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Q4VIT5 (CALR_CHLAE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 48. 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:
Calreticulin
Gene names
Name:CALR
OrganismChlorocebus aethiops (Green monkey) (Cercopithecus aethiops)
Taxonomic identifier9534 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Chlorocebus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis By similarity.

Subunit structure

Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with GABARAP, NR3C1, PDIA3/ERp57 and TRIM21 By similarity.

Subcellular location

Endoplasmic reticulum lumen By similarity. Sarcoplasmic reticulum lumen By similarity.

Domain

Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity By similarity.

The interaction with glycans occurs through a binding site in the globular lectin domain By similarity.

The zinc binding sites are localized to the N-domain By similarity.

Associates with PDIA3 through the tip of the extended arm formed by the P-domain By similarity.

Sequence similarities

Belongs to the calreticulin family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Sarcoplasmic reticulum
   DomainRepeat
Signal
   LigandCalcium
Lectin
Metal-binding
Zinc
   Molecular functionChaperone
   PTMAcetylation
Disulfide bond
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: InterPro

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentsarcoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 By similarity
Chain18 – 417400Calreticulin
PRO_0000246152

Regions

Repeat191 – 202121-1
Repeat210 – 221121-2
Repeat227 – 238121-3
Repeat244 – 255121-4
Repeat259 – 269112-1
Repeat273 – 283112-2
Repeat287 – 297112-3
Region18 – 197180N-domain
Region191 – 255654 X approximate repeats
Region198 – 308111P-domain
Region259 – 297393 X approximate repeats
Region309 – 417109C-domain
Motif414 – 4174Prevents secretion from ER By similarity
Compositional bias351 – 40858Asp/Glu/Lys-rich

Sites

Metal binding261Calcium; via carbonyl oxygen By similarity
Metal binding621Calcium; via carbonyl oxygen By similarity
Metal binding641Calcium; via carbonyl oxygen By similarity
Metal binding3281Calcium By similarity
Binding site1091Carbohydrate By similarity
Binding site1111Carbohydrate By similarity
Binding site1281Carbohydrate By similarity
Binding site1351Carbohydrate By similarity
Binding site3171Carbohydrate By similarity

Amino acid modifications

Modified residue481N6-acetyllysine By similarity
Modified residue1591N6-acetyllysine By similarity
Modified residue2091N6-acetyllysine By similarity
Disulfide bond105 ↔ 137 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4VIT5 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 65506C9D1C341804

FASTA41748,114
        10         20         30         40         50         60 
MLLSVPLLLG LLGLAAAEPA VYFKEQFLDG DGWTSRWIES KHKSDFGKFV LSSGKFYGDE 

        70         80         90        100        110        120 
EKDKGLQTSQ DARFYALSAS FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPNSLDQT 

       130        140        150        160        170        180 
DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN 

       190        200        210        220        230        240 
TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDASKPEDWD ERAKIDDPTD SKPEDWDKPE 

       250        260        270        280        290        300 
HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS 

       310        320        330        340        350        360 
PDPSIYAYDN FGVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK 

       370        380        390        400        410 
QDEEQRLKEE EEDKKRKEEE EAEDKEDDED KDEDEEDEED KEEDEEEDVP GQAKDEL

« Hide

References

[1]"A mutant cell with a novel defect in MHC class I quality control."
York I.A., Grant E.P., Dahl A.M., Rock K.L.
J. Immunol. 174:6839-6846(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY901963 mRNA. Translation: AAX86983.1.

3D structure databases

ProteinModelPortalQ4VIT5.
SMRQ4VIT5. Positions 206-305.
ModBaseSearch...

Proteomic databases

PRIDEQ4VIT5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG005407.
OrthoDBEOG41JZCD.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PANTHERPTHR11073. PTHR11073. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFPIRSF002356. Calreticulin. 1 hit.
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF49899. ConA_like_lec_gl. 2 hits.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALR_CHLAE
AccessionPrimary (citable) accession number: Q4VIT5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 5, 2005
Last modified: March 6, 2013
This is version 48 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

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