LECA_DIOVI
ID LECA_DIOVI Reviewed; 237 AA.
AC P58907;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Lectin alpha chain;
DE Contains:
DE RecName: Full=Lectin beta chain;
DE Contains:
DE RecName: Full=Lectin gamma-1 chain;
DE Contains:
DE RecName: Full=Lectin gamma-2 chain;
OS Dioclea virgata.
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; Dioclea.
OX NCBI_TaxID=167618;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC TISSUE=Seed;
RA Simoes R.C., Delatorre P., Marinho E.S., Pereira-Junior F.N., Silva H.C.,
RA Gadelha C.A.A., Santi-Gadelha T., Rocha B.A.M., Sampaio A.H.,
RA Nascimento K.S., Cavada B.S., Nagano C.S.;
RL Submitted (JUL-2010) to UniProtKB.
RN [2]
RP PROTEIN SEQUENCE OF 1-25 AND 119-143, SUBUNIT, MASS SPECTROMETRY,
RP CRYSTALLIZATION, AND PRELIMINARY X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
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 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 [4]
RP FUNCTION, AND MANGANESE-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 [5]
RP FUNCTION, AND MANGANESE-BINDING.
RX PubMed=8891754; DOI=10.1007/bf02252314;
RA Ferreira R.R., Cavada B.S., Moreira R.A., Oliveira J.T., Gomes J.C.;
RT "Characteristics of the histamine release from hamster cheek pouch mast
RT cells stimulated by lectins from Brazilian beans and concanavalin A.";
RL Inflamm. Res. 45:442-447(1996).
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).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin. Has anti-inflammatory
CC activity in rats. Induces histamine release in mast cells from hamster
CC and rat. Induces lymphocyte proliferation and IFNG production. Shows
CC toxicity against the aquatic snail B.glabrata at concentrations higher
CC than 20 ug/ml. {ECO:0000269|PubMed:10747944,
CC ECO:0000269|PubMed:1398779, ECO:0000269|PubMed:18472821,
CC ECO:0000269|PubMed:19765980, ECO:0000269|PubMed:7524287,
CC ECO:0000269|PubMed:8891754, ECO:0000269|PubMed:9575151,
CC ECO:0000269|Ref.1}.
CC -!- SUBUNIT: Equilibrium between homodimer and homotetramer.
CC Oligomerization is pH-dependent with homotetramers forming at pH 6.5
CC and above. {ECO:0000269|PubMed:10082964, ECO:0000269|Ref.1}.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain.
CC -!- TISSUE SPECIFICITY: Seed.
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=25412; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|Ref.1};
CC -!- MASS SPECTROMETRY: [Lectin alpha chain]: Mass=25402; Mass_error=6;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin beta chain]: Mass=12810; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin gamma-1 chain]: Mass=12607; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin gamma-2 chain]: Mass=12036; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- TOXIC DOSE: LD(50) is 2.77 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}.
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DR PDB; 3RRD; X-ray; 2.46 A; A=1-237.
DR PDB; 3RS6; X-ray; 1.80 A; A=1-237.
DR PDB; 5UUY; X-ray; 1.88 A; A=1-237.
DR PDBsum; 3RRD; -.
DR PDBsum; 3RS6; -.
DR PDBsum; 5UUY; -.
DR AlphaFoldDB; P58907; -.
DR SMR; P58907; -.
DR UniLectin; P58907; -.
DR PRIDE; P58907; -.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
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 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; Vacuole.
FT CHAIN 1..237
FT /note="Lectin alpha chain"
FT /id="PRO_0000017593"
FT CHAIN 1..118
FT /note="Lectin beta chain"
FT /id="PRO_0000017594"
FT CHAIN 119..237
FT /note="Lectin gamma-1 chain"
FT /id="PRO_0000017595"
FT CHAIN 125..237
FT /note="Lectin gamma-2 chain"
FT /id="PRO_0000017596"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 24
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 /evidence="ECO:0000250"
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:0000250"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3RS6"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:3RS6"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:3RS6"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:3RS6"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:3RS6"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:3RS6"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3RS6"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3RS6"
SQ SEQUENCE 237 AA; 25412 MW; 5B0EFA307FD1EAA3 CRC64;
ADTIVAVELD SYPNTDIGDP SYPHIGIDIK SVRSKSTARW NMQTGKVGTA HISYNSVAKR
LSAVVSYTGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY KETNTILSWS FTSKLKTNSI
ADANSLHFSF NQFSQNPKDL ILQGDATTDS DGNLQLTRVS SDGSPQGSSV GRALFYAPVH
IWEKSAVVAS FDATFTFLIK SPDRDPADGI TFFIANTDTS IPSGSGGRLL GLFPDAN
