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Protein

Calreticulin

Gene
N/A
Organism
Prunus armeniaca (Apricot) (Armeniaca vulgaris)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 sitei114CarbohydrateBy similarity1
Binding sitei116CarbohydrateBy similarity1
Binding sitei133CarbohydrateBy similarity1
Binding sitei140CarbohydrateBy similarity1
Binding sitei323CarbohydrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
OrganismiPrunus armeniaca (Apricot) (Armeniaca vulgaris)
Taxonomic identifieri36596 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000000419423 – 421CalreticulinAdd BLAST399

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi56N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi110 ↔ 142By similarity
Glycosylationi156N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9XF98.

Structurei

3D structure databases

ProteinModelPortaliQ9XF98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati196 – 2071-1Add BLAST12
Repeati215 – 2261-2Add BLAST12
Repeati232 – 2431-3Add BLAST12
Repeati250 – 2611-4Add BLAST12
Repeati265 – 2752-1Add BLAST11
Repeati279 – 2892-2Add BLAST11
Repeati293 – 3032-3Add BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni196 – 2614 X approximate repeatsAdd BLAST66
Regioni265 – 3033 X approximate repeatsAdd BLAST39

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi418 – 421Prevents secretion from ERPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi357 – 417Asp/Glu/Lys-richAdd BLAST61

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

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.

Q9XF98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFRVPNSSL LSLILLSLLA IASAKVFFEE RFEDGWDKRW VTSEWKKDEN
60 70 80 90 100
LAGEWNYTSG KWNGDPNDKG IQTSEDYRFY AISAEFPEFS NKDKTLVFQF
110 120 130 140 150
SVKHEQKLDC GGGYIKLLSG DVDQKKFGGD TPYSIMFGPD ICGYSTKKVH
160 170 180 190 200
AILNYNNTNN LIKKDVPCET DQLTHVYTFI IRPDATYSIL IDNLEKQTGS
210 220 230 240 250
LYSDWDLLPA KKIKDPEAKK PEDWEDQEYI PDPEDKKPEG YDDIPKEITD
260 270 280 290 300
PDAKKPEDWD DEEDGEWTAP TIPNPEYKGE WKPKKIKNPN FKGKWKAPLI
310 320 330 340 350
DNPEFKDDPE LYVYPNLKYV GIELWQVKSG TLFDNILITD EPEYAKQLAE
360 370 380 390 400
ETWGKQKDAE KAAFEELEKK LQEEESKEDP VDSDAEDDDN EAEDGEESDS
410 420
ESKPDSTEES AETEAEKHDE L
Length:421
Mass (Da):48,416
Last modified:November 1, 1999 - v1
Checksum:i4F5F94CBAA6C6690
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134733 mRNA. Translation: AAD32207.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF134733 mRNA. Translation: AAD32207.1.

3D structure databases

ProteinModelPortaliQ9XF98.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ9XF98.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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 nameiCALR_PRUAR
AccessioniPrimary (citable) accession number: Q9XF98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: October 5, 2016
This is version 89 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

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.