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Protein

Calreticulin

Gene
N/A
Organism
Euglena gracilis
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei107 – 1071CarbohydrateBy similarity
Binding sitei109 – 1091CarbohydrateBy similarity
Binding sitei125 – 1251CarbohydrateBy similarity
Binding sitei132 – 1321CarbohydrateBy similarity
Binding sitei314 – 3141CarbohydrateBy 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
OrganismiEuglena gracilis
Taxonomic identifieri3039 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaEuglenidaEuglenalesEuglenaceaeEuglena

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

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 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 401383CalreticulinPRO_0000004190Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi103 ↔ 134By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliQ9ZNY3.
SMRiQ9ZNY3. Positions 202-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati187 – 198121-1Add
BLAST
Repeati206 – 217121-2Add
BLAST
Repeati223 – 234121-3Add
BLAST
Repeati241 – 252121-4Add
BLAST
Repeati256 – 266112-1Add
BLAST
Repeati270 – 280112-2Add
BLAST
Repeati284 – 294112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni187 – 252664 X approximate repeatsAdd
BLAST
Regioni256 – 294393 X approximate repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi398 – 4014Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi348 – 39750Asp/Glu/Lys-richAdd
BLAST

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

Family and domain databases

Gene3Di2.60.120.200. 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. 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. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9ZNY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKELWLGLL LSSQAVLSTI YYKETFEPDW ETRWTHSTAK SDYGKFKLTS
60 70 80 90 100
GKFYGDKAKD AGIQTSQDAK FYAISSPIAS SFSNEGKDLV LQFSVKHEQD
110 120 130 140 150
IDCGGGYLKL LPSVDAAKFT GDTPYHIMFG PDICGATKKI HFILTYKGKN
160 170 180 190 200
LLWKKEPRCE TDTLSHTYTA VIKADRTYEV LVDQVKKESG TLEEDWEILK
210 220 230 240 250
PKTIPDPEDK KPADWVDEPD MVDPEDKKPE DWDKEPAQIP DPDATQPDDW
260 270 280 290 300
DEEEDGKWEA PMISNPKYKG EWKAKKIPNP AYKGVWKPRD IPNPEYEADD
310 320 330 340 350
KVHIFDEIAA VGFDLWQVKS GTIFDNIIVT DSLAEAKAFY DQTNGATKDA
360 370 380 390 400
EKKAFDSAEA DKRKKEEDER KKQEEEEKKT AEEDEDDDDE EEEEDDKKDE

L
Length:401
Mass (Da):45,911
Last modified:April 30, 1999 - v1
Checksum:i056B074C16292674
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09816 mRNA. Translation: CAA70945.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y09816 mRNA. Translation: CAA70945.1.

3D structure databases

ProteinModelPortaliQ9ZNY3.
SMRiQ9ZNY3. Positions 202-275.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di2.60.120.200. 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. 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. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Evidence for conservation of a calcium homeostat component: purification characterization and cloning of calreticulin from Euglena gracilis."
    Navazzio L., Baldan B., Martin W., Mariani P.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiCALR_EUGGR
AccessioniPrimary (citable) accession number: Q9ZNY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 30, 2000
Last sequence update: April 30, 1999
Last modified: January 6, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.