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P35564

- CALX_MOUSE

UniProt

P35564 - CALX_MOUSE

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Protein

Calnexin

Gene
Canx
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi75 – 751Calcium; via carbonyl oxygen By similarity
Metal bindingi118 – 1181Calcium; via carbonyl oxygen By similarity
Binding sitei165 – 1651Carbohydrate By similarity
Binding sitei167 – 1671Carbohydrate By similarity
Binding sitei186 – 1861Carbohydrate By similarity
Binding sitei217 – 2171Carbohydrate By similarity
Metal bindingi437 – 4371Calcium By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. protein binding Source: IntAct

GO - Biological processi

  1. aging Source: Ensembl
  2. chaperone-mediated protein folding Source: Ensembl
  3. clathrin-mediated endocytosis Source: UniProtKB
  4. synaptic vesicle endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_198616. Calnexin/calreticulin cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Calnexin
Gene namesi
Name:Canx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:88261. Canx.

Subcellular locationi

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.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 482462Lumenal Reviewed predictionAdd
BLAST
Transmembranei483 – 50321Helical; Reviewed predictionAdd
BLAST
Topological domaini504 – 59188Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. axon Source: Ensembl
  2. dendrite cytoplasm Source: Ensembl
  3. dendritic spine Source: Ensembl
  4. endoplasmic reticulum Source: MGI
  5. integral component of lumenal side of endoplasmic reticulum membrane Source: Reactome
  6. integral component of membrane Source: MGI
  7. melanosome Source: UniProtKB-SubCell
  8. membrane Source: MGI
  9. neuronal cell body Source: Ensembl
  10. protein complex Source: Ensembl
  11. ribosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020 Reviewed predictionAdd
BLAST
Chaini21 – 591571CalnexinPRO_0000004199Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381N6-acetyllysine By similarity
Disulfide bondi161 ↔ 195 By similarity
Disulfide bondi361 ↔ 367 By similarity
Lipidationi503 – 5031S-palmitoyl cysteine By similarity
Lipidationi504 – 5041S-palmitoyl cysteine By similarity
Modified residuei553 – 5531Phosphoserine2 Publications
Modified residuei561 – 5611Phosphothreonine By similarity
Modified residuei563 – 5631Phosphoserine; by MAPK31 Publication
Modified residuei582 – 5821Phosphoserine2 Publications

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP35564.
PaxDbiP35564.
PRIDEiP35564.

PTM databases

PhosphoSiteiP35564.

Miscellaneous databases

PMAP-CutDBP35564.

Expressioni

Gene expression databases

ArrayExpressiP35564.
BgeeiP35564.
CleanExiMM_CANX.
GenevestigatoriP35564.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Sgip1Q8VD373EBI-738422,EBI-776269

Protein-protein interaction databases

BioGridi198467. 8 interactions.
IntActiP35564. 17 interactions.
MINTiMINT-1862151.

Structurei

3D structure databases

ProteinModelPortaliP35564.
SMRiP35564. Positions 61-458.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati279 – 291131-1Add
BLAST
Repeati296 – 308131-2Add
BLAST
Repeati315 – 327131-3Add
BLAST
Repeati334 – 346131-4Add
BLAST
Repeati349 – 359112-1Add
BLAST
Repeati368 – 378112-2Add
BLAST
Repeati382 – 392112-3Add
BLAST
Repeati396 – 406112-4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni277 – 410134P domain (Extended arm) By similarityAdd
BLAST
Regioni279 – 346684 X approximate repeatsAdd
BLAST
Regioni327 – 36034Interaction with PPIB By similarityAdd
BLAST
Regioni349 – 406584 X approximate repeatsAdd
BLAST
Regioni504 – 59188Sufficient to mediate interaction with SGIP1Add
BLAST

Sequence similaritiesi

Belongs to the calreticulin family.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG305105.
HOGENOMiHOG000192436.
HOVERGENiHBG005407.
InParanoidiP35564.
KOiK08054.
OMAiEAHDGHD.
OrthoDBiEOG77126Z.
PhylomeDBiP35564.
TreeFamiTF300618.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35564-1 [UniParc]FASTAAdd to Basket

