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Q9STD3 (CALR_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 85. 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
OrganismChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifier3055 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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
Gene Ontology (GO)
   Biological_processanthocyanin-containing compound metabolic process

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

calcium ion homeostasis

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

defense response signaling pathway, resistance gene-independent

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

defense response to bacterium

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

plant-type hypersensitive response

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

protein folding

Inferred from electronic annotation. Source: InterPro

response to cadmium ion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to oxidative stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

response to salt stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentapoplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

chloroplast

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

mitochondrion

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

plasmodesma

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

vacuolar membrane

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   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 – 1818 Potential
Chain19 – 420402Calreticulin
PRO_0000004189

Regions

Repeat194 – 205121-1
Repeat213 – 224121-2
Repeat230 – 241121-3
Repeat248 – 259121-4
Repeat263 – 273112-1
Repeat277 – 287112-2
Repeat291 – 301112-3
Region194 – 259664 X approximate repeats
Region263 – 301393 X approximate repeats
Motif417 – 4204Prevents secretion from ER Potential
Compositional bias355 – 41460Asp/Glu/Lys-rich

Sites

Binding site1101Carbohydrate By similarity
Binding site1121Carbohydrate By similarity
Binding site1311Carbohydrate By similarity
Binding site1381Carbohydrate By similarity
Binding site3211Carbohydrate By similarity

Amino acid modifications

Disulfide bond106 ↔ 140 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9STD3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: DD3BA3AFFBF61C9B

FASTA42047,328
        10         20         30         40         50         60 
MKWGVVAVLA TLVVAASAKD YFKETFDGSW ADRWTKSSWK VSDGSAGEFK LTAGKWYGDA 

        70         80         90        100        110        120 
EADKGIQTGP DSKFFAISAP LATVFDNTGK DTVVQFSVKH EQDLDCGGGY IKVVPATSEK 

       130        140        150        160        170        180 
QMGEFGGDTP YSIMFGPDIC GYSTRKVHVI LTYKGKNYLI KKDIKAETDQ LTHVYTLVIK 

       190        200        210        220        230        240 
PDNTYQVLID LKEVASGSLY EDWDMLPPKT IKDPKASKPE DWDEREEIAD PEDKKPEGWD 

       250        260        270        280        290        300 
DIPATIADKD AKKPEDWDDE EDGTWEPPMI PNPEYKGEWK AKMIKNPAYK GIWVAPDIDN 

       310        320        330        340        350        360 
PDYVHDDKLY NFKDLKFVGF ELWQVKSGSI FDNILVTDDL EAAKKFAEDT WGKHKDEEKA 

       370        380        390        400        410        420 
MFDKVKKEED EKKAKDAPPP PVDAEAAEEE DDEYEDKEEP SGMGSIKIPK EEEESGHDEL 

« Hide

References

[1]"Cloning and characterization of a cDNA encoding Chlamydomonas reinhardtii calreticulin."
Zuppini A., Kaydamov C.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 137c / CC-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ000765 mRNA. Translation: CAB54526.1.
RefSeqXP_001689661.1. XM_001689609.1.
UniGeneCre.14231.

3D structure databases

ProteinModelPortalQ9STD3.
SMRQ9STD3. Positions 209-306.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9STD3.
ProMEXQ9STD3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5715514.
KEGGcre:CHLREDRAFT_78954.

Phylogenomic databases

eggNOGNOG305105.
KOK08057.
OMARWVNSKH.
ProtClustDBCLSN2920675.

Family and domain databases

Gene3D2.60.120.200. 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. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALR_CHLRE
AccessionPrimary (citable) accession number: Q9STD3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: March 19, 2014
This is version 85 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