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Identification
HMDB Protein ID HMDBP07535
Secondary Accession Numbers
  • 13243
Name Calnexin
Synonyms
  1. IP90
  2. Major histocompatibility complex class I antigen-binding protein p88
  3. p90
Gene Name CANX
Protein Type Unknown
Biological Properties
General Function Involved in calcium ion binding
Specific Function Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins
Pathways Not Available
Reactions Not Available
GO Classification
Component
endoplasmic reticulum
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
Function
ion binding
cation binding
metal ion binding
binding
unfolded protein binding
protein binding
calcium ion binding
Process
metabolic process
macromolecule metabolic process
cellular protein metabolic process
protein folding
protein metabolic process
Cellular Location
  1. Melanosome
  2. Endoplasmic reticulum membrane
  3. Single-pass type I membrane protein
Gene Properties
Chromosome Location Chromosome:5
Locus 5q35
SNPs CANX
Gene Sequence
>1779 bp
ATGGAAGGGAAGTGGTTGCTGTGTATGTTACTGGTGCTTGGAACTGCTATTGTTGAGGCT
CATGATGGACATGATGATGATGTGATTGATATTGAGGATGACCTTGACGATGTCATTGAA
GAGGTAGAAGACTCAAAACCAGATACCACTGCTCCTCCTTCATCTCCCAAGGTTACTTAC
AAAGCTCCAGTTCCAACAGGGGAAGTATATTTTGCTGATTCTTTTGACAGAGGAACTCTG
TCAGGGTGGATTTTATCCAAAGCCAAGAAAGACGATACCGATGATGAAATTGCCAAATAT
GATGGAAAGTGGGAGGTAGAGGAAATGAAGGAGTCAAAGCTTCCAGGTGATAAAGGACTT
GTGTTGATGTCTCGGGCCAAGCATCATGCGATCTCTGCTAAACTGAACAAGCCCTTCCTG
TTTGACACCAAGCCTCTCATTGTTCAGTATGAGGTTAATTTCCAAAATGGAATAGAATGT
GGTGGTGCCTATGTGAAACTGCTTTCTAAAACACCAGAACTCAACCTGGATCAGTTCCAT
GACAAGACCCCTTATACGATTATGTTTGGTCCAGATAAATGTGGAGAGGACTATAAACTG
CACTTCATCTTCCGACACAAAAACCCCAAAACGGGTATCTATGAAGAAAAACATGCTAAG
AGGCCAGATGCAGATCTGAAGACCTATTTTACTGATAAGAAAACACATCTTTACACACTA
ATCTTGAATCCAGATAATAGTTTTGAAATACTGGTTGACCAATCTGTGGTGAATAGTGGA
AATCTGCTCAATGACATGACTCCTCCTGTAAATCCTTCACGTGAAATTGAGGACCCAGAA
GACCGGAAGCCCGAGGATTGGGATGAAAGACCAAAAATCCCAGATCCAGAAGCTGTCAAG
CCAGATGACTGGGATGAAGATGCCCCTGCTAAGATTCCAGATGAAGAGGCCACAAAACCC
GAAGGCTGGTTAGATGATGAGCCTGAGTACGTACCTGATCCAGACGCAGAGAAACCTGAG
GATTGGGATGAAGACATGGATGGAGAATGGGAGGCTCCTCAGATTGCCAACCCTAGATGT
GAGTCAGCTCCTGGATGTGGTGTCTGGCAGCGACCTGTGATTGACAACCCCAATTATAAA
GGCAAATGGAAGCCTCCTATGATTGACAATCCCAGTTACCAGGGAATCTGGAAACCCAGG
AAAATACCAAATCCAGATTTCTTTGAAGATCTGGAACCTTTCAGAATGACTCCTTTTAGT
GCTATTGGTTTGGAGCTGTGGTCCATGACCTCTGACATTTTTTTTGACAACTTTATCATT
TGTGCTGATCGAAGAATAGTTGATGATTGGGCCAATGATGGATGGGGCCTGAAGAAAGCT
GCTGATGGGGCTGCTGAGCCAGGCGTTGTGGGGCAGATGATCGAGGCAGCTGAAGAGCGC
CCGTGGCTGTGGGTAGTCTATATTCTAACTGTAGCCCTTCCTGTGTTCCTGGTTATCCTC
TTCTGCTGTTCTGGAAAGAAACAGACCAGTGGTATGGAGTATAAGAAAACTGATGCACCT
CAACCGGATGTGAAGGAAGAGGAAGAAGAGAAGGAAGAGGAAAAGGACAAGGGAGATGAG
GAGGAGGAAGGAGAAGAGAAACTTGAAGAGAAACAGAAAAGTGATGCTGAAGAAGATGGT
GGCACTGTCAGTCAAGAGGAGGAAGACAGAAAACCTAAAGCAGAGGAGGATGAAATTTTG
AACAGATCACCAAGAAACAGAAAGCCACGAAGAGAGTGA
Protein Properties
Number of Residues 592
Molecular Weight 67567.7
Theoretical pI 4.21
Pfam Domain Function
Signals
  • 1-20
Transmembrane Regions
  • 482-502
Protein Sequence
>Calnexin
MEGKWLLCMLLVLGTAIVEAHDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTY
KAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGL
VLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFH
DKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTL
ILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVK
PDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRC
ESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFS
AIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEER
PWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDE
EEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P27824
UniProtKB/Swiss-Prot Entry Name CALX_HUMAN
PDB IDs
GenBank Gene ID L10284
GeneCard ID CANX
GenAtlas ID CANX
HGNC ID HGNC:1473
References
General References
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  22. Honore B, Rasmussen HH, Celis A, Leffers H, Madsen P, Celis JE: The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin. Electrophoresis. 1994 Mar-Apr;15(3-4):482-90. [PubMed:8055875 ]
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