CONA_CANBR
ID CONA_CANBR Reviewed; 237 AA.
AC P55915;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Concanavalin-Br;
DE Short=Con Br;
OS Canavalia brasiliensis (Brazilian jack bean).
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; Canavalia.
OX NCBI_TaxID=61861;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Seed;
RA Grangeiro T.B.;
RL Thesis (1996), Universidade Federale do Ceara, Brazil.
RN [2]
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 [3]
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 [4]
RP FUNCTION, AND CALCIUM-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 [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 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 [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9094437; DOI=10.1016/s0014-5793(97)00137-3;
RA Sanz-Aparicio J., Hermoso J., Grangeiro T.B., Calvete J.J., Cavada B.S.;
RT "The crystal structure of Canavalia brasiliensis lectin suggests a
RT correlation between its quaternary conformation and its distinct biological
RT properties from Concanavalin A.";
RL FEBS Lett. 405:114-118(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE.
RX PubMed=10506175; DOI=10.1074/jbc.274.41.29188;
RA Bouckaert J., Hamelryck T.W., Wyns L., Loris R.;
RT "The crystal structures of Man(alpha1-3)Man(alpha1-O)Me and Man(alpha1-
RT 6)Man(alpha1-O)Me in complex with concanavalin A.";
RL J. Biol. Chem. 274:29188-29195(1999).
CC -!- FUNCTION: Glucose/D-mannose specific 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 -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10506175}.
CC -!- TOXIC DOSE: LD(50) is 15.4 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; 1AZD; X-ray; 3.00 A; A/B/C/D=1-237.
DR PDB; 1QDC; X-ray; 2.00 A; A/B/C/D=1-237.
DR PDB; 1QDO; X-ray; 2.80 A; A/B/C/D=1-237.
DR PDB; 2CYF; X-ray; 1.80 A; A/C=1-237.
DR PDB; 3JU9; X-ray; 2.10 A; A=1-237.
DR PDB; 4H55; X-ray; 2.07 A; A=1-237.
DR PDB; 4P14; X-ray; 2.00 A; A=1-237.
DR PDB; 4PCR; X-ray; 2.15 A; A/D=1-237.
DR PDB; 5YGM; X-ray; 1.60 A; A=1-237.
DR PDB; 6VB8; X-ray; 2.20 A; A=1-237.
DR PDBsum; 1AZD; -.
DR PDBsum; 1QDC; -.
DR PDBsum; 1QDO; -.
DR PDBsum; 2CYF; -.
DR PDBsum; 3JU9; -.
DR PDBsum; 4H55; -.
DR PDBsum; 4P14; -.
DR PDBsum; 4PCR; -.
DR PDBsum; 5YGM; -.
DR PDBsum; 6VB8; -.
DR AlphaFoldDB; P55915; -.
DR SMR; P55915; -.
DR UniLectin; P55915; -.
DR PRIDE; P55915; -.
DR EvolutionaryTrace; P55915; -.
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="Concanavalin-Br"
FT /id="PRO_0000105085"
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 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:10506175"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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:10506175"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:5YGM"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:5YGM"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1QDO"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5YGM"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 105..121
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:5YGM"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:5YGM"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4H55"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:5YGM"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:5YGM"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:5YGM"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:5YGM"
SQ SEQUENCE 237 AA; 25568 MW; 4D62F2113A36C38F CRC64;
ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA HIIYNSVGKR
LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSASTGLY KETNTILSWS FTSKLKSNST
HETNALHFMF NQFSKDQKDL ILQGDATTGT EGNLRLTRVS SNGSPQGSSV GRALFYAPVH
IWESSAVVAS FEATFTFLIK SPDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN