Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P29413

- CALR_DROME

UniProt

P29413 - CALR_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Calreticulin

Gene

Crc

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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. endoplasmic reticulum Source: UniProtKB-KW
  2. extracellular space Source: FlyBase
  3. fusome Source: FlyBase
  4. 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.
OMAiKNWVYSE.
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 .
PIRi A56637.
RefSeqi NP_001262430.1. NM_001275501.1.
NP_524293.2. NM_079569.5.
UniGenei Dm.2457.

3D structure databases

ProteinModelPortali P29413.
SMRi P29413. Positions 21-365.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 66325. 89 interactions.
DIPi DIP-19046N.
IntActi P29413. 3 interactions.
MINTi MINT-755481.

Proteomic databases

PaxDbi P29413.
PRIDEi P29413.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0082103 ; FBpp0081581 ; FBgn0005585 .
GeneIDi 41166.
KEGGi dme:Dmel_CG9429.

Organism-specific databases

CTDi 41166.
FlyBasei FBgn0005585. Crc.

Phylogenomic databases

eggNOGi NOG305105.
GeneTreei ENSGT00430000030841.
InParanoidi P29413.
KOi K08057.
OMAi KNWVYSE.
OrthoDBi EOG77126Z.
PhylomeDBi P29413.

Enzyme and pathway databases

Reactomei REACT_180278. Calnexin/calreticulin cycle.
REACT_252409. Scavenging by Class F Receptors.
REACT_93794. ATF6-alpha activates chaperone genes.

Miscellaneous databases

ChiTaRSi Crc. fly.
GenomeRNAii 41166.
NextBioi 822514.
PROi P29413.

Gene expression databases

Bgeei P29413.
ExpressionAtlasi P29413. differential.

Family and domain databases

Gene3Di 2.60.120.200. 2 hits.
InterProi IPR001580. Calret/calnex.
IPR018124. Calret/calnex_CS.
IPR009169. Calreticulin.
IPR009033. Calreticulin/calnexin_P_dom.
IPR013320. ConA-like_dom.
[Graphical view ]
PANTHERi PTHR11073. PTHR11073. 1 hit.
Pfami PF00262. Calreticulin. 1 hit.
[Graphical view ]
PIRSFi PIRSF002356. Calreticulin. 1 hit.
PRINTSi PR00626. CALRETICULIN.
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF63887. SSF63887. 1 hit.
PROSITEi PS00803. CALRETICULIN_1. 1 hit.
PS00804. CALRETICULIN_2. 1 hit.
PS00805. CALRETICULIN_REPEAT. 3 hits.
PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: November 26, 2014
This is version 133 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