LECT6_ARATH
ID LECT6_ARATH Reviewed; 274 AA.
AC Q9LZF5; Q84R25;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Lectin-like protein {ECO:0000303|PubMed:17496105};
DE AltName: Full=Apoplastic EDS1-dependent protein 9 {ECO:0000303|PubMed:24755512};
DE AltName: Full=SA-induced legume lectin-like protein 1 {ECO:0000303|PubMed:24006883};
DE Flags: Precursor;
GN Name=LLP {ECO:0000303|PubMed:17496105};
GN Synonyms=AED9 {ECO:0000303|PubMed:24755512},
GN LLP1 {ECO:0000303|PubMed:24006883}, SAI-LLP1 {ECO:0000303|PubMed:24006883};
GN OrderedLocusNames=At5g03350 {ECO:0000312|Araport:AT5G03350};
GN ORFNames=F12E4.80 {ECO:0000312|EMBL:CAB83291.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INDUCTION BY SALICYLIC ACID.
RX PubMed=17496105; DOI=10.1104/pp.107.100842;
RA Krinke O., Ruelland E., Valentova O., Vergnolle C., Renou J.P.,
RA Taconnat L., Flemr M., Burketova L., Zachowski A.;
RT "Phosphatidylinositol 4-kinase activation is an early response to salicylic
RT acid in Arabidopsis suspension cells.";
RL Plant Physiol. 144:1347-1359(2007).
RN [7]
RP FUNCTION, AND INDUCTION BY SALICYLIC ACID AND PATHOGEN.
RX PubMed=19199050; DOI=10.1007/s11103-009-9458-1;
RA Blanco F., Salinas P., Cecchini N.M., Jordana X., Van Hummelen P.,
RA Alvarez M.E., Holuigue L.;
RT "Early genomic responses to salicylic acid in Arabidopsis.";
RL Plant Mol. Biol. 70:79-102(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY SALICYLIC
RP ACID AND PATHOGEN, AND GLYCOSYLATION AT ASN-129.
RX PubMed=24006883; DOI=10.1094/mpmi-02-13-0044-r;
RA Armijo G., Salinas P., Monteoliva M.I., Seguel A., Garcia C.,
RA Villarroel-Candia E., Song W., van der Krol A.R., Alvarez M.E.,
RA Holuigue L.;
RT "A salicylic acid-induced lectin-like protein plays a positive role in the
RT effector-triggered immunity response of Arabidopsis thaliana to Pseudomonas
RT syringae Avr-Rpm1.";
RL Mol. Plant Microbe Interact. 26:1395-1406(2013).
RN [10]
RP FUNCTION, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24755512; DOI=10.1104/pp.114.239665;
RA Breitenbach H.H., Wenig M., Wittek F., Jorda L., Maldonado-Alconada A.M.,
RA Sarioglu H., Colby T., Knappe C., Bichlmeier M., Pabst E., Mackey D.,
RA Parker J.E., Vlot A.C.;
RT "Contrasting roles of the apoplastic aspartyl protease APOPLASTIC, ENHANCED
RT DISEASE SUSCEPTIBILITY1-DEPENDENT1 and LEGUME LECTIN-LIKE PROTEIN1 in
RT Arabidopsis systemic acquired resistance.";
RL Plant Physiol. 165:791-809(2014).
CC -!- FUNCTION: Plays a positive role in the effector-triggered immunity
CC (ETI) response (PubMed:19199050, PubMed:24006883). Involved in
CC salicylic acid (SA)-mediated processes occurring in ETI response, but
CC is not involved in the autophagy process (PubMed:24006883). Promotes
CC systemic rather than local immunity (PubMed:24755512). Essential for
CC systemic acquired resistance (SAR), but not necessary for immune
CC signaling downstream of SA (PubMed:24755512). May act in parallel with
CC SA (PubMed:24755512). {ECO:0000269|PubMed:19199050,
CC ECO:0000269|PubMed:24006883, ECO:0000269|PubMed:24755512}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:24006883, ECO:0000269|PubMed:24755512}. Cell
CC membrane {ECO:0000269|PubMed:24006883}. Note=Tightly bound to the
CC apoplastic side of the plasma membrane. {ECO:0000269|PubMed:24006883}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings and leaves of adult plants.
