Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Calreticulin-2 is localized in the lumen of the endoplasmic reticulum but is not a Ca2+ -binding protein.
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CALR3 (CRT-2) is localized in the lumen of the endoplasmic reticulum, colocalizing with calnexin and protein disulfide isomerase, confirmed by immunoelectron microscopy.
"Immunoelectron microscopy confirmed that HA-CRT-2 was localized in the lumen of the endoplasmic reticulum."
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Unlike calreticulin-1, CALR3 does not bind calcium (or binds it with much lower capacity), as shown by Stains-all staining.
"CRT-2 capacity for Ca(2+)-binding may be absent or much lower than that of CRT-1."
Falcon deep research report for CALR3
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CALR3 is a testis-specific ER-lumen molecular chaperone that, unlike the broad-spectrum lectin chaperones CALR/CANX, has narrow substrate specificity and selectively supports folding/maturation of the sperm protein ADAM3.
"Unlike the ubiquitous calreticulin (CALR) and calnexin (CANX), which serve as broad-spectrum lectin chaperones for nascent glycoproteins, CALR3 exhibits a remarkably narrow substrate specificity"
UniProt entry Q96L12 (CALR3_HUMAN)
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CALR3 acts during spermatogenesis as a chaperone for client proteins such as ADAM3 and is required for sperm fertility; calcium-binding capacity may be absent or much lower than that of CALR.
"During spermatogenesis, may act as a lectin-independent chaperone for specific client proteins such as ADAM3. Required for sperm fertility (By similarity). CALR3 capacity for calcium-binding may be absent or much lower than that of CALR."