P29413 (CALR_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Calreticulin

Gene names

Name:	Crc
ORF Names:	CG9429

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Endoplasmic reticulum
Domain	Repeat Signal
Ligand	Calcium Lectin Metal-binding Zinc
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brain morphogenesis Inferred from mutant phenotype PubMed 18713854. 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_component	endoplasmic 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_function	calcium ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 406	389	Calreticulin		PRO_0000004182
Regions
	Repeat	191 – 202	12	1-1
	Repeat	210 – 221	12	1-2
	Repeat	227 – 238	12	1-3
	Repeat	244 – 255	12	1-4
	Repeat	259 – 269	11	2-1
	Repeat	273 – 283	11	2-2
	Repeat	287 – 297	11	2-3
	Region	191 – 255	65	4 X approximate repeats
	Region	259 – 297	39	3 X approximate repeats
	Compositional bias	353 – 402	50	Asp/Glu/Lys-rich
Sites
	Binding site	109	1	Carbohydrate By similarity
	Binding site	111	1	Carbohydrate By similarity
	Binding site	128	1	Carbohydrate By similarity
	Binding site	135	1	Carbohydrate By similarity
	Binding site	317	1	Carbohydrate By similarity
Amino acid modifications
	Disulfide bond	105 ↔ 137		By similarity
Experimental info
	Sequence conflict	107	1	G → A AA sequence Ref.4
	Sequence conflict	184	1	V → L AA sequence Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P29413 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 65D72C69D0BEC427	FASTA	406	46,808
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
PIR	A56637.
RefSeq	NP_001262430.1. NM_001275501.1. NP_524293.2. NM_079569.5.
UniGene	Dm.2457.
3D structure databases
ProteinModelPortal	P29413.
SMR	P29413. Positions 21-365.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-19046N.
IntAct	P29413. 3 interactions.
MINT	MINT-755481.
Proteomic databases
PaxDb	P29413.
PRIDE	P29413.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082103; FBpp0081581; FBgn0005585.
GeneID	41166.
KEGG	dme:Dmel_CG9429.
Organism-specific databases
CTD	41166.
FlyBase	FBgn0005585. Crc.
Phylogenomic databases
eggNOG	NOG305105.
GeneTree	ENSGT00430000030841.
InParanoid	P29413.
KO	K08057.
OMA	DGWTDRW.
OrthoDB	EOG4GMSCJ.
PhylomeDB	P29413.
Gene expression databases
Bgee	P29413.
GermOnline	CG9429. Drosophila melanogaster.
Family and domain databases
Gene3D	2.60.120.200. 2 hits.
InterPro	IPR001580. Calret/calnex. IPR018124. Calret/calnex_CS. IPR009169. Calreticulin. IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. [Graphical view]
PANTHER	PTHR11073. PTHR11073. 1 hit.
Pfam	PF00262. Calreticulin. 1 hit. [Graphical view]
PIRSF	PIRSF002356. Calreticulin. 1 hit.
PRINTS	PR00626. CALRETICULIN.
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS00803. CALRETICULIN_1. 1 hit. PS00804. CALRETICULIN_2. 1 hit. PS00805. CALRETICULIN_REPEAT. 3 hits. PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	Crc. drosophila.
GenomeRNAi	41166.
NextBio	822514.

Entry information

Entry name

CALR_DROME

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project