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Q38858

- CALR2_ARATH

UniProt

Q38858 - CALR2_ARATH

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Protein

Calreticulin-2

Gene

CRT2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei112 – 1121CarbohydrateBy similarity
Binding sitei114 – 1141CarbohydrateBy similarity
Binding sitei131 – 1311CarbohydrateBy similarity
Binding sitei138 – 1381CarbohydrateBy similarity
Binding sitei321 – 3211CarbohydrateBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. carbohydrate binding Source: UniProtKB-KW

GO - Biological processi

  1. protein folding Source: InterPro
  2. response to oxidative stress Source: TAIR
  3. response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin-2
Gene namesi
Name:CRT2
Synonyms:CRTL
Ordered Locus Names:At1g09210
ORF Names:T12M4.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G09210.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. endoplasmic reticulum Source: TAIR
  3. mitochondrion Source: TAIR
  4. vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 424402Calreticulin-2PRO_0000004185Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi108 ↔ 140By similarity
Modified residuei381 – 3811PhosphoserineBy similarity
Modified residuei396 – 3961PhosphoserineBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ38858.
PRIDEiQ38858.

2D gel databases

SWISS-2DPAGEQ38858.

Expressioni

Gene expression databases

ExpressionAtlasiQ38858. baseline and differential.
GenevestigatoriQ38858.

Interactioni

Protein-protein interaction databases

BioGridi22682. 4 interactions.
STRINGi3702.AT1G09210.1-P.

Structurei

3D structure databases

ProteinModelPortaliQ38858.
SMRiQ38858. Positions 23-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati194 – 205121-1Add
BLAST
Repeati213 – 224121-2Add
BLAST
Repeati230 – 241121-3Add
BLAST
Repeati248 – 259121-4Add
BLAST
Repeati263 – 273112-1Add
BLAST
Repeati277 – 287112-2Add
BLAST
Repeati291 – 301112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 259664 X approximate repeatsAdd
BLAST
Regioni263 – 301393 X approximate repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi421 – 4244Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi355 – 41763Asp/Glu/Lys-richAdd
BLAST

Domaini

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).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 similaritiesi

Belongs to the calreticulin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG305105.
HOGENOMiHOG000192435.
InParanoidiQ38858.
KOiK08057.
OMAiRWVNSKH.
PhylomeDBiQ38858.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProiIPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view]
PANTHERiPTHR11073. PTHR11073. 1 hit.
PfamiPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFiPIRSF002356. Calreticulin. 1 hit.
PRINTSiPR00626. CALRETICULIN.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEiPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q38858 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKMIPSLVS LILIGLVAIA SAAVIFEERF DDGWENRWVK SEWKKDDNTA
60 70 80 90 100
GEWKHTAGNW SGDANDKGIQ TSEDYRFYAI SAEFPEFSNK DKTLVFQFSV
110 120 130 140 150
KHEQKLDCGG GYMKLLSGDV DQKKFGGDTP YSIMFGPDIC GYSTKKVHAI
160 170 180 190 200
LTYNEANHLI KKDVPCETDQ LTHVYTFILR PDATYSILID NVEKQTGSLY
210 220 230 240 250
SDWDLLPPKK IKDPSAKKPE DWDEQEYISD PEDKKPDGYD DIPKEIPDTD
260 270 280 290 300
SKKPEDWDDE EDGEWTAPTI PNPEYMGEWK PKQIKNPNYK GKWEAPLIDN
310 320 330 340 350
PDFKDDPELY VFPKLKYVGL ELWQVKSGSL FDNVLICDDP DYAKKLADET
360 370 380 390 400
WGKLKDAEKA AFDEAEKKNE EEESKDAPAE SDAEDEPEDD EGGDDSDSES
410 420
KAEETKSVDS EETSEKDATA HDEL
Length:424
Mass (Da):48,157
Last modified:May 29, 2007 - v3
Checksum:i51421329AE81A7F5
GO

Sequence cautioni

The sequence AAC49696.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAC24083.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 194LVAI → NSAR in AAA80652. 1 PublicationCurated
Sequence conflicti155 – 1551E → G in AAC49696. (PubMed:9159940)Curated
Sequence conflicti155 – 1551E → G in AAA80652. 1 PublicationCurated
Sequence conflicti236 – 2361P → T in AAA80652. 1 PublicationCurated
Sequence conflicti408 – 4081V → E in AAA80652. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiH86224.
RefSeqiNP_172392.1. NM_100791.3.
UniGeneiAt.1529.

Genome annotation databases

EnsemblPlantsiAT1G09210.1; AT1G09210.1; AT1G09210.
GeneIDi837441.
KEGGiath:AT1G09210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi H86224.
RefSeqi NP_172392.1. NM_100791.3.
UniGenei At.1529.

3D structure databases

ProteinModelPortali Q38858.
SMRi Q38858. Positions 23-372.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 22682. 4 interactions.
STRINGi 3702.AT1G09210.1-P.

2D gel databases

SWISS-2DPAGE Q38858.

Proteomic databases

PaxDbi Q38858.
PRIDEi Q38858.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G09210.1 ; AT1G09210.1 ; AT1G09210 .
GeneIDi 837441.
KEGGi ath:AT1G09210.

Organism-specific databases

TAIRi AT1G09210.

Phylogenomic databases

eggNOGi NOG305105.
HOGENOMi HOG000192435.
InParanoidi Q38858.
KOi K08057.
OMAi RWVNSKH.
PhylomeDBi Q38858.

Gene expression databases

ExpressionAtlasi Q38858. baseline and differential.
Genevestigatori Q38858.

Family and domain databases

Gene3Di 2.10.250.10. 1 hit.
2.60.120.200. 1 hit.
InterProi IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002356. Calreticulin. 1 hit.
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 2 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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].

Entry informationi

Entry nameiCALR2_ARATH
AccessioniPrimary (citable) accession number: Q38858
Secondary accession number(s): O04152, O80486, Q94AW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 29, 2007
Last modified: October 29, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3