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P29413 (CALR_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

Endoplasmic reticulum lumen.

Domain

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 similarities

Belongs to the calreticulin family.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
   DomainRepeat
Signal
   LigandCalcium
Lectin
Metal-binding
Zinc
   Molecular functionChaperone
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbrain morphogenesis

Inferred from mutant phenotype PubMed 18713854. Source: FlyBase

central nervous system development

Inferred from mutant phenotype PubMed 11102367. Source: FlyBase

imaginal disc-derived wing morphogenesis

Inferred from mutant phenotype PubMed 21635778. Source: FlyBase

locomotion involved in locomotory behavior

Inferred from mutant phenotype PubMed 18713854. Source: FlyBase

neurogenesis

Inferred from mutant phenotype PubMed 21549331. Source: FlyBase

olfactory behavior

Inferred from mutant phenotype PubMed 12756487PubMed 17028343. Source: FlyBase

peripheral nervous system development

Traceable author statement PubMed 11102367. Source: FlyBase

protein folding

Inferred from electronic annotation. Source: InterPro

sleep

Inferred from mutant phenotype PubMed 18430954. Source: FlyBase

startle response

Inferred from mutant phenotype PubMed 18713854. Source: FlyBase

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from direct assay PubMed 16670001. Source: FlyBase

fusome

Inferred from direct assay PubMed 18355804. Source: FlyBase

lipid particle

Inferred from direct assay PubMed 16543254. Source: FlyBase

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 406389Calreticulin
PRO_0000004182

Regions

Repeat191 – 202121-1
Repeat210 – 221121-2
Repeat227 – 238121-3
Repeat244 – 255121-4
Repeat259 – 269112-1
Repeat273 – 283112-2
Repeat287 – 297112-3
Region191 – 255654 X approximate repeats
Region259 – 297393 X approximate repeats
Compositional bias353 – 40250Asp/Glu/Lys-rich

Sites

Binding site1091Carbohydrate By similarity
Binding site1111Carbohydrate By similarity
Binding site1281Carbohydrate By similarity
Binding site1351Carbohydrate By similarity
Binding site3171Carbohydrate By similarity

Amino acid modifications

Disulfide bond105 ↔ 137 By similarity

Experimental info

Sequence conflict1071G → A AA sequence Ref.4
Sequence conflict1841V → L AA sequence Ref.4

Sequences

Sequence LengthMass (Da)Tools
P29413 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 65D72C69D0BEC427

FASTA40646,808
        10         20         30         40         50         60 
MMWCKTVIVL LATVGFISAE VYLKENFDNE NWEDTWIYSK HPGKEFGKFV LTPGTFYNDA 

        70         80         90        100        110        120 
EADKGIQTSQ DARFYAASRK FDGFSNEDKP LVVQFSVKHE QNIDCGGGYV KLFDCSLDQT 

       130        140        150        160        170        180 
DMHGESPYEI MFGPDICGPG TKKVHVIFSY KGKNHLISKD IRCKDDVYTH FYTLIVRPDN 

       190        200        210        220        230        240 
TYEVLIDNEK VESGNLEDDW DFLAPKKIKD PTATKPEDWD DRATIPDPDD KKPEDWDKPE 

       250        260        270        280        290        300 
HIPDPDATKP EDWDDEMDGE WEPPMIDNPE FKGEWQPKQL DNPNYKGAWE HPEIANPEYV 

       310        320        330        340        350        360 
PDDKLYLRKE ICTLGFDLWQ VKSGTIFDNV LITDDVELAA KAAAEVKNTQ AGEKKMKEAQ 

       370        380        390        400 
DEVQRKKDEE EAKKASDKDD EDEDDDDEEK DDESKQDKDQ SEHDEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X64461 Genomic DNA. Translation: CAA45791.1.
AE014297 Genomic DNA. Translation: AAF54416.1.
PIRA56637.
RefSeqNP_001262430.1. NM_001275501.1.
NP_524293.2. NM_079569.5.
UniGeneDm.2457.

3D structure databases

ProteinModelPortalP29413.
SMRP29413. Positions 21-365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66325. 89 interactions.
DIPDIP-19046N.
IntActP29413. 3 interactions.
MINTMINT-755481.

Proteomic databases

PaxDbP29413.
PRIDEP29413.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0082103; FBpp0081581; FBgn0005585.
GeneID41166.
KEGGdme:Dmel_CG9429.

Organism-specific databases

CTD41166.
FlyBaseFBgn0005585. Crc.

Phylogenomic databases

eggNOGNOG305105.
GeneTreeENSGT00430000030841.
InParanoidP29413.
KOK08057.
OMAKNWVYSE.
OrthoDBEOG77126Z.
PhylomeDBP29413.

Gene expression databases

BgeeP29413.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR001580. 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]
PANTHERPTHR11073. PTHR11073. 1 hit.
PfamPF00262. Calreticulin. 1 hit.
[Graphical view]
PIRSFPIRSF002356. Calreticulin. 1 hit.
PRINTSPR00626. CALRETICULIN.
SUPFAMSSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEPS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCrc. drosophila.
GenomeRNAi41166.
NextBio822514.
PROP29413.

Entry information

Entry nameCALR_DROME
AccessionPrimary (citable) accession number: P29413
Secondary accession number(s): Q9VHA3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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