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FLASH GENE
Symbol CANX contributors: mct - updated : 03-11-2016
HGNC name calnexin
HGNC id 1473
Location 5q35.3      Physical location : 179.125.929 - 179.158.637
Synonym name major histocompatibility complex class I antigen-binding protein p88
Synonym symbol(s) CNX, IP90, P90, FLJ26570
DNA
TYPE functioning gene
STRUCTURE 32.71 kb     15 Exon(s)
10 Kb 5' upstream gene genomic sequence study
MAPPING cloned Y linked   status confirmed
RNA
TRANSCRIPTS type messenger
text variants 1 and 2 encode the same protein
identificationnb exonstypebpproduct
ProteinkDaAAspecific expressionYearPubmed
15 - 4900 65.4 592 - 1994 8136357
precursor
15 - 4953 65.4 592 - 1994 8136357
precursor
EXPRESSION
Type ubiquitous
   expressed in (based on citations)
organ(s)
SystemOrgan level 1Organ level 2Organ level 3Organ level 4LevelPubmedSpeciesStageRna symbol
Digestiveesophagus   highly
 liver   highly
Reproductivemale systemtestis  highly
Respiratoryrespiratory tracttrachea  highly
tissue
SystemTissueTissue level 1Tissue level 2LevelPubmedSpeciesStageRna symbol
Epithelialabsorptive excretorydigestive epithelium (mucosa)  
cell lineage
cell lines
fluid/secretion
at STAGE
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • a cytosolic domain whose phosphorylation state and association with PACS2 sort this chaperone between domains of the ER and the plasma membrane
  • cysteine residues within calnexin important for the structure and function of CANX
  • conjugated GlycoP
    HOMOLOGY
    interspecies homolog to murine Canx (93.4pc)
    homolog to rattus Canx (94.4pc)
    Homologene
    FAMILY
  • calreticulin family
  • CATEGORY chaperone/stress
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,lumen
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,endoplasmic reticulum
    intracellular,cytoplasm,cytosolic,ribosome
    text
  • interaction of CANX with the cytosolic sorting protein PACS2 distributes CANX between the rough ER, the MAM (mitochondria-associated membrane), and the plasma membrane
  • type I ER membrane protein
  • shuttles between the rough ER and the shuttles between the rough ER and the mitochondria-associated membrane (MAM) depending on its palmitoylation status
  • basic FUNCTION
  • calcium binding protein, chaperone, molecular and quality control functions of ER
  • may be playing a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins
  • decreased plasma membrane expression of the GNRHR, an effect that was mediated by a physical interaction between the receptor and the calnexin
  • molecular lectin-like chaperone, and together with calreticulin, the protein promotes folding of glycosylated proteins
  • endoplasmic reticulum (ER) lectin that mediates protein folding on the rough ER
  • retaining GNRHR in the ER, an effect that decreases GNRHR signaling capacity
  • decreases with aging and might contribute to a cytoprotection in a variety of human age-related diseases
  • plays an important role in the pathogenesis of peripheral neuropathies
  • CANX discriminates between different conformational states of SLC6A5 displaying a lectin-independent chaperone activity
  • transmembrane chaperone involved in the folding of newly synthesized glycoproteins in the lumen of the endoplasmic reticulum (ER)
  • capacity of calnexin to sense ER stress and, in response, prevent the EGF-induced processing of its cytosolic domain
  • has a specific role in cardiomyocyte viability and Ca(2+) cycling through its effects on ER stress, apoptosis and Ca(2+) channel expression
  • soluble placental CNX may have a physiological chaperone function similar to that of CALR
  • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS
    PATHWAY
    metabolism
    signaling
    calnexin cycle (has evolved with a specialized oxidoreductase to facilitate native disulfide formation in complex glycoproteins)
    a component ADAM7 forms complexes with calnexin (CANX), heat shock protein 5 (HSPA5), and integral membrane protein 2B (ITM2B)
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • calreticulin
  • interacting with CALR, and GRP58 for disulfide bond formation in CD1D heavy chain
  • interacting with SERP1
  • interacting with PACS2 (distributes calnexin between the rough ER, the mitochondria-associated membrane (MAM), and the plasma membrane)
  • interacts with PDIA3 (PDIA3 physically associated with the calnexin cycle to catalyze isomerization reactions with most of its substrates
  • interacting with Hiv env glycoprotein and protein-disulfide isomerase
  • potential interaction with PMP22, and in the absence of calnexin, it is possible that PMP22 folding and function are modified, leading to dysmyelination
  • interacting with ZNRF4 (ectopic expression of ZNRF4 induced a specific RING finger-dependent down-regulation of calnexin, indicating a role for ZNRF4 in the regulation of calnexin levels)
  • CANX binds transiently to an intermediate under-glycosylated transporter precursor and facilitates SLC6A5 processing
  • controls the STAT3-mediated transcriptional response to EGF
  • EDEM2 interacts with CANX and SEL1L, suggesting a potential avenue by which misfolded glycoproteins may be shunted towards SEL1L and ERAD rather than being released into the secretory pathway
  • interaction between the CANX cytoplasmic domain and UBE2I, a SUMOylation E2 ligase, which modified the calnexin cytoplasmic domain by the addition of SUMO
  • FUNDC1 integrates mitochondrial fission and mitophagy at the interface of the MAM (ER-mitochondrial contact site (MAM)) by working in concert with DNM1L and CANX under hypoxic conditions in mammalian cells
  • KDELR2 competes with MV envelope proteins for binding to calnexin and HSPA5, and this interaction limits the availability of the chaperones for Measles Virus (MV) proteins, causing the reduction of virus spread and titers
  • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s)
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • calnexin deficiency leads to myelinopathy in mouse