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O04153 (CALR3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 125. 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

Names and origin

Protein namesRecommended name:
Calreticulin-3
Alternative name(s):
Protein PRIORITY IN SWEET LIFE 1
Gene names
Name:CRT3
Ordered Locus Names:At1g08450
ORF Names:T27G7.13
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length424 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. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. Ref.5 Ref.6

Subcellular location

Endoplasmic reticulum lumen Ref.6.

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.

Disruption phenotype

Loss of seedling growth inhibition in response to the pathogen-associated molecular pattern (PAMP) elf18 and increased susceptibility to phytopathogenic bacteria. Ref.6

Sequence similarities

Belongs to the calreticulin family.

Sequence caution

The sequence AAF22902.1 differs from that shown. Reason: Erroneous gene model prediction.

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: O04153-1)

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 – 2828 Potential
Chain29 – 424396Calreticulin-3
PRO_0000004186

Regions

Repeat200 – 211121-1
Repeat219 – 230121-2
Repeat236 – 247121-3
Repeat254 – 265121-4
Repeat269 – 279112-1
Repeat283 – 293112-2
Repeat297 – 307112-3
Region200 – 265664 X approximate repeats
Region269 – 307393 X approximate repeats
Motif421 – 4244Prevents secretion from ER Potential
Compositional bias361 – 41454Arg/Glu/Lys-rich

Sites

Binding site1181Carbohydrate By similarity
Binding site1201Carbohydrate By similarity
Binding site1371Carbohydrate By similarity
Binding site1441Carbohydrate By similarity
Binding site3271Carbohydrate By similarity

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Potential
Disulfide bond114 ↔ 146 By similarity

Experimental info

Mutagenesis671P → L in psl1-1; no effect on EFR accumulation, but decreased response to the PAMP elf18. Ref.5
Mutagenesis1151G → D in crt3-3; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. Ref.6
Mutagenesis1421G → E in crt3-4; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. Ref.6
Mutagenesis1471G → E in crt3-5; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. Ref.6
Mutagenesis1791H → Y in crt3-6; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. Ref.6
Mutagenesis2031G → D in crt3-7; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. Ref.6
Mutagenesis2441G → S in psl1-3; no effect on EFR accumulation, but decreased response to the PAMP elf18. Ref.5
Mutagenesis2931P → S in crt3-10; loss of response to the PAMP elf18, but no effect on the response to PAMP flg22. Ref.6
Mutagenesis3351S → L in psl1-4; loss of EFR accumulation and loss of response to the PAMP elf18. Ref.5
Sequence conflict2791S → F in AAC49697. Ref.1

Sequences

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

Last modified February 5, 2008. Version 2.
Checksum: 64445A06359F0B8C

FASTA42449,844
        10         20         30         40         50         60 
MGLPQNKLSF FCFFFLVSVL TLAPLAFSEI FLEEHFEGGW KSRWVLSDWK RNEGKAGTFK 

        70         80         90        100        110        120 
HTAGKWPGDP DNKGIQTYND AKHYAISAKI PEFSNKNRTL VVQYSVKIEQ DIECGGAYIK 

       130        140        150        160        170        180 
LLSGYVNQKQ FGGDTPYSLM FGPDICGTQT KKLHVIVSYQ GQNYPIKKDL QCETDKLNHF 

       190        200        210        220        230        240 
YTFILRPDAS YSVLVDNKER EFGSMYTDWD ILPPRKIKVK NAKKPEDWDD REYIDDPNDV 

       250        260        270        280        290        300 
KPEGFDSIPR EIPDRKAKEP EDWDEEENGL WEPPKIPNSA YKGPWKAKRI KNPNYKGKWK 

       310        320        330        340        350        360 
NPWIDNPEFE DDPDLYVLKS IKYAGIEVWQ VKAGSIFDNI LICDDPAYAR SIVDDYFAQH 

       370        380        390        400        410        420 
RESEKELFAE AEKERKARED EEARIAREEG ERRRKERDHR YGDRRRRYKR PNPRDYMDDY 


HDEL 

« 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]"Receptor quality control in the endoplasmic reticulum for plant innate immunity."
Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H., Dong X., Robatzek S., Schulze-Lefert P.
EMBO J. 28:3439-3449(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF PRO-67; GLY-244 AND SER-335.
[6]"Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR."
Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D., Zipfel C., Jones J.D.
Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLY-115; GLY-142; GLY-147; HIS-179; GLY-203 AND PRO-293, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U66345 mRNA. Translation: AAC49697.1.
AC006932 Genomic DNA. Translation: AAF22902.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28291.1.
AY056320 mRNA. Translation: AAL07169.1.
RefSeqNP_563816.1. NM_100718.4. [O04153-1]
UniGeneAt.24804.

3D structure databases

ProteinModelPortalO04153.
SMRO04153. Positions 30-385.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48930N.

Proteomic databases

PaxDbO04153.
PRIDEO04153.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G08450.1; AT1G08450.1; AT1G08450. [O04153-1]
GeneID837365.
KEGGath:AT1G08450.

Organism-specific databases

TAIRAT1G08450.

Phylogenomic databases

eggNOGNOG295283.
HOGENOMHOG000192435.
InParanoidO04153.
KOK08057.
OMAFGSMYTD.
PhylomeDBO04153.

Gene expression databases

ArrayExpressO04153.
GenevestigatorO04153.

Family and domain databases

Gene3D2.60.120.200. 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. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCALR3_ARATH
AccessionPrimary (citable) accession number: O04153
Secondary accession number(s): Q93ZR4, Q9SJE7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 5, 2008
Last modified: June 11, 2014
This is version 125 of the entry and version 2 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names