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Protein

Calnexin

Gene

Canx

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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.

Sites

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

GO - Molecular functioni

  • apolipoprotein binding Source: RGD
  • calcium ion binding Source: InterPro
  • carbohydrate binding Source: UniProtKB-KW
  • glycoprotein binding Source: RGD
  • ionotropic glutamate receptor binding Source: RGD
  • poly(A) RNA binding Source: Ensembl
  • unfolded protein binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • chaperone-mediated protein folding Source: RGD
  • clathrin-mediated endocytosis Source: UniProtKB
  • synaptic vesicle endocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding

Enzyme and pathway databases

ReactomeiR-RNO-2132295. MHC class II antigen presentation.
R-RNO-901042. Calnexin/calreticulin cycle.
R-RNO-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Names & Taxonomyi

Protein namesi
Recommended name:
Calnexin
Gene namesi
Name:Canx
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi2266. Canx.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Single-pass type I membrane protein Sequence analysis
  • Endoplasmic reticulum By similarity
  • Melanosome By similarity

  • Note: The palmitoylated form preferentially localizes to the perinuclear rough ER.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 482462LumenalSequence analysisAdd
BLAST
Transmembranei483 – 50321HelicalSequence analysisAdd
BLAST
Topological domaini504 – 59188CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon Source: RGD
  • cytoplasm Source: RGD
  • cytosol Source: GOC
  • dendrite cytoplasm Source: RGD
  • dendritic spine Source: RGD
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: AgBase
  • ER-mitochondrion membrane contact site Source: Ensembl
  • extracellular exosome Source: Ensembl
  • integral component of membrane Source: UniProtKB-KW
  • melanosome Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: RGD
  • protein complex Source: RGD
  • ribosome Source: RGD
  • smooth endoplasmic reticulum Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 591571CalnexinPRO_0000004201Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei138 – 1381N6-acetyllysineBy similarity
Disulfide bondi161 ↔ 195By similarity
Disulfide bondi361 ↔ 367By similarity
Lipidationi503 – 5031S-palmitoyl cysteineBy similarity
Lipidationi504 – 5041S-palmitoyl cysteineBy similarity
Modified residuei553 – 5531PhosphoserineBy similarity
Modified residuei561 – 5611PhosphothreonineBy similarity
Modified residuei563 – 5631Phosphoserine; by MAPK31 Publication
Modified residuei582 – 5821PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated at Ser-563 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes.1 Publication
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).By similarity
Ubiquitinated, leading to proteasomal degradation. Probably ubiquitinated by ZNRF4.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP35565.
PRIDEiP35565.

PTM databases

iPTMnetiP35565.
PhosphoSiteiP35565.
SwissPalmiP35565.

Expressioni

Gene expression databases

GenevisibleiP35565. RN.

Interactioni

Subunit structurei

Interacts with MAPK3/ERK1 (PubMed:10393181). Interacts with KCNH2 (By similarity). Associates with ribosomes (PubMed:10393181). Interacts with SGIP1; involved in negative regulation of endocytosis (By similarity). 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 PPIB (By similarity). Interacts with ZNRF4 (By similarity).By similarity1 Publication

GO - Molecular functioni

  • apolipoprotein binding Source: RGD
  • glycoprotein binding Source: RGD
  • ionotropic glutamate receptor binding Source: RGD
  • unfolded protein binding Source: RGD

Protein-protein interaction databases

BioGridi247827. 6 interactions.
IntActiP35565. 11 interactions.
MINTiMINT-4996673.
STRINGi10116.ENSRNOP00000040859.

Structurei

3D structure databases

ProteinModelPortaliP35565.
SMRiP35565. Positions 61-458.
ModBaseiSearch...
MobiDBiSearch...

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 PPIBBy similarityAdd
BLAST
Regioni349 – 406584 X approximate repeatsAdd
BLAST
Regioni504 – 59188Sufficient to mediate interaction with SGIP1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0675. Eukaryota.
ENOG410XP7T. LUCA.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192436.
HOVERGENiHBG005407.
InParanoidiP35565.
KOiK08054.
OMAiLVILFCC.
OrthoDBiEOG77126Z.
PhylomeDBiP35565.

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.
IPR013320. ConA-like_dom.
[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.

