LECT5_ARATH
ID LECT5_ARATH Reviewed; 276 AA.
AC Q9LK72;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Lectin-like protein At3g16530;
DE Flags: Precursor;
GN OrderedLocusNames=At3g16530; ORFNames=MDC8.16;
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=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(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 INDUCTION BY CHITIN.
RX PubMed=12236603; DOI=10.1094/mpmi.2002.15.9.963;
RA Zhang B., Ramonell K., Somerville S., Stacey G.;
RT "Characterization of early, chitin-induced gene expression in
RT Arabidopsis.";
RL Mol. Plant Microbe Interact. 15:963-970(2002).
RN [5]
RP SUBCELLULAR LOCATION, INDUCTION BY OLIGOGALACTURONIDES, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=18324730; DOI=10.1002/pmic.200700523;
RA Casasoli M., Spadoni S., Lilley K.S., Cervone F., De Lorenzo G., Mattei B.;
RT "Identification by 2-D DIGE of apoplastic proteins regulated by
RT oligogalacturonides in Arabidopsis thaliana.";
RL Proteomics 8:1042-1054(2008).
RN [6]
RP INDUCTION BY CHITIN.
RC STRAIN=cv. Columbia;
RX PubMed=15923325; DOI=10.1104/pp.105.060947;
RA Ramonell K., Berrocal-Lobo M., Koh S., Wan J., Edwards H., Stacey G.,
RA Somerville S.;
RT "Loss-of-function mutations in chitin responsive genes show increased
RT susceptibility to the powdery mildew pathogen Erysiphe cichoracearum.";
RL Plant Physiol. 138:1027-1036(2005).
RN [7]
RP INDUCTION BY HYALOPERONOSPORA ARABIDOPSIDIS.
RX PubMed=21711359; DOI=10.1111/j.1365-3040.2011.02390.x;
RA Hok S., Danchin E.G., Allasia V., Panabieres F., Attard A., Keller H.;
RT "An Arabidopsis (malectin-like) leucine-rich repeat receptor-like kinase
RT contributes to downy mildew disease.";
RL Plant Cell Environ. 34:1944-1957(2011).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000269|PubMed:18324730}.
CC -!- INDUCTION: By oligogalacturonides and chitin (e.g. chito-octamer and
CC crab-shell chitin CSC). Accumulates upon Hyaloperonospora arabidopsidis
CC infection, during both early and late stages of infection.
CC {ECO:0000269|PubMed:12236603, ECO:0000269|PubMed:15923325,
CC ECO:0000269|PubMed:18324730, ECO:0000269|PubMed:21711359}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; AP000373; BAB01152.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE75832.1; -; Genomic_DNA.
DR EMBL; AF428361; AAL16291.1; -; mRNA.
DR EMBL; AY054194; AAL06855.1; -; mRNA.
DR EMBL; AY066032; AAL47399.1; -; mRNA.
DR RefSeq; NP_188274.1; NM_112525.3.
DR AlphaFoldDB; Q9LK72; -.
DR SMR; Q9LK72; -.
DR BioGRID; 6235; 2.
DR IntAct; Q9LK72; 1.
DR STRING; 3702.AT3G16530.1; -.
DR PaxDb; Q9LK72; -.
DR PRIDE; Q9LK72; -.
DR ProteomicsDB; 238454; -.
DR EnsemblPlants; AT3G16530.1; AT3G16530.1; AT3G16530.
DR GeneID; 820901; -.
DR Gramene; AT3G16530.1; AT3G16530.1; AT3G16530.
DR KEGG; ath:AT3G16530; -.
DR Araport; AT3G16530; -.
DR TAIR; locus:2088349; AT3G16530.
DR eggNOG; ENOG502QRZ3; Eukaryota.
DR HOGENOM; CLU_000288_62_2_1; -.
DR InParanoid; Q9LK72; -.
DR OMA; ERFKAWV; -.
DR OrthoDB; 972171at2759; -.
DR PhylomeDB; Q9LK72; -.
DR PRO; PR:Q9LK72; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK72; baseline and differential.
DR Genevisible; Q9LK72; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0010200; P:response to chitin; IEP:TAIR.
DR GO; GO:0002239; P:response to oomycetes; IEP:UniProtKB.
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; Glycoprotein; Lectin; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..276
FT /note="Lectin-like protein At3g16530"
FT /id="PRO_0000428921"
FT REGION 20..270
FT /note="Legume-lectin like"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 276 AA; 30509 MW; BAA4906B68FE6969 CRC64;
MQIHKLCFLV LFLANAAFAV KFNFDSFDGS NLLFLGDAEL GPSSDGVSRS GALSMTRDEN
PFSHGQGLYI NQIPFKPSNT SSPFSFETSF TFSITPRTKP NSGQGFAFII TPEADNSGAS
DGGYLGILNK TNDGKPENHI LAIEFDTFQN KEFLDISGNH VGVNINSMTS LVAEKAGYWV
QTRVGKRKVW SFKDVNLSSG ERFKAWVEFR NKDSTITVTL APENVKKPKR ALIEAPRVLN
EVLLQNMYAG FAGSMGRAVE RHDIWSWSFE NAAKNN
