ABL_AGABI
ID ABL_AGABI Reviewed; 143 AA.
AC Q00022;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Agaricus bisporus lectin;
DE Short=ABL;
DE AltName: Full=Agaricus bisporus agglutinin;
DE Short=ABA;
DE AltName: Full=Gal-beta-1,3-GalNAc-binding lectin;
DE AltName: Full=TF antigen-binding lectin;
OS Agaricus bisporus (White button mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX NCBI_TaxID=5341;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Fruiting body;
RX PubMed=7770537; DOI=10.1104/pp.107.4.1465;
RA Crenshaw R.W., Harper S.N., Moyer M., Privalle L.S.;
RT "Isolation and characterization of a cDNA clone encoding a lectin gene from
RT Agaricus bisporus.";
RL Plant Physiol. 107:1465-1466(1995).
RN [2]
RP FUNCTION.
RX PubMed=4343164; DOI=10.1016/s0021-9258(19)44676-0;
RA Presant C.A., Kornfeld S.;
RT "Characterization of the cell surface receptor for the Agaricus bisporus
RT hemagglutinin.";
RL J. Biol. Chem. 247:6937-6945(1972).
RN [3]
RP FUNCTION.
RX PubMed=8402638;
RA Yu L.-G., Fernig D.G., Smith J.A., Milton J.D., Rhodes J.M.;
RT "Reversible inhibition of proliferation of epithelial cell lines by
RT Agaricus bisporus (edible mushroom) lectin.";
RL Cancer Res. 53:4627-4632(1993).
RN [4]
RP FUNCTION.
RX PubMed=9988731; DOI=10.1074/jbc.274.8.4890;
RA Yu L.-G., Fernig D.G., White M.R., Spiller D.G., Appleton P., Evans R.C.,
RA Grierson I., Smith J.A., Davies H., Gerasimenko O.V., Petersen O.H.,
RA Milton J.D., Rhodes J.M.;
RT "Edible mushroom (Agaricus bisporus) lectin, which reversibly inhibits
RT epithelial cell proliferation, blocks nuclear localization sequence-
RT dependent nuclear protein import.";
RL J. Biol. Chem. 274:4890-4899(1999).
RN [5] {ECO:0007744|PDB:1Y2T, ECO:0007744|PDB:1Y2U, ECO:0007744|PDB:1Y2V, ECO:0007744|PDB:1Y2W, ECO:0007744|PDB:1Y2X}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE,
RP SEQUENCE REVISION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15596442; DOI=10.1074/jbc.m411989200;
RA Carrizo M.E., Capaldi S., Perduca M., Irazoqui F.J., Nores G.A.,
RA Monaco H.L.;
RT "The antineoplastic lectin of the common edible mushroom (Agaricus
RT bisporus) has two binding sites, each specific for a different
RT configuration at a single epimeric hydroxyl.";
RL J. Biol. Chem. 280:10614-10623(2005).
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 galactose-beta-1,3-N-acetylglucosamine. Does not bind monosaccharides.
CC Can be internalized by clathrin-coated vesicles after binding to
CC surface glycoproteins. After internalization it inhibits nuclear import
CC of nuclear localization signal dependent proteins. Inhibits
CC proliferation of malignant cells without cytotoxicity for normal cells.
CC {ECO:0000269|PubMed:4343164, ECO:0000269|PubMed:8402638,
CC ECO:0000269|PubMed:9988731}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15596442}.
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. Sold under
CC the name lectin from Agaricus bisporus by Sigma-Aldrich and under the
CC name of Agaricus bisporus (Mushroom) agglutinin (ABA) by USBiological.
CC -!- MISCELLANEOUS: Each monomer has 2 distinct carbohydrate binding sites,
CC one for galactose-beta-1,3-N-acetylgalactosamine and another for
CC galactose-beta-1,3-N-acetylglucosamine.
CC -!- SIMILARITY: Belongs to the fungal fruit body lectin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85813.1; Type=Frameshift; Note=Frameshift correction allows the C-terminal sequence to be compatible with the results of mass spectrometry and X-ray crystallography.; Evidence={ECO:0000305};
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DR EMBL; U14936; AAA85813.1; ALT_FRAME; mRNA.
DR PDB; 1Y2T; X-ray; 1.50 A; A/B=2-133.
DR PDB; 1Y2U; X-ray; 1.85 A; A/B=2-143.
DR PDB; 1Y2V; X-ray; 1.90 A; A/B=2-143.
DR PDB; 1Y2W; X-ray; 1.74 A; A/B=2-143.
DR PDB; 1Y2X; X-ray; 2.36 A; A/B/C/D=2-143.
DR PDBsum; 1Y2T; -.
DR PDBsum; 1Y2U; -.
DR PDBsum; 1Y2V; -.
DR PDBsum; 1Y2W; -.
DR PDBsum; 1Y2X; -.
DR AlphaFoldDB; Q00022; -.
DR SMR; Q00022; -.
DR UniLectin; Q00022; -.
DR EvolutionaryTrace; Q00022; -.
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; Hemagglutinin; Lectin.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..143
FT /note="Agaricus bisporus lectin"
FT /id="PRO_0000223094"
FT REGION 48..49
FT /note="beta-D-Gal-(1->3)-alpha-D-GalNAc"
FT /evidence="ECO:0000269|PubMed:15596442,
FT ECO:0007744|PDB:1Y2X"
FT BINDING 29
FT /ligand="beta-D-Gal-(1->3)-alpha-D-GalNAc"
FT /ligand_id="ChEBI:CHEBI:61820"
FT /evidence="ECO:0000269|PubMed:15596442,
FT ECO:0007744|PDB:1Y2X"
FT BINDING 73
FT /ligand="beta-D-Gal-(1->3)-alpha-D-GalNAc"
FT /ligand_id="ChEBI:CHEBI:61820"
FT /evidence="ECO:0000269|PubMed:15596442,
FT ECO:0007744|PDB:1Y2X"
FT BINDING 82
FT /ligand="N-acetyl-beta-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:28009"
FT /evidence="ECO:0000269|PubMed:15596442,
FT ECO:0007744|PDB:1Y2X"
FT BINDING 103
FT /ligand="N-acetyl-beta-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:28009"
FT /evidence="ECO:0000269|PubMed:15596442,
FT ECO:0007744|PDB:1Y2X"
FT BINDING 114
FT /ligand="N-acetyl-beta-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:28009"
FT /evidence="ECO:0000269|PubMed:15596442,
FT ECO:0007744|PDB:1Y2X"
FT CONFLICT 64
FT /note="S -> I (in Ref. 1; AAA85813)"
FT /evidence="ECO:0000305"
FT CONFLICT 134..143
FT /note="DNLKANLIIG -> IISRPISSSDKCFIRLPSQKS (in Ref. 1; AA
FT sequence)"
FT /evidence="ECO:0000305"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:1Y2T"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 40..49
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1Y2T"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:1Y2T"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:1Y2T"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:1Y2T"
FT HELIX 101..108
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:1Y2T"
FT STRAND 132..142
FT /evidence="ECO:0007829|PDB:1Y2T"
SQ SEQUENCE 143 AA; 16185 MW; 5704CFD273E1FB78 CRC64;
MTYTISIRVY QTTPKGFFRP VERTNWKYAN GGTWDEVRGE YVLTMGGSGT SGSLRFVSSD
TDESFVATFG VHNYKRWCDI VTNLTNEQTA LVINQEYYGV PIRDQARENQ LTSYNVANAK
GRRFAIEYTV TEGDNLKANL IIG
