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P35565 (CALX_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Calnexin
Gene names
Name:Canx
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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.

Subunit structure

Interacts with MAPK3/ERK1. Associates with ribosomes. Ref.4

Subcellular location

Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome By similarity.

Post-translational modification

Phosphorylated at Ser-563 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes. Ref.4 Ref.5

Sequence similarities

Belongs to the calreticulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 591571Calnexin
PRO_0000004201

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
Region349 – 406584 X approximate repeats

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.5
Modified residue5611Phosphothreonine By similarity
Modified residue5631Phosphoserine; by MAPK3 Ref.4 Ref.5
Modified residue5691Phosphoserine By similarity
Modified residue5821Phosphoserine Ref.5
Disulfide bond161 ↔ 195 By similarity
Disulfide bond361 ↔ 367 By similarity

Sequences

Sequence LengthMass (Da)Tools
P35565 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: DF91D099593C62B2

FASTA59167,255
        10         20         30         40         50         60 
MEGKWLLCLL LVLGTAAIQA HDGHDDDMID IEDDLDDVIE EVEDSKSKSD TSTPPSPKVT 

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

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

       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 DLEPFRMTPF 

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

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

       550        560        570        580        590 
EEEEEKLEEK QKSDAEEDGG 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: 8136357] [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, 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: 8440713] [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: 10393181] [Abstract]
Cited for: PHOSPHORYLATION AT SER-563, INTERACTION WITH MAPK3/ERK1.
[5]"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
Moser K., White F.M.
J. Proteome Res. 5:98-104(2006) [PubMed: 16396499] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563 AND SER-582, MASS SPECTROMETRY.
Strain: Fischer.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L18889 mRNA. Translation: AAA21015.1.
IPIIPI00199636.
PIRC54354.
RefSeqNP_742005.1. NM_172008.2.
UniGeneRn.1762.

3D structure databases

ProteinModelPortalP35565.
SMRP35565. Positions 61-458.
ModBaseSearch...

Protein-protein interaction databases

IntActP35565. 2 interactions.
MINTMINT-4996673.
STRINGP35565.

PTM databases

PhosphoSiteP35565.

Proteomic databases

PRIDEP35565.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29144.
KEGGrno:29144.

Organism-specific databases

CTD821.
RGD2266. Canx.

Phylogenomic databases

eggNOGmaNOG11201.
GeneTreeENSGT00430000030841.
HOVERGENHBG005407.
InParanoidP35565.
OrthoDBEOG4DBTDB.
PhylomeDBP35565.

Gene expression databases

ArrayExpressP35565.
GenevestigatorP35565.
GermOnlineENSRNOG00000003343. Rattus norvegicus.

Family and domain databases

InterProIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009033. Calreticulin/calnexin_P.
IPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
[Graphical view]
Gene3DG3DSA:2.10.250.10. Calreticulin/calnexin_P. 2 hits.
G3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
KOK08054.
PANTHERPTHR11073. Calret/calnex. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF63887. Calret_calnex_P. 1 hit.
SSF49899. ConA_like_lec_gl. 2 hits.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio608127.

Entry information

Entry nameCALX_RAT
AccessionPrimary (citable) accession number: P35565
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 25, 2012
This is version 110 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents