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PMID:12446677

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Citation

Hosoda, A, Kimata, Y, Tsuru, A and Kohno, K (2003) JPDI, a novel endoplasmic reticulum-resident protein containing both a BiP-interacting J-domain and thioredoxin-like motifs. J. Biol. Chem. 278:2669-76

Abstract

Several endoplasmic reticulum (ER)-resident luminal proteins have a characteristic ER retrieval signal, KDEL, or its variants at their C terminus. Our previous work searching EST databases for proteins containing the C-terminal KDEL motif predicted some novel murine proteins, one of which designated JPDI (J-domain-containing protein disulfide isomerase-like protein) is characterized in this study. The primary structure of JPDI is unique, because in addition to a J-domain motif adjacent to the N-terminal translocation signal sequence, four thioredoxin-like motifs were found in a single polypeptide. As examined by Northern blotting, the expression of JPDI was essentially ubiquitous in tissues and almost independent of ER stress. A computational prediction that JPDI is an ER-resident luminal protein was experimentally supported by immunofluorescent staining of epitope-tagged JPDI-expressing cells together with glycosylation and protease protection studies of this protein. JPDI probably acts as a DnaJ-like partner of BiP, because a recombinant protein carrying the J-domain of JPDI associated with BiP in an ATP-dependent manner and enhanced its ATPase activity. We speculate that for the folding of some proteins in the ER, chaperoning by BiP and formation of proper disulfide bonds may synchronously occur in a JPDI-dependent manner.

Links

PubMed Online version:10.1074/jbc.M208346200

Keywords

3T3 Cells; Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Motifs; Amino Acid Sequence; Animals; Blotting, Northern; Carrier Proteins/chemistry; Carrier Proteins/metabolism; Endoplasmic Reticulum/metabolism; Glutathione Transferase/metabolism; HSP40 Heat-Shock Proteins; HeLa Cells; Heat-Shock Proteins; Humans; Hydrolysis; Mice; Microscopy, Fluorescence; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Molecular Sequence Data; Protein Binding; Protein Biosynthesis; Protein Structure, Tertiary; Proteins/chemistry; Proteins/physiology; RNA, Messenger/metabolism; Recombinant Fusion Proteins/metabolism; Recombinant Proteins/metabolism; Reverse Transcriptase Polymerase Chain Reaction; Sequence Homology, Amino Acid; Thioredoxins/chemistry; Time Factors; Tissue Distribution

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

MESAU:BIP

enables

GO:0016887: ATP hydrolysis activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

MESAU:BIP

located_in

GO:0043231: intracellular membrane-bounded organelle

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

MESAU:BIP

enables

GO:0019904: protein domain specific binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:Q9DC23

F

Seeded From UniProt

complete

MOUSE:DJC10

located_in

GO:0005783: endoplasmic reticulum

ECO:0000314: direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

MOUSE:DJC10

enables

GO:0001671: ATPase activator activity

ECO:0000315: mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

MOUSE:DJC10

involved_in

GO:0032781: positive regulation of ATP-dependent activity

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

MOUSE:DJC10

enables

GO:0051117: ATPase binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P07823

F

Seeded From UniProt

complete


See also

References

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