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O81919 (CALR_BETVU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. 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
OrganismBeta vulgaris (Sugar beet)
Taxonomic identifier161934 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeBeta

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER By similarity.

Subcellular location

Endoplasmic 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.

Sequence similarities

Belongs to the calreticulin family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 416391Calreticulin
PRO_0000004188

Regions

Repeat197 – 208121-1
Repeat216 – 227121-2
Repeat233 – 244121-3
Repeat251 – 262121-4
Repeat266 – 276112-1
Repeat280 – 290112-2
Repeat294 – 304112-3
Region197 – 262664 X approximate repeats
Region266 – 304393 X approximate repeats
Motif413 – 4164Prevents secretion from ER Potential
Compositional bias358 – 41154Asp/Glu/Lys-rich

Sites

Binding site1151Carbohydrate By similarity
Binding site1171Carbohydrate By similarity
Binding site1341Carbohydrate By similarity
Binding site1411Carbohydrate By similarity
Binding site3241Carbohydrate By similarity

Amino acid modifications

Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation1571N-linked (GlcNAc...) Potential
Disulfide bond111 ↔ 143 By similarity

Sequences

Sequence LengthMass (Da)Tools
O81919 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 565FEC3489F77CA7

FASTA41648,136
        10         20         30         40         50         60 
MENRGRNPSF LSLLLLLSLF AIASAKVFFE ERFEDGWEKR WVKSEWKKDE SMAGEWNYTS 

        70         80         90        100        110        120 
GKWNGDANDK GIQTSEDYRF YAISAEFPEF SNKDNTLVFQ FSVKHEQKLD CGGGYMKLLS 

       130        140        150        160        170        180 
GEVDQKKFGG DTPYSIMFGP DICGYSTKKV HAIFNYNDTN HLIKKDVPCE TDQLTHVYTF 

       190        200        210        220        230        240 
ILRPDATYSI LIDNQEKQTG SLYTDWDLLP AKKIKDPEAK KPEDWDDKEF IPDPEDKKPE 

       250        260        270        280        290        300 
GYDDIPAEIT DPEAKKPEDW DDEEDGEWTA PTIPNPEYKG PWKAKKIKNP NYKGKWKAPM 

       310        320        330        340        350        360 
IDNPEFKDDP ELYVYPKLRY VGVELWQVKS GTLFDNVLVC DDPEYAKQLA EETWGKQKDA 

       370        380        390        400        410 
EKAAFEELEK KREEEETKDD PVESDAEDED EAEADDSDKD DADKSDDKDD DQHDEL 

« Hide

References

[1]"Nucleotide sequence from sugar beet calreticulin."
Viereck R.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: VV-D/ZR5.
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ002057 mRNA. Translation: CAA05161.1.
PIRT14554.

3D structure databases

ProteinModelPortalO81919.
SMRO81919. Positions 211-312.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

PhylomeDBO81919.

Family and domain databases

Gene3D2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
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. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALR_BETVU
AccessionPrimary (citable) accession number: O81919
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families