CALR2_ARATH
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 03-AUG-2022, entry version 176.
DE RecName: Full=Calreticulin-2;
DE Flags: Precursor;
GN Name=CRT2; Synonyms=CRTL; OrderedLocusNames=At1g09210; 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.AT1G09210.1; -.
DR iPTMnet; Q38858; -.
DR SWISS-2DPAGE; Q38858; -.
DR PaxDb; Q38858; -.
DR PRIDE; Q38858; -.
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; locus:2195326; AT1G09210.
DR eggNOG; KOG0674; Eukaryota.
DR HOGENOM; CLU_018224_0_2_1; -.
DR InParanoid; Q38858; -.
DR OMA; MMWCKTV; -.
DR OrthoDB; 822188at2759; -.
DR PhylomeDB; Q38858; -.
DR PRO; PR:Q38858; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38858; baseline and differential.
DR Genevisible; Q38858; 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: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; 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 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
