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Protein

Calreticulin

Gene
N/A
Organism
Berberis stolonifera (Barberry)
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 sitei112 – 1121CarbohydrateBy similarity
Binding sitei114 – 1141CarbohydrateBy similarity
Binding sitei131 – 1311CarbohydrateBy similarity
Binding sitei138 – 1381CarbohydrateBy similarity
Binding sitei321 – 3211CarbohydrateBy 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
OrganismiBerberis stolonifera (Barberry)
Taxonomic identifieri33814 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesBerberidaceaeBerberidoideaeBerberis

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
Chaini? – 416CalreticulinPRO_0000004187
Signal peptidei1 – ?Sequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi108 ↔ 140By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ9ZPP1.
SMRiQ9ZPP1. Positions 209-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati194 – 205121-1Add
BLAST
Repeati213 – 224121-2Add
BLAST
Repeati230 – 241121-3Add
BLAST
Repeati248 – 259121-4Add
BLAST
Repeati263 – 273112-1Add
BLAST
Repeati277 – 287112-2Add
BLAST
Repeati291 – 301112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 259664 X approximate repeatsAdd
BLAST
Regioni263 – 301393 X approximate repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi413 – 4164Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi355 – 41157Asp/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

Gene3Di2.10.250.10. 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. 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. 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.

Q9ZPP1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIAERRSRS HLALRVRDRV SAEVFFEERF EDGWESKWVK SDWKRDENMA
60 70 80 90 100
GEWNFTSGKW NGDANDKGIQ TSEDYRFYAI SAAFPEFSNK GKTLVFQFSV
110 120 130 140 150
KHEQKLDCGG GYMKLLSGDV DQKKFGGDTP YSIMFGPDIC GYSTKKVHAI
160 170 180 190 200
LTKGETNHLI KKDVPCETDQ LTHVYTFILR PDASYSILID NVEKQSGSVY
210 220 230 240 250
TDWDILPPKQ IKDPEAKKPE DWEDKEYIPD PEDKKPEGYD DIPKEITDPE
260 270 280 290 300
AKKPEDWDDE EDGEWTAPTI PNPDYKGEWK PKKIKNPNFK GKWKAPMIDN
310 320 330 340 350
PDFKDDPDIY VFPKLKYVGI ELWQVKSGTM FDNVLICDDP DYAKKLAEET
360 370 380 390 400
WGKNKDAEKA AFDEAEKKKE EEEAKDDPTE SDDEKPDEEG ESDGEGDDES
410
KDIDNEEDDE DVHDEL
Length:416
Mass (Da):47,927
Last modified:May 1, 1999 - v1
Checksum:i08AC46885BF69114
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052040 mRNA. Translation: AAD17490.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF052040 mRNA. Translation: AAD17490.1.

3D structure databases

ProteinModelPortaliQ9ZPP1.
SMRiQ9ZPP1. Positions 209-282.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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

Publicationsi

  1. "Calreticulin from Berberis stolonifera."
    Chou W.-M., Kutchan T.M.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiCALR_BERST
AccessioniPrimary (citable) accession number: Q9ZPP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: January 7, 2015
This is version 79 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

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.