ATLE_AGRAE
ID ATLE_AGRAE Reviewed; 158 AA.
AC Q6WY08;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Anti-tumor lectin;
DE EC=3.1.21.-;
DE AltName: Full=AAL;
DE Flags: Fragment;
OS Agrocybe aegerita (Black poplar mushroom) (Agaricus aegerita).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Bolbitiaceae; Cyclocybe.
OX NCBI_TaxID=1973307;
RN [1] {ECO:0000312|EMBL:AAP93924.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tong X., Sun H., Zhao C., Qi Y.;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 1-8 AND 75-85, FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fruiting body {ECO:0000269|PubMed:12757412};
RX PubMed=12757412; DOI=10.1042/bj20030300;
RA Zhao C., Sun H., Tong X., Qi Y.;
RT "An antitumour lectin from the edible mushroom Agrocybe aegerita.";
RL Biochem. J. 374:321-327(2003).
RN [3] {ECO:0007744|PDB:1WW4, ECO:0007744|PDB:1WW5, ECO:0007744|PDB:1WW6, ECO:0007744|PDB:1WW7}
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-158 OF APOPROTEIN AND COMPLEXES
RP WITH CARBOHYDRATES INCLUDING N-ACETYLNEURAMINYL LACTOSE, FUNCTION, AND
RP SUBUNIT.
RX PubMed=16051274; DOI=10.1016/j.jmb.2005.06.045;
RA Ban M., Yoon H.-J., Demirkan E., Utsumi S., Mikami B., Yagi F.;
RT "Structural basis of a fungal galectin from Agrocybe cylindracea for
RT recognizing sialoconjugate.";
RL J. Mol. Biol. 351:695-706(2005).
CC -!- FUNCTION: Anti-tumor lectin with DNase activity. Inhibits the growth of
CC several tumor cell lines in vitro. Induces lymphocyte infiltration and
CC necrosis of tumor cells in a mouse tumor model. Induces apoptosis in
CC HeLa cells. Binds N-acetylneuraminyl lactose (N-acetyl-alpha-
CC neuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucose)
CC (PubMed:16051274). {ECO:0000269|PubMed:12757412,
CC ECO:0000269|PubMed:16051274}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12757412,
CC ECO:0000269|PubMed:16051274}.
CC -!- TISSUE SPECIFICITY: Detected in the fruiting body.
CC {ECO:0000269|PubMed:12757412}.
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DR EMBL; AY264782; AAP93924.1; -; mRNA.
DR PDB; 1WW4; X-ray; 2.30 A; A/B/C/D=3-158.
DR PDB; 1WW5; X-ray; 2.20 A; A/B/C/D=3-158.
DR PDB; 1WW6; X-ray; 2.20 A; A/B/C/D=3-158.
DR PDB; 1WW7; X-ray; 1.90 A; A/B/C/D=3-158.
DR PDB; 2ZGK; X-ray; 3.00 A; A=1-158.
DR PDB; 2ZGL; X-ray; 1.90 A; A/B=1-158.
DR PDB; 2ZGM; X-ray; 1.90 A; A/B=1-158.
DR PDB; 2ZGN; X-ray; 2.50 A; A/B=1-158.
DR PDB; 2ZGO; X-ray; 2.00 A; A/B=1-158.
DR PDB; 2ZGP; X-ray; 2.70 A; A/B=1-158.
DR PDB; 2ZGQ; X-ray; 1.90 A; A/B=1-158.
DR PDB; 2ZGR; X-ray; 1.90 A; A=1-158.
DR PDB; 2ZGS; X-ray; 1.90 A; A/B=1-158.
DR PDB; 2ZGT; X-ray; 2.80 A; A/B=1-158.
DR PDB; 2ZGU; X-ray; 2.40 A; A/B=1-158.
DR PDB; 3AFK; X-ray; 1.95 A; A/B=1-158.
DR PDB; 3M3C; X-ray; 2.00 A; A/B=1-158.
