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O04151 (CALR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calreticulin-1
Gene names
Name:CRT1
Ordered Locus Names:At1g56340
ORF Names:F13N6.20, F14G9.5
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: O04151-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 425403Calreticulin-1
PRO_0000004184

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
Motif422 – 4254Prevents secretion from ER Potential
Compositional bias355 – 41965Asp/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

Modified residue3811Phosphoserine Ref.5 Ref.6
Modified residue3971Phosphoserine Ref.6
Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation1541N-linked (GlcNAc...) Potential
Glycosylation3991N-linked (GlcNAc...) Potential
Disulfide bond108 ↔ 140 By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: BCEC08E2F342642E

FASTA42548,527
        10         20         30         40         50         60 
MAKLNPKFIS LILFALVVIV SAEVIFEEKF EDGWEKRWVK SDWKKDDNTA GEWKHTAGNW 

        70         80         90        100        110        120 
SGDANDKGIQ TSEDYRFYAI SAEFPEFSNK DKTLVFQFSV KHEQKLDCGG GYMKLLSDDV 

       130        140        150        160        170        180 
DQTKFGGDTP YSIMFGPDIC GYSTKKVHAI LTYNGTNHLI KKEVPCETDQ LTHVYTFVLR 

       190        200        210        220        230        240 
PDATYSILID NVEKQTGSLY SDWDLLPAKK IKDPSAKKPE DWDDKEYIPD PEDTKPAGYD 

       250        260        270        280        290        300 
DIPKEIPDTD AKKPEDWDDE EDGEWTAPTI PNPEYNGEWK PKKIKNPAYK GKWKAPMIDN 

       310        320        330        340        350        360 
PEFKDDPELY VFPKLKYVGV ELWQVKSGSL FDNVLVSDDP EYAKKLAEET WGKHKDAEKA 

       370        380        390        400        410        420 
AFDEAEKKRE EEESKDAPAE SDAEEEAEDD DNEGDDSDNE SKSEETKEAE ETKEAEETDA 


AHDEL

« Hide

References

« Hide 'large scale' references
[1]"Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana."
Nelson D.E., Glaunsinger B., Bohnert H.J.
Plant Physiol. 114:29-37(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, MASS SPECTROMETRY.
Strain: cv. Columbia.
[6]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381 AND SER-397, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U66343 mRNA. Translation: AAC49695.1.
AC058785 Genomic DNA. Translation: AAG51504.1.
AC069159 Genomic DNA. Translation: AAG50908.1.
CP002684 Genomic DNA. Translation: AEE33379.1.
AY062628 mRNA. Translation: AAL32706.1.
BT008511 mRNA. Translation: AAP37870.1.
IPIIPI00529815.
PIRC96605.
RefSeqNP_176030.1. NM_104513.4.
UniGeneAt.10808.

3D structure databases

ProteinModelPortalO04151.
SMRO04151. Positions 24-369.
ModBaseSearch...

Protein-protein interaction databases

STRING3702.AT1G56340.1-P.

2D gel databases

SWISS-2DPAGEO04151.

Proteomic databases

PaxDbO04151.
PRIDEO04151.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G56340.1; AT1G56340.1; AT1G56340.
GeneID842087.
KEGGath:AT1G56340.

Organism-specific databases

TAIRAt1g56340.

Phylogenomic databases

eggNOGNOG305105.
HOGENOMHOG000192435.
InParanoidO04151.
KOK08057.
OMAEWEAPTI.
PhylomeDBO04151.
ProtClustDBCLSN2682885.

Gene expression databases

ArrayExpressO04151.
GenevestigatorO04151.
GermOnlineAT1G56340. Arabidopsis thaliana.

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.
SUPFAMSSF63887. Calret_calnex_P. 1 hit.
SSF49899. ConA_like_lec_gl. 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 nameCALR1_ARATH
AccessionPrimary (citable) accession number: O04151
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 1, 1997
Last modified: May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents