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Protein

Calreticulin

Gene

Crc

Organism
Drosophila melanogaster (Fruit fly)
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 sitei109 – 1091CarbohydrateBy similarity
Binding sitei111 – 1111CarbohydrateBy similarity
Binding sitei128 – 1281CarbohydrateBy similarity
Binding sitei135 – 1351CarbohydrateBy similarity
Binding sitei317 – 3171CarbohydrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. brain morphogenesis Source: FlyBase
  2. central nervous system development Source: FlyBase
  3. imaginal disc-derived wing morphogenesis Source: FlyBase
  4. locomotion involved in locomotory behavior Source: FlyBase
  5. neurogenesis Source: FlyBase
  6. olfactory behavior Source: FlyBase
  7. peripheral nervous system development Source: FlyBase
  8. protein folding Source: InterPro
  9. sleep Source: FlyBase
  10. startle response Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Calcium, Lectin, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_180278. Calnexin/calreticulin cycle.
REACT_252409. Scavenging by Class F Receptors.
REACT_93794. ATF6-alpha activates chaperone genes.

Names & Taxonomyi

Protein namesi
Recommended name:
Calreticulin
Gene namesi
Name:Crc
ORF Names:CG9429
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0005585. Crc.

Subcellular locationi

GO - Cellular componenti

  1. endomembrane system Source: FlyBase
  2. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  3. extracellular space Source: FlyBase
  4. fusome Source: FlyBase
  5. lipid particle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 406389CalreticulinPRO_0000004182Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi105 ↔ 137By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP29413.
PRIDEiP29413.

Expressioni

Gene expression databases

BgeeiP29413.
ExpressionAtlasiP29413. differential.

Interactioni

Protein-protein interaction databases

BioGridi66325. 89 interactions.
DIPiDIP-19046N.
IntActiP29413. 3 interactions.
MINTiMINT-755481.

Structurei

3D structure databases

ProteinModelPortaliP29413.
SMRiP29413. Positions 21-365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati191 – 202121-1Add
BLAST
Repeati210 – 221121-2Add
BLAST
Repeati227 – 238121-3Add
BLAST
Repeati244 – 255121-4Add
BLAST
Repeati259 – 269112-1Add
BLAST
Repeati273 – 283112-2Add
BLAST
Repeati287 – 297112-3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 255654 X approximate repeatsAdd
BLAST
Regioni259 – 297393 X approximate repeatsAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi353 – 40250Asp/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.
InParanoidiP29413.
KOiK08057.
OMAiERWIESK.
OrthoDBiEOG77126Z.
PhylomeDBiP29413.

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.

P29413-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MMWCKTVIVL LATVGFISAE VYLKENFDNE NWEDTWIYSK HPGKEFGKFV
60 70 80 90 100
LTPGTFYNDA EADKGIQTSQ DARFYAASRK FDGFSNEDKP LVVQFSVKHE
110 120 130 140 150
QNIDCGGGYV KLFDCSLDQT DMHGESPYEI MFGPDICGPG TKKVHVIFSY
160 170 180 190 200
KGKNHLISKD IRCKDDVYTH FYTLIVRPDN TYEVLIDNEK VESGNLEDDW
210 220 230 240 250
DFLAPKKIKD PTATKPEDWD DRATIPDPDD KKPEDWDKPE HIPDPDATKP
260 270 280 290 300
EDWDDEMDGE WEPPMIDNPE FKGEWQPKQL DNPNYKGAWE HPEIANPEYV
310 320 330 340 350
PDDKLYLRKE ICTLGFDLWQ VKSGTIFDNV LITDDVELAA KAAAEVKNTQ
360 370 380 390 400
AGEKKMKEAQ DEVQRKKDEE EAKKASDKDD EDEDDDDEEK DDESKQDKDQ

SEHDEL
Length:406
Mass (Da):46,808
Last modified:October 1, 1993 - v2
Checksum:i65D72C69D0BEC427
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071G → A AA sequence (PubMed:2365822)Curated
Sequence conflicti184 – 1841V → L AA sequence (PubMed:2365822)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64461 Genomic DNA. Translation: CAA45791.1.
AE014297 Genomic DNA. Translation: AAF54416.1.
PIRiA56637.
RefSeqiNP_001262430.1. NM_001275501.1.
NP_524293.2. NM_079569.5.
UniGeneiDm.2457.

Genome annotation databases

EnsemblMetazoaiFBtr0082103; FBpp0081581; FBgn0005585.
GeneIDi41166.
KEGGidme:Dmel_CG9429.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64461 Genomic DNA. Translation: CAA45791.1.
AE014297 Genomic DNA. Translation: AAF54416.1.
PIRiA56637.
RefSeqiNP_001262430.1. NM_001275501.1.
NP_524293.2. NM_079569.5.
UniGeneiDm.2457.

3D structure databases

ProteinModelPortaliP29413.
SMRiP29413. Positions 21-365.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66325. 89 interactions.
DIPiDIP-19046N.
IntActiP29413. 3 interactions.
MINTiMINT-755481.

Proteomic databases

PaxDbiP29413.
PRIDEiP29413.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082103; FBpp0081581; FBgn0005585.
GeneIDi41166.
KEGGidme:Dmel_CG9429.

Organism-specific databases

CTDi41166.
FlyBaseiFBgn0005585. Crc.

Phylogenomic databases

eggNOGiNOG305105.
GeneTreeiENSGT00430000030841.
InParanoidiP29413.
KOiK08057.
OMAiERWIESK.
OrthoDBiEOG77126Z.
PhylomeDBiP29413.

Enzyme and pathway databases

ReactomeiREACT_180278. Calnexin/calreticulin cycle.
REACT_252409. Scavenging by Class F Receptors.
REACT_93794. ATF6-alpha activates chaperone genes.

Miscellaneous databases

ChiTaRSiCrc. fly.
GenomeRNAii41166.
NextBioi822514.
PROiP29413.

Gene expression databases

BgeeiP29413.
ExpressionAtlasiP29413. differential.

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. "Nucleotide sequence of a Drosophila melanogaster gene encoding a calreticulin homologue."
    Smith M.J.
    DNA Seq. 3:247-250(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "A human Ro/SS-A autoantigen is the homologue of calreticulin and is highly homologous with onchocercal RAL-1 antigen and an aplysia 'memory molecule'."
    McCauliffe D.P., Zappi E., Lieu T.S., Michalak M., Sontheimer R.D., Capra J.D.
    J. Clin. Invest. 86:332-335(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 91-124 AND 182-220.

Entry informationi

Entry nameiCALR_DROME
AccessioniPrimary (citable) accession number: P29413
Secondary accession number(s): Q9VHA3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1993
Last modified: January 7, 2015
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.