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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.

Sites

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

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
Complete GO annotation...

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:crt
OrganismiBombyx mori (Silk moth)
Taxonomic identifieri7091 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaBombycoideaBombycidaeBombycinaeBombyx
ProteomesiUP000005204: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 398379Calreticulin
PRO_0000279696Add
BLAST

Amino acid modifications

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

Structurei

3D structure databases

ProteinModelPortaliQ7Z1E6.
SMRiQ7Z1E6. Positions 205-305.

Family & Domainsi

Domains and Repeats

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

Region

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

Motif

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

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

Sequence similaritiesi

Belongs to the calreticulin family.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

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.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[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

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MKAVVLVVVS LLALSSINCD VFFEEKFPDD SWESNWVYSE HPGKEFGKFK    50
LTAGKFFSDP EDDKGLKTSE DARFYALSRK FKPFSNEGKP LVVQFTVKHE 100
QDIDCGGGYL KVFDCKLEQK DMHGETPYEI MFGPDICGPG TKKVHVIFSY 150
KGKNHLIKKD IRCKDDVYTH LYTLIVKPDN TYEVLIDNEK VESGDLEADW 200
DFLPNKKIKD PEAKKPEDWD DKPTIPDPED KKPEDWDKPE HIPDPDATKP 250
EDWDDEMDGE WEPPMIDNPD YKGVWAPKQI DNPAYKGPWV HPEIDNPEYT 300
PDSNLYKRDE ICAVGLDLWQ VKSGTIFDDF LITDDPAAAK ERGEVIKKRQ 350
EGEKKMKSEQ DEAEREKEKA EKPDDEEDDE DLDDETGDAA PVEEHDEL 398
Length:398
Mass (Da):45,802
Last modified:October 1, 2003 - v1
Checksum:i0BC049839F5950EA
GO

Sequence conflict

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

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...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 692629.
KEGGi bmor:692629.

Organism-specific databases

CTDi 45841.

Phylogenomic databases

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.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[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 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.

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: December 11, 2013
This is version 61 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

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