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calnexin; major histocompatibility complex class I antigen-binding protein p88; p90; IP90 (CANX)
Function:
- molecular chaperone
- transiently associates with newly synthesized glycoproteins in the endoplasmic reticulum (ER)
- may act in assisting protein assembly &/or in retention within the ER of unassembled protein subunits
- activity of protein disulfide isomerase may coincide with release of glycoprotein from calnexin
- seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins
- possibly responsible for retention in the ER of mutant forms of LDL receptor, CFTR, & alpha-1 antitrypsin leading to familial hypercholesterolemia type II, cystic fibrosis, & juvenile pulmonary emphysema, respectively
Structure: belongs to the calreticulin family
Compartment:
- endoplasmic reticulum membrane
- melanosome
General
Ca+2 binding protein
chaperonin; chaperone
phosphoprotein
Properties
SIZE: entity length = 592 aa
MW = 68 kD
COMPARTMENT: endoplasmic reticulum
MOTIF: signal sequence {1-20}
4 X approximate repeats {278-345}
MOTIF: 1-1 {278-290}
1-2 {295-307}
1-3 {314-326}
1-4 {333-345}
4 X approximate repeats {348-405}
MOTIF: 2-1 {348-358}
2-2 {367-377}
2-3 {381-391}
2-4 {395-405}
transmembrane domain {482-502}
Ser phosphorylation site {S554}
Thr phosphorylation site {T562}
Ser phosphorylation site {S564}
Ser phosphorylation site {S583}
Database Correlations
OMIM 114217
UniProt P27824
Pfam PF00262
Entrez Gene 821
Kegg hsa:821
References
- Ou WJ et al
Association of folding intermediates of glycoproteins with
calnexin during protein maturation.
Nature 364:771 1993
PMID: 8102790
- Entrez Gene :accession 821