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   24-JAN-2024, entry version 178.
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.O04153; -.
DR   GlyCosmos; O04153; 1 site, No reported glycans.
DR   PaxDb; 3702-AT1G08450-1; -.
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; AT1G08450; CRT3.
DR   eggNOG; KOG0674; Eukaryota.
DR   HOGENOM; CLU_018224_0_2_1; -.
DR   InParanoid; O04153; -.
DR   OMA; SRWVNSE; -.
DR   OrthoDB; 5489154at2759; -.
DR   PhylomeDB; O04153; -.
DR   PRO; PR:O04153; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; O04153; baseline and differential.
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; IEA:InterPro.
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; IEA:InterPro.
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; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   Genevisible; O04153; AT.
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
//