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Protein

Calreticulin

Gene

crt-1

Organism
Caenorhabditis elegans
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei105 – 1051CarbohydrateBy similarity
Binding sitei107 – 1071CarbohydrateBy similarity
Binding sitei124 – 1241CarbohydrateBy similarity
Binding sitei131 – 1311CarbohydrateBy similarity
Binding sitei312 – 3121CarbohydrateBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: WormBase
  2. carbohydrate binding Source: UniProtKB-KW

GO - Biological processi

  1. defecation Source: WormBase
  2. endoplasmic reticulum unfolded protein response Source: WormBase
  3. hemidesmosome assembly Source: WormBase
  4. multicellular organismal reproductive process Source: WormBase
  5. programmed cell death Source: WormBase
  6. protein folding Source: InterPro
  7. response to ethanol Source: WormBase
  8. response to heat Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_315447. 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
ProteomesiUP000001940 Componenti: Chromosome V

Organism-specific databases

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

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 395380CalreticulinPRO_0000004180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi101 ↔ 133By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP27798.

2D gel databases

World-2DPAGE0020:P27798.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliP27798.
SMRiP27798. Positions 17-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati186 – 197121-1Add
BLAST
Repeati205 – 216121-2Add
BLAST
Repeati222 – 233121-3Add
BLAST
Repeati239 – 250121-4Add
BLAST
Repeati254 – 264112-1Add
BLAST
Repeati268 – 278112-2Add
BLAST
Repeati282 – 292112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni? – 192N-domain
Regioni186 – 250654 X approximate repeatsAdd
BLAST
Regioni193 – 301109P-domainAdd
BLAST
Regioni254 – 292393 X approximate repeatsAdd
BLAST
Regioni302 – 39594C-domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi392 – 3954Prevents secretion from ERPROSITE-ProRule annotation

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi332 – 39059Asp/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.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
InParanoidiP27798.
KOiK08057.
OMAiDDFSNKG.
OrthoDBiEOG77126Z.
PhylomeDBiP27798.

Family and domain databases

Gene3Di2.60.120.200. 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. 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. 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:July 31, 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. Positions 17-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

2D gel databases

World-2DPAGE0020:P27798.

Proteomic databases

PaxDbiP27798.

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

eggNOGiNOG305105.
GeneTreeiENSGT00430000030841.
HOGENOMiHOG000192435.
InParanoidiP27798.
KOiK08057.
OMAiDDFSNKG.
OrthoDBiEOG77126Z.
PhylomeDBiP27798.

Enzyme and pathway databases

ReactomeiREACT_315447. Calnexin/calreticulin cycle.

Miscellaneous databases

NextBioi903464.
PROiP27798.

Family and domain databases

Gene3Di2.60.120.200. 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. 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. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A C. elegans gene encodes a protein homologous to mammalian calreticulin."
    Smith M.J.
    DNA Seq. 2:235-240(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Bristol N2.
  2. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiCALR_CAEEL
AccessioniPrimary (citable) accession number: P27798
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1992
Last sequence update: July 31, 1992
Last modified: March 31, 2015
This is version 130 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

External Data

Dasty 3

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 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.