P35565-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEGKWLLCLL LVLGTAAIQA HDGHDDDMID IEDDLDDVIE EVEDSKSKSD
60 70 80 90 100
TSTPPSPKVT YKAPVPTGEV YFADSFDRGS LSGWILSKAK KDDTDDEIAK
110 120 130 140 150
YDGKWEVDEM KETKLPGDKG LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ
160 170 180 190 200
YEVNFQNGIE CGGAYVKLLS KTSELNLDQF HDKTPYTIMF GPDKCGEDYK
210 220 230 240 250
LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT LILNPDNSFE
260 270 280 290 300
ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIADPDAV
310 320 330 340 350
KPDDWDEDAP SKIPDEEATK PEGWLDDEPE YIPDPDAEKP EDWDEDMDGE
360 370 380 390 400
WEAPQIANPK CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP
410 420 430 440 450
RKIPNPDFFE DLEPFRMTPF SAIGLELWSM TSDIFFDNFI ISGDRRVVDD
460 470 480 490 500
WANDGWGLKK AADGAAEPGV VGQMLEAAEE RPWLWVVYIL TVALPVFLVI
510 520 530 540 550
LFCCSGKKQS NAMEYKKTDA PQPDVKDEEG KEEEKNKGDE EEEEEKLEEK
560 570 580 590
QKSDAEEDGG TGSQDEEDSK PKAEEDEILN RSPRNRKPRR E
Length:591
Mass (Da):67,255
Last modified:June 1, 1994 - v1
Checksum:iDF91D099593C62B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18889 mRNA. Translation: AAA21015.1.
PIRiC54354.
RefSeqiNP_742005.1. NM_172008.2.
XP_008765901.1. XM_008767679.1.
XP_008765902.1. XM_008767680.1.
UniGeneiRn.1762.

Genome annotation databases

EnsembliENSRNOT00000049942; ENSRNOP00000040859; ENSRNOG00000003343.
GeneIDi29144.
KEGGirno:29144.
UCSCiRGD:2266. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L18889 mRNA. Translation: AAA21015.1.
PIRiC54354.
RefSeqiNP_742005.1. NM_172008.2.
XP_008765901.1. XM_008767679.1.
XP_008765902.1. XM_008767680.1.
UniGeneiRn.1762.

3D structure databases

ProteinModelPortaliP35565.
SMRiP35565. Positions 61-458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247827. 6 interactions.
IntActiP35565. 11 interactions.
MINTiMINT-4996673.
STRINGi10116.ENSRNOP00000040859.

PTM databases

iPTMnetiP35565.
PhosphoSiteiP35565.
SwissPalmiP35565.

Proteomic databases

PaxDbiP35565.
PRIDEiP35565.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000049942; ENSRNOP00000040859; ENSRNOG00000003343.
GeneIDi29144.
KEGGirno:29144.
UCSCiRGD:2266. rat.

Organism-specific databases

CTDi821.
RGDi2266. Canx.

Phylogenomic databases

eggNOGiKOG0675. Eukaryota.
ENOG410XP7T. LUCA.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192436.
HOVERGENiHBG005407.
InParanoidiP35565.
KOiK08054.
OMAiLVILFCC.
OrthoDBiEOG77126Z.
PhylomeDBiP35565.

Enzyme and pathway databases

ReactomeiR-RNO-2132295. MHC class II antigen presentation.
R-RNO-901042. Calnexin/calreticulin cycle.
R-RNO-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

PROiP35565.

Gene expression databases

GenevisibleiP35565. RN.

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.
IPR013320. ConA-like_dom.
[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]
ProtoNetiSearch...

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].
    Tissue: T-cell.
  2. Lubec G., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 49-58, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "Identification and purification of a calcium-binding protein in hepatic nuclear membranes."
    Gilchrist J.S., Pierce G.N.
    J. Biol. Chem. 268:4291-4299(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  4. "Phosphorylation by CK2 and MAPK enhances calnexin association with ribosomes."
    Chevet E., Wong H.N., Gerber D., Cochet C., Fazel A., Cameron P.H., Gushue J.N., Thomas D.Y., Bergeron J.J.
    EMBO J. 18:3655-3666(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-563, INTERACTION WITH MAPK3/ERK1, ASSOCIATION WITH RIBOSOMES.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCALX_RAT
AccessioniPrimary (citable) accession number: P35565
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 8, 2016
This is version 149 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, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.