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Q9STD3

- CALR_CHLRE

UniProt

Q9STD3 - CALR_CHLRE

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Protein

Calreticulin

Gene
N/A
Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101Carbohydrate By similarity
Binding sitei112 – 1121Carbohydrate By similarity
Binding sitei131 – 1311Carbohydrate By similarity
Binding sitei138 – 1381Carbohydrate By similarity
Binding sitei321 – 3211Carbohydrate By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. anthocyanin-containing compound metabolic process Source: EnsemblPlants/Gramene
  2. calcium ion homeostasis Source: EnsemblPlants/Gramene
  3. defense response signaling pathway, resistance gene-independent Source: EnsemblPlants/Gramene
  4. defense response to bacterium Source: EnsemblPlants/Gramene
  5. plant-type hypersensitive response Source: EnsemblPlants/Gramene
  6. protein folding Source: InterPro
  7. response to cadmium ion Source: EnsemblPlants/Gramene
  8. response to oxidative stress Source: EnsemblPlants/Gramene
  9. response to salt stress Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
Taxonomic identifieri3055 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas

Subcellular locationi

GO - Cellular componenti

  1. apoplast Source: EnsemblPlants/Gramene
  2. chloroplast Source: EnsemblPlants/Gramene
  3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  4. endoplasmic reticulum membrane Source: EnsemblPlants/Gramene
  5. mitochondrion Source: EnsemblPlants/Gramene
  6. plasmodesma Source: EnsemblPlants/Gramene
  7. vacuolar membrane Source: EnsemblPlants/Gramene
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818 Reviewed predictionAdd
BLAST
Chaini19 – 420402CalreticulinPRO_0000004189Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi106 ↔ 140 By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ9STD3.
ProMEXiQ9STD3.

Structurei

3D structure databases

ProteinModelPortaliQ9STD3.
SMRiQ9STD3. Positions 209-306.

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
Motifi417 – 4204Prevents secretion from ER Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi355 – 41460Asp/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.
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.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG305105.
KOiK08057.
OMAiRWVNSKH.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR001580. 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]
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. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9STD3-1 [UniParc]FASTAAdd to Basket

« Hide

MKWGVVAVLA TLVVAASAKD YFKETFDGSW ADRWTKSSWK VSDGSAGEFK    50
LTAGKWYGDA EADKGIQTGP DSKFFAISAP LATVFDNTGK DTVVQFSVKH 100
EQDLDCGGGY IKVVPATSEK QMGEFGGDTP YSIMFGPDIC GYSTRKVHVI 150
LTYKGKNYLI KKDIKAETDQ LTHVYTLVIK PDNTYQVLID LKEVASGSLY 200
EDWDMLPPKT IKDPKASKPE DWDEREEIAD PEDKKPEGWD DIPATIADKD 250
AKKPEDWDDE EDGTWEPPMI PNPEYKGEWK AKMIKNPAYK GIWVAPDIDN 300
PDYVHDDKLY NFKDLKFVGF ELWQVKSGSI FDNILVTDDL EAAKKFAEDT 350
WGKHKDEEKA MFDKVKKEED EKKAKDAPPP PVDAEAAEEE DDEYEDKEEP 400
SGMGSIKIPK EEEESGHDEL 420
Length:420
Mass (Da):47,328
Last modified:May 1, 2000 - v1
Checksum:iDD3BA3AFFBF61C9B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ000765 mRNA. Translation: CAB54526.1.
RefSeqiXP_001689661.1. XM_001689609.1.
UniGeneiCre.14231.

Genome annotation databases

GeneIDi5715514.
KEGGicre:CHLREDRAFT_78954.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ000765 mRNA. Translation: CAB54526.1 .
RefSeqi XP_001689661.1. XM_001689609.1.
UniGenei Cre.14231.

3D structure databases

ProteinModelPortali Q9STD3.
SMRi Q9STD3. Positions 209-306.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q9STD3.
ProMEXi Q9STD3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5715514.
KEGGi cre:CHLREDRAFT_78954.

Phylogenomic databases

eggNOGi NOG305105.
KOi K08057.
OMAi RWVNSKH.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR001580. 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 ]
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. 1 hit.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and characterization of a cDNA encoding Chlamydomonas reinhardtii calreticulin."
    Zuppini A., Kaydamov C.
    Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 137c / CC-125.

Entry informationi

Entry nameiCALR_CHLRE
AccessioniPrimary (citable) accession number: Q9STD3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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