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Protein

Calreticulin

Gene
N/A
Organism
Beta vulgaris (Sugar beet)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 sitei115CarbohydrateBy similarity1
Binding sitei117CarbohydrateBy similarity1
Binding sitei134CarbohydrateBy similarity1
Binding sitei141CarbohydrateBy similarity1
Binding sitei324CarbohydrateBy 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
OrganismiBeta vulgaris (Sugar beet)
Taxonomic identifieri161934 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesChenopodiaceaeBetoideaeBeta

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
ChainiPRO_000000418826 – 416CalreticulinAdd BLAST391

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi57N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi111 ↔ 143By similarity
Glycosylationi157N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO81919.

Structurei

3D structure databases

ProteinModelPortaliO81919.
SMRiO81919.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati197 – 2081-1Add BLAST12
Repeati216 – 2271-2Add BLAST12
Repeati233 – 2441-3Add BLAST12
Repeati251 – 2621-4Add BLAST12
Repeati266 – 2762-1Add BLAST11
Repeati280 – 2902-2Add BLAST11
Repeati294 – 3042-3Add BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni197 – 2624 X approximate repeatsAdd BLAST66
Regioni266 – 3043 X approximate repeatsAdd BLAST39

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi413 – 416Prevents secretion from ERPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi358 – 411Asp/Glu/Lys-richAdd BLAST54

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.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

KOiK08057.
PhylomeDBiO81919.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
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. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O81919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENRGRNPSF LSLLLLLSLF AIASAKVFFE ERFEDGWEKR WVKSEWKKDE
60 70 80 90 100
SMAGEWNYTS GKWNGDANDK GIQTSEDYRF YAISAEFPEF SNKDNTLVFQ
110 120 130 140 150
FSVKHEQKLD CGGGYMKLLS GEVDQKKFGG DTPYSIMFGP DICGYSTKKV
160 170 180 190 200
HAIFNYNDTN HLIKKDVPCE TDQLTHVYTF ILRPDATYSI LIDNQEKQTG
210 220 230 240 250
SLYTDWDLLP AKKIKDPEAK KPEDWDDKEF IPDPEDKKPE GYDDIPAEIT
260 270 280 290 300
DPEAKKPEDW DDEEDGEWTA PTIPNPEYKG PWKAKKIKNP NYKGKWKAPM
310 320 330 340 350
IDNPEFKDDP ELYVYPKLRY VGVELWQVKS GTLFDNVLVC DDPEYAKQLA
360 370 380 390 400
EETWGKQKDA EKAAFEELEK KREEEETKDD PVESDAEDED EAEADDSDKD
410
DADKSDDKDD DQHDEL
Length:416
Mass (Da):48,136
Last modified:November 1, 1998 - v1
Checksum:i565FEC3489F77CA7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002057 mRNA. Translation: CAA05161.1.
PIRiT14554.
RefSeqiNP_001289994.1. NM_001303065.1.

Genome annotation databases

GeneIDi104890403.
KEGGibvg:104890403.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002057 mRNA. Translation: CAA05161.1.
PIRiT14554.
RefSeqiNP_001289994.1. NM_001303065.1.

3D structure databases

ProteinModelPortaliO81919.
SMRiO81919.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO81919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi104890403.
KEGGibvg:104890403.

Phylogenomic databases

KOiK08057.
PhylomeDBiO81919.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
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. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCALR_BETVU
AccessioniPrimary (citable) accession number: O81919
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.