CALR1_ARATH
ID CALR1_ARATH Reviewed; 425 AA.
AC O04151;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Calreticulin-1;
DE Flags: Precursor;
GN Name=CRT1; OrderedLocusNames=At1g56340; ORFNames=F13N6.20, F14G9.5;
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 INDUCTION BY CADMIUM.
RC STRAIN=cv. Columbia;
RX PubMed=16502469; DOI=10.1002/pmic.200500543;
RA Sarry J.-E., Kuhn L., Ducruix C., Lafaye A., Junot C., Hugouvieux V.,
RA Jourdain A., Bastien O., Fievet J.B., Vailhen D., Amekraz B., Moulin C.,
RA Ezan E., Garin J., Bourguignon J.;
RT "The early responses of Arabidopsis thaliana cells to cadmium exposure
RT explored by protein and metabolite profiling analyses.";
RL Proteomics 6:2180-2198(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND IDENTIFICATION BY
RP 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 -!- 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=O04151-1; Sequence=Displayed;
CC -!- INDUCTION: Induced by cadmium. {ECO:0000269|PubMed:16502469}.
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}.
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DR EMBL; U66343; AAC49695.1; -; mRNA.
DR EMBL; AC058785; AAG51504.1; -; Genomic_DNA.
DR EMBL; AC069159; AAG50908.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33379.1; -; Genomic_DNA.
DR EMBL; AY062628; AAL32706.1; -; mRNA.
DR EMBL; BT008511; AAP37870.1; -; mRNA.
DR PIR; C96605; C96605.
DR RefSeq; NP_176030.1; NM_104513.5. [O04151-1]
DR AlphaFoldDB; O04151; -.
DR SMR; O04151; -.
DR BioGRID; 27312; 15.
DR STRING; 3702.AT1G56340.1; -.
DR iPTMnet; O04151; -.
DR SWISS-2DPAGE; O04151; -.
DR PaxDb; O04151; -.
DR PRIDE; O04151; -.
DR ProteomicsDB; 222776; -. [O04151-1]
DR EnsemblPlants; AT1G56340.1; AT1G56340.1; AT1G56340. [O04151-1]
DR GeneID; 842087; -.
DR Gramene; AT1G56340.1; AT1G56340.1; AT1G56340. [O04151-1]
DR KEGG; ath:AT1G56340; -.
DR Araport; AT1G56340; -.
DR TAIR; locus:2010723; AT1G56340.
DR eggNOG; KOG0674; Eukaryota.
DR HOGENOM; CLU_018224_0_2_1; -.
DR InParanoid; O04151; -.
DR OMA; DDRAMID; -.
DR PhylomeDB; O04151; -.
DR PRO; PR:O04151; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04151; baseline and differential.
DR Genevisible; O04151; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; 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:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IPI:TAIR.
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; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Lectin; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Zinc.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..425
FT /note="Calreticulin-1"
FT /id="PRO_0000004184"
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 213..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..301
FT /note="3 X approximate repeats"
FT REGION 348..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 422..425
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 213..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..376
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..399
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..425
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:0007744|PubMed:19245862,
FT ECO:0007744|PubMed:19376835"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P29402"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..140
FT /evidence="ECO:0000250"
SQ SEQUENCE 425 AA; 48527 MW; BCEC08E2F342642E CRC64;
MAKLNPKFIS LILFALVVIV SAEVIFEEKF EDGWEKRWVK SDWKKDDNTA GEWKHTAGNW
SGDANDKGIQ TSEDYRFYAI SAEFPEFSNK DKTLVFQFSV KHEQKLDCGG GYMKLLSDDV
DQTKFGGDTP YSIMFGPDIC GYSTKKVHAI LTYNGTNHLI KKEVPCETDQ LTHVYTFVLR
PDATYSILID NVEKQTGSLY SDWDLLPAKK IKDPSAKKPE DWDDKEYIPD PEDTKPAGYD
DIPKEIPDTD AKKPEDWDDE EDGEWTAPTI PNPEYNGEWK PKKIKNPAYK GKWKAPMIDN
PEFKDDPELY VFPKLKYVGV ELWQVKSGSL FDNVLVSDDP EYAKKLAEET WGKHKDAEKA
AFDEAEKKRE EEESKDAPAE SDAEEEAEDD DNEGDDSDNE SKSEETKEAE ETKEAEETDA
AHDEL
