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O04151

- CALR1_ARATH

UniProt

O04151 - CALR1_ARATH

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Protein

Calreticulin-1

Gene

CRT1

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. calcium ion homeostasis Source: TAIR
  2. protein folding Source: InterPro
  3. response to cadmium ion Source: TAIR
  4. response to oxidative stress Source: TAIR
  5. response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_108190. ATF6-alpha activates chaperone genes.
REACT_190967. Calnexin/calreticulin cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin-1
Gene namesi
Name:CRT1
Ordered Locus Names:At1g56340
ORF Names:F13N6.20, F14G9.5
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G56340.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. apoplast Source: TAIR
  2. chloroplast Source: TAIR
  3. endoplasmic reticulum Source: TAIR
  4. mitochondrion Source: TAIR
  5. plasmodesma Source: TAIR
  6. vacuolar membrane 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 – 425403Calreticulin-1PRO_0000004184Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi108 ↔ 140By similarity
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Modified residuei381 – 3811Phosphoserine2 Publications
Modified residuei397 – 3971PhosphoserineBy similarity
Glycosylationi399 – 3991N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO04151.
PRIDEiO04151.

2D gel databases

SWISS-2DPAGEO04151.

Expressioni

Gene expression databases

ExpressionAtlasiO04151. baseline and differential.
GenevestigatoriO04151.

Interactioni

Protein-protein interaction databases

BioGridi27312. 4 interactions.
STRINGi3702.AT1G56340.1-P.

Structurei

3D structure databases

ProteinModelPortaliO04151.
SMRiO04151. Positions 24-369.
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
Motifi422 – 4254Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi355 – 41965Asp/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.
InParanoidiO04151.
KOiK08057.
OMAiPEDWEDE.
PhylomeDBiO04151.

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.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: O04151-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAKLNPKFIS LILFALVVIV SAEVIFEEKF EDGWEKRWVK SDWKKDDNTA
60 70 80 90 100
GEWKHTAGNW SGDANDKGIQ TSEDYRFYAI SAEFPEFSNK DKTLVFQFSV
110 120 130 140 150
KHEQKLDCGG GYMKLLSDDV DQTKFGGDTP YSIMFGPDIC GYSTKKVHAI
160 170 180 190 200
LTYNGTNHLI KKEVPCETDQ LTHVYTFVLR PDATYSILID NVEKQTGSLY
210 220 230 240 250
SDWDLLPAKK IKDPSAKKPE DWDDKEYIPD PEDTKPAGYD DIPKEIPDTD
260 270 280 290 300
AKKPEDWDDE EDGEWTAPTI PNPEYNGEWK PKKIKNPAYK GKWKAPMIDN
310 320 330 340 350
PEFKDDPELY VFPKLKYVGV ELWQVKSGSL FDNVLVSDDP EYAKKLAEET
360 370 380 390 400
WGKHKDAEKA AFDEAEKKRE EEESKDAPAE SDAEEEAEDD DNEGDDSDNE
410 420
SKSEETKEAE ETKEAEETDA AHDEL
Length:425
Mass (Da):48,527
Last modified:July 1, 1997 - v1
Checksum:iBCEC08E2F342642E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiC96605.
RefSeqiNP_176030.1. NM_104513.4. [O04151-1]
UniGeneiAt.10808.

Genome annotation databases

EnsemblPlantsiAT1G56340.1; AT1G56340.1; AT1G56340. [O04151-1]
GeneIDi842087.
KEGGiath:AT1G56340.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi C96605.
RefSeqi NP_176030.1. NM_104513.4. [O04151-1 ]
UniGenei At.10808.

3D structure databases

ProteinModelPortali O04151.
SMRi O04151. Positions 24-369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 27312. 4 interactions.
STRINGi 3702.AT1G56340.1-P.

2D gel databases

SWISS-2DPAGE O04151.

Proteomic databases

PaxDbi O04151.
PRIDEi O04151.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G56340.1 ; AT1G56340.1 ; AT1G56340 . [O04151-1 ]
GeneIDi 842087.
KEGGi ath:AT1G56340.

Organism-specific databases

TAIRi AT1G56340.

Phylogenomic databases

eggNOGi NOG305105.
HOGENOMi HOG000192435.
InParanoidi O04151.
KOi K08057.
OMAi PEDWEDE.
PhylomeDBi O04151.

Enzyme and pathway databases

Reactomei REACT_108190. ATF6-alpha activates chaperone genes.
REACT_190967. Calnexin/calreticulin cycle.

Gene expression databases

ExpressionAtlasi O04151. baseline and differential.
Genevestigatori O04151.

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. "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.
    , 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.
    , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCALR1_ARATH
AccessioniPrimary (citable) accession number: O04151
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: July 1, 1997
Last modified: November 26, 2014
This is version 137 of the entry and version 1 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