ID   CALR2_ARATH             Reviewed;         424 AA.
AC   Q38858; O04152; O80486; Q94AW7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 3.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Calreticulin-2;
DE   Flags: Precursor;
GN   Name=CRT2; Synonyms=CRTL; OrderedLocusNames=At1g09210;
GN   ORFNames=T12M4.8;
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 [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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-174.
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 16-424.
RC   STRAIN=cv. Landsberg erecta; TISSUE=Flower;
RA   Benedetti C.E., Turner J.G.;
RT   "Nucleotide sequence of an Arabidopsis thaliana cDNA encoding a protein
RT   homologous to plant and animal calreticulins.";
RL   (er) Plant Gene Register PGR95-047(1995).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC       ProRule:PRU10138}.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC24083.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAC49696.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC003114; AAC24083.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE28414.1; -; Genomic_DNA.
DR   EMBL; AY045656; AAK74014.1; -; mRNA.
DR   EMBL; AY059662; AAL31155.1; -; mRNA.
DR   EMBL; U66344; AAC49696.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U27698; AAA80652.1; -; mRNA.
DR   PIR; H86224; H86224.
DR   RefSeq; NP_172392.1; NM_100791.4.
DR   AlphaFoldDB; Q38858; -.
DR   SMR; Q38858; -.
DR   BioGRID; 22682; 15.
DR   STRING; 3702.Q38858; -.
DR   GlyCosmos; Q38858; 1 site, No reported glycans.
DR   iPTMnet; Q38858; -.
DR   PaxDb; 3702-AT1G09210-1; -.
DR   ProteomicsDB; 240245; -.
DR   EnsemblPlants; AT1G09210.1; AT1G09210.1; AT1G09210.
DR   GeneID; 837441; -.
DR   Gramene; AT1G09210.1; AT1G09210.1; AT1G09210.
DR   KEGG; ath:AT1G09210; -.
DR   Araport; AT1G09210; -.
DR   TAIR; AT1G09210; CRT1B.
DR   eggNOG; KOG0674; Eukaryota.
DR   HOGENOM; CLU_018224_0_2_1; -.
DR   InParanoid; Q38858; -.
DR   OMA; DNRAGEW; -.
DR   OrthoDB; 5489154at2759; -.
DR   PhylomeDB; Q38858; -.
DR   PRO; PR:Q38858; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q38858; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; 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:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IPI:TAIR.
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:SF25; CALRETICULIN-2; 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   SWISS-2DPAGE; Q38858; -.
DR   Genevisible; Q38858; AT.
PE   1: Evidence at protein level;
KW   Calcium; Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Lectin; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Signal;
KW   Zinc.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..424
FT                   /note="Calreticulin-2"
FT                   /id="PRO_0000004185"
FT   REPEAT          194..205
FT                   /note="1-1"
FT   REPEAT          213..224
FT                   /note="1-2"
FT   REPEAT          230..241
FT                   /note="1-3"
FT   REPEAT          248..259
FT                   /note="1-4"
FT   REPEAT          263..273
FT                   /note="2-1"
FT   REPEAT          277..287
FT                   /note="2-2"
FT   REPEAT          291..301
FT                   /note="2-3"
FT   REGION          194..259
FT                   /note="4 X approximate repeats"
FT   REGION          210..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          263..301
FT                   /note="3 X approximate repeats"
FT   REGION          362..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        210..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..398
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..424
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         112
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         114
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   BINDING         131
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         321
FT                   /ligand="an alpha-D-glucoside"
FT                   /ligand_id="ChEBI:CHEBI:22390"
FT                   /evidence="ECO:0000250|UniProtKB:P14211"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O04151"
FT   MOD_RES         396
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P29402"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        108..140
FT                   /evidence="ECO:0000250"
FT   CONFLICT        16..19
FT                   /note="LVAI -> NSAR (in Ref. 5; AAA80652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155
FT                   /note="E -> G (in Ref. 4; AAC49696 and 5; AAA80652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="P -> T (in Ref. 5; AAA80652)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="V -> E (in Ref. 5; AAA80652)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   424 AA;  48157 MW;  51421329AE81A7F5 CRC64;
     MAKMIPSLVS LILIGLVAIA SAAVIFEERF DDGWENRWVK SEWKKDDNTA GEWKHTAGNW
     SGDANDKGIQ TSEDYRFYAI SAEFPEFSNK DKTLVFQFSV KHEQKLDCGG GYMKLLSGDV
     DQKKFGGDTP YSIMFGPDIC GYSTKKVHAI LTYNEANHLI KKDVPCETDQ LTHVYTFILR
     PDATYSILID NVEKQTGSLY SDWDLLPPKK IKDPSAKKPE DWDEQEYISD PEDKKPDGYD
     DIPKEIPDTD SKKPEDWDDE EDGEWTAPTI PNPEYMGEWK PKQIKNPNYK GKWEAPLIDN
     PDFKDDPELY VFPKLKYVGL ELWQVKSGSL FDNVLICDDP DYAKKLADET WGKLKDAEKA
     AFDEAEKKNE EEESKDAPAE SDAEDEPEDD EGGDDSDSES KAEETKSVDS EETSEKDATA
     HDEL
//