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Protein

Calreticulin

Gene

crt-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Protein inferred from homologyi

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 sitei105CarbohydrateBy similarity1
Binding sitei107CarbohydrateBy similarity1
Binding sitei124CarbohydrateBy similarity1
Binding sitei131CarbohydrateBy similarity1
Binding sitei312CarbohydrateBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: WormBase
  • carbohydrate binding Source: UniProtKB-KW

GO - Biological processi

  • defecation Source: WormBase
  • endoplasmic reticulum unfolded protein response Source: WormBase
  • hemidesmosome assembly Source: WormBase
  • multicellular organismal reproductive process Source: WormBase
  • programmed cell death Source: WormBase
  • protein folding Source: InterPro
  • regulation of gene expression Source: WormBase
  • response to ethanol Source: WormBase
  • response to heat Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-CEL-901042. Calnexin/calreticulin cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
Gene namesi
Name:crt-1
ORF Names:Y38A10A.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiY38A10A.5; CE21562; WBGene00000802; crt-1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: WormBase
  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 15Sequence analysisAdd BLAST15
ChainiPRO_000000418016 – 395CalreticulinAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi101 ↔ 133By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP27798.
PaxDbiP27798.
PeptideAtlasiP27798.
PRIDEiP27798.

2D gel databases

World-2DPAGE0020:P27798.

Expressioni

Gene expression databases

BgeeiWBGene00000802.

Interactioni

Protein-protein interaction databases

BioGridi44045. 7 interactors.
DIPiDIP-25701N.
IntActiP27798. 4 interactors.
MINTiMINT-226928.
STRINGi6239.Y38A10A.5.1.

Structurei

3D structure databases

ProteinModelPortaliP27798.
SMRiP27798.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati186 – 1971-1Add BLAST12
Repeati205 – 2161-2Add BLAST12
Repeati222 – 2331-3Add BLAST12
Repeati239 – 2501-4Add BLAST12
Repeati254 – 2642-1Add BLAST11
Repeati268 – 2782-2Add BLAST11
Repeati282 – 2922-3Add BLAST11

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni? – 192N-domain
Regioni186 – 2504 X approximate repeatsAdd BLAST65
Regioni193 – 301P-domainAdd BLAST109
Regioni254 – 2923 X approximate repeatsAdd BLAST39
Regioni302 – 395C-domainAdd BLAST94

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi392 – 395Prevents secretion from ERPROSITE-ProRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi332 – 390Asp/Glu/Lys-richAdd BLAST59

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.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
InParanoidiP27798.
KOiK08057.
OMAiRWVNSKH.
OrthoDBiEOG091G0AP1.
PhylomeDBiP27798.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 2 hits.
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. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P27798-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLCLLAIV AVVSAEVYFK EEFNDASWEK RWVQSKHKDD FGAFKLSAGK
60 70 80 90 100
FFDVESRDQG IQTSQDAKFY SRAAKFDKDF SNKGKTLVIQ YTVKHEQGID
110 120 130 140 150
CGGGYVKVMR ADADLGDFHG ETPYNVMFGP DICGPTRRVH VILNYKGENK
160 170 180 190 200
LIKKEITCKS DELTHLYTLI LNSDNTYEVK IDGESAQTGS LEEDWDLLPA
210 220 230 240 250
KKIKDPDAKK PEDWDEREYI DDAEDAKPED WEKPEHIPDP DAKKPEDWDD
260 270 280 290 300
EMDGEWEPPM IDNPEYKGEW KPKQIKNPAY KGKWIHPEIE NPEYTPDDEL
310 320 330 340 350
YSYESWGAIG FDLWQVKSGT IFDNIIITDS VEEAEAHAAE TFDKLKTVEK
360 370 380 390
EKKEKADEET RKAEEEARKK AEEEKEAKKD DDEEEKEEEE GHDEL
Length:395
Mass (Da):45,616
Last modified:August 1, 1992 - v1
Checksum:i35CA7D2EC1D56B03
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59589 Genomic DNA. Translation: CAA42159.1.
FO081168 Genomic DNA. Translation: CCD69629.1.
PIRiS25851.
RefSeqiNP_504575.1. NM_072174.3.
UniGeneiCel.4918.

Genome annotation databases

EnsemblMetazoaiY38A10A.5.1; Y38A10A.5.1; WBGene00000802.
Y38A10A.5.2; Y38A10A.5.2; WBGene00000802.
GeneIDi178997.
KEGGicel:CELE_Y38A10A.5.
UCSCiY38A10A.5.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59589 Genomic DNA. Translation: CAA42159.1.
FO081168 Genomic DNA. Translation: CCD69629.1.
PIRiS25851.
RefSeqiNP_504575.1. NM_072174.3.
UniGeneiCel.4918.

3D structure databases

ProteinModelPortaliP27798.
SMRiP27798.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44045. 7 interactors.
DIPiDIP-25701N.
IntActiP27798. 4 interactors.
MINTiMINT-226928.
STRINGi6239.Y38A10A.5.1.

2D gel databases

World-2DPAGE0020:P27798.

Proteomic databases

EPDiP27798.
PaxDbiP27798.
PeptideAtlasiP27798.
PRIDEiP27798.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiY38A10A.5.1; Y38A10A.5.1; WBGene00000802.
Y38A10A.5.2; Y38A10A.5.2; WBGene00000802.
GeneIDi178997.
KEGGicel:CELE_Y38A10A.5.
UCSCiY38A10A.5.1. c. elegans.

Organism-specific databases

CTDi178997.
WormBaseiY38A10A.5; CE21562; WBGene00000802; crt-1.

Phylogenomic databases

eggNOGiKOG0674. Eukaryota.
ENOG410XRR7. LUCA.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
InParanoidiP27798.
KOiK08057.
OMAiRWVNSKH.
OrthoDBiEOG091G0AP1.
PhylomeDBiP27798.

Enzyme and pathway databases

ReactomeiR-CEL-901042. Calnexin/calreticulin cycle.

Miscellaneous databases

PROiP27798.

Gene expression databases

BgeeiWBGene00000802.

Family and domain databases

Gene3Di2.10.250.10. 1 hit.
2.60.120.200. 2 hits.
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. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCALR_CAEEL
AccessioniPrimary (citable) accession number: P27798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: November 30, 2016
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  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.