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Protein

Calreticulin

Gene

crt

Organism
Bombyx mori (Silk moth)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei109CarbohydrateBy similarity1
Binding sitei111CarbohydrateBy similarity1
Binding sitei128CarbohydrateBy similarity1
Binding sitei135CarbohydrateBy similarity1
Binding sitei317CarbohydrateBy similarity1

GO - Molecular functioni

GO - Biological processi

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
Proteomesi
  • UP000005204 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000027969620 – 398CalreticulinSequence analysisAdd BLAST379

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi105 ↔ 137By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ7Z1E6.

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

Protein-protein interaction databases

STRINGi7091.BGIBMGA000475-TA.

Structurei

3D structure databases

ProteinModelPortaliQ7Z1E6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati191 – 2021-1Sequence analysisAdd BLAST12
Repeati210 – 2211-2Sequence analysisAdd BLAST12
Repeati227 – 2381-3Sequence analysisAdd BLAST12
Repeati244 – 2551-4Sequence analysisAdd BLAST12
Repeati259 – 2692-1Sequence analysisAdd BLAST11
Repeati273 – 2832-2Sequence analysisAdd BLAST11
Repeati287 – 2972-3Sequence analysisAdd BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni20 – 197N-domainSequence analysisAdd BLAST178
Regioni191 – 2554 X approximate repeatsSequence analysisAdd BLAST65
Regioni198 – 308P-domainSequence analysisAdd BLAST111
Regioni259 – 2973 X approximate repeatsSequence analysisAdd BLAST39
Regioni309 – 398C-domainSequence analysisAdd BLAST90

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi395 – 398Prevents secretion from ERSequence analysis4

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

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
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. 2 hits.
[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)DescriptionActionsGraphical viewLength
Sequence conflicti36W → K AA sequence (PubMed:11280994).Curated1
Sequence conflicti41H → A AA sequence (PubMed:11280994).Curated1
Sequence conflicti45E → D AA sequence (PubMed:11280994).Curated1
Sequence conflicti47G → E AA sequence (PubMed:11280994).Curated1
Sequence conflicti49F → K AA sequence (PubMed:11280994).Curated1
Sequence conflicti205N → P in BAC57964 (Ref. 3) Curated1
Sequence conflicti285Y → F in BAC57964 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AY297158 mRNA. Translation: AAP50845.1.
AB090887 mRNA. Translation: BAC57964.1.
RefSeqiNP_001037075.1. NM_001043610.1.
UniGeneiBmo.1394.

3D structure databases

ProteinModelPortaliQ7Z1E6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7091.BGIBMGA000475-TA.

Proteomic databases

PRIDEiQ7Z1E6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi692629.
KEGGibmor:692629.

Organism-specific databases

CTDi45841.

Phylogenomic databases

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
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. 2 hits.
[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]
ProtoNetiSearch...

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 5, 2016
This is version 71 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.