Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00466
Entry Name
UniProt Accession
Theoretical PI
4.46
Molecular Weight
67568.3
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calnexin
Protein Synonyms/Alias
IP90; Major histocompatibility complex class I antigen-binding protein p88; p90;
Gene Name
CANX
Gene Synonyms/Alias
Created Date
01-AUG-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
8
Canonical
MEGKWLLCMLLVLGT
[2]
S-Palmitoylation
502
Canonical
VFLVILFCCSGKKQT
[1]
S-Palmitoylation
503
Canonical
FLVILFCCSGKKQTS
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Lakkaraju AK, Abrami L, Lemmin T, Blaskovic S, Kunz B, Kihara A, Dal Peraro M,van der Goot FG. Palmitoylated calnexin is a key component of theribosome-translocon complex. EMBO J. 2012 Apr 4;31(7):1823-35. doi:10.1038/emboj.2012.15. Epub 2012 Feb 7.[PMID:22314232]
[2] Predicted from GPS-Lipid
Functional Description
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. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor- mediated endocytosis at the synapse.
Sequence Annotation
Topological domain: 21 481 Lumenal.
Transmembrane: 482 502 Helical.
Topological domain: 503 592 Cytoplasmic.
Region: 276 409 P domain (Extended arm).
Region: 278 345 4 X approximate repeats.
Region: 326 359 Interaction with PPIB.
Region: 348 405 4 X approximate repeats.
Region: 503 592 Sufficient to mediate interaction withSGIP1.
Metal binding site: 74 74 Calcium; via carbonyl oxygen.
Metal binding site: 117 117 Calcium; via carbonyl oxygen.
Metal binding site: 436 436 Calcium.
Binding site: 164 164 Carbohydrate.
Binding site: 166 166 Carbohydrate.
Binding site: 185 185 Carbohydrate.
Binding site: 216 216 Carbohydrate.
Modified residue: 137 137 N6-acetyllysine.
Modified residue: 554 554 Phosphoserine.
Modified residue: 562 562 Phosphothreonine.
Modified residue: 564 564 Phosphoserine; by MAPK3.
Modified residue: 583 583 Phosphoserine.
Protein Length
592 AA.
Protein Sequence
(Canonical)
MEGKWLLCML LVLGTAIVEA HDGHDDDVID IEDDLDDVIE EVEDSKPDTT APPSSPKVTY  60
KAPVPTGEVY FADSFDRGTL SGWILSKAKK DDTDDEIAKY DGKWEVEEMK ESKLPGDKGL  120
VLMSRAKHHA ISAKLNKPFL FDTKPLIVQY EVNFQNGIEC GGAYVKLLSK TPELNLDQFH  180
DKTPYTIMFG PDKCGEDYKL HFIFRHKNPK TGIYEEKHAK RPDADLKTYF TDKKTHLYTL  240
ILNPDNSFEI LVDQSVVNSG NLLNDMTPPV NPSREIEDPE DRKPEDWDER PKIPDPEAVK  300
PDDWDEDAPA KIPDEEATKP EGWLDDEPEY VPDPDAEKPE DWDEDMDGEW EAPQIANPRC  360
ESAPGCGVWQ RPVIDNPNYK GKWKPPMIDN PSYQGIWKPR KIPNPDFFED LEPFRMTPFS  420
AIGLELWSMT SDIFFDNFII CADRRIVDDW ANDGWGLKKA ADGAAEPGVV GQMIEAAEER  480
PWLWVVYILT VALPVFLVIL FCCSGKKQTS GMEYKKTDAP QPDVKEEEEE KEEEKDKGDE  540
EEEGEEKLEE KQKSDAEEDG GTVSQEEEDR KPKAEEDEIL NRSPRNRKPR RE          592
FASTA
(Canonical)
>LipidDB-9606-00466|P27824
MEGKWLLCMLLVLGTAIVEAHDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTY
KAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGL
VLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFH
DKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTL
ILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVK
PDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRC
ESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFS
AIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEER
PWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDE
EEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE
Gene Ontology
GO:0030424; C:axon; IEA:Ensembl
GO:0032839; C:dendrite cytoplasm; IEA:Ensembl
GO:0043197; C:dendritic spine; IEA:Ensembl
GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB
GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome
GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI
GO:0044233; C:ER-mitochondrion membrane contact site; IDA:MGI
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome
GO:0016020; C:membrane; IDA:UniProtKB
GO:0043025; C:neuronal cell body; IEA:Ensembl
GO:0043234; C:protein complex; IEA:Ensembl
GO:0005840; C:ribosome; IEA:Ensembl
GO:0005509; F:calcium ion binding; TAS:ProtInc
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB
GO:0007568; P:aging; IEA:Ensembl
GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome
GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome
GO:0044267; P:cellular protein metabolic process; TAS:Reactome
GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl
GO:0072583; P:clathrin-mediated endocytosis; ISS:UniProtKB
GO:0043687; P:post-translational protein modification; TAS:Reactome
GO:0006457; P:protein folding; TAS:Reactome
GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome
GO:0009306; P:protein secretion; TAS:ProtInc
GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB
Interpro
InterPro; IPR001580; Calret/calnex
InterPro; IPR018124; Calret/calnex_CS
InterPro; IPR009033; Calreticulin/calnexin_P_dom
InterPro; IPR013320; ConA-like_dom
Pfam
Pfam; PF00262; Calreticulin;
SMART
PROSITE
PROSITE; PS00803; CALRETICULIN_1;
PROSITE; PS00804; CALRETICULIN_2;
PROSITE; PS00805; CALRETICULIN_REPEAT;
PRINTS
PRINTS; PR00626; CALRETICULIN;