CALR_DICDI
ID CALR_DICDI Reviewed; 424 AA.
AC Q23858; Q54QX4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 3.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Calreticulin;
DE Flags: Precursor;
GN Name=crtA; ORFNames=DDB_G0283539;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AX3;
RA Mueller-Taubenberger A., Gerisch G.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=AX2;
RX PubMed=16926386; DOI=10.1074/mcp.m600113-mcp200;
RA Gotthardt D., Blancheteau V., Bosserhoff A., Ruppert T., Delorenzi M.,
RA Soldati T.;
RT "Proteomics fingerprinting of phagosome maturation and evidence for the
RT role of a Galpha during uptake.";
RL Mol. Cell. Proteomics 5:2228-2243(2006).
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}.
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DR EMBL; U36937; AAB87719.1; -; mRNA.
DR EMBL; AAFI02000055; EAL65647.1; -; Genomic_DNA.
DR RefSeq; XP_639010.1; XM_633918.1.
DR AlphaFoldDB; Q23858; -.
DR SMR; Q23858; -.
DR IntAct; Q23858; 1.
DR STRING; 44689.DDB0191384; -.
DR PaxDb; Q23858; -.
DR EnsemblProtists; EAL65647; EAL65647; DDB_G0283539.
DR GeneID; 8624140; -.
DR KEGG; ddi:DDB_G0283539; -.
DR dictyBase; DDB_G0283539; crtA.
DR eggNOG; KOG0674; Eukaryota.
DR HOGENOM; CLU_018224_0_2_1; -.
DR InParanoid; Q23858; -.
DR OMA; MMWCKTV; -.
DR PhylomeDB; Q23858; -.
DR Reactome; R-DDI-901042; Calnexin/calreticulin cycle.
DR PRO; PR:Q23858; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:dictyBase.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:dictyBase.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
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:0006911; P:phagocytosis, engulfment; IGI:dictyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0051707; P:response to other organism; TAS:dictyBase.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR Gene3D; 2.10.250.10; -; 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; PTHR11073; 1.
DR Pfam; PF00262; Calreticulin; 2.
DR PIRSF; PIRSF002356; Calreticulin; 1.
DR PRINTS; PR00626; CALRETICULIN.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF63887; SSF63887; 1.
DR PROSITE; PS00804; CALRETICULIN_2; 1.
DR PROSITE; PS00805; CALRETICULIN_REPEAT; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Lectin;
KW Metal-binding; Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..424
FT /note="Calreticulin"
FT /id="PRO_0000004181"
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 246..256
FT /note="1-4"
FT REPEAT 260..270
FT /note="2-1"
FT REPEAT 274..284
FT /note="2-2"
FT REPEAT 288..298
FT /note="2-3"
FT REGION 191..256
FT /note="4 X 12 AA approximate repeats"
FT REGION 260..298
FT /note="3 X 11 AA approximate repeats"
FT REGION 370..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 421..424
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 370..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..401
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..424
FT /note="Basic and 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 318
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 183
FT /note="K -> N (in Ref. 1; AAB87719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 48365 MW; EAF3D804F96E4AEC CRC64;
MRLLLCLIFL VFVFNFALST VHFKDTFDND WESRWVVSDW HKEDGKSGKL VHTAGKWFGD
ENQKGIQTSE DARFYAVSAK FPSFSNKGKD LVLQYTVKNE QKVDCGGSYI KLLPSKLDQS
AFDGESEYSI MFGPDVCGAS KRVHVILNYK GKNHLIKKEI NKVETDQLTH QYTLVISPDN
TYKVLVDNKE IQAGNLADDW ELLPSKQIKD PKQSKPVDWV DVKEIDDPED VKPAGHDDIP
ASIVDPEAVK PEDWNEEDDG EWEAPTIANP EYKGEWKAKK IPNPEYKGEW VHPLIDNPEY
AEDNELYLFN DLGAIGFELW QVKSGSIFNN MIVTDSVEEA KDFSEKTFVA NQEAEKKMFD
DLEAAKAEER KKADEKLAAE KAAEKEAEEA DEEEEEVAEE DLVKTDDKKE EVKKSTKKVD
HDEL
