LECA2_LABPU
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 25-MAY-2022, entry version 24.
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}.
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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 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 Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 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