CC {ECO:0000269|PubMed:24006883}.
CC -!- INDUCTION: Strongly induced locally by salicylic acid (SA)
CC (PubMed:17496105, PubMed:24755512). Completely dependent on NPR1 for
CC early up-regulation by SA (PubMed:19199050). Up-regulated upon
CC avirulent pathogen infection via an SA-mediated pathway
CC (PubMed:19199050, PubMed:24006883). Up-regulated locally and
CC systematically during systemic acquired resistance (SAR)
CC (PubMed:24755512). The local induction is independent of EDS1 while the
CC systemic transcriptional regulation is EDS1-dependent
CC (PubMed:24755512). {ECO:0000269|PubMed:17496105,
CC ECO:0000269|PubMed:19199050, ECO:0000269|PubMed:24006883,
CC ECO:0000269|PubMed:24755512}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; AL162751; CAB83291.1; -; Genomic_DNA.
DR EMBL; CP002688; AED90590.1; -; Genomic_DNA.
DR EMBL; BT006141; AAP04126.1; -; mRNA.
DR EMBL; AK229686; BAF01527.1; -; mRNA.
DR EMBL; BT015683; AAU15182.1; -; mRNA.
DR PIR; T48356; T48356.
DR RefSeq; NP_195955.1; NM_120414.4.
DR AlphaFoldDB; Q9LZF5; -.
DR SMR; Q9LZF5; -.
DR BioGRID; 17139; 1.
DR STRING; 3702.AT5G03350.1; -.
DR iPTMnet; Q9LZF5; -.
DR PaxDb; Q9LZF5; -.
DR PRIDE; Q9LZF5; -.
DR ProteomicsDB; 238413; -.
DR EnsemblPlants; AT5G03350.1; AT5G03350.1; AT5G03350.
DR GeneID; 831863; -.
DR Gramene; AT5G03350.1; AT5G03350.1; AT5G03350.
DR KEGG; ath:AT5G03350; -.
DR Araport; AT5G03350; -.
DR TAIR; locus:2142679; AT5G03350.
DR eggNOG; ENOG502QRZ3; Eukaryota.
DR HOGENOM; CLU_000288_62_2_1; -.
DR InParanoid; Q9LZF5; -.
DR OMA; NESHFML; -.
DR OrthoDB; 1133055at2759; -.
DR PhylomeDB; Q9LZF5; -.
DR PRO; PR:Q9LZF5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LZF5; baseline and differential.
DR Genevisible; Q9LZF5; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0071446; P:cellular response to salicylic acid stimulus; IEP:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009617; P:response to bacterium; IEP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IDA:TAIR.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW Apoplast; Cell membrane; Glycoprotein; Kinase; Lectin; Membrane;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..274
FT /note="Lectin-like protein"
FT /id="PRO_0000428922"
FT REGION 28..268
FT /note="Legume-lectin like"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24006883"
FT CONFLICT 137
FT /note="K -> I (in Ref. 3; AAP04126 and 4; BAF01527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 30162 MW; F10790BC6F8BDA4C CRC64;
MKIHKLCFLA LLLAHTTSAV NLNLNLKTSE LVFLGDAELG PASDGVSRSG ALSMTRDENP
FSHGQSLWST PVPFKPSSNS SSPYPFETSF TFSISTRIKP APGHGLAFVV VPSIESDGPG
PAGYLGIFNK TNNGNPKNHI FAVEFDVFQD KGFGDINDNH VGININSVTS VVAEKAGYWV
QTGIGKMKHW SFKEFKLSNG ERYKAWIEYR NSKVTVTLAP ETVKKPKKPL IVAHLDLSKV
FLQNMYPGFS GAMGRGVERH DIWSWTFQNS AKRI
