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P24643 (CALX_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calnexin
Alternative name(s):
pp90
Gene names
Name:CANX
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length593 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 By similarity.

Subunit structure

Interacts with MAPK3/ERK1. Interacts with KCNH2. Associates with ribosomes. Interacts with SGIP1; involved in negative regulation of endocytosis. 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. Interacts with PPIB. Ref.3

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.

Post-translational modification

Phosphorylated at Ser-565 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. Ref.4

Sequence similarities

Belongs to the calreticulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 593573Calnexin
PRO_0000004197

Regions

Topological domain21 – 482462Lumenal Potential
Transmembrane483 – 50321Helical; Potential
Topological domain504 – 59390Cytoplasmic Potential
Repeat279 – 290121-1
Repeat296 – 307121-2
Repeat315 – 326121-3
Repeat334 – 345121-4
Repeat349 – 359112-1
Repeat368 – 378112-2
Repeat382 – 392112-3
Repeat396 – 406112-4
Region277 – 410134P domain (Extended arm)
Region279 – 345674 X approximate repeats
Region327 – 36034Interaction with PPIB
Region349 – 406584 X approximate repeats
Region504 – 59390Sufficient to mediate interaction with SGIP1 By similarity

Sites

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

Amino acid modifications

Modified residue1381N6-acetyllysine By similarity
Modified residue5551Phosphoserine By similarity
Modified residue5631Phosphothreonine By similarity
Modified residue5651Phosphoserine; by MAPK3 By similarity
Modified residue5841Phosphoserine By similarity
Lipidation5031S-palmitoyl cysteine By similarity
Lipidation5041S-palmitoyl cysteine By similarity
Disulfide bond161 ↔ 195 Ref.4
Disulfide bond361 ↔ 367 Ref.4

Experimental info

Mutagenesis3481D → K: Abolishes interaction with PPIB. Ref.3

Secondary structure

............................................................. 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24643 [UniParc].

Last modified July 15, 1998. Version 3.
Checksum: A2969701B1EB7B6A

FASTA59367,603
        10         20         30         40         50         60 
MEGKWLLCML LVLGTTIVQA HEGHDDDMID IEDDLDDVIE EVEDSKSKPD TSAPTSPKVT 

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

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

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

       250        260        270        280        290        300 
LILNPDNSFE ILVDQSIVNS GNLLNDMTPP VNPSREIEDP EDQKPEDWDE RPKIPDPDAV 

       310        320        330        340        350        360 
KPDDWNEDAP AKIPDEEATK PDGWLDDEPE YVPDPDAEKP EDWDEDMDGE WEAPQIANPK 

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

       430        440        450        460        470        480 
SAIGLELWSM TSDIFFDNFI VCGDRRVVDD WANDGWGLKK AADGAAEPGV VGQMIEAAEE 

       490        500        510        520        530        540 
RPWLWVVYVL TVALPVFLVI LFCCSGKKQS SPVEYKKTDA PQPDVKEEEE EKEEEKDKGD 

       550        560        570        580        590 
EEEEGEEKLE EKQKSDAEED GGTASQEEDD RKPKAEEDEI LNRSPRNRKP RRE 

« Hide

References

[1]"SSR alpha and associated calnexin are major calcium binding proteins of the endoplasmic reticulum membrane."
Wada I., Rindress D., Cameron P.H., Ou W.-J., Doherty J.J. II, Louvard D., Bell A.W., Dignard D., Thomas D.Y., Bergeron J.J.M.
J. Biol. Chem. 266:19599-19610(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]Dignard D.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 67.
[3]"Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain."
Kozlov G., Bastos-Aristizabal S., Maattanen P., Rosenauer A., Zheng F., Killikelly A., Trempe J.F., Thomas D.Y., Gehring K.
J. Biol. Chem. 285:35551-35557(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PPIB, MUTAGENESIS OF ASP-348.
[4]"The Structure of calnexin, an ER chaperone involved in quality control of protein folding."
Schrag J.D., Bergeron J.J., Li Y., Borisova S., Hahn M., Thomas D.Y., Cygler M.
Mol. Cell 8:633-644(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 45-468, DISULFIDE BONDS CALCIUM-BINDING SITES, PROBABLE CARBOHYDRATE-INTERACTING SITES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53616 mRNA. Translation: CAA37678.1.
PIRA37273.
RefSeqNP_001003232.1. NM_001003232.1.
UniGeneCfa.3766.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JHNX-ray2.90A45-468[»]
ProteinModelPortalP24643.
SMRP24643. Positions 61-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29133N.
STRING9615.ENSCAFP00000000498.

Proteomic databases

PaxDbP24643.
PRIDEP24643.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403908.
KEGGcfa:403908.

Organism-specific databases

CTD821.

Phylogenomic databases

eggNOGNOG305105.
HOGENOMHOG000192436.
HOVERGENHBG005407.
InParanoidP24643.
KOK08054.

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

EvolutionaryTraceP24643.
NextBio20817400.

Entry information

Entry nameCALX_CANFA
AccessionPrimary (citable) accession number: P24643
Secondary accession number(s): P79140
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 118 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references