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P35564 (CALX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calnexin
Gene names
Name:Canx
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. 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. Ref.5 Ref.11

Subunit structure

Interacts with MAPK3/ERK1 By similarity. Interacts with KCNH2 By similarity. Associates with ribosomes. The palmitoylated form interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins By similarity. Interacts with SERPINA2P/SERPINA2 and with the S and Z variants of SERPINA1 By similarity. Part of a complex which includes CANX, DERL1, DERL2, DDOST/OST48, RPN1, RPN2, SELK, STT3A, VCP AND VIMP By similarity. Interacts with SGIP1; involved in negative regulation of endocytosis. Interacts with PPIB. Ref.11

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein. Endoplasmic reticulum By similarity. Melanosome By similarity. Note: The palmitoylated form preferentially localizes to the perinuclear rough ER By similarity. When bound to CD3 epsilon chains, calnexin's ER retention signal can be masked, permitting it to escape ER retention. Ref.5

Post-translational modification

Phosphorylated at Ser-563 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes By similarity.

Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins By similarity.

Sequence similarities

Belongs to the calreticulin family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Lectin
Metal-binding
   Molecular functionChaperone
   PTMAcetylation
Disulfide bond
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

chaperone-mediated protein folding

Inferred from electronic annotation. Source: Ensembl

clathrin-mediated endocytosis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

synaptic vesicle endocytosis

Inferred from mutant phenotype Ref.11. Source: UniProtKB

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

dendrite cytoplasm

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay PubMed 12646573PubMed 15152008PubMed 15184384PubMed 15452145PubMed 16204232PubMed 17204322PubMed 19766735PubMed 21606205PubMed 23093945PubMed 9034150PubMed 9094723. Source: MGI

integral component of lumenal side of endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from direct assay PubMed 12927782. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from direct assay PubMed 22375059. Source: MGI

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

ribosome

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.11. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sgip1Q8VD373EBI-738422,EBI-776269

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 591571Calnexin
PRO_0000004199

Regions

Topological domain21 – 482462Lumenal Potential
Transmembrane483 – 50321Helical; Potential
Topological domain504 – 59188Cytoplasmic Potential
Repeat279 – 291131-1
Repeat296 – 308131-2
Repeat315 – 327131-3
Repeat334 – 346131-4
Repeat349 – 359112-1
Repeat368 – 378112-2
Repeat382 – 392112-3
Repeat396 – 406112-4
Region277 – 410134P domain (Extended arm) By similarity
Region279 – 346684 X approximate repeats
Region327 – 36034Interaction with PPIB By similarity
Region349 – 406584 X approximate repeats
Region504 – 59188Sufficient to mediate interaction with SGIP1

Sites

Metal binding751Calcium; via carbonyl oxygen By similarity
Metal binding1181Calcium; via carbonyl oxygen By similarity
Metal binding4371Calcium By similarity
Binding site1651Carbohydrate By similarity
Binding site1671Carbohydrate By similarity
Binding site1861Carbohydrate By similarity
Binding site2171Carbohydrate By similarity

Amino acid modifications

Modified residue1381N6-acetyllysine By similarity
Modified residue5531Phosphoserine Ref.6 Ref.9
Modified residue5611Phosphothreonine By similarity
Modified residue5631Phosphoserine; by MAPK3 Ref.9
Modified residue5821Phosphoserine Ref.9 Ref.10
Lipidation5031S-palmitoyl cysteine By similarity
Lipidation5041S-palmitoyl cysteine By similarity
Disulfide bond161 ↔ 195 By similarity
Disulfide bond361 ↔ 367 By similarity

Experimental info

Sequence conflict4161K → R in AAA62450. Ref.4
Sequence conflict4681P → L in AAA62450. Ref.4
Sequence conflict4721L → G in AAA62450. Ref.4
Sequence conflict5381R → G in AAA62450. Ref.4
Sequence conflict5601V → G in AAA62450. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P35564 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 0D9F8FE03434BADC

FASTA59167,278
        10         20         30         40         50         60 
MEGKWLLCLL LVLGTAAVEA HDGHDDDAID IEDDLDDVIE EVEDSKSKSD ASTPPSPKVT 

        70         80         90        100        110        120 
YKAPVPTGEV YFADSFDRGS LSGWILSKAK KDDTDDEIAK YDGKWEVDEM KETKLPGDKG 

