LECA_DIOGR
ID LECA_DIOGR Reviewed; 237 AA.
AC P08902;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lectin alpha chain;
DE Contains:
DE RecName: Full=Lectin beta chain;
DE Contains:
DE RecName: Full=Lectin gamma chain;
OS Dioclea grandiflora (Mucana).
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; Macropsychanthus.
OX NCBI_TaxID=3837;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RX PubMed=6383825; DOI=10.1111/j.1432-1033.1984.tb08436.x;
RA Richardson M., Campos F.D.A.P., Moreira R.A., Ainouz I.L., Begbie R.,
RA Watt W.B., Pusztai A.;
RT "The complete amino acid sequence of the major alpha subunit of the lectin
RT from the seeds of Dioclea grandiflora (Mart).";
RL Eur. J. Biochem. 144:101-111(1984).
RN [2]
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Seed;
RX PubMed=10082964; DOI=10.1016/s0167-4838(99)00020-5;
RA Calvete J.J., Thole H.H., Raida M., Urbanke C., Romero A., Grangeiro T.B.,
RA Ramos M.V., Almeida da Rocha I.M., Guimaraes F.N., Cavada B.S.;
RT "Molecular characterization and crystallization of Diocleinae lectins.";
RL Biochim. Biophys. Acta 1430:367-375(1999).
RN [3]
RP PROTEIN SEQUENCE OF 1-23; 37-107; 110-151; 159-184 AND 201-237.
RC TISSUE=Seed;
RA Ainouz I.L., Moreira R.A., Campos F.D.A.P., Richardson M., Begbie R.,
RA Stewart J.C., Watt W.B., Pusztai A.;
RT "The isolation and amino acid sequence of the beta- and gamma-subunits of
RT the lectin from the seeds of Dioclea grandiflora.";
RL Phytochemistry 26:1435-1440(1987).
RN [4]
RP FUNCTION.
RX PubMed=1398779; DOI=10.3109/08820139209069369;
RA Barral-Netto M., Santos S.B., Barral A., Moreira L.I., Santos C.F.,
RA Moreira R.A., Oliveira J.T., Cavada B.S.;
RT "Human lymphocyte stimulation by legume lectins from the Diocleae tribe.";
RL Immunol. Invest. 21:297-303(1992).
RN [5]
RP FUNCTION, AND CALCIUM-BINDING.
RX PubMed=7524287; DOI=10.1007/bf02001905;
RA Gomes J.C., Ferreira R.R., Cavada B.S., Moreira R.A., Oliveira J.T.;
RT "Histamine release induced by glucose (mannose)-specific lectins isolated
RT from Brazilian beans. Comparison with concanavalin A.";
RL Agents Actions 41:132-135(1994).
RN [6]
RP FUNCTION.
RX PubMed=18472821; DOI=10.1080/09629359791695;
RA Assreuy A.M., Shibuya M.D., Martins G.J., De Souza M.L., Cavada B.S.,
RA Moreira R.A., Oliveira J.T., Ribeiro R.A., Flores C.A.;
RT "Anti-inflammatory effect of glucose-mannose binding lectins isolated from
RT Brazilian beans.";
RL Mediators Inflamm. 6:201-210(1997).
RN [7]
RP FUNCTION.
RX PubMed=9575151; DOI=10.1074/jbc.273.20.12082;
RA Dam T.K., Cavada B.S., Grangeiro T.B., Santos C.F., de Sousa F.A.M.,
RA Oscarson S., Brewer C.F.;
RT "Diocleinae lectins are a group of proteins with conserved binding sites
RT for the core trimannoside of asparagine-linked oligosaccharides and
RT differential specificities for complex carbohydrates.";
RL J. Biol. Chem. 273:12082-12088(1998).
RN [8]
RP MANGANESE-BINDING.
RX PubMed=10694401; DOI=10.1021/bi992102b;
RA Lee H.C., Goroncy A.K., Peisach J., Cavada B.S., Grangeiro T.B.,
RA Ramos M.V., Sampaio A.H., Dam T.K., Brewer C.F.;
RT "Demonstration of a conserved histidine and two water ligands at the Mn2+
RT site in Diocleinae lectins by pulsed EPR spectroscopy.";
RL Biochemistry 39:2340-2346(2000).
RN [9]
RP FUNCTION.
RX PubMed=10747944; DOI=10.1074/jbc.m000670200;
RA Dam T.K., Cavada B.S., Grangeiro T.B., Santos C.F., Ceccatto V.M.,
RA de Sousa F.A., Oscarson S., Brewer C.F.;
RT "Thermodynamic binding studies of lectins from the diocleinae subtribe to
RT deoxy analogs of the core trimannoside of asparagine-linked
RT oligosaccharides.";
RL J. Biol. Chem. 275:16119-16126(2000).
RN [10]
RP FUNCTION, AND TOXIC DOSE.
RX PubMed=19765980; DOI=10.1016/j.biortech.2009.07.062;
RA dos Santos A.F., Cavada B.S., da Rocha B.A., do Nascimento K.S.,
RA Sant'Ana A.E.;
RT "Toxicity of some glucose/mannose-binding lectins to Biomphalaria glabrata
RT and Artemia salina.";
RL Bioresour. Technol. 101:794-798(2010).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CALCIUM AND MANGANESE
RP IONS.
