ID   CALR_DROME              Reviewed;         406 AA.
AC   P29413; Q9VHA3;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   24-JAN-2024, entry version 187.
DE   RecName: Full=Calreticulin {ECO:0000303|PubMed:1296819};
DE   Flags: Precursor;
GN   Name=Calr {ECO:0000312|FlyBase:FBgn0005585};
GN   Synonyms=Crc {ECO:0000312|FlyBase:FBgn0005585};
GN   ORFNames=CG9429 {ECO:0000312|FlyBase:FBgn0005585};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1296819; DOI=10.3109/10425179209034025;
RA   Smith M.J.;
RT   "Nucleotide sequence of a Drosophila melanogaster gene encoding a
RT   calreticulin homologue.";
RL   DNA Seq. 3:247-250(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4]
RP   PROTEIN SEQUENCE OF 91-124 AND 182-220.
RX   PubMed=2365822; DOI=10.1172/jci114704;
RA   McCauliffe D.P., Zappi E., Lieu T.S., Michalak M., Sontheimer R.D.,
RA   Capra J.D.;
RT   "A human Ro/SS-A autoantigen is the homologue of calreticulin and is highly
RT   homologous with onchocercal RAL-1 antigen and an aplysia 'memory
RT   molecule'.";
RL   J. Clin. Invest. 86:332-335(1990).
CC   -!- FUNCTION: Molecular calcium-binding chaperone promoting folding,
CC       oligomeric assembly and quality control in the ER via the
CC       calreticulin/calnexin cycle. This lectin may interact transiently with
CC       almost all of the monoglucosylated glycoproteins that are synthesized
CC       in the ER (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- DOMAIN: Can be divided into a N-terminal globular domain, a proline-
CC       rich P-domain forming an elongated arm-like structure and a C-terminal
CC       acidic domain. The P-domain binds one molecule of calcium with high
CC       affinity, whereas the acidic C-domain binds multiple calcium ions with
CC       low affinity (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The interaction with glycans occurs through a binding site in
CC       the globular lectin domain. {ECO:0000250}.
CC   -!- DOMAIN: The zinc binding sites are localized to the N-domain.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X64461; CAA45791.1; -; Genomic_DNA.
DR   EMBL; AE014297; AAF54416.1; -; Genomic_DNA.
DR   PIR; A56637; A56637.
DR   RefSeq; NP_001262430.1; NM_001275501.1.
DR   RefSeq; NP_524293.2; NM_079569.5.
DR   AlphaFoldDB; P29413; -.
DR   SMR; P29413; -.
DR   BioGRID; 66325; 93.
DR   DIP; DIP-19046N; -.
DR   IntAct; P29413; 4.
DR   STRING; 7227.FBpp0306685; -.
DR   GlyGen; P29413; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7227-FBpp0081581; -.
DR   DNASU; 41166; -.
DR   EnsemblMetazoa; FBtr0082103; FBpp0081581; FBgn0005585.
DR   EnsemblMetazoa; FBtr0334618; FBpp0306685; FBgn0005585.
DR   GeneID; 41166; -.
DR   KEGG; dme:Dmel_CG9429; -.
DR   AGR; FB:FBgn0005585; -.
DR   CTD; 811; -.
DR   FlyBase; FBgn0005585; Calr.
DR   VEuPathDB; VectorBase:FBgn0005585; -.
DR   eggNOG; KOG0674; Eukaryota.
DR   HOGENOM; CLU_018224_0_2_1; -.
DR   InParanoid; P29413; -.
DR   OMA; NWVYSEH; -.
DR   OrthoDB; 5489154at2759; -.
DR   PhylomeDB; P29413; -.
DR   Reactome; R-DME-901042; Calnexin/calreticulin cycle.
DR   SignaLink; P29413; -.
DR   BioGRID-ORCS; 41166; 1 hit in 3 CRISPR screens.
DR   ChiTaRS; Calr; fly.
DR   GenomeRNAi; 41166; -.
DR   PRO; PR:P29413; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0005585; Expressed in seminal fluid secreting gland and 46 other cell types or tissues.
DR   ExpressionAtlas; P29413; baseline and differential.
DR   GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR   GO; GO:0045169; C:fusome; IDA:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0042048; P:olfactory behavior; IMP:FlyBase.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0030431; P:sleep; IMP:FlyBase.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.10.250.10; Calreticulin/calnexin, P domain; 1.
DR   InterPro; IPR001580; Calret/calnex.
DR   InterPro; IPR018124; Calret/calnex_CS.
DR   InterPro; IPR009169; Calreticulin.
DR   InterPro; IPR009033; Calreticulin/calnexin_P_dom_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   PANTHER; PTHR11073:SF45; CALRETICULIN; 1.
DR   PANTHER; PTHR11073; CALRETICULIN AND CALNEXIN; 1.
DR   Pfam; PF00262; Calreticulin; 2.
DR   PIRSF; PIRSF002356; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF63887; P-domain of calnexin/calreticulin; 1.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; P29413; DM.
PE   1: Evidence at protein level;
KW   Calcium; Chaperone; Direct protein sequencing; Disulfide bond;
KW   Endoplasmic reticulum; Lectin; Metal-binding; Reference proteome; Repeat;
KW   Signal; Zinc.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..406
FT                   /note="Calreticulin"
FT                   /id="PRO_0000004182"
FT   REPEAT          191..202
FT                   /note="1-1"
FT   REPEAT          210..221
FT                   /note="1-2"
FT   REPEAT          227..238
FT                   /note="1-3"
FT   REPEAT          244..255
FT                   /note="1-4"
FT   REPEAT          259..269
FT                   /note="2-1"
FT   REPEAT          273..283
FT                   /note="2-2"
FT   REPEAT          287..297
FT                   /note="2-3"
FT   REGION          191..255
FT                   /note="4 X approximate repeats"
FT   REGION          207..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..297
FT                   /note="3 X approximate repeats"
FT   REGION          347..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        348..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..393
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         109
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         111
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         128
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         135
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         317
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   DISULFID        105..137
FT                   /evidence="ECO:0000250"
FT   CONFLICT        107
FT                   /note="G -> A (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="V -> L (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   406 AA;  46808 MW;  65D72C69D0BEC427 CRC64;
     MMWCKTVIVL LATVGFISAE VYLKENFDNE NWEDTWIYSK HPGKEFGKFV LTPGTFYNDA
     EADKGIQTSQ DARFYAASRK FDGFSNEDKP LVVQFSVKHE QNIDCGGGYV KLFDCSLDQT
     DMHGESPYEI MFGPDICGPG TKKVHVIFSY KGKNHLISKD IRCKDDVYTH FYTLIVRPDN
     TYEVLIDNEK VESGNLEDDW DFLAPKKIKD PTATKPEDWD DRATIPDPDD KKPEDWDKPE
     HIPDPDATKP EDWDDEMDGE WEPPMIDNPE FKGEWQPKQL DNPNYKGAWE HPEIANPEYV
     PDDKLYLRKE ICTLGFDLWQ VKSGTIFDNV LITDDVELAA KAAAEVKNTQ AGEKKMKEAQ
     DEVQRKKDEE EAKKASDKDD EDEDDDDEEK DDESKQDKDQ SEHDEL
//