CALR3_ARATH
ID CALR3_ARATH Reviewed; 424 AA.
AC O04153; Q93ZR4; Q9SJE7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Calreticulin-3;
DE AltName: Full=Protein PRIORITY IN SWEET LIFE 1;
DE Flags: Precursor;
GN Name=CRT3; OrderedLocusNames=At1g08450; ORFNames=T27G7.13;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9159940; DOI=10.1104/pp.114.1.29;
RA Nelson D.E., Glaunsinger B., Bohnert H.J.;
RT "Abundant accumulation of the calcium-binding molecular chaperone
RT calreticulin in specific floral tissues of Arabidopsis thaliana.";
RL Plant Physiol. 114:29-37(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND MUTAGENESIS OF PRO-67; GLY-244 AND SER-335.
RX PubMed=19763087; DOI=10.1038/emboj.2009.263;
RA Saijo Y., Tintor N., Lu X., Rauf P., Pajerowska-Mukhtar K., Haeweker H.,
RA Dong X., Robatzek S., Schulze-Lefert P.;
RT "Receptor quality control in the endoplasmic reticulum for plant innate
RT immunity.";
RL EMBO J. 28:3439-3449(2009).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLY-115; GLY-142; GLY-147; HIS-179; GLY-203 AND
RP PRO-293, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=19717464; DOI=10.1073/pnas.0905532106;
RA Li J., Zhao-Hui C., Batoux M., Nekrasov V., Roux M., Chinchilla D.,
RA Zipfel C., Jones J.D.;
RT "Specific ER quality control components required for biogenesis of the
RT plant innate immune receptor EFR.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15973-15978(2009).
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. Required for elongation factor Tu receptor (EFR)
CC accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling.
CC {ECO:0000269|PubMed:19717464, ECO:0000269|PubMed:19763087}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138, ECO:0000269|PubMed:19717464}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=O04153-1; Sequence=Displayed;
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 -!- DISRUPTION PHENOTYPE: Loss of seedling growth inhibition in response to
CC the pathogen-associated molecular pattern (PAMP) elf18 and increased
CC susceptibility to phytopathogenic bacteria.
CC {ECO:0000269|PubMed:19717464}.
CC -!- SIMILARITY: Belongs to the calreticulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF22902.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U66345; AAC49697.1; -; mRNA.
DR EMBL; AC006932; AAF22902.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28291.1; -; Genomic_DNA.
DR EMBL; AY056320; AAL07169.1; -; mRNA.
DR RefSeq; NP_563816.1; NM_100718.5. [O04153-1]
DR AlphaFoldDB; O04153; -.
DR SMR; O04153; -.
DR BioGRID; 22606; 4.
DR DIP; DIP-48930N; -.
DR IntAct; O04153; 1.
DR STRING; 3702.AT1G08450.1; -.
DR PaxDb; O04153; -.
DR PRIDE; O04153; -.
DR ProteomicsDB; 240246; -. [O04153-1]
DR EnsemblPlants; AT1G08450.1; AT1G08450.1; AT1G08450. [O04153-1]
DR GeneID; 837365; -.
DR Gramene; AT1G08450.1; AT1G08450.1; AT1G08450. [O04153-1]
DR KEGG; ath:AT1G08450; -.
DR Araport; AT1G08450; -.
DR TAIR; locus:2201816; AT1G08450.
DR eggNOG; KOG0674; Eukaryota.
DR HOGENOM; CLU_018224_0_2_1; -.
DR InParanoid; O04153; -.
DR OMA; SRWVNSE; -.
DR PhylomeDB; O04153; -.
DR PRO; PR:O04153; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04153; baseline and differential.
DR Genevisible; O04153; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
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:0046283; P:anthocyanin-containing compound metabolic process; IMP:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0009626; P:plant-type hypersensitive response; IMP:TAIR.
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; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Chaperone; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Lectin; Metal-binding;
KW Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..424
FT /note="Calreticulin-3"
FT /id="PRO_0000004186"
FT REPEAT 200..211
FT /note="1-1"
FT REPEAT 219..230
FT /note="1-2"
FT REPEAT 236..247
FT /note="1-3"
FT REPEAT 254..265
FT /note="1-4"
FT REPEAT 269..279
FT /note="2-1"
FT REPEAT 283..293
FT /note="2-2"
FT REPEAT 297..307
FT /note="2-3"
FT REGION 200..265
FT /note="4 X approximate repeats"
FT REGION 228..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..307
FT /note="3 X approximate repeats"
FT REGION 368..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 228..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 118
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 120
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 137
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 144
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT BINDING 327
FT /ligand="an alpha-D-glucoside"
FT /ligand_id="ChEBI:CHEBI:22390"
FT /evidence="ECO:0000250|UniProtKB:P14211"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 114..146
FT /evidence="ECO:0000250"
FT MUTAGEN 67
FT /note="P->L: In psl1-1; no effect on EFR accumulation, but
FT decreased response to the PAMP elf18."
FT /evidence="ECO:0000269|PubMed:19763087"
FT MUTAGEN 115
FT /note="G->D: In crt3-3; loss of response to the PAMP elf18,
FT but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT MUTAGEN 142
FT /note="G->E: In crt3-4; loss of response to the PAMP elf18,
FT but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT MUTAGEN 147
FT /note="G->E: In crt3-5; loss of response to the PAMP elf18,
FT but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT MUTAGEN 179
FT /note="H->Y: In crt3-6; loss of response to the PAMP elf18,
FT but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT MUTAGEN 203
FT /note="G->D: In crt3-7; loss of response to the PAMP elf18,
FT but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT MUTAGEN 244
FT /note="G->S: In psl1-3; no effect on EFR accumulation, but
FT decreased response to the PAMP elf18."
FT /evidence="ECO:0000269|PubMed:19763087"
FT MUTAGEN 293
FT /note="P->S: In crt3-10; loss of response to the PAMP
FT elf18, but no effect on the response to PAMP flg22."
FT /evidence="ECO:0000269|PubMed:19717464"
FT MUTAGEN 335
FT /note="S->L: In psl1-4; loss of EFR accumulation and loss
FT of response to the PAMP elf18."
FT /evidence="ECO:0000269|PubMed:19763087"
FT CONFLICT 279
FT /note="S -> F (in Ref. 1; AAC49697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 49844 MW; 64445A06359F0B8C CRC64;
MGLPQNKLSF FCFFFLVSVL TLAPLAFSEI FLEEHFEGGW KSRWVLSDWK RNEGKAGTFK
HTAGKWPGDP DNKGIQTYND AKHYAISAKI PEFSNKNRTL VVQYSVKIEQ DIECGGAYIK
LLSGYVNQKQ FGGDTPYSLM FGPDICGTQT KKLHVIVSYQ GQNYPIKKDL QCETDKLNHF
YTFILRPDAS YSVLVDNKER EFGSMYTDWD ILPPRKIKVK NAKKPEDWDD REYIDDPNDV
KPEGFDSIPR EIPDRKAKEP EDWDEEENGL WEPPKIPNSA YKGPWKAKRI KNPNYKGKWK
NPWIDNPEFE DDPDLYVLKS IKYAGIEVWQ VKAGSIFDNI LICDDPAYAR SIVDDYFAQH
RESEKELFAE AEKERKARED EEARIAREEG ERRRKERDHR YGDRRRRYKR PNPRDYMDDY
HDEL