RX PubMed=8812975; DOI=10.1006/jsbi.1996.0065;
RA Kanellopoulos P.N., Tucker P.A., Pavlou K., Agianian B., Hamodrakas S.J.;
RT "A triclinic crystal form of the lectin concanavalin A.";
RL J. Struct. Biol. 117:16-23(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE; CALCIUM
RP AND MANGANESE IONS.
RX PubMed=9830028; DOI=10.1074/jbc.273.49.32818;
RA Rozwarski D.A., Swami B.M., Brewer C.F., Sacchettini J.C.;
RT "Crystal structure of the lectin from Dioclea grandiflora complexed with
RT core trimannoside of asparagine-linked carbohydrates.";
RL J. Biol. Chem. 273:32818-32825(1998).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin. Has anti-inflammatory
CC activity in rats. Induces histamine release in mast cells from rat.
CC Induces lymphocyte proliferation and IFNG production. Shows toxicity
CC against the aquatic snail B.glabrata at concentrations higher than 50
CC ug/ml. {ECO:0000269|PubMed:10747944, ECO:0000269|PubMed:1398779,
CC ECO:0000269|PubMed:18472821, ECO:0000269|PubMed:19765980,
CC ECO:0000269|PubMed:7524287, ECO:0000269|PubMed:9575151}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:8812975,
CC ECO:0000269|PubMed:9830028}.
CC -!- INTERACTION:
CC P08902; P08902: -; NbExp=3; IntAct=EBI-11191228, EBI-11191228;
CC -!- PTM: The beta and gamma chains are produced by partial proteolytic
CC processing of the lectin alpha chain by an asparaginyl endopeptidase.
CC Mixture of 60% alpha lectin and 40% of its beta and gamma proteolytic
CC fragments.
CC -!- MASS SPECTROMETRY: [Lectin alpha chain]: Mass=26602; Mass_error=4;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin beta chain]: Mass=12872; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin gamma chain]: Mass=12752; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- TOXIC DOSE: LD(50) is 2.52 ug/ml against the brine shrimp A.salina.
CC {ECO:0000269|PubMed:19765980}.
CC -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion
CC and one calcium ion. The metal ions are essential for the saccharide-
CC binding and cell-agglutinating activities.
CC -!- MISCELLANEOUS: Is being tested as a molluscicide with potential
CC application in controlling schistosomiasis. The causative agent of
CC schistosomiasis depends on freshwater snails of the genus Biomphalaria
CC as hosts during its larval stages.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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 PIR; JU0176; JU0176.
DR PDB; 1DGL; X-ray; 2.40 A; A/B=1-237.
DR PDB; 1VLN; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-237.
DR PDB; 2GDF; X-ray; 2.40 A; A/B/C/D=1-237.
DR PDB; 2JE9; X-ray; 2.10 A; A/B/C/D=1-237.
DR PDB; 2JEC; X-ray; 2.00 A; A/B/C/D=1-237.
DR PDB; 4Z8B; X-ray; 1.95 A; A=1-237.
DR PDBsum; 1DGL; -.
DR PDBsum; 1VLN; -.
DR PDBsum; 2GDF; -.
DR PDBsum; 2JE9; -.
DR PDBsum; 2JEC; -.
DR PDBsum; 4Z8B; -.
DR AlphaFoldDB; P08902; -.
DR SMR; P08902; -.
DR MINT; P08902; -.
DR UniLectin; P08902; -.
DR EvolutionaryTrace; P08902; -.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
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; 2.
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; Calcium; Direct protein sequencing; Lectin; Manganese;
KW Mannose-binding; Metal-binding; Toxin.
FT CHAIN 1..237
FT /note="Lectin alpha chain"
FT /id="PRO_0000017597"
FT CHAIN 1..118
FT /note="Lectin beta chain"
FT /id="PRO_0000017598"
FT CHAIN 119..237
FT /note="Lectin gamma chain"
FT /id="PRO_0000017599"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8812975,
FT ECO:0000269|PubMed:9830028"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:9830028"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8812975,
FT ECO:0000269|PubMed:9830028"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8812975,
FT ECO:0000269|PubMed:9830028"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:8812975,
FT ECO:0000269|PubMed:9830028"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 34
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 99..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:9830028"
FT CONFLICT 10
FT /note="D -> N (in Ref. 1; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="E -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="H -> N (in Ref. 1; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="K -> Q (in Ref. 1; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="S -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="T -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="T -> W (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="R -> H (in Ref. 1; AA sequence and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4Z8B"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:4Z8B"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:4Z8B"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1DGL"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:1DGL"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1VLN"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2JEC"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:4Z8B"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:4Z8B"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4Z8B"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4Z8B"
SQ SEQUENCE 237 AA; 25567 MW; AF27C8A9B138861D CRC64;
ADTIVAVELD SYPNTDIGDP NYPHIGIDIK SIRSKSTARW NMQTGKVGTV HISYNSVAKR
LSAVVSYSGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY KETNTILSWS FTSKLKTNSI
ADENSLHFSF HKFSQNPKDL ILQGDAFTDS DGNLELTKVS SSGDPQGNSV GRALFYAPVH
IWESSAVVAS FDATFTFLIK SPDREPADGI TFFIANTDTS IPSGSGGRLL GLFPDAN
