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Q06814 (CALR_SCHMA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 86. 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):
Protein SM4
OrganismSchistosoma mansoni (Blood fluke)
Taxonomic identifier6183 [NCBI]
Taxonomic lineageEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

Protein attributes

Sequence length393 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.

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 – 1616 Potential
Chain17 – 393377Calreticulin
PRO_0000004183

Regions

Repeat189 – 200121-1
Repeat208 – 219121-2
Repeat225 – 236121-3
Repeat242 – 253121-4
Repeat257 – 267112-1
Repeat271 – 281112-2
Repeat285 – 295112-3
Region189 – 253654 X 12 AA approximate repeats
Region257 – 295393 X 11 AA approximate repeats
Motif390 – 3934Prevents secretion from ER
Compositional bias350 – 38940Asp/Glu/Lys-rich

Sites

Binding site1071Carbohydrate By similarity
Binding site1091Carbohydrate By similarity
Binding site1261Carbohydrate By similarity
Binding site1331Carbohydrate By similarity
Binding site3151Carbohydrate By similarity

Amino acid modifications

Glycosylation271N-linked (GlcNAc...) Potential
Disulfide bond103 ↔ 135 By similarity

Experimental info

Sequence conflict89 – 902MV → IL in AAA19024. Ref.2
Sequence conflict188 – 20720Missing in AAA19024. Ref.2
Sequence conflict3781Y → D in AAA19024. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q06814 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 45F59857C21940D2

FASTA39345,398
        10         20         30         40         50         60 
MLSILLTLLL SKYALGHEVW FSETFPNESI ENWVQSTYNA EKQGEFKVEA GKSPVDPIED 

        70         80         90        100        110        120 
LGLKTTQDAR FYGIARKISE PFSNRGKTMV LQFTVKFDKT VSCGGAYIKL LGSDIDPKKF 

       130        140        150        160        170        180 
HGESPYKIMF GPDICGMATK KVHVIFNYKG KNHLIKKEIP CKDDLKTHLY TLIVNPNNKY 

       190        200        210        220        230        240 
EVLVDNAKVE EGSLEDDWDM LPPKKIDDPN DKKPDDWVDE QFIDDPDDKK PDNWDQPKTI 

       250        260        270        280        290        300 
PDMDAKKPDD WDDAMDGEWE RPQKDNPEYK GEWTPRRIDN PKYKGEWKPV QIDNPEYKHD 

       310        320        330        340        350        360 
PELYVLNDIG YVGFDLWQVD SGSIFDNILI TDSPDFAKEE GERLWRKRYD AEVAKEQSSA 

       370        380        390 
KDDKEEAEET KERKELPYDA KASDEPSGDH DEL 

« Hide

References

[1]"Cloning of the gene encoding a Schistosoma mansoni antigen homologous to human Ro/SS-A autoantigen."
Khalife J., Trottein F., Schacht A.-M., Godin C., Pierce R.J., Capron A.
Mol. Biochem. Parasitol. 57:193-202(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Puerto Rican.
[2]"Cloning and sequencing of the gene encoding Schistosoma mansoni calreticulin."
Khalife J., Pierce R.J., Godin C., Capron A.
Mol. Biochem. Parasitol. 62:313-315(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Puerto Rican.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M93097 mRNA. Translation: AAA29854.1.
L24159 Genomic DNA. Translation: AAA19024.1.
PIRA48573.

3D structure databases

ProteinModelPortalQ06814.
SMRQ06814. Positions 204-303.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ06814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOGENOMHOG000192435.

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

Entry information

Entry nameCALR_SCHMA
AccessionPrimary (citable) accession number: Q06814
Secondary accession number(s): Q26562
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: February 1, 1996
Last modified: October 16, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families