Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01234
Entry Name
UniProt Accession
Theoretical PI
4.49
Molecular Weight
67277.92
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calnexin
Protein Synonyms/Alias
Gene Name
Canx
Gene Synonyms/Alias
Created Date
01-JUN-1994
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
8
Canonical
MEGKWLLCLLLVLGT
[1]
S-Palmitoylation
503
Canonical
VFLVILFCCSGKKQS
[1]
S-Palmitoylation
504
Canonical
FLVILFCCSGKKQSN
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] 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: 21 482 Lumenal.
Transmembrane: 483 503 Helical.
Topological domain: 504 591 Cytoplasmic.
Region: 277 410 P domain (Extended arm).
Region: 279 346 4 X approximate repeats.
Region: 327 360 Interaction with PPIB.
Region: 349 406 4 X approximate repeats.
Region: 504 591 Sufficient to mediate interaction withSGIP1.
Metal binding site: 75 75 Calcium; via carbonyl oxygen.
Metal binding site: 118 118 Calcium; via carbonyl oxygen.
Metal binding site: 437 437 Calcium.
Binding site: 165 165 Carbohydrate.
Binding site: 167 167 Carbohydrate.
Binding site: 186 186 Carbohydrate.
Binding site: 217 217 Carbohydrate.
Modified residue: 138 138 N6-acetyllysine.
Modified residue: 553 553 Phosphoserine.
Modified residue: 561 561 Phosphothreonine.
Modified residue: 563 563 Phosphoserine; by MAPK3.
Modified residue: 582 582 Phosphoserine.
Protein Length
591 AA.
Protein Sequence
(Canonical)
MEGKWLLCLL LVLGTAAVEA HDGHDDDAID IEDDLDDVIE EVEDSKSKSD ASTPPSPKVT  60
YKAPVPTGEV YFADSFDRGS LSGWILSKAK KDDTDDEIAK YDGKWEVDEM KETKLPGDKG  120
LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTAELSLDQF  180
HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT  240
LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIADPDAV  300
KPDDWDEDAP SKIPDEEATK PEGWLDDEPE YIPDPDAEKP EDWDEDMDGE WEAPQIANPK  360
CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP RKIPNPDFFE DLEPFKMTPF  420
SAIGLELWSM TSDIFFDNFI ISGDRRVVDD WANDGWGLKK AADGAAEPGV VLQMLEAAEE  480
RPWLWVVYIL TVALPVFLVI LFCCSGKKQS NAMEYKKTDA PQPDVKDEEG KEEEKNKRDE  540
EEEEEKLEEK QKSDAEEDGV TGSQDEEDSK PKAEEDEILN RSPRNRKPRR E           591
FASTA
(Canonical)
>LipidDB-10090-01234|P35564
MEGKWLLCLLLVLGTAAVEAHDGHDDDAIDIEDDLDDVIEEVEDSKSKSDASTPPSPKVT
YKAPVPTGEVYFADSFDRGSLSGWILSKAKKDDTDDEIAKYDGKWEVDEMKETKLPGDKG
LVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTAELSLDQF
HDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGVYEEKHAKRPDADLKTYFTDKKTHLYT
LILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIADPDAV
KPDDWDEDAPSKIPDEEATKPEGWLDDEPEYIPDPDAEKPEDWDEDMDGEWEAPQIANPK
CESAPGCGVWQRPMIDNPNYKGKWKPPMIDNPNYQGIWKPRKIPNPDFFEDLEPFKMTPF
SAIGLELWSMTSDIFFDNFIISGDRRVVDDWANDGWGLKKAADGAAEPGVVLQMLEAAEE
RPWLWVVYILTVALPVFLVILFCCSGKKQSNAMEYKKTDAPQPDVKDEEGKEEEKNKRDE
EEEEEKLEEKQKSDAEEDGVTGSQDEEDSKPKAEEDEILNRSPRNRKPRRE
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:MGI
GO:0070062; C:extracellular vesicular exosome; IEA:Ensembl
GO:0071556; C:integral component of lumenal side of endoplasmic reticulum membrane; TAS:Reactome
GO:0016021; C:integral component of membrane; IDA:MGI
GO:0016020; C:membrane; IDA:MGI
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; IEA:InterPro
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0044822; F:poly(A) RNA binding; IEA:Ensembl
GO:0007568; P:aging; IEA:Ensembl
GO:0061077; P:chaperone-mediated protein folding; IEA:Ensembl
GO:0072583; P:clathrin-mediated endocytosis; IMP:UniProtKB
GO:0048488; P:synaptic vesicle endocytosis; IMP: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;