ERLEC1 on SARS-2 viruksen ORF8-tekijän interaktioproteiini. Glukosidaasi II poistaa alimmat 2 glukoosia ja UGGT2:n asettaman glukoosin.

ERLEC1 on endoplasmisen retikulumin lektiini 1.

Aliases for ERLEC1 Gene

• Endoplasmic Reticulum Lectin 1 ^{2 3 4 5}
• XTP3-Transactivated Gene B Protein ^{3 4}
• Erlectin 1 ^{2 3}
• ER Lectin ^{3 4}
• C2orf30 ^{3 4}
• XTP3TPB ^{3 4}
• Cancer Invasion And Metastasis-Related ³
• Chromosome 2 Open Reading Frame 30 ²

• Epididymis Luminal Protein 117 ³
• XTP3-Transactivated Protein B ³
• Erlectin ⁴
• CL24936 ³
• CL25084 ³
• HEL117 ³
• XTP3-B ³
• CIM ³

• 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 (ERAD)  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. [provided by RefSeq, Aug 2011]
  

GeneCards Summary for ERLEC1 Gene

ERLEC1 (Endoplasmic Reticulum Lectin 1) is a Protein Coding gene. Diseases associated with ERLEC1 include Myeloproliferative Syndrome, Transient. Among its related pathways are Signaling by GPCR and Signaling by Hedgehog. An important paralog of this gene is OS9.

UniProtKB/Swiss-Prot Summary for ERLEC1 Gene

• Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control (ERQC) and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins.
  

  • ERLEC_HUMAN,Q96DZ1

   https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6583763/figure/cwz029F1/
  
   https://www.jbc.org/content/288/23/16460.short
  
   (LÄHDETIETOA)
  

  Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the

  Background: Glucosidase II is an endoplasmic reticulum enzyme involved in quality control of glycoprotein folding.

  Results: The structure of the lectin domain of GII was determined by NMR spectroscopy.

  Conclusion: GII lectin domain structure contains a unique Trp residue critical for GII activity.

  Significance: GIIβ MRH domain structure is the first determined of an MRH domain present in a protein with enzymatic activity.  Endoplasmic Reticulum* Linda J. Olson^‡,  Ramiro Orsi^§, et al. 

  Abstract
  

  Here we report for the first time the three-dimensional structure of a mannose 6-phosphate receptor homology (MRH) domain present in a protein with enzymatic activity, glucosidase II (GII). GII is involved in glycoprotein folding in the endoplasmic reticulum. GII removes the two innermost glucose residues from the Glc₃Man₉GlcNAc₂ transferred to nascent proteins and the glucose added by UDP-Glc:glycoprotein glucosyltransferase. GII is composed of a catalytic GIIα subunit and a regulatory GIIβ subunit. GIIβ participates in the endoplasmic reticulum localization of GIIα and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GIIβ MRH domain by NMR spectroscopy. It adopts a β-barrel fold similar to that of other MRH domains, but its binding pocket is the most shallow known to date as it accommodates a single mannose residue. In addition, we identified a conserved residue outside the binding pocket (Trp-409) present in GIIβ but not in other MRHs that influences GII glucose trimming activity.

  • Endoplasmic Reticulum (ER)
  • Glycobiology
  • Glycoprotein
  • NMR
  • Structural Biology
  • MRH Domain
  • N-Glycan
  • Glucosidase II β
  •  

  Sitten  on proteiini EDEM3 niitä, joihin SARS2  ORF8 viruksen apuproteiini  tekee interaktion  viruksen   koettaesaa  välttää silppurin ja päästä  kvalitettikontrollista   Golgin puolelle jatkoon.
  Jos  kvaliteettikontrolli (ERQC)  havaitsee petoksen, se lähettäisi  viruksen proteiinin  hajoitustielle ERAD- koneistoon.  Jos virusta onnistaa se pääsee ERGIC  alueeseen.
   https://www.genecards.org/cgi-bin/carddisp.pl?gene=EDEM3&keywords=EDEM3
  
  

  Aliases for EDEM3 Gene

  • ER Degradation Enhancing Alpha-Mannosidase Like Protein 3 ^{2 3 5}
  • ER Degradation-Enhancing Alpha-Mannosidase-Like Protein 3 ^{3 4}
  • ER Degradation Enhancer, Mannosidase Alpha-Like 3 ^{2 3}
  • Alpha-1,2-Mannosidase EDEM3 ^{3 4}
  • C1orf22 ^{3 4}
  • ER Degradation-Enhancing -Mannosidase-Like Protein 3 ³
  • ER Degradation-Enhancing Alpha-Mannosidase-Like 3 ³
  • Chromosome 1 Open Reading Frame 22 ²
  • EC 3.2.1.113 ⁴

  External Ids for EDEM3 Gene
  
  

  Entrez Gene Summary for EDEM3 Gene

  • Quality control in the endoplasmic reticulum (ER) ensures that only properly folded proteins are retained in the cell through recognition and degradation of misfolded or unassembled proteins. EDEM3 belongs to a group of proteins that accelerate degradation of misfolded glycoproteins in the ER (Hirao et al., 2006 [PubMed 16431915]).[supplied by OMIM, Mar 2008]
    

  GeneCards Summary for EDEM3 Gene
  

  EDEM3 (ER Degradation Enhancing Alpha-Mannosidase Like Protein 3) is a Protein Coding gene. Among its related pathways are Metabolism of proteins and Calnexin/calreticulin cycle. Gene Ontology (GO) annotations related to this gene include calcium ion binding and glycoprotein endo-alpha-1,2-mannosidase activity. An important paralog of this gene is EDEM1.
  

  UniProtKB/Swiss-Prot Summary for EDEM3 Gene
  

  • Involved in endoplasmic reticulum-associated degradation (ERAD). Accelerates the glycoprotein ERAD by proteasomes, by catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2 in the N-glycans. Seems to have alpha 1,2-mannosidase activity (By similarity).

    • EDEM3_HUMAN,Q9BZQ6

  
   https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6583763/bin/cwz029f01.jpg