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Q7Z1E6 (CALR_BOMMO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 61. 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
Gene names
Name:crt
OrganismBombyx mori (Silk moth) [Reference proteome]
Taxonomic identifier7091 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx

Protein attributes

Sequence length398 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.

Subunit structure

Monomer By similarity. UniProtKB P27797

Subcellular location

Endoplasmic reticulum lumen.

Tissue specificity

Expressed in fat bodies. Not expressed in midgut, silk gland, ovary or testis. Ref.1 Ref.2

Induction

Induced by disturbances in intracellular calcium levels caused by the chelators BAPTA-AM and EDTA, the endoplasmic reticulum calcium-ATPase inhibitor thapsigargin and by calcium. Not induced by the endoplasmic reticulum stress-inducing drugs brefeldin A, DTT and tunicamycin, or by heat stress and hydrogen peroxide. Ref.2

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. UniProtKB P27797

The interaction with glycans occurs through a binding site in the globular lectin domain By similarity. UniProtKB P27797

The zinc binding sites are localized to the N-domain By similarity. UniProtKB P27797

Sequence similarities

Belongs to the calreticulin family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainRepeat
Signal
   LigandCalcium
Lectin
Metal-binding
Zinc
   Molecular functionChaperone
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
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 – 1919 Potential
Chain20 – 398379Calreticulin
PRO_0000279696

Regions

Repeat191 – 202121-1
Repeat210 – 221121-2
Repeat227 – 238121-3
Repeat244 – 255121-4
Repeat259 – 269112-1
Repeat273 – 283112-2
Repeat287 – 297112-3
Region20 – 197178N-domain
Region191 – 255654 X approximate repeats
Region198 – 308111P-domain
Region259 – 297393 X approximate repeats
Region309 – 39890C-domain
Motif395 – 3984Prevents secretion from ER

Sites

Binding site1091Carbohydrate By similarity
Binding site1111Carbohydrate By similarity
Binding site1281Carbohydrate By similarity
Binding site1351Carbohydrate By similarity
Binding site3171Carbohydrate By similarity

Amino acid modifications

Disulfide bond105 ↔ 137 By similarity UniProtKB P27797

Experimental info

Sequence conflict361W → K AA sequence Ref.4
Sequence conflict411H → A AA sequence Ref.4
Sequence conflict451E → D AA sequence Ref.4
Sequence conflict471G → E AA sequence Ref.4
Sequence conflict491F → K AA sequence Ref.4
Sequence conflict2051N → P in BAC57964. Ref.3
Sequence conflict2851Y → F in BAC57964. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q7Z1E6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 0BC049839F5950EA

FASTA39845,802
        10         20         30         40         50         60 
MKAVVLVVVS LLALSSINCD VFFEEKFPDD SWESNWVYSE HPGKEFGKFK LTAGKFFSDP 

        70         80         90        100        110        120 
EDDKGLKTSE DARFYALSRK FKPFSNEGKP LVVQFTVKHE QDIDCGGGYL KVFDCKLEQK 

       130        140        150        160        170        180 
DMHGETPYEI MFGPDICGPG TKKVHVIFSY KGKNHLIKKD IRCKDDVYTH LYTLIVKPDN 

       190        200        210        220        230        240 
TYEVLIDNEK VESGDLEADW DFLPNKKIKD PEAKKPEDWD DKPTIPDPED KKPEDWDKPE 

       250        260        270        280        290        300 
HIPDPDATKP EDWDDEMDGE WEPPMIDNPD YKGVWAPKQI DNPAYKGPWV HPEIDNPEYT 

       310        320        330        340        350        360 
PDSNLYKRDE ICAVGLDLWQ VKSGTIFDDF LITDDPAAAK ERGEVIKKRQ EGEKKMKSEQ 

       370        380        390 
DEAEREKEKA EKPDDEEDDE DLDDETGDAA PVEEHDEL 

« Hide

References

[1]"Molecular cloning of a cDNA encoding putative calreticulin from the silkworm, Bombyx mori."
Kim S.R., Lee K.S., Kim I., Kang S.W., Nho S.K., Sohn H.D., Jin B.R.
Int. J. Ind. Entomol. 6:93-97(2003)
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Endoplasmic reticulum stress response of Bombyx mori calreticulin."
Goo T.W., Park S., Jin B.R., Yun E.Y., Kim I., Nho S.-K., Kang S.-W., Kwon O.-Y.
Mol. Biol. Rep. 32:133-139(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[3]Takahashi T., Yamashita T.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: p50T.
Tissue: Fat body.
[4]"Protein database for several tissues derived from five instar of silkworm."
Zhong B.-X.
Yi Chuan Xue Bao 28:217-224(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-49.
Strain: Xinhang X Keming.
Tissue: Body wall and Fat body.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY297158 mRNA. Translation: AAP50845.1.
AB090887 mRNA. Translation: BAC57964.1.
RefSeqNP_001037075.1. NM_001043610.1.
UniGeneBmo.1394.

3D structure databases

ProteinModelPortalQ7Z1E6.
SMRQ7Z1E6. Positions 205-305.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID692629.
KEGGbmor:692629.

Organism-specific databases

CTD45841.

Phylogenomic databases

KOK08057.

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_BOMMO
AccessionPrimary (citable) accession number: Q7Z1E6
Secondary accession number(s): P82199, Q869E0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 1, 2003
Last modified: December 11, 2013
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families