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Q7Z1E6

- CALR_BOMMO

UniProt

Q7Z1E6 - CALR_BOMMO

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Protein

Calreticulin

Gene

crt

Organism
Bombyx mori (Silk moth)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei109 – 1091CarbohydrateBy similarity
Binding sitei111 – 1111CarbohydrateBy similarity
Binding sitei128 – 1281CarbohydrateBy similarity
Binding sitei135 – 1351CarbohydrateBy similarity
Binding sitei317 – 3171CarbohydrateBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. carbohydrate binding Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
Gene namesi
Name:crtImported
OrganismiBombyx mori (Silk moth)
Taxonomic identifieri7091 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
ProteomesiUP000005204: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 398379CalreticulinSequence AnalysisPRO_0000279696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi105 ↔ 137By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

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

Inductioni

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.1 Publication

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ7Z1E6.
SMRiQ7Z1E6. Positions 205-305.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati191 – 202121-1Sequence AnalysisAdd
BLAST
Repeati210 – 221121-2Sequence AnalysisAdd
BLAST
Repeati227 – 238121-3Sequence AnalysisAdd
BLAST
Repeati244 – 255121-4Sequence AnalysisAdd
BLAST
Repeati259 – 269112-1Sequence AnalysisAdd
BLAST
Repeati273 – 283112-2Sequence AnalysisAdd
BLAST
Repeati287 – 297112-3Sequence AnalysisAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 197178N-domainSequence AnalysisAdd
BLAST
Regioni191 – 255654 X approximate repeatsSequence AnalysisAdd
BLAST
Regioni198 – 308111P-domainSequence AnalysisAdd
BLAST
Regioni259 – 297393 X approximate repeatsSequence AnalysisAdd
BLAST
Regioni309 – 39890C-domainSequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi395 – 3984Prevents secretion from ERSequence Analysis

Domaini

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).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 similaritiesi

Belongs to the calreticulin family.Sequence Analysis

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

InParanoidiQ7Z1E6.
KOiK08057.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q7Z1E6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKAVVLVVVS LLALSSINCD VFFEEKFPDD SWESNWVYSE HPGKEFGKFK
60 70 80 90 100
LTAGKFFSDP EDDKGLKTSE DARFYALSRK FKPFSNEGKP LVVQFTVKHE
110 120 130 140 150
QDIDCGGGYL KVFDCKLEQK DMHGETPYEI MFGPDICGPG TKKVHVIFSY
160 170 180 190 200
KGKNHLIKKD IRCKDDVYTH LYTLIVKPDN TYEVLIDNEK VESGDLEADW
210 220 230 240 250
DFLPNKKIKD PEAKKPEDWD DKPTIPDPED KKPEDWDKPE HIPDPDATKP
260 270 280 290 300
EDWDDEMDGE WEPPMIDNPD YKGVWAPKQI DNPAYKGPWV HPEIDNPEYT
310 320 330 340 350
PDSNLYKRDE ICAVGLDLWQ VKSGTIFDDF LITDDPAAAK ERGEVIKKRQ
360 370 380 390
EGEKKMKSEQ DEAEREKEKA EKPDDEEDDE DLDDETGDAA PVEEHDEL
Length:398
Mass (Da):45,802
Last modified:October 1, 2003 - v1
Checksum:i0BC049839F5950EA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti36 – 361W → K AA sequence (PubMed:11280994)Curated
Sequence conflicti41 – 411H → A AA sequence (PubMed:11280994)Curated
Sequence conflicti45 – 451E → D AA sequence (PubMed:11280994)Curated
Sequence conflicti47 – 471G → E AA sequence (PubMed:11280994)Curated
Sequence conflicti49 – 491F → K AA sequence (PubMed:11280994)Curated
Sequence conflicti205 – 2051N → P in BAC57964. 1 PublicationCurated
Sequence conflicti285 – 2851Y → F in BAC57964. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY297158 mRNA. Translation: AAP50845.1.
AB090887 mRNA. Translation: BAC57964.1.
RefSeqiNP_001037075.1. NM_001043610.1.
UniGeneiBmo.1394.

Genome annotation databases

GeneIDi692629.
KEGGibmor:692629.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY297158 mRNA. Translation: AAP50845.1 .
AB090887 mRNA. Translation: BAC57964.1 .
RefSeqi NP_001037075.1. NM_001043610.1.
UniGenei Bmo.1394.

3D structure databases

ProteinModelPortali Q7Z1E6.
SMRi Q7Z1E6. Positions 205-305.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 692629.
KEGGi bmor:692629.

Organism-specific databases

CTDi 45841.

Phylogenomic databases

InParanoidi Q7Z1E6.
KOi K08057.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002356. Calreticulin. 1 hit.
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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 bodyImported.
  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 Keming1 Publication.
    Tissue: Body wall1 Publication and Fat body1 Publication.

Entry informationi

Entry nameiCALR_BOMMO
AccessioniPrimary (citable) accession number: Q7Z1E6
Secondary accession number(s): P82199, Q869E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: October 1, 2003
Last modified: October 29, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3