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Protein

Calreticulin-2

Gene

CRT2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei112CarbohydrateBy similarity1
Binding sitei114CarbohydrateBy similarity1
Binding sitei131CarbohydrateBy similarity1
Binding sitei138CarbohydrateBy similarity1
Binding sitei321CarbohydrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • protein folding Source: InterPro
  • response to oxidative stress Source: TAIR
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-ATH-901042. Calnexin/calreticulin cycle.

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
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G09210.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  • apoplast Source: TAIR
  • endoplasmic reticulum Source: TAIR
  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
  • mitochondrion Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000000418523 – 424Calreticulin-2Add BLAST402

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi59N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi108 ↔ 140By similarity
Modified residuei381PhosphoserineBy similarity1
Modified residuei396PhosphoserineBy similarity1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ38858.
PRIDEiQ38858.

2D gel databases

SWISS-2DPAGEQ38858.

PTM databases

iPTMnetiQ38858.

Expressioni

Gene expression databases

GenevisibleiQ38858. AT.

Interactioni

Protein-protein interaction databases

BioGridi22682. 4 interactors.
STRINGi3702.AT1G09210.1.

Structurei

3D structure databases

ProteinModelPortaliQ38858.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati194 – 2051-1Add BLAST12
Repeati213 – 2241-2Add BLAST12
Repeati230 – 2411-3Add BLAST12
Repeati248 – 2591-4Add BLAST12
Repeati263 – 2732-1Add BLAST11
Repeati277 – 2872-2Add BLAST11
Repeati291 – 3012-3Add BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni194 – 2594 X approximate repeatsAdd BLAST66
Regioni263 – 3013 X approximate repeatsAdd BLAST39

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi421 – 424Prevents secretion from ERPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi355 – 417Asp/Glu/Lys-richAdd BLAST63

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

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
HOGENOMiHOG000192435.
InParanoidiQ38858.
KOiK08057.
OMAiIPNPEYM.
OrthoDBiEOG09360F0J.
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. 2 hits.
[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.

Q38858-1 [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 AAC24083 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence AAC49696 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti16 – 19LVAI → NSAR in AAA80652 (Ref. 5) Curated4
Sequence conflicti155E → G in AAC49696 (PubMed:9159940).Curated1
Sequence conflicti155E → G in AAA80652 (Ref. 5) Curated1
Sequence conflicti236P → T in AAA80652 (Ref. 5) Curated1
Sequence conflicti408V → E in AAA80652 (Ref. 5) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_100791.4.
UniGeneiAt.1529.

Genome annotation databases

EnsemblPlantsiAT1G09210.1; AT1G09210.1; AT1G09210.
GeneIDi837441.
GrameneiAT1G09210.1; AT1G09210.1; AT1G09210.
KEGGiath:AT1G09210.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_100791.4.
UniGeneiAt.1529.

3D structure databases

ProteinModelPortaliQ38858.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22682. 4 interactors.
STRINGi3702.AT1G09210.1.

PTM databases

iPTMnetiQ38858.

2D gel databases

SWISS-2DPAGEQ38858.

Proteomic databases

PaxDbiQ38858.
PRIDEiQ38858.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G09210.1; AT1G09210.1; AT1G09210.
GeneIDi837441.
GrameneiAT1G09210.1; AT1G09210.1; AT1G09210.
KEGGiath:AT1G09210.

Organism-specific databases

TAIRiAT1G09210.

Phylogenomic databases

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
HOGENOMiHOG000192435.
InParanoidiQ38858.
KOiK08057.
OMAiIPNPEYM.
OrthoDBiEOG09360F0J.
PhylomeDBiQ38858.

Enzyme and pathway databases

ReactomeiR-ATH-901042. Calnexin/calreticulin cycle.

Miscellaneous databases

PROiQ38858.

Gene expression databases

GenevisibleiQ38858. AT.

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. 2 hits.
[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]
ProtoNetiSearch...

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: November 30, 2016
This is version 147 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.