Dnaja1 - DnaJ heat shock protein family (Hsp40) member A1 (house mouse)
Gene
Symbol
Taxonomy
Dates
- Create:2016-09-14
- Modify:2025-01-29
Description
The protein encoded by the Dnaja1 gene is a member of the DnaJ family, whose members act as cochaperones of heat shock protein 70. Heat shock proteins facilitate protein folding, trafficking, prevention of aggregation, and proteolytic degradation. Members of this family are characterized by a highly conserved N-terminal J domain, a glycine/phenylalanine-rich region, four CxxCxGxG zinc finger repeats, and a C-terminal substrate-binding domain. The J domain mediates the interaction with heat shock protein 70 to recruit substrates and regulate ATP hydrolysis activity. Mice deficient for this gene display reduced levels of activation‐induced deaminase, an enzyme that deaminates deoxycytidine at the immunoglobulin genes during immune responses. In addition, mice lacking this gene exhibit severe defects in spermatogenesis. Several pseudogenes of this gene are found on other chromosomes. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Sep 2015]
Predicted to enable several functions, including C3HC4-type RING finger domain binding activity; Hsp70 protein binding activity; and signaling receptor binding activity. Acts upstream of or within androgen receptor signaling pathway; flagellated sperm motility; and spermatogenesis. Predicted to be located in membrane and microtubule cytoskeleton. Predicted to be active in cytosol. Is expressed in several structures, including 1st branchial arch mandibular component; alimentary system; brain; genitourinary system; and hemolymphoid system. Orthologous to human DNAJA1 (DnaJ heat shock protein family (Hsp40) member A1).
- HSJ-2
- Hsj2
- Nedd7
- dnaJ homolog subfamily A member 1
- DnaJ (Hsp40) homolog, subfamily A, member 1
- dnaJ protein homolog 2
- heat shock 40 kDa protein 4
- heat shock protein J2
- heat shock protein, Dnaj-like 2
- neural precursor cell expressed, developmentally down-regulated gene 7
Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis.
Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605
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