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Q9SP22 (CALR_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 83. 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 namesRecommended name:
Calreticulin
Gene names
Name:CRT
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length420 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
   PTMGlycoprotein
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 – 2525 Potential
Chain26 – 420395Calreticulin
PRO_0000004191

Regions

Repeat197 – 208121-1
Repeat216 – 227121-2
Repeat233 – 244121-3
Repeat251 – 262121-4
Repeat266 – 276112-1
Repeat280 – 290112-2
Repeat294 – 304112-3
Region197 – 262664 X approximate repeats
Region266 – 304393 X approximate repeats
Motif417 – 4204Prevents secretion from ER Potential
Compositional bias358 – 41659Asp/Glu/Lys-rich

Sites

Binding site1151Carbohydrate By similarity
Binding site1171Carbohydrate By similarity
Binding site1341Carbohydrate By similarity
Binding site1411Carbohydrate By similarity
Binding site3241Carbohydrate By similarity

Amino acid modifications

Glycosylation571N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9SP22 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: E73B7F43E7494735

FASTA42047,940
        10         20         30         40         50         60 
MAIRKGSSYA VAALLALASV AAVAGEVFFQ EKFEDGWESR WVKSEWKKDE NMAGEWNHTS 

        70         80         90        100        110        120 
GKWNGDAEDK GIQTSEDYRF YAISAEYPEF SNKDKTLVLQ FSVKHEQKLD CGGGYVKLLG 

       130        140        150        160        170        180 
GDVDQKTLGG DTSYSIISRP DISRYSTKKV HTILTKDGKN HLIKKDVPCQ TDQLTHVYTF 

       190        200        210        220        230        240 
IIRPDATYSI LIDNEEKHTG SIYEHWDILP PKKIKDPEAK KPEDWDDKEY IPDPEDKKPE 

       250        260        270        280        290        300 
GYDDIPKEIP DPDAKKPEDW DDEEDGEWTA PTIPNPEYKG PWKQKKIKNP NYQGKWKAPM 

       310        320        330        340        350        360 
IDNPDFKDDP YIYAFDSLKY IGIELWQVKS GTLFDNIIIT DDPALAKTFA EETWGKHKEA 

       370        380        390        400        410        420 
EKAAFDEAEK KKEEEDAAKG GDDEDDDLED EEDDEKADED KADSDAEDGK DSDDEKHDEL 

« Hide

References

[1]"Expression of the high capacity calcium-binding domain of calreticulin increases bioavailable calcium stores in plants."
Wyatt S.E., Tsou P.-L., Robertson D.
Transgenic Res. 11:1-10(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF190454 mRNA. Translation: AAF01470.1.

3D structure databases

ProteinModelPortalQ9SP22.
SMRQ9SP22. Positions 212-312.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ9SP22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ9SP22.

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.
PS00805. CALRETICULIN_REPEAT. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALR_MAIZE
AccessionPrimary (citable) accession number: Q9SP22
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 83 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