LECA_CANBL
ID LECA_CANBL Reviewed; 237 AA.
AC A0A023GPI8; P86474;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 11-JUN-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Lectin alpha chain {ECO:0000303|PubMed:24865454};
DE Short=CboL {ECO:0000303|PubMed:19705102, ECO:0000303|PubMed:24865454};
DE Contains:
DE RecName: Full=Lectin beta chain {ECO:0000303|PubMed:24865454};
DE Contains:
DE RecName: Full=Lectin gamma chain {ECO:0000303|PubMed:24865454};
OS Canavalia boliviana.
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=232300 {ECO:0000312|PDB:4K20};
RN [1] {ECO:0000312|PDB:4K1Y, ECO:0000312|PDB:4K1Z, ECO:0000312|PDB:4K21}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH
RP CARBOHYDRATE; CALCIUM AND MANGANESE, FUNCTION, SUBUNIT, MASS SPECTROMETRY,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000303|PubMed:24865454};
RX PubMed=24865454; DOI=10.1371/journal.pone.0097015;
RA Bezerra G.A., Viertlmayr R., Moura T.R., Delatorre P., Rocha B.A.,
RA do Nascimento K.S., Figueiredo J.G., Bezerra I.G., Teixeira C.S.,
RA Simoes R.C., Nagano C.S., de Alencar N.M., Gruber K., Cavada B.S.;
RT "Structural studies of an anti-inflammatory lectin from Canavalia boliviana
RT seeds in complex with dimannosides.";
RL PLoS ONE 9:E97015-E97015(2014).
RN [2] {ECO:0000305}
RP FUNCTION.
RX PubMed=19705102; DOI=10.1007/s00210-009-0448-2;
RA Figueiredo J.G., da Silveira Bitencourt F., Beserra I.G., Teixeira C.S.,
RA Luz P.B., Bezerra E.H., Mota M.R., Assreuy A.M., de Queiroz Cunha F.,
RA Cavada B.S., de Alencar N.M.;
RT "Antinociceptive activity and toxicology of the lectin from Canavalia
RT boliviana seeds in mice.";
RL Naunyn Schmiedebergs Arch. Pharmacol. 380:407-414(2009).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin (PubMed:24865454). Has
CC anti-inflammatory activity in animal models when applied intravenously
CC (PubMed:24865454). Has antinociceptive activity in mice when applied
CC intravenously (PubMed:19705102). {ECO:0000269|PubMed:19705102,
CC ECO:0000269|PubMed:24865454}.
CC -!- SUBUNIT: Homodimer and homotetramer. Oligomerization is pH-dependent
CC with homotetramers forming at pH 4 and above.
CC {ECO:0000269|PubMed:24865454}.
CC -!- MASS SPECTROMETRY: [Lectin alpha chain]: Mass=25572; Mass_error=2;
CC Method=Electrospray; Note=Alpha chain.;
CC Evidence={ECO:0000269|PubMed:24865454};
CC -!- MASS SPECTROMETRY: [Lectin beta chain]: Mass=12878; Mass_error=1;
CC Method=Electrospray; Note=Beta chain.;
CC Evidence={ECO:0000269|PubMed:24865454};
CC -!- MASS SPECTROMETRY: [Lectin gamma chain]: Mass=12710; Mass_error=1;
CC Method=Electrospray; Note=Gamma chain.;
CC Evidence={ECO:0000269|PubMed:24865454};
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 {ECO:0000269|PubMed:24865454}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 4K1Y; X-ray; 2.50 A; A/B/C/D=1-237.
DR PDB; 4K1Z; X-ray; 2.30 A; A/B/C/D=1-237.
DR PDB; 4K20; X-ray; 3.40 A; A/B=1-237.
DR PDB; 4K21; X-ray; 1.60 A; A=1-237.
DR PDBsum; 4K1Y; -.
DR PDBsum; 4K1Z; -.
DR PDBsum; 4K20; -.
DR PDBsum; 4K21; -.
DR AlphaFoldDB; A0A023GPI8; -.
DR SMR; A0A023GPI8; -.
DR UniLectin; A0A023GPI8; -.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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.
FT CHAIN 1..237
FT /note="Lectin alpha chain"
FT /evidence="ECO:0000269|PubMed:24865454"
FT /id="PRO_0000436146"
FT CHAIN 1..118
FT /note="Lectin beta chain"
FT /evidence="ECO:0000269|PubMed:24865454"
FT /id="PRO_0000436147"
FT CHAIN 119..237
FT /note="Lectin gamma chain"
FT /evidence="ECO:0000269|PubMed:24865454"
FT /id="PRO_0000436148"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 14
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 99..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:24865454"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P86624"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4K21"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:4K21"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4K21"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 105..119
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4K21"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4K1Y"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4K1Y"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:4K21"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4K1Z"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:4K21"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4K21"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4K21"
SQ SEQUENCE 237 AA; 25571 MW; C1549BDE376537A5 CRC64;
ADTIVAVELD TYPNTDIGDP SYPHIGIDIK SVRSKKTAKW NMQNGKVGTA HIIYNSVGKR
LSAVVSYPNG DSATVSYDVD LDNVLPEWVR VGLSATTGLY KETNTILSWS FTSKLKSNST
HETNALHFMF NQFSKDQKDL ILQGDATTGR DGNLELTRVS SNGSPQGSSV GRALFYAPVH
IWESSAVVAS FDATFTFLIK SSDSHPADGI AFFISNIDSS IPSGSTGRLL GLFPDAN
