LECA_CRAAG
ID LECA_CRAAG Reviewed; 236 AA.
AC P81517; P81636;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Lectin alpha chain;
DE Contains:
DE RecName: Full=Lectin beta chain;
DE Contains:
DE RecName: Full=Lectin gamma chain;
OS Cratylia argentea (Cratylia floribunda).
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; Cratylia.
OX NCBI_TaxID=83131;
RN [1]
RP PROTEIN SEQUENCE, SUBUNIT, MASS SPECTROMETRY, CRYSTALLIZATION, AND
RP PRELIMINARY X-RAY CRYSTALLOGRAPHY (3.5 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 [2]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RA Cavada B.S., Nogueira N.A.P., Farias C.M.A.S., Grangeiro T.B., Romas M.V.,
RA Thole H.H., Raida M., Rouge P., Calvete J.J.;
RT "Primary structure and kinetic interaction with glycoproteins of the lectin
RT from seeds of Cratylia floribunda.";
RL Protein Pept. Lett. 6:27-34(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 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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP 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 rat.
CC Induces lymphocyte proliferation and IFNG production.
CC {ECO:0000269|PubMed:10747944, ECO:0000269|PubMed:1398779,
CC ECO:0000269|PubMed:18472821, ECO:0000269|PubMed:7524287,
CC ECO:0000269|PubMed:9575151}.
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}.
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=25397; Mass_error=3;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin beta chain]: Mass=12847; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin gamma chain]: Mass=12568; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- TOXIC DOSE: LD(50) is 4.75 ug/ml against the brine shrimp A.salina.
CC {ECO:0000269|PubMed:19765980}.
CC -!- TOXIC DOSE: LD(50) is 25.5 ug/ml against the aquatic snail B.glabrata.
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; 2D3P; X-ray; 2.80 A; A/B/C/D=1-236.
DR PDB; 2D3R; X-ray; 2.90 A; A/B/C/D=1-236.
DR PDBsum; 2D3P; -.
DR PDBsum; 2D3R; -.
DR AlphaFoldDB; P81517; -.
DR SMR; P81517; -.
DR UniLectin; P81517; -.
DR EvolutionaryTrace; P81517; -.
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 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; 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; Calcium; Direct protein sequencing; Lectin; Manganese;
KW Mannose-binding; Metal-binding; Toxin.
FT CHAIN 1..236
FT /note="Lectin alpha chain"
FT /id="PRO_0000017588"
FT CHAIN 1..118
FT /note="Lectin beta chain"
FT /id="PRO_0000017589"
FT CHAIN 119..236
FT /note="Lectin gamma chain"
FT /id="PRO_0000017590"
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 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 /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2D3P"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:2D3P"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:2D3P"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:2D3P"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 118..121
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 186..197
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:2D3P"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:2D3P"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:2D3P"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:2D3P"
SQ SEQUENCE 236 AA; 25398 MW; CA73BC77F4324251 CRC64;
ADTIVAVELD TYPNTDIGDP NYQHIGINIK SIRSKATTRW NVQDGKVGTA HISYNSVAKR
LSAIVSYPGG SSATVSYDVD LNNILPEWVR VGLSASTGLY KETNTILSWS FTSKLKTNST
ADAQSLHFTF NQFSQNPKDL ILQGDASTDS DGNLQLTRVS NGSPQSNSVG RALYYAPVHV
WDKSAVVASF DATFTFLIKS TDSDIADGIA WFIANTDSSI PHGSGGRLLG LFPDAN
