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P15253 (CALR_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calreticulin
Alternative name(s):
CRP55
Calregulin
Endoplasmic reticulum resident protein 60
Short name=ERp60
HACBP
Gene names
Name:CALR
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length418 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 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. Ref.6

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. Interacts with PPIB By similarity.

Subcellular location

Endoplasmic reticulum lumen. 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. Ref.7

The interaction with glycans occurs through a binding site in the globular lectin domain By similarity. Ref.7

The zinc binding sites are localized to the N-domain. Ref.7

Associates with PDIA3 through the tip of the extended arm formed by the P-domain By similarity. Ref.7

Sequence similarities

Belongs to the calreticulin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

APPP050673EBI-9005200,EBI-77613From a different organism.
AppP120232EBI-9005200,EBI-78814From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.3 Ref.4
Chain18 – 418401Calreticulin
PRO_0000004176

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
Region237 – 27034Interaction with PPIB By similarity
Region259 – 297393 X approximate repeats
Region309 – 418110C-domain
Motif415 – 4184Prevents secretion from ER
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

Natural variations

Natural variant351E → D.

Experimental info

Mutagenesis1701H → A: Loss of activity. Ref.8
Sequence conflict901P → T AA sequence Ref.5

Sequences

Sequence LengthMass (Da)Tools
P15253 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: B6082B689DC763A6

FASTA41848,275
        10         20         30         40         50         60 
MLLPVPLLLG LLGLAAAEPV VYFKEQFLDG DGWTERWIES KHKSDFGKFV LSSGKFYGDQ 

        70         80         90        100        110        120 
EKDKGLQTSQ DARFYALSAR FEPFSNKGQP LVVQFTVKHE QNIDCGGGYV KLFPAGLDQK 

       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 
PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KTAEKQMKDK 

       370        380        390        400        410 
QDEEQRLKEE EEEKKRKEEE EAEEDEEDKD DKEDEDEDEE DKDEEEEEAA AGQAKDEL 

« Hide

References

[1]"Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum."
Fliegel L., Burns K., Maclennan D.H., Reithmeier R.A.F., Michalak M.
J. Biol. Chem. 264:21522-21528(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Slow-twitch skeletal muscle.
[2]"Fast-twitch and slow-twitch skeletal muscles express the same isoform of calreticulin."
Fliegel L., Michalak M.
Biochem. Biophys. Res. Commun. 177:979-984(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fast-twitch skeletal muscle.
[3]"Calreticulin is a candidate for a calsequestrin-like function in Ca2(+)-storage compartments (calciosomes) of liver and brain."
Treves S., de Mattei M., Lanfredi M., Villa A., Green N.M., Maclennan D.H., Meldolesi J., Pozzan T.
Biochem. J. 271:473-480(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-36.
[4]"Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum."
Milner R.E., Baksh S., Shemanko C., Carpenter M.R., Smillie L., Vance J.E., Opas M., Michalak M.
J. Biol. Chem. 266:7155-7165(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-46.
[5]"Evidence for complex formation between rabbit lung flavin-containing monooxygenase and calreticulin."
Guan S., Falick A.M., Williams D.E., Cashman J.R.
Biochemistry 30:9892-9900(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Lung.
[6]"Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins."
Saito Y., Ihara Y., Leach M.R., Cohen-Doyle M.F., Williams D.B.
EMBO J. 18:6718-6729(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Identification of the Zn2+ binding region in calreticulin."
Baksh S., Spamer C., Heilmann C., Michalak M.
FEBS Lett. 376:53-57(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: ZINC-BINDING DOMAIN.
[8]"Identification of an N-domain histidine essential for chaperone function in calreticulin."
Guo L., Groenendyk J., Papp S., Dabrowska M., Knoblach B., Kay C., Parker J.M., Opas M., Michalak M.
J. Biol. Chem. 278:50645-50653(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-170.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J05138 mRNA. Translation: AAA31188.1.
PIRA34154.
C33208.
D33208.
S13046.
RefSeqNP_001075704.1. NM_001082235.1.
UniGeneOcu.1840.

3D structure databases

ProteinModelPortalP15253.
SMRP15253. Positions 206-305.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid1172073. 1 interaction.
IntActP15253. 4 interactions.

Proteomic databases

PRIDEP15253.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009050.

Organism-specific databases

CTD811.

Phylogenomic databases

HOVERGENHBG005407.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
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]
PIRSFPIRSF002356. Calreticulin. 1 hit.
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
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_RABIT
AccessionPrimary (citable) accession number: P15253
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: June 11, 2014
This is version 117 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