EULS3_ARATH
ID EULS3_ARATH Reviewed; 317 AA.
AC Q945P1; Q9ZV03;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ricin B-like lectin EULS3 {ECO:0000305};
DE AltName: Full=Euonymus lectin S3 {ECO:0000305};
DE Short=AtEULS3 {ECO:0000303|PubMed:21945438};
GN Name=EULS3 {ECO:0000303|PubMed:21945438};
GN OrderedLocusNames=At2g39050 {ECO:0000312|Araport:AT2G39050};
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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 [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INDUCTION.
RX PubMed=19930663; DOI=10.1186/1471-2229-9-136;
RA Fouquaert E., Peumans W.J., Vandekerckhove T.T., Ongenaert M.,
RA Van Damme E.J.;
RT "Proteins with an Euonymus lectin-like domain are ubiquitous in
RT Embryophyta.";
RL BMC Plant Biol. 9:136-136(2009).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21945438; DOI=10.1016/j.bbrc.2011.09.031;
RA Van Hove J., Fouquaert E., Smith D.F., Proost P., Van Damme E.J.;
RT "Lectin activity of the nucleocytoplasmic EUL protein from Arabidopsis
RT thaliana.";
RL Biochem. Biophys. Res. Commun. 414:101-105(2011).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=25238657; DOI=10.1016/j.jplph.2014.08.009;
RA Van Hove J., Stefanowicz K., De Schutter K., Eggermont L., Lannoo N.,
RA Al Atalah B., Van Damme E.J.;
RT "Transcriptional profiling of the lectin ArathEULS3 from Arabidopsis
RT thaliana toward abiotic stresses.";
RL J. Plant Physiol. 171:1763-1773(2014).
RN [8]
RP FUNCTION, INTERACTION WITH ATS3A AND ATS3B, TISSUE SPECIFICITY, AND
RP INDUCTION BY PATHOGEN INFECTION.
RX PubMed=26259197; DOI=10.1016/j.plantsci.2015.07.005;
RA Van Hove J., De Jaeger G., De Winne N., Guisez Y., Van Damme E.J.;
RT "The Arabidopsis lectin EULS3 is involved in stomatal closure.";
RL Plant Sci. 238:312-322(2015).
CC -!- FUNCTION: Lectin which binds carbohydrates in vitro. Interacts through
CC its lectin domain with glycan structures containing one or more Lewis
CC X, Lewis Y or lactosamine motifs (PubMed:21945438). May play a role in
CC abiotic stress responses (Probable). May play a role in abscisic acid-
CC induced stomatal closure. May play a role in disease resistance against
CC Pseudomonas syringae through its involvement in stomatal movement
CC (PubMed:26259197). {ECO:0000269|PubMed:21945438,
CC ECO:0000269|PubMed:26259197, ECO:0000305|PubMed:25238657}.
CC -!- SUBUNIT: Interacts (via N-terminus) with ATS3A and ATS3B.
CC {ECO:0000269|PubMed:26259197}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21945438}. Cytoplasm
CC {ECO:0000269|PubMed:21945438}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, rosette leaves, stems, cauline
CC leaves and flowers. {ECO:0000269|PubMed:26259197}.
CC -!- INDUCTION: Induced by osmotic shock and salt stress (PubMed:19930663,
CC PubMed:25238657). Induced by abscisic acid (ABA) (PubMed:19930663,
CC PubMed:25238657, PubMed:26259197). Induced by methyl jasmonate
CC (PubMed:25238657). Induced by infection with the fungal pathogen
CC B.cinerea and the bacterial pathogen P.synrigae pv. tomato
CC (PubMed:19930663, PubMed:26259197). {ECO:0000269|PubMed:19930663,
CC ECO:0000269|PubMed:25238657, ECO:0000269|PubMed:26259197}.
CC -!- DOMAIN: The ricin B-type lectin domain binds glycan structures.
CC {ECO:0000269|PubMed:21945438}.
CC -!- MISCELLANEOUS: Plants silencing EULS3 exhibit an aberrant abscisic
CC acid-induced stomatal closure. {ECO:0000269|PubMed:26259197}.
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DR EMBL; AC005770; AAC79615.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC09630.1; -; Genomic_DNA.
DR EMBL; AF411801; AAL06490.1; -; mRNA.
DR EMBL; AY093795; AAM10411.1; -; mRNA.
DR EMBL; AY087909; AAM65460.1; -; mRNA.
DR PIR; E84812; E84812.
DR RefSeq; NP_565899.1; NM_129462.3.
DR AlphaFoldDB; Q945P1; -.
DR SMR; Q945P1; -.
DR STRING; 3702.AT2G39050.1; -.
DR PaxDb; Q945P1; -.
DR PRIDE; Q945P1; -.
DR ProMEX; Q945P1; -.
DR ProteomicsDB; 222355; -.
DR EnsemblPlants; AT2G39050.1; AT2G39050.1; AT2G39050.
DR GeneID; 818491; -.
DR Gramene; AT2G39050.1; AT2G39050.1; AT2G39050.
DR KEGG; ath:AT2G39050; -.
DR Araport; AT2G39050; -.
DR TAIR; locus:2064965; AT2G39050.
DR eggNOG; ENOG502QTCR; Eukaryota.
DR HOGENOM; CLU_073954_0_0_1; -.
DR InParanoid; Q945P1; -.
DR OMA; HHEPPYP; -.
DR OrthoDB; 1069623at2759; -.
DR PhylomeDB; Q945P1; -.
DR PRO; PR:Q945P1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q945P1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IDA:TAIR.
DR GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR GO; GO:0090332; P:stomatal closure; IMP:TAIR.
DR InterPro; IPR040249; Ricin_B-like_lectin_EULS3-like.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR31257; PTHR31257; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Lectin; Nucleus; Reference proteome; Stress response.
FT CHAIN 1..317
FT /note="Ricin B-like lectin EULS3"
FT /id="PRO_0000438376"
FT DOMAIN 168..315
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 1..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 317 AA; 35648 MW; 06BD82790AC792BF CRC64;
MEHHHQHHRH HQRDDGEDDR QSFGVPPPHV DAPPQPHGLY QSQPHFDPYA PTPQAPAPYR
SETQFEPHAP PPYRSEPYFE TPAPPPSFGH VSHVGHQSPN ESYPPEHHRY GGYQQPSNSL
LESHGDHSGV THVAHHSSNQ PQSSSGVYHK PDENRLPDNL AGLAGRATVK VYSKAEPNYN
LTIRDGKVIL APADPSDEAQ HWYKDEKYST KVKDADGHPC FALVNKATGE AMKHSVGATH
PVHLIRYVPD KLDESVLWTE SKDFGDGYRT IRMVNNTRLN VDAYHGDSKS GGVRDGTTIV
LWDWNKGDNQ LWKIFPF