« Hide

MEGKWLLCLL LVLGTAAVEA HDGHDDDAID IEDDLDDVIE EVEDSKSKSD    50
ASTPPSPKVT YKAPVPTGEV YFADSFDRGS LSGWILSKAK KDDTDDEIAK 100
YDGKWEVDEM KETKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ 150
YEVNFQNGIE CGGAYVKLLS KTAELSLDQF HDKTPYTIMF GPDKCGEDYK 200
LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE 250
ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIADPDAV 300
KPDDWDEDAP SKIPDEEATK PEGWLDDEPE YIPDPDAEKP EDWDEDMDGE 350
WEAPQIANPK CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP 400
RKIPNPDFFE DLEPFKMTPF SAIGLELWSM TSDIFFDNFI ISGDRRVVDD 450
WANDGWGLKK AADGAAEPGV VLQMLEAAEE RPWLWVVYIL TVALPVFLVI 500
LFCCSGKKQS NAMEYKKTDA PQPDVKDEEG KEEEKNKRDE EEEEEKLEEK 550
QKSDAEEDGV TGSQDEEDSK PKAEEDEILN RSPRNRKPRR E 591
Length:591
Mass (Da):67,278
Last modified:June 1, 1994 - v1
Checksum:i0D9F8FE03434BADC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti416 – 4161K → R in AAA62450. 1 Publication
Sequence conflicti468 – 4681P → L in AAA62450. 1 Publication
Sequence conflicti472 – 4721L → G in AAA62450. 1 Publication
Sequence conflicti538 – 5381R → G in AAA62450. 1 Publication
Sequence conflicti560 – 5601V → G in AAA62450. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS24633.1.
PIRiB54354.
RefSeqiNP_001103969.1. NM_001110499.1.
NP_001103970.1. NM_001110500.1.
NP_031623.1. NM_007597.3.
UniGeneiMm.248827.

Genome annotation databases

EnsembliENSMUST00000020637; ENSMUSP00000020637; ENSMUSG00000020368.
ENSMUST00000179865; ENSMUSP00000137440; ENSMUSG00000020368.
GeneIDi12330.
KEGGimmu:12330.
UCSCiuc007isf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS24633.1.
PIRi B54354.
RefSeqi NP_001103969.1. NM_001110499.1.
NP_001103970.1. NM_001110500.1.
NP_031623.1. NM_007597.3.
UniGenei Mm.248827.

3D structure databases

ProteinModelPortali P35564.
SMRi P35564. Positions 61-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198467. 8 interactions.
IntActi P35564. 17 interactions.
MINTi MINT-1862151.

PTM databases

PhosphoSitei P35564.

Proteomic databases

MaxQBi P35564.
PaxDbi P35564.
PRIDEi P35564.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000020637 ; ENSMUSP00000020637 ; ENSMUSG00000020368 .
ENSMUST00000179865 ; ENSMUSP00000137440 ; ENSMUSG00000020368 .
GeneIDi 12330.
KEGGi mmu:12330.
UCSCi uc007isf.2. mouse.

Organism-specific databases

CTDi 821.
MGIi MGI:88261. Canx.

Phylogenomic databases

eggNOGi NOG305105.
HOGENOMi HOG000192436.
HOVERGENi HBG005407.
InParanoidi P35564.
KOi K08054.
OMAi EAHDGHD.
OrthoDBi EOG77126Z.
PhylomeDBi P35564.
TreeFami TF300618.

Enzyme and pathway databases

Reactomei REACT_196550. MHC class II antigen presentation.
REACT_198616. Calnexin/calreticulin cycle.

Miscellaneous databases

ChiTaRSi CANX. mouse.
NextBioi 280926.
PMAP-CutDB P35564.
PROi P35564.
SOURCEi Search...

Gene expression databases

ArrayExpressi P35564.
Bgeei P35564.
CleanExi MM_CANX.
Genevestigatori P35564.

Family and domain databases

Gene3Di 2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProi IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 2 hits.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCALX_MOUSE
AccessioniPrimary (citable) accession number: P35564
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: September 3, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi