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ERLEC1 encodes a resident endoplasmic reticulum (ER) protein that functions in N-glycan recognition.
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Data indicate that the interaction of OS-9 and XTP3-B with CD147(CG) was inhibited by mutations to conserved residues in their lectin domains.
Lectin activity of XTP3-B is required for its interaction with the misfolded glycoprotein alpha1-antitrypsin variant.
mannose trimming enables delivery of a substrate glycoprotein from EDEM1 (show EDEM1 Antibodies) to late endoplsmic reticulum degredation steps through association with XTP3-B
Findings shed light on how tolerance to multiple cellular stresses at a metastatic site can be evoked by an integrated mechanism involving CIM, ERLEC1, which can function to coordinate those responses in a manner that promotes metastatic cell survival.
XTP3-B specifically binds to AT(NHK), which is a well-known substrate of ERAD, via a C-terminal MRH domain in a glycan-dependent manner.
Erlectin functions in N-glycan recognition in the endoplasmic reticulum and may regulate glycoprotein traffic
XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1 (show SYVN1 Antibodies)-SEL1L (show SEL1L Antibodies) ubiquitin ligase complex and BiP (show GDF10 Antibodies)
This gene encodes a resident endoplasmic reticulum (ER) protein that functions in N-glycan recognition. This protein is thought to be involved in ER-associated degradation via its interaction with the membrane-associated ubiquitin ligase complex. It also functions as a regulator of multiple cellular stress-response pathways in a manner that promotes metastatic cell survival. Alternative splicing results in multiple transcript variants. A related pseudogene has been identified on chromosome 21.
, XTP3-transactivated gene B protein
, XTP3-transactivated protein B
, cancer invasion and metastasis-related
, erlectin 1