CALR_ORYSJ
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 03-AUG-2022, entry version 139.
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; 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. [Q9SLY8-1]
DR AlphaFoldDB; Q9SLY8; -.
DR SMR; Q9SLY8; -.
DR STRING; 4530.OS07T0246200-03; -.
DR PaxDb; Q9SLY8; -.
DR PRIDE; 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; MMWCKTV; -.
DR Proteomes; UP000000763; Chromosome 7.
DR Proteomes; UP000059680; Chromosome 7.
DR ExpressionAtlas; Q9SLY8; baseline and differential.
DR Genevisible; Q9SLY8; OS.
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; 2.10.250.10; -; 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; PS00803; CALRETICULIN_1; 1.
DR PROSITE; PS00804; CALRETICULIN_2; 1.
DR PROSITE; PS00805; CALRETICULIN_REPEAT; 2.
DR PROSITE; PS00014; ER_TARGET; 1.
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
