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Q9ZPP1 (CALR_BERST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subcellular location

Endoplasmic reticulum lumen By similarity.

Domain

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.

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 similarities

Belongs to the calreticulin family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainRepeat
Signal
   LigandCalcium
Lectin
Metal-binding
Zinc
   Molecular functionChaperone
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological_processprotein folding

Inferred from electronic annotation. Source: InterPro

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Chain? – 416CalreticulinPRO_0000004187

Regions

Repeat194 – 205121-1
Repeat213 – 224121-2
Repeat230 – 241121-3
Repeat248 – 259121-4
Repeat263 – 273112-1
Repeat277 – 287112-2
Repeat291 – 301112-3
Region194 – 259664 X approximate repeats
Region263 – 301393 X approximate repeats
Motif413 – 4164Prevents secretion from ER Potential
Compositional bias355 – 41157Asp/Glu/Lys-rich

Sites

Binding site1121Carbohydrate By similarity
Binding site1141Carbohydrate By similarity
Binding site1311Carbohydrate By similarity
Binding site1381Carbohydrate By similarity
Binding site3211Carbohydrate By similarity

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Disulfide bond108 ↔ 140 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZPP1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 08AC46885BF69114

FASTA41647,927
        10         20         30         40         50         60 
MAIAERRSRS HLALRVRDRV SAEVFFEERF EDGWESKWVK SDWKRDENMA GEWNFTSGKW 

        70         80         90        100        110        120 
NGDANDKGIQ TSEDYRFYAI SAAFPEFSNK GKTLVFQFSV KHEQKLDCGG GYMKLLSGDV 

       130        140        150        160        170        180 
DQKKFGGDTP YSIMFGPDIC GYSTKKVHAI LTKGETNHLI KKDVPCETDQ LTHVYTFILR 

       190        200        210        220        230        240 
PDASYSILID NVEKQSGSVY TDWDILPPKQ IKDPEAKKPE DWEDKEYIPD PEDKKPEGYD 

       250        260        270        280        290        300 
DIPKEITDPE AKKPEDWDDE EDGEWTAPTI PNPDYKGEWK PKKIKNPNFK GKWKAPMIDN 

       310        320        330        340        350        360 
PDFKDDPDIY VFPKLKYVGI ELWQVKSGTM FDNVLICDDP DYAKKLAEET WGKNKDAEKA 

       370        380        390        400        410 
AFDEAEKKKE EEEAKDDPTE SDDEKPDEEG ESDGEGDDES KDIDNEEDDE DVHDEL 

« Hide

References

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF052040 mRNA. Translation: AAD17490.1.

3D structure databases

ProteinModelPortalQ9ZPP1.
SMRQ9ZPP1. Positions 209-282.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProIPR001580. 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]
PANTHERPTHR11073. PTHR11073. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFPIRSF002356. Calreticulin. 1 hit.
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALR_BERST
AccessionPrimary (citable) accession number: Q9ZPP1
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families