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P28491 (CALR_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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·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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length417 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 By similarity. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis. Ref.1

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. Cytoplasmperinuclear region. Membrane. Note: During oocyte maturation and after parthenogenetic activation accumulates in the plasma membrane region. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex. Ref.1 Ref.4

Tissue specificity

In blastocyst expressed in all blastomeres (at protein level). In embryos, expressed in spleen, kidney, liver, fat, muscle, ovary, granulosa cells and cumulus cells. Ref.1

Developmental stage

Expressed in immature GV-stage oocytes, mature MII-stage oocytes, parthenogenetically activated MII-stage oocytes and in pronuclear embryos (at protein level). During in vitro oocyte maturation, expression initially increases after 12 hours of culture, followed by a strong decline at 30 hours (MI stage) and 44 hours (MII stage). Expression remains constant in MII-stage oocytes after parthenogenetic activation, increasing in two- and four-cell parthenotes. Not detected in blastocyst stage embryos. Ref.1

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.

Sequence similarities

Belongs to the calreticulin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Endoplasmic reticulum
Membrane
Sarcoplasmic reticulum
   DomainRepeat
Signal
   LigandCalcium
Lectin
Metal-binding
Zinc
   Molecular functionChaperone
   PTMAcetylation
Disulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle arrest

Inferred from electronic annotation. Source: Ensembl

cellular senescence

Inferred from electronic annotation. Source: Ensembl

cortical actin cytoskeleton organization

Inferred from electronic annotation. Source: Ensembl

negative regulation of intracellular steroid hormone receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of retinoic acid receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

peptide antigen assembly with MHC class I protein complex

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA replication

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of dendritic cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

positive regulation of phagocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of substrate adhesion-dependent cell spreading

Inferred from electronic annotation. Source: Ensembl

protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

protein folding

Inferred from electronic annotation. Source: InterPro

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

protein stabilization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentMHC class I peptide loading complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

polysome

Inferred from electronic annotation. Source: Ensembl

sarcoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from sequence or structural similarity. Source: UniProtKB

carbohydrate binding

Inferred from electronic annotation. Source: Ensembl

mRNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Ref.4
Chain18 – 417400Calreticulin
PRO_0000004175

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 – 417109C-domain
Motif414 – 4174Prevents secretion from ER By similarity
Compositional bias351 – 40757Asp/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 residue1591N6-acetyllysine By similarity
Modified residue2091N6-acetyllysine By similarity
Disulfide bond137 ↔ 163 By similarity

Experimental info

Sequence conflict151A → V in CAA23142. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P28491 [UniParc].

Last modified May 16, 2012. Version 3.
Checksum: 31A9E4CC95F2D54F

FASTA41748,288
        10         20         30         40         50         60 
MLLPVPLLLG LVGLAAAEPT IYFKEQFLDG DGWTDRWIES KHKPDFGRFV LSSGKFYGDQ 

        70         80         90        100        110        120 
EKDKGLQTSQ DARFYALSAR FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPDGLDQT 

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

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

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

       310        320        330        340        350        360 
PDSNIYAYEN FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK 

       370        380        390        400        410 
QDEEQRLKEE EEEKKRKEEE EVDKEDEEDK DEDEEEEDEK EEEEEEDAAA GQAKDEL 

« Hide

References

« Hide 'large scale' references
[1]"Involvement of ER-calreticulin-Ca2+ signaling in the regulation of porcine oocyte meiotic maturation and maternal gene expression."
Zhang D.X., Li X.P., Sun S.C., Shen X.H., Cui X.S., Kim N.H.
Mol. Reprod. Dev. 77:462-471(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Oocyte.
[2]Porcine genome sequencing project
Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
Winteroe A.K., Fredholm M., Davies W.
Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-105.
Tissue: Small intestine.
[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 18-32, SUBCELLULAR LOCATION.
Tissue: Uterus.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GQ984146 mRNA. Translation: ADD52600.1.
CU463133 Genomic DNA. No translation available.
F14591 mRNA. Translation: CAA23142.1.
PIRB33208.
RefSeqNP_001167604.1. NM_001174133.1.
UniGeneSsc.48945.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9823.ENSSSCP00000014615.

Proteomic databases

PaxDbP28491.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000015020; ENSSSCP00000014615; ENSSSCG00000013746.
GeneID100381266.
KEGGssc:100381266.

Organism-specific databases

CTD811.

Phylogenomic databases

eggNOGNOG305105.
GeneTreeENSGT00430000030841.
HOGENOMHOG000192435.
KOK08057.
OMAVKLFPDG.
OrthoDBEOG77126Z.
TreeFamTF338438.

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_PIG
AccessionPrimary (citable) accession number: P28491
Secondary accession number(s): D4N5N1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: May 16, 2012
Last modified: April 16, 2014
This is version 92 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