ID   CALR_ORYSJ              Reviewed;         424 AA.
AC   Q9SLY8; Q6ZLM7; Q6ZLM8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   27-MAR-2024, entry version 147.
DE   RecName: Full=Calreticulin {ECO:0000303|PubMed:10651810};
DE   AltName: Full=56 kDa protein {ECO:0000303|PubMed:8888618};
DE   Flags: Precursor;
GN   Name=CRO1 {ECO:0000303|PubMed:10651810};
GN   Synonyms=pp56 {ECO:0000303|PubMed:8888618};
GN   OrderedLocusNames=Os07g0246200, LOC_Os07g14270;
GN   ORFNames=OJ1058_C08.34-1, OJ1058_C08.34-2, OSJNBa0003K21.18-1,
GN   OSJNBa0003K21.18-2;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=cv. Nipponbare;
RX   PubMed=10651810; DOI=10.1046/j.1432-1327.2000.01052.x;
RA   Li Z., Komatsu S.;
RT   "Molecular cloning and characterization of calreticulin, a calcium-binding
RT   protein involved in the regeneration of rice cultured suspension cells.";
RL   Eur. J. Biochem. 267:737-745(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [5]
RP   PROTEIN SEQUENCE OF 30-39; 81-90; 94-103; 111-120 AND 245-253.
RC   STRAIN=cv. Nipponbare;
RC   TISSUE=Anther, Embryo, Panicle, Sheath, and Stem;
RX   PubMed=14681440; DOI=10.1093/nar/gkh020;
RA   Komatsu S., Kojima K., Suzuki K., Ozaki K., Higo K.;
RT   "Rice proteome database based on two-dimensional polyacrylamide gel
RT   electrophoresis: its status in 2003.";
RL   Nucleic Acids Res. 32:D388-D392(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 30-39; 93-103; 110-120 AND 244-254, AND
RP   PHOSPHORYLATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=8888618; DOI=10.1093/oxfordjournals.pcp.a029009;
RA   Komatsu S., Masuda T., Abe K.;
RT   "Phosphorylation of a protein (pp56) is related to the regeneration of rice
RT   cultured suspension cells.";
RL   Plant Cell Physiol. 37:748-753(1996).
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 {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9SLY8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9SLY8-2; Sequence=VSP_016726;
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   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:8888618}.
CC   -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
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DR   EMBL; AB021259; BAA88900.1; -; mRNA.
DR   EMBL; AP003738; BAC82932.1; -; Genomic_DNA.
DR   EMBL; AP003738; BAC82933.1; -; Genomic_DNA.
DR   EMBL; AP006266; BAD31961.1; -; Genomic_DNA.
DR   EMBL; AP006266; BAD31962.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT00809.1; -; Genomic_DNA.
DR   EMBL; AP014963; BAT00810.1; -; Genomic_DNA.
DR   EMBL; AK065341; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK104328; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015647166.1; XM_015791680.1. [Q9SLY8-2]
DR   RefSeq; XP_015647167.1; XM_015791681.1.
DR   AlphaFoldDB; Q9SLY8; -.
DR   SMR; Q9SLY8; -.
DR   STRING; 39947.Q9SLY8; -.
DR   GlyCosmos; Q9SLY8; 1 site, No reported glycans.
DR   PaxDb; 39947-Q9SLY8; -.
DR   EnsemblPlants; Os07t0246200-01; Os07t0246200-01; Os07g0246200. [Q9SLY8-1]
DR   EnsemblPlants; Os07t0246200-02; Os07t0246200-02; Os07g0246200. [Q9SLY8-1]
DR   EnsemblPlants; Os07t0246200-03; Os07t0246200-03; Os07g0246200. [Q9SLY8-2]
DR   GeneID; 4342826; -.
DR   Gramene; Os07t0246200-01; Os07t0246200-01; Os07g0246200. [Q9SLY8-1]
DR   Gramene; Os07t0246200-02; Os07t0246200-02; Os07g0246200. [Q9SLY8-1]
DR   Gramene; Os07t0246200-03; Os07t0246200-03; Os07g0246200. [Q9SLY8-2]
DR   KEGG; osa:4342826; -.
DR   eggNOG; KOG0674; Eukaryota.
DR   HOGENOM; CLU_018224_0_2_1; -.
DR   InParanoid; Q9SLY8; -.
DR   OMA; ANYIMLV; -.
DR   OrthoDB; 5489154at2759; -.
DR   Proteomes; UP000000763; Chromosome 7.
DR   Proteomes; UP000059680; Chromosome 7.
DR   ExpressionAtlas; Q9SLY8; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:Gramene.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; ISS:Gramene.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:Gramene.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
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; CALRETICULIN AND CALNEXIN; 1.
DR   PANTHER; PTHR11073:SF2; CALRETICULIN-1; 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; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; Q9SLY8; OS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Chaperone; Direct protein sequencing;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein; Lectin; Metal-binding;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Zinc.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000269|PubMed:14681440"
FT   CHAIN           30..424
FT                   /note="Calreticulin"
FT                   /id="PRO_0000004193"
FT   REPEAT          201..212
FT                   /note="1-1"
FT   REPEAT          220..231
FT                   /note="1-2"
FT   REPEAT          237..248
FT                   /note="1-3"
FT   REPEAT          255..266
FT                   /note="1-4"
FT   REPEAT          270..280
FT                   /note="2-1"
FT   REPEAT          284..294
FT                   /note="2-2"
FT   REPEAT          298..308
FT                   /note="2-3"
FT   REGION          201..266
FT                   /note="4 X approximate repeats"
FT   REGION          217..289
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..308
FT                   /note="3 X approximate repeats"
FT   REGION          356..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        217..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        356..382
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..413
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         119
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         121
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         138
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         145
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         328
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        115..147
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         422..424
FT                   /note="DEL -> VCNTPAFS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12869764"
FT                   /id="VSP_016726"
FT   CONFLICT        193
FT                   /note="T -> S (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        263..265
FT                   /note="DWD -> AGA (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        278
FT                   /note="P -> R (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        302
FT                   /note="A -> P (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306..307
FT                   /note="DN -> AT (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="K -> Q (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="Y -> S (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        341
FT                   /note="F -> I (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347..348
FT                   /note="PE -> AA (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        359
FT                   /note="G -> A (in Ref. 1; BAA88900)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   424 AA;  48309 MW;  EFAE5723CB03BAE0 CRC64;
     MAIRARSSSY AAAAVALALA LASVAAVAGE VFFQEKFEDG WESRWVKSEW KKDENMAGEW
     NHTSGKWNGD PEDKGIQTSE DYRFYAISAE YPEFSNKDKT LVLQFSVKHE QKLDCGGGYV
     KLLGGDVDQK KFGGDTPYSI MFGPDICGYS TKKVHTIFTK NDKNHLIKKD VPCETDQLSH
     VYTLIIHPDA TYTILIDNVE KQSGSIYEHW DILPPKQIKD PEAKKPEDWD DKEYIPDPED
     KKPEGYDDIP KEIPDPDAKK PEDWDDEEDG EWTAPTIPNP EYKGPWKQKK IKNPNYQGKW
     KAPMIDNPDF KDDPYIYAFD SLKYIGIELW QVKSGTLFDN FLITDDPELA KTFAEETWGK
     HKDAEKAAFD EAEKKKEEEE AAKAGEDDDD LDDEDAEDED KADEKADSDA EDGKDSDDEK
     HDEL
//