hsp-3 encodes one of two C. elegans heat shock response 70 (hsp70) proteins homologous to mammalian grp78/BiP (glucose regulated protein 78/immunoglobulin heavy chain-binding protein, OMIM:138120); HSP-3 likely functions as a molecular chaperone, and is expressed constitutively (expression is not heat inducible) throughout development with greatest abundance during the L1 larval stage; hsp-3 transcription is, however, upregulated in response to endoplasmic reticulum stress induced by dithiothreitol (DTT) or tunicamycin; HSP-3 contains a long hydrophobic amino terminus and a carboxyl terminal KDEL sequence suggesting that it may be retained in the endoplasmic reticulum.
Predicted to enable ATP hydrolysis activity; heat shock protein binding activity; and protein folding chaperone. Involved in IRE1-mediated unfolded protein response. Predicted to be located in endoplasmic reticulum lumen; membrane; and nucleus. Predicted to be part of endoplasmic reticulum chaperone complex. Expressed in several structures, including germ line; hypodermis; intestinal muscle; pharyngeal-intestinal valve; and tail. Human ortholog(s) of this gene implicated in several diseases, including dopamine beta-hydroxylase deficiency; inflammatory bowel disease; and rheumatoid arthritis. Is an ortholog of human HSPA5 (heat shock protein family A (Hsp70) member 5).
Map position created from combination of previous interpolated map position (based on known location of sequence) and allele information. Therefore this is not a genetic map position based on recombination frequencies or genetic experiments. This was done on advice of the CGC.