ID LECA2_LABPU Reviewed; 281 AA. AC B3EWQ9; DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2012, sequence version 1. DT 22-FEB-2023, entry version 26. DE RecName: Full=Lectin alpha chain {ECO:0000303|PubMed:18787949}; DE AltName: Full=DLL-II {ECO:0000303|PubMed:18787949}; DE Contains: DE RecName: Full=Lectin beta chain {ECO:0000303|PubMed:18787949}; OS Lablab purpureus (Hyacinth bean) (Dolichos lablab). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Lablab. OX NCBI_TaxID=35936; RN [1] {ECO:0000305} RP PROTEIN SEQUENCE, SUBUNIT, AND MASS SPECTROMETRY. RC TISSUE=Seed {ECO:0000269|PubMed:18787949}; RX PubMed=18787949; DOI=10.1007/s10719-008-9173-1; RA Rameshwaram N.R., Karanam N.K., Scharf C., Volker U., Nadimpalli S.K.; RT "Complete primary structure of a newly characterized galactose-specific RT lectin from the seeds of Dolichos lablab."; RL Glycoconj. J. 26:161-172(2009). RN [2] {ECO:0000305} RP PROTEIN SEQUENCE OF 1-10, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP AND GLYCOSYLATION. RC TISSUE=Seed {ECO:0000269|PubMed:16125971}; RX PubMed=16125971; DOI=10.1016/j.pep.2005.06.010; RA Latha V.L., Rao R.N., Nadimpalli S.K.; RT "Affinity purification, physicochemical and immunological characterization RT of a galactose-specific lectin from the seeds of Dolichos lablab (Indian RT lablab beans)."; RL Protein Expr. Purif. 45:296-306(2006). RN [3] {ECO:0000305} RP CRYSTALLIZATION, PRELIMINARY X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND RP SUBUNIT. RC TISSUE=Seed {ECO:0000269|PubMed:16511291}; RX PubMed=16511291; DOI=10.1107/s1744309106001448; RA Latha V.L., Kulkarni K.A., Rao R.N., Kumar N.S., Suguna K.; RT "Crystallization and preliminary X-ray crystallographic analysis of a RT galactose-specific lectin from Dolichos lablab."; RL Acta Crystallogr. F 62:163-165(2006). CC -!- FUNCTION: D-galactose-binding lectin. {ECO:0000269|PubMed:16125971}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.4. No activity between pH 4.0 and pH 6.0, 80% CC activity at pH 8.0 and 20% activity at pH 9.0. CC {ECO:0000269|PubMed:16125971}; CC Temperature dependence: CC Activity stable between 4 and 40 degrees Celsius, declines at higher CC temperatures and is lost at 90 degrees Celsius. CC {ECO:0000269|PubMed:16125971}; CC -!- SUBUNIT: Tetramer of 2 alpha and 2 beta chains. CC {ECO:0000269|PubMed:16125971, ECO:0000269|PubMed:16511291, CC ECO:0000269|PubMed:18787949}. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16125971}. CC -!- PTM: The beta chain is produced by partial proteolytic processing of CC the alpha chain. {ECO:0000303|PubMed:18787949}. CC -!- MASS SPECTROMETRY: [Lectin alpha chain]: Mass=30746; CC Method=Electrospray; Note=Alpha chain.; CC Evidence={ECO:0000269|PubMed:18787949}; CC -!- MASS SPECTROMETRY: [Lectin beta chain]: Mass=28815; CC Method=Electrospray; Note=Beta chain.; CC Evidence={ECO:0000269|PubMed:18787949}; CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR PDB; 3UJO; X-ray; 2.00 A; A/B/C/D=1-281. DR PDB; 3UJQ; X-ray; 2.06 A; A/B/C/D=1-281. DR PDB; 3UK9; X-ray; 3.11 A; A/B/C/D/E/F/G/H=1-281. DR PDB; 3UL2; X-ray; 2.50 A; A/B/C/D=1-281. DR PDBsum; 3UJO; -. DR PDBsum; 3UJQ; -. DR PDBsum; 3UK9; -. DR PDBsum; 3UL2; -. DR AlphaFoldDB; B3EWQ9; -. DR SMR; B3EWQ9; -. DR UniLectin; B3EWQ9; -. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW. DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW. DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW. DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1. DR Gene3D; 2.60.120.200; -; 1. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR016363; L-lectin. DR InterPro; IPR000985; Lectin_LegA_CS. DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS. DR InterPro; IPR001220; Legume_lectin_dom. DR PANTHER; PTHR32401; CONCANAVALIN A-LIKE LECTIN FAMILY PROTEIN; 1. DR PANTHER; PTHR32401:SF45; LECTIN; 1. DR Pfam; PF00139; Lectin_legB; 1. DR PIRSF; PIRSF002690; L-type_lectin_plant; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1. DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1. PE 1: Evidence at protein level; KW 3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing; KW Fungicide; Glycoprotein; Lectin. FT CHAIN 1..281 FT /note="Lectin alpha chain" FT /id="PRO_0000420130" FT CHAIN 1..263 FT /note="Lectin beta chain" FT /evidence="ECO:0000269|PubMed:18787949" FT /id="PRO_0000420131" FT SITE 263..264 FT /note="Cleavage" FT /evidence="ECO:0000269|PubMed:18787949" FT CARBOHYD 35 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 82 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 140 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT STRAND 25..33 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 68..75 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 82..84 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 87..97 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 108..116 FT /evidence="ECO:0007829|PDB:3UJO" FT HELIX 125..127 FT /evidence="ECO:0007829|PDB:3UJO" FT TURN 128..130 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 143..147 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 154..156 FT /evidence="ECO:0007829|PDB:3UJQ" FT STRAND 158..169 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 174..176 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 185..191 FT /evidence="ECO:0007829|PDB:3UJO" FT TURN 193..195 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 197..203 FT /evidence="ECO:0007829|PDB:3UJO" FT TURN 205..207 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 211..216 FT /evidence="ECO:0007829|PDB:3UJO" FT TURN 220..222 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 225..235 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 237..241 FT /evidence="ECO:0007829|PDB:3UJQ" FT STRAND 246..256 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:3UJO" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:3UJO" FT TURN 273..275 FT /evidence="ECO:0007829|PDB:3UJO" SQ SEQUENCE 281 AA; 30422 MW; CC15AD7445BD170A CRC64; NNLISFTMKR IVLFLILLTK AASANLISFT FKRFNETNLI LQRDATVSSG KLRITKAAEN GVPTAGSLGR AFYSTPIQIW DNTTGTVAAW ATSFTFNLQA PNAASPADGL AFALVPVGSQ PKDKGGFLGL FDSKNYASSN QTVAVEFDTF YNGGWDPTER HIGIDVNSIK SIKTTSWDFA NGENAEVLIT YDSSTNLLVA SLVHPSQKTS FIVSERVDLT SVLPEWVSVG FSATTGLSKG YVETNEVLSW SFASKISINK EDEENKLLIS NLEGKAINNL A //