LECA_DIORO
ID LECA_DIORO Reviewed; 237 AA.
AC P58908; P85306;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 91.
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 rostrata.
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=192416;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MASS
RP SPECTROMETRY, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RC TISSUE=Seed;
RX PubMed=18682294; DOI=10.1016/j.jsb.2008.05.012;
RA de Oliveira T.M., Delatorre P., da Rocha B.A.M., de Souza E.P.,
RA Nascimento K.S., Bezerra G.A., Moura T.R., Benevides R.G., Bezerra E.H.S.,
RA Moreno F.B.M.B., Freire V.N., de Azevedo W.F. Jr., Cavada B.S.;
RT "Crystal structure of Dioclea rostrata lectin: insights into understanding
RT the pH-dependent dimer-tetramer equilibrium and the structural basis for
RT carbohydrate recognition in Diocleinae lectins.";
RL J. Struct. Biol. 164:177-182(2008).
RN [2]
RP PROTEIN SEQUENCE OF 1-25 AND 119-142, SUBUNIT, AND MASS SPECTROMETRY.
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 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, 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 [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).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin. Induces histamine release
CC in mast cells from hamster and rat. Induces lymphocyte proliferation
CC and IFNG production. {ECO:0000269|PubMed:10747944,
CC ECO:0000269|PubMed:1398779, ECO:0000269|PubMed:18682294,
CC ECO:0000269|PubMed:7524287, ECO:0000269|PubMed:8891754,
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, ECO:0000269|PubMed:18682294}.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain
CC {ECO:0000269|PubMed:18682294}. Vacuole {ECO:0000269|PubMed:18682294}.
CC Note=Cotyledonary membrane-bound vacuolar protein bodies.
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=25490; Mass_error=1;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:18682294};
CC -!- MASS SPECTROMETRY: [Lectin alpha chain]: Mass=25550; Mass_error=3;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin beta chain]: Mass=12844; Mass_error=1;
CC Method=Electrospray; Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin gamma-1 chain]: Mass=12723; Mass_error=4;
CC Method=Electrospray; Note=Gamma chain isolectin.;
CC Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin gamma-2 chain]: Mass=12650; Mass_error=2;
CC Method=Electrospray; Note=Gamma chain isolectin.;
CC Evidence={ECO:0000269|PubMed:10082964};
CC -!- MASS SPECTROMETRY: [Lectin gamma-2 chain]: Mass=12537; Mass_error=1;
CC Method=Electrospray; Note=Gamma chain isolectin.;
CC Evidence={ECO:0000269|PubMed:10082964};
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:0000305}.
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DR PDB; 2ZBJ; X-ray; 2.05 A; A=1-237.
DR PDBsum; 2ZBJ; -.
DR AlphaFoldDB; P58908; -.
DR SMR; P58908; -.
DR UniLectin; P58908; -.
DR EvolutionaryTrace; P58908; -.
DR GO; GO:0033095; C:aleurone grain; IDA:UniProtKB.
DR GO; GO:0000325; C:plant-type vacuole; IDA:UniProtKB.
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:1903595; P:positive regulation of histamine secretion by mast cell; IDA:UniProtKB.
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; Vacuole.
FT CHAIN 1..237
FT /note="Lectin alpha chain"
FT /id="PRO_0000017604"
FT CHAIN 1..118
FT /note="Lectin beta chain"
FT /id="PRO_0000017605"
FT CHAIN 119..237
FT /note="Lectin gamma-1 chain"
FT /id="PRO_0000017606"
FT CHAIN 125..237
FT /note="Lectin gamma-2 chain"
FT /id="PRO_0000017607"
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:0000250"
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 /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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:2ZBJ"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 187..198
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2ZBJ"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:2ZBJ"
SQ SEQUENCE 237 AA; 25491 MW; B2C322C01892153D CRC64;
ADTIVAVELD SYPNTDIGDP NYPHIGIDIK SIRSKSTARW NMQTGKVGTV HISYNSVAKR
LSAVVSYTGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY KETNTILSWS FTSKLKTNSI
ADANSLHFTF NQFSQNPKDL ILQGDATTDS DGNLELTKVS SSGDPQGNSV GRALFYAPVH
IWEKSAVVAS FDATFTFLIK SPDRDPADGI TFFIANPDTS IPSGSGGRLL GLFPDAN