       130        140        150        160        170        180 
LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTAELSLDQF 

       190        200        210        220        230        240 
HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT 

       250        260        270        280        290        300 
LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIADPDAV 

       310        320        330        340        350        360 
KPDDWDEDAP SKIPDEEATK PEGWLDDEPE YIPDPDAEKP EDWDEDMDGE WEAPQIANPK 

       370        380        390        400        410        420 
CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP RKIPNPDFFE DLEPFKMTPF 

       430        440        450        460        470        480 
SAIGLELWSM TSDIFFDNFI ISGDRRVVDD WANDGWGLKK AADGAAEPGV VLQMLEAAEE 

       490        500        510        520        530        540 
RPWLWVVYIL TVALPVFLVI LFCCSGKKQS NAMEYKKTDA PQPDVKDEEG KEEEKNKRDE 

       550        560        570        580        590 
EEEEEKLEEK QKSDAEEDGV TGSQDEEDSK PKAEEDEILN RSPRNRKPRR E 

« Hide

References

« Hide 'large scale' references
[1]"Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5."
Tjoelker L.W., Seyfried C.E., Eddy R.L. Jr., Shows T.B. Jr., Calderon J., Schreiber R.B., Gray P.W.
Biochemistry 33:3229-3236(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary gland.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-155.
Strain: C57BL/6J.
Tissue: Eye.
[4]"Class II histocompatibility molecules associate with calnexin during assembly in the endoplasmic reticulum."
Schreiber K.L., Bell M.P., Huntoon C.J., Rajagopalan S., Brenner M.B., McKean D.J.
Int. Immunol. 6:101-111(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-591.
Strain: BALB/c.
[5]"The molecular chaperone calnexin is expressed on the surface of immature thymocytes in association with clonotype-independent CD3 complexes."
Wiest D.L., Burgess W.H., McKean D., Kearse K.P., Singer A.
EMBO J. 14:3425-3433(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THYMOCYTE MATURATION, SUBCELLULAR LOCATION.
[6]"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Teratocarcinoma.
[7]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
[8]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563 AND SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[11]"Enhanced clathrin-dependent endocytosis in the absence of calnexin."
Li H.D., Liu W.X., Michalak M.
PLoS ONE 6:E21678-E21678(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SGIP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L18888 mRNA. Translation: AAA21014.1.
BC012408 mRNA. Translation: AAH12408.1.
BC040244 mRNA. Translation: AAH40244.1.
AK084175 mRNA. Translation: BAC39133.1.
L23865 mRNA. Translation: AAA62450.1.
CCDSCCDS24633.1.
PIRB54354.
RefSeqNP_001103969.1. NM_001110499.1.
NP_001103970.1. NM_001110500.1.
NP_031623.1. NM_007597.3.
UniGeneMm.248827.

3D structure databases

ProteinModelPortalP35564.
SMRP35564. Positions 61-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198467. 8 interactions.
IntActP35564. 17 interactions.
MINTMINT-1862151.

PTM databases

PhosphoSiteP35564.

Proteomic databases

MaxQBP35564.
PaxDbP35564.
PRIDEP35564.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000020637; ENSMUSP00000020637; ENSMUSG00000020368.
ENSMUST00000179865; ENSMUSP00000137440; ENSMUSG00000020368.
GeneID12330.
KEGGmmu:12330.
UCSCuc007isf.2. mouse.

Organism-specific databases

CTD821.
MGIMGI:88261. Canx.

Phylogenomic databases

eggNOGNOG305105.
HOGENOMHOG000192436.
HOVERGENHBG005407.
InParanoidP35564.
KOK08054.
OMAEAHDGHD.
OrthoDBEOG77126Z.
PhylomeDBP35564.
TreeFamTF300618.

Gene expression databases

ArrayExpressP35564.
BgeeP35564.
CleanExMM_CANX.
GenevestigatorP35564.

Family and domain databases

Gene3D2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PANTHERPTHR11073. PTHR11073. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCANX. mouse.
NextBio280926.
PMAP-CutDBP35564.
PROP35564.
SOURCESearch...

Entry information

Entry nameCALX_MOUSE
AccessionPrimary (citable) accession number: P35564
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot