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Q38858 (CALR2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calreticulin-2
Gene names
Name:CRT2
Synonyms:CRTL
Ordered Locus Names:At1g09210
ORF Names:T12M4.8
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 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.

Sequence caution

The sequence AAC24083.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC49696.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 424402Calreticulin-2
PRO_0000004185

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
Motif421 – 4244Prevents secretion from ER Potential
Compositional bias355 – 41763Asp/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 By similarity
Modified residue3961Phosphoserine By similarity
Glycosylation591N-linked (GlcNAc...) Potential
Disulfide bond108 ↔ 140 By similarity

Experimental info

Sequence conflict16 – 194LVAI → NSAR in AAA80652. Ref.5
Sequence conflict1551E → G in AAC49696. Ref.4
Sequence conflict1551E → G in AAA80652. Ref.5
Sequence conflict2361P → T in AAA80652. Ref.5
Sequence conflict4081V → E in AAA80652. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q38858 [UniParc].

Last modified May 29, 2007. Version 3.
Checksum: 51421329AE81A7F5

FASTA42448,157
        10         20         30         40         50         60 
MAKMIPSLVS LILIGLVAIA SAAVIFEERF DDGWENRWVK SEWKKDDNTA GEWKHTAGNW 

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

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

       190        200        210        220        230        240 
PDATYSILID NVEKQTGSLY SDWDLLPPKK IKDPSAKKPE DWDEQEYISD PEDKKPDGYD 

       250        260        270        280        290        300 
DIPKEIPDTD SKKPEDWDDE EDGEWTAPTI PNPEYMGEWK PKQIKNPNYK GKWEAPLIDN 

       310        320        330        340        350        360 
PDFKDDPELY VFPKLKYVGL ELWQVKSGSL FDNVLICDDP DYAKKLADET WGKLKDAEKA 

       370        380        390        400        410        420 
AFDEAEKKNE EEESKDAPAE SDAEDEPEDD EGGDDSDSES KAEETKSVDS EETSEKDATA 


HDEL 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"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.
[4]"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 [GENOMIC DNA] OF 1-174.
[5]"Nucleotide sequence of an Arabidopsis thaliana cDNA encoding a protein homologous to plant and animal calreticulins."
Benedetti C.E., Turner J.G.
Plant Gene Register PGR95-047
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-424.
Strain: cv. Landsberg erecta.
Tissue: Flower.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC003114 Genomic DNA. Translation: AAC24083.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE28414.1.
AY045656 mRNA. Translation: AAK74014.1.
AY059662 mRNA. Translation: AAL31155.1.
U66344 Genomic DNA. Translation: AAC49696.1. Different initiation.
U27698 mRNA. Translation: AAA80652.1.
PIRH86224.
RefSeqNP_172392.1. NM_100791.3.
UniGeneAt.1529.

3D structure databases

ProteinModelPortalQ38858.
SMRQ38858. Positions 23-372.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid22682. 4 interactions.
STRING3702.AT1G09210.1-P.

2D gel databases

SWISS-2DPAGEQ38858.

Proteomic databases

PaxDbQ38858.
PRIDEQ38858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G09210.1; AT1G09210.1; AT1G09210.
GeneID837441.
KEGGath:AT1G09210.

Organism-specific databases

TAIRAT1G09210.

Phylogenomic databases

eggNOGNOG305105.
HOGENOMHOG000192435.
InParanoidQ38858.
KOK08057.
OMARWVNSKH.
PhylomeDBQ38858.

Gene expression databases

ArrayExpressQ38858.
GenevestigatorQ38858.

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 nameCALR2_ARATH
AccessionPrimary (citable) accession number: Q38858
Secondary accession number(s): O04152, O80486, Q94AW7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 29, 2007
Last modified: July 9, 2014
This is version 129 of the entry and version 3 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