LECA_DIOSC
ID LECA_DIOSC Reviewed; 237 AA.
AC B3EWJ2;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Lectin alpha chain {ECO:0000303|PubMed:22037666};
DE AltName: Full=DSL {ECO:0000303|PubMed:22037666};
DE Contains:
DE RecName: Full=Lectin beta chain {ECO:0000303|PubMed:22037666};
DE Contains:
DE RecName: Full=Lectin gamma chain {ECO:0000303|PubMed:22037666};
OS Dioclea sclerocarpa (Dioclea reflexa var. glabrescens).
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=1176036;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PTM, AND MASS
RP SPECTROMETRY.
RC TISSUE=Seed {ECO:0000269|PubMed:22037666};
RX PubMed=22037666; DOI=10.3390/molecules16119077;
RA Correia J.L., do Nascimento A.S., Cajazeiras J.B., Gondim A.C.,
RA Pereira R.I., de Sousa B.L., da Silva A.L., Garcia W., Teixeira E.H.,
RA do Nascimento K.S., da Rocha B.A., Nagano C.S., Sampaio A.H., Cavada B.S.;
RT "Molecular characterization and tandem mass spectrometry of the lectin
RT extracted from the seeds of Dioclea sclerocarpa Ducke.";
RL Molecules 16:9077-9089(2011).
CC -!- FUNCTION: D-mannose/D-glucose-binding lectin. Has hemagglutinating
CC activity towards rabbit erythrocytes. {ECO:0000269|PubMed:22037666}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-8 for hemagglutinating activity. Activity is reduced
CC to 50% at pH 8.5. {ECO:0000269|PubMed:22037666};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P08902}.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain
CC {ECO:0000250|UniProtKB:P86624}.
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. {ECO:0000269|PubMed:22037666}.
CC -!- MASS SPECTROMETRY: [Lectin alpha chain]: Mass=25606; Mass_error=2;
CC Method=Electrospray; Note=Alpha chain.;
CC Evidence={ECO:0000269|PubMed:22037666};
CC -!- MASS SPECTROMETRY: [Lectin beta chain]: Mass=12873; Mass_error=2;
CC Method=Electrospray; Note=Beta chain.;
CC Evidence={ECO:0000269|PubMed:22037666};
CC -!- MASS SPECTROMETRY: [Lectin gamma chain]: Mass=12752; Mass_error=2;
CC Method=Electrospray; Note=Gamma chain.;
CC Evidence={ECO:0000269|PubMed:22037666};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 4NOT; X-ray; 2.35 A; A=1-237.
DR PDBsum; 4NOT; -.
DR AlphaFoldDB; B3EWJ2; -.
DR SMR; B3EWJ2; -.
DR UniLectin; B3EWJ2; -.
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; Lectin; Manganese;
KW Mannose-binding; Metal-binding; Vacuole.
FT CHAIN 1..237
FT /note="Lectin alpha chain"
FT /id="PRO_0000417934"
FT CHAIN 1..118
FT /note="Lectin beta chain"
FT /evidence="ECO:0000269|PubMed:22037666"
FT /id="PRO_0000417935"
FT CHAIN 119..237
FT /note="Lectin gamma chain"
FT /evidence="ECO:0000269|PubMed:22037666"
FT /id="PRO_0000417936"
FT BINDING 8
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 10
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 10
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 12
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 12
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 14
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 19
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 24
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 34
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 99..100
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT BINDING 228
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:P08902"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4NOT"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 24..33
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:4NOT"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:4NOT"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 105..117
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:4NOT"
FT STRAND 209..215
FT /evidence="ECO:0007829|PDB:4NOT"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4NOT"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4NOT"
SQ SEQUENCE 237 AA; 25607 MW; F33FD269ABF01D6A CRC64;
ADTIVAVELD SYPNTDIGDP NYPHIGIDIK SIRSKSTARW NMQTGKVGTV HISYNSVAKR
LSAVVSYSGS SSTTVSYDVD LNNVLPEWVR VGLSATTGLY KETNTILSWS FTSKLKTNSI
ADENSLHFSF HKFSQNPKDL ILQGDAFTDS DGNLQLTKVS SSGDPQGNSV GRALFYAPVH
IWEKSAVVAS FDATFTFLIK SPDREPADGI TFFIANTDTS IPSGSGGRLL GLFPDAN
