – 10433TPR 2
Repeat105 – 13834TPR 3
Repeat154 – 18734TPR 4
Repeat188 – 22134TPR 5
Repeat222 – 25534TPR 6
Repeat268 – 30134TPR 7
Repeat306 – 33934TPR 8
Repeat340 – 37334TPR 9
Domain394 – 46269J
Region375 – 39319Flexible linker By similarity

Amino acid modifications

Disulfide bond248 ↔ 258 By similarity
Disulfide bond313 ↔ 329 By similarity

Experimental info

Mutagenesis481L → D: Reduces binding affinity for misfolded proteins by 40%. Ref.4
Mutagenesis711Y → A: Reduces binding affinity for misfolded proteins by 40%. Ref.4
Mutagenesis751Y → H: Reduces binding affinity for misfolded proteins by 40%. Ref.4
Mutagenesis1041F → A: Reduces binding affinity for misfolded proteins by 40%. Ref.4
Mutagenesis1861W → A: Doesn't affect binding of misfolded proteins. Ref.4
Sequence conflict89 – 913AAL → RRV in AAC52592. Ref.1
Sequence conflict1341S → C in AAC52592. Ref.1
Sequence conflict4051A → T in AAC52592. Ref.1

Secondary structure

....................................... 504
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q91YW3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 510C27782C6EDF66

FASTA50457,464
        10         20         30         40         50         60 
MVAPGSVGSR LGAVFPFLLV LVDLQYEGAE CGVNADVEKH LELGKKLLAA GQLADALSQF 

        70         80         90        100        110        120 
HAAVDGDPDN YIAYYRRATV FLAMGKSKAA LPDLTKVIAL KMDFTAARLQ RGHLLLKQGK 

       130        140        150        160        170        180 
LDEAEDDFKK VLKSNPSEQE EKEAESQLVK ADEMQRLRSQ ALDAFDGADY TAAITFLDKI 

       190        200        210        220        230        240 
LEVCVWDAEL RELRAECFIK EGEPRKAISD LKAASKLKSD NTEAFYKIST LYYQLGDHEL 

       250        260        270        280        290        300 
SLSEVRECLK LDQDHKRCFA HYKQVKKLNK LIESAEELIR DGRYTDATSK YESVMKTEPS 

       310        320        330        340        350        360 
VAEYTVRSKE RICHCFSKDE KPVEAIRICS EVLQMEPDNV NALKDRAEAY LIEEMYDEAI 

       370        380        390        400        410        420 
QDYEAAQEHN ENDQQIREGL EKAQRLLKQS QKRDYYKILG VKRNAKKQEI IKAYRKLALQ 

       430        440        450        460        470        480 
WHPDNFQNEE EKKKAEKKFI DIAAAKEVLS DPEMRKKFDD GEDPLDAESQ QGGGGNPFHR 

       490        500 
SWNSWQGFNP FSSGGPFRFK FHFN 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase."
Korth M.J., Lyons C.N., Wambach M., Katze M.G.
Gene 170:181-188(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Czech II.
Tissue: Mammary tumor.
[3]"Control of PERK eIF2alpha kinase activity by the endoplasmic reticulum stress-induced molecular chaperone P58IPK."
Yan W., Frank C.L., Korth M.J., Sopher B.L., Novoa I., Ron D., Katze M.G.
Proc. Natl. Acad. Sci. U.S.A. 99:15920-15925(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF2AK3, INDUCTION.
[4]"Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPR."
Tao J., Petrova K., Ron D., Sha B.
J. Mol. Biol. 397:1307-1315(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.51 ANGSTROMS) OF 35-393, FUNCTION, MUTAGENESIS OF LEU-48; TYR-71; TYR-75; PHE-104 AND TRP-186.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28423 mRNA. Translation: AAC52592.1.
BC013766 mRNA. Translation: AAH13766.1.
CCDSCCDS37012.1.
RefSeqNP_032955.2. NM_008929.3.
UniGeneMm.12616.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3IEGX-ray2.51A/B35-393[»]
ProteinModelPortalQ91YW3.
SMRQ91YW3. Positions 35-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid781938. 1 interaction.
IntActQ91YW3. 4 interactions.
MINTMINT-1838284.

PTM databases

PhosphoSiteQ91YW3.

2D gel databases

REPRODUCTION-2DPAGEQ91YW3.

Proteomic databases

MaxQBQ91YW3.
PaxDbQ91YW3.
PRIDEQ91YW3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022734; ENSMUSP00000022734; ENSMUSG00000022136.
GeneID100037258.
KEGGmmu:100037258.
UCSCuc007uzd.2. mouse.

Organism-specific databases

CTD5611.
MGIMGI:107373. Dnajc3.

Phylogenomic databases

eggNOGCOG0484.
GeneTreeENSGT00720000108760.
HOGENOMHOG000193351.
HOVERGENHBG053820.
InParanoidQ91YW3.
KOK09523.
OMAQSERRDY.
OrthoDBEOG70KGPH.
PhylomeDBQ91YW3.
TreeFamTF105162.

Gene expression databases

ArrayExpressQ91YW3.
BgeeQ91YW3.
GenevestigatorQ91YW3.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
1.25.40.10. 3 hits.
InterProIPR001623. DnaJ_domain.
IPR026901. DNAJC3.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR001440. TPR_1.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR24078:SF165. PTHR24078:SF165. 1 hit.
PfamPF00226. DnaJ. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
SM00028. TPR. 7 hits.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
PROSITEPS50076. DNAJ_2. 1 hit.
PS50005. TPR. 8 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ91YW3.
NextBio444137.
PROQ91YW3.
SOURCESearch...

Entry information

Entry nameDNJC3_MOUSE
AccessionPrimary (citable) accession number: Q91YW3
Secondary accession number(s): Q60873
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 109 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot