background:
DnaJ-like proteins interact with HSP 70 molecular chaperones and function to facilitate protein folding and mitochondrial protein import. HSP 40-4, also known as HDJ2, is the human DnaJ homolog that functions as a co-chaperone with a cysteine-rich zinc finger domain. The cellular redox enzyme thioredoxin interacts with HSP 40-4, and oxidation and reduction reversibly regulate HSP 40-4 function in response to the changing redox states of the cell. The zinc finger domain of HSP 40-4 may act as a redox sensor of chaperone-mediated protein-folding machinery, since HSP 40-4 inactivation leads to the oxidation of cysteine thiols and a simultaneous release of coordinated zinc. Loss of the HSP 40-4 protein may be linked to severe defects in spermatogenesis that involve aberrant androgen signaling.
Function:
Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria.
Subcellular Location:
Membrane.
Similarity:
Contains 1 CR-type zinc finger.
Contains 1 J domain.
Database links:
Entrez Gene: 3301 Human
Entrez Gene: 15502 Mouse
Entrez Gene: 10052408 Pig
Entrez Gene: 65028 Rat
Omim: 602837 Human
SwissProt: P31689 Human
SwissProt: P63037 Mouse
SwissProt: P63036 Rat
Unigene: 445203 Human
Unigene: 27897 Mouse
Unigene: 64562 Rat
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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