DR PDB; 3M3E; X-ray; 2.10 A; A/B/C/D=1-158.
DR PDB; 3M3O; X-ray; 2.10 A; A=1-158.
DR PDB; 3M3Q; X-ray; 2.20 A; A/B=1-158.
DR PDB; 3WG1; X-ray; 1.90 A; A/B=3-158.
DR PDB; 3WG2; X-ray; 2.20 A; A/B=3-158.
DR PDB; 3WG3; X-ray; 1.35 A; A/B=3-158.
DR PDB; 3WG4; X-ray; 1.60 A; A/B=3-158.
DR PDBsum; 1WW4; -.
DR PDBsum; 1WW5; -.
DR PDBsum; 1WW6; -.
DR PDBsum; 1WW7; -.
DR PDBsum; 2ZGK; -.
DR PDBsum; 2ZGL; -.
DR PDBsum; 2ZGM; -.
DR PDBsum; 2ZGN; -.
DR PDBsum; 2ZGO; -.
DR PDBsum; 2ZGP; -.
DR PDBsum; 2ZGQ; -.
DR PDBsum; 2ZGR; -.
DR PDBsum; 2ZGS; -.
DR PDBsum; 2ZGT; -.
DR PDBsum; 2ZGU; -.
DR PDBsum; 3AFK; -.
DR PDBsum; 3M3C; -.
DR PDBsum; 3M3E; -.
DR PDBsum; 3M3O; -.
DR PDBsum; 3M3Q; -.
DR PDBsum; 3WG1; -.
DR PDBsum; 3WG2; -.
DR PDBsum; 3WG3; -.
DR PDBsum; 3WG4; -.
DR AlphaFoldDB; Q6WY08; -.
DR SMR; Q6WY08; -.
DR MINT; Q6WY08; -.
DR UniLectin; Q6WY08; -.
DR EvolutionaryTrace; Q6WY08; -.
DR GO; GO:0004536; F:deoxyribonuclease activity; IDA:UniProtKB.
DR GO; GO:0030247; F:polysaccharide binding; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001079; Galectin_CRD.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SMART; SM00276; GLECT; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Direct protein sequencing; Hydrolase; Lectin;
KW Nuclease.
FT CHAIN <1..158
FT /note="Anti-tumor lectin"
FT /id="PRO_0000076969"
FT DOMAIN 12..155
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 43
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:16051274,
FT ECO:0000312|PDB:1WW4"
FT BINDING 59
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:16051274,
FT ECO:0000312|PDB:1WW4"
FT BINDING 63
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:16051274,
FT ECO:0000312|PDB:1WW4"
FT BINDING 72
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:16051274,
FT ECO:0000312|PDB:1WW4"
FT BINDING 74
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:16051274,
FT ECO:0000312|PDB:1WW4"
FT BINDING 80
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:16051274,
FT ECO:0000312|PDB:1WW4"
FT BINDING 83
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:16051274,
FT ECO:0000312|PDB:1WW4"
FT MOD_RES 1
FT /note="Blocked amino end (Gln)"
FT /evidence="ECO:0000269|PubMed:12757412"
FT NON_TER 1
FT /evidence="ECO:0000303|PubMed:12757412"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:2ZGU"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:3WG3"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3M3C"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3WG3"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:2ZGT"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:3WG3"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3WG3"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:2ZGL"
FT STRAND 147..155
FT /evidence="ECO:0007829|PDB:3WG3"
SQ SEQUENCE 158 AA; 16995 MW; FB977ED58C22EBF0 CRC64;
QGVNIYNISA GTSVDLAAPV TTGDIVTFFS SALNLNAGAG NPNNTTLNLF AENGAYLLHI
AFRLQENVII FNSRQPDGPW LVEQRVSDVA NQFAGIDGKA MVTVFDHGDK YQVVINEKTV
IQYTKQISGL TLSLSYNATE ETSIFSTVVE AVTYTGLA
