BiP, Hsc3, Hsc70, Grp78, Hsc-70-3
Please see the JBrowse view of Dmel\Hsc70-3 for information on other features
To submit a correction to a gene model please use the Contact FlyBase form
AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.
Gene model reviewed during 5.51
Low-frequency RNA-Seq exon junction(s) not annotated.
Annotated transcripts do not represent all supported alternative splices within 5' UTR.
Gene model reviewed during 5.55
The group(s) of polypeptides indicated below share identical sequence to each other.
AMPylation at Thr-518 by Fic inactivates the chaperome activity (PubMed:25395623, PubMed:29089387). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, Fic, restores the chaperone activity (PubMed:29089387).
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\Hsc70-3 using the Feature Mapper tool.
GBrowse - Visual display of RNA-Seq signals
View Dmel\Hsc70-3 in GBrowse 21-36
1-36.8
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
polyclonal
Source for merge of: Hsc70-3 CG1579
Source for merge of: Hsc70-3 l(1)G0102 l(1)G0341 l(1)G0111 l(1)G0292 l(1)G0407
Source for merge of: Hsc70-3 anon-WO0138581.7
Source for merge of Hsc70-3 anon-WO0138581.7 was sequence comparison ( date:051113 ).
Hsc70-3 can substitute for its mammalian counterpart and chaperone the secretion of active IgGs (human monoclonal antibody heavy and light chains expressed in Schneider cells). Hsc70-3 can also uniquely chaperone heavy chain dimers indicating mechanistic differences that may relate to the evolved need for retaining immature IgGs in vertebrates.
Members of the hsc70 gene family (heat shock cognate genes) that reside within the same intracellular compartment in different organisms share greater amino acid identity than hsc70 proteins from the same organism but different organelles. This pattern of conservation indicates specialisation of hsc70 function.
Hsc70-3 genomic and cDNA clones have been analyzed and sequenced.