BEL_BOLED
ID BEL_BOLED Reviewed; 143 AA.
AC F2Z266;
DT 16-NOV-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 28.
DE RecName: Full=Boletus edulis lectin;
DE Short=BEL;
OS Boletus edulis (King bolete).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Boletineae; Boletaceae; Boletoideae; Boletus.
OX NCBI_TaxID=36056;
RN [1] {ECO:0007744|PDB:3QDS, ECO:0007744|PDB:3QDT, ECO:0007744|PDB:3QDU, ECO:0007744|PDB:3QDV, ECO:0007744|PDB:3QDW, ECO:0007744|PDB:3QDX, ECO:0007744|PDB:3QDY}
RP PROTEIN SEQUENCE OF 2-143, X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN
RP COMPLEXES WITH T-ANTIGEN DISACCHARIDE; DIACETYLCHITOBIOSE AND OTHER SUGAR
RP MOIETIES, FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21303815; DOI=10.1093/glycob/cwr012;
RA Bovi M., Carrizo M.E., Capaldi S., Perduca M., Chiarelli L.R., Galliano M.,
RA Monaco H.L.;
RT "Structure of a lectin with antitumoral properties in king bolete (Boletus
RT edulis) mushrooms.";
RL Glycobiology 21:1000-1009(2011).
CC -!- FUNCTION: Lectin that recognizes O-linked galactose-beta-1,3-N-
CC acetylgalactosamine, a disaccharide (Thomsen-Friedenreich antigen or T-
CC disaccharide), present on cell surface glycoproteins. Can also bind
CC chitin, N,N'-diacetylchitobiose, N-acetylgalactosamine and N-
CC acetylglucosamine. Inhibits proliferation of colon, breast and liver
CC cancer cell lines (in vitro). {ECO:0000269|PubMed:21303815}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:21303815}.
CC -!- BIOTECHNOLOGY: Lectins can be used to recognize and purifiy specific
CC glycoproteins, and for the purification of cells with specific surface
CC glycoproteins. Has potential as anti-proliferative agent.
CC -!- SIMILARITY: Belongs to the fungal fruit body lectin family.
CC {ECO:0000305}.
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DR PDB; 3QDS; X-ray; 1.15 A; A/B=2-143.
DR PDB; 3QDT; X-ray; 1.30 A; A/B=2-143.
DR PDB; 3QDU; X-ray; 2.00 A; A/B/C/D=2-143.
DR PDB; 3QDV; X-ray; 1.30 A; A/B=2-143.
DR PDB; 3QDW; X-ray; 1.90 A; A/B=2-143.
DR PDB; 3QDX; X-ray; 1.70 A; A/B=2-143.
DR PDB; 3QDY; X-ray; 2.00 A; A/B=2-143.
DR PDBsum; 3QDS; -.
DR PDBsum; 3QDT; -.
DR PDBsum; 3QDU; -.
DR PDBsum; 3QDV; -.
DR PDBsum; 3QDW; -.
DR PDBsum; 3QDX; -.
DR PDBsum; 3QDY; -.
DR AlphaFoldDB; F2Z266; -.
DR SMR; F2Z266; -.
DR Allergome; 11373; Bol ed Lectin.
DR UniLectin; F2Z266; -.
DR EvolutionaryTrace; F2Z266; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR Gene3D; 2.60.270.20; -; 1.
DR InterPro; IPR015926; Cytolysin/lectin.
DR InterPro; IPR009960; Fruit_body_lectin_fun.
DR Pfam; PF07367; FB_lectin; 1.
DR SUPFAM; SSF63724; SSF63724; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Lectin.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:21303815"
FT CHAIN 2..143
FT /note="Boletus edulis lectin"
FT /id="PRO_0000413861"
FT REGION 49..50
FT /note="beta-D-Gal-(1->3)-alpha-D-GalNAc"
FT /evidence="ECO:0007744|PDB:3QDT"
FT REGION 49..50
FT /note="N-acetyl-alpha-D-galactosamine"
FT /evidence="ECO:0007744|PDB:3QDV"
FT REGION 72..73
FT /note="beta-D-Gal-(1->3)-alpha-D-GalNAc"
FT /evidence="ECO:0007744|PDB:3QDT"
FT REGION 72..73
FT /note="N-acetyl-alpha-D-galactosamine"
FT /evidence="ECO:0007744|PDB:3QDV"
FT BINDING 30
FT /ligand="beta-D-Gal-(1->3)-alpha-D-GalNAc"
FT /ligand_id="ChEBI:CHEBI:61820"
FT /evidence="ECO:0007744|PDB:3QDT"
FT BINDING 79..82
FT /ligand="N,N'-diacetylchitobiose"
FT /ligand_id="ChEBI:CHEBI:28681"
FT /evidence="ECO:0007744|PDB:3QDU"
FT BINDING 79..82
FT /ligand="N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:44278"
FT /evidence="ECO:0007744|PDB:3QDV"
FT BINDING 103
FT /ligand="N,N'-diacetylchitobiose"
FT /ligand_id="ChEBI:CHEBI:28681"
FT /evidence="ECO:0007744|PDB:3QDU"
FT BINDING 103
FT /ligand="N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:44278"
FT /evidence="ECO:0007744|PDB:3QDV"
FT BINDING 114
FT /ligand="N,N'-diacetylchitobiose"
FT /ligand_id="ChEBI:CHEBI:28681"
FT /evidence="ECO:0007744|PDB:3QDU"
FT BINDING 114
FT /ligand="N-acetyl-alpha-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:44278"
FT /evidence="ECO:0007744|PDB:3QDV"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:3QDS"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 19..26
FT /evidence="ECO:0007829|PDB:3QDS"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 41..50
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 75..81
FT /evidence="ECO:0007829|PDB:3QDS"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:3QDS"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:3QDS"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3QDS"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:3QDS"
SQ SEQUENCE 143 AA; 15939 MW; 0FB92D82B139CA2A CRC64;
MTYSITLRVF QRNPGRGFFS IVEKTVFHYA NGGTWSEAKG THTLTMGGSG TSGVLRFMSD
KGELITVAVG VHNYKRWCDV VTGLKPEETA LVINPQYYNN GPRAYTREKQ LAEYNVTSVV
GTRFEVKYTV VEGNNLEANV IFS
