LECA_DIOWI
ID LECA_DIOWI Reviewed; 237 AA.
AC P86624;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Lectin alpha chain {ECO:0000303|PubMed:21694673};
DE AltName: Full=DwL {ECO:0000303|PubMed:21694673};
DE Contains:
DE RecName: Full=Lectin beta chain {ECO:0000303|PubMed:21694673};
DE Contains:
DE RecName: Full=Lectin gamma chain {ECO:0000303|PubMed:21694673};
OS Dioclea wilsonii (Wilson's clusterpea).
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=763456;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS
RP SPECTROMETRY, MANGANESE-BINDING, AND CALCIUM-BINDING.
RC TISSUE=Seed {ECO:0000269|PubMed:21694673};
RX PubMed=21694673; DOI=10.3390/molecules16065087;
RA Rangel T.B., Assreuy A.M., Pires Ade F., Carvalho A.U., Benevides R.G.,
RA Simoes Rda C., Silva H.C., Bezerra M.J., Nascimento A.S., Nascimento K.S.,
RA Nagano C.S., Sampaio A.H., Delatorre P., Rocha B.A., Fernandes P.M.,
RA Cavada B.S.;
RT "Crystallization and characterization of an inflammatory lectin purified
RT from the seeds of Dioclea wilsonii.";
RL Molecules 16:5087-5103(2011).
RN [2] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), IN COMPLEX WITH CARBOHYDRATE;
RP CALCIUM AND MANGANESE IONS, FUNCTION, AND SUBUNIT.
RC TISSUE=Seed {ECO:0000269|PubMed:21924319};
RX PubMed=21924319; DOI=10.1016/j.biochi.2011.09.001;
RA Rangel T.B., Rocha B.A., Bezerra G.A., Assreuy A.M., Pires Ade F.,
RA do Nascimento A.S., Bezerra M.J., do Nascimento K.S., Nagano C.S.,
RA Sampaio A.H., Gruber K., Delatorre P., Fernandes P.M., Cavada B.S.;
RT "Crystal structure of a pro-inflammatory lectin from the seeds of Dioclea
RT wilsonii Standl.";
RL Biochimie 94:525-532(2012).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin with hemagglutinating
CC activity towards rabbit and human erythrocytes. In rats, elicits an
CC acute inflammatory response by inducing neutrophil migration and
CC induces dose-dependent paw edema. {ECO:0000269|PubMed:21694673,
CC ECO:0000269|PubMed:21924319}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Hemagglutinating activity stable up to 60 degrees Celsius but
CC diminishes with higher temperatures and is absent at 100 degrees
CC Celsius. {ECO:0000269|PubMed:21694673};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21694673,
CC ECO:0000269|PubMed:21924319}.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain
CC {ECO:0000250|UniProtKB:P58907}.
CC -!- PTM: The beta and gamma chains are produced by partial proteolytic
CC processing of the lectin alpha chain by an asparaginyl endopeptidase.
CC {ECO:0000250|UniProtKB:P08902}.
CC -!- MASS SPECTROMETRY: [Lectin alpha chain]: Mass=25636; Mass_error=2;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:21694673};
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 -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000255}.
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DR PDB; 3SH3; X-ray; 2.30 A; A=1-237.
DR PDBsum; 3SH3; -.
DR AlphaFoldDB; P86624; -.
DR SMR; P86624; -.
DR UniLectin; P86624; -.
DR EvolutionaryTrace; P86624; -.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005536; F:glucose binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0005537; F:mannose binding; IDA:UniProtKB.
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; Hemagglutinin; Lectin;
KW Manganese; Mannose-binding; Metal-binding; Vacuole.
FT CHAIN 1..237
FT /note="Lectin alpha chain"
FT /id="PRO_0000395393"
FT CHAIN 1..118
FT /note="Lectin beta chain"
FT /evidence="ECO:0000269|PubMed:21694673"
FT /id="PRO_0000395394"
FT CHAIN 119..237
FT /note="Lectin gamma chain"
FT /evidence="ECO:0000269|PubMed:21694673"
FT /id="PRO_0000395395"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 99..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:21924319"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:21924319"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:3SH3"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:3SH3"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:3SH3"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:3SH3"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:3SH3"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:3SH3"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3SH3"
SQ SEQUENCE 237 AA; 25635 MW; 68D5F8A9AB19F46A CRC64;
ADTIVAVELD SYPNTDIGDP NYPHIGIDIK SIRSKSTARW NMQTGKVGTV HISYNSVAKR
LSAVVSYSGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY KETNTILSWS FTSKLKTNSI
ADENSLHFSF HKFSQNPKDL ILQGDAFTDS DGNLELTKVS NSGDPQGNSV GRALFYAPVH
IWEKSAVVAS FDATFTFLIK SPDREPADGI TFFIANTDTS IPSGSGGRLL GLFPDAN
