LECF_ASPOR
ID LECF_ASPOR Reviewed; 311 AA.
AC Q2UNX8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Fucose-specific lectin {ECO:0000303|PubMed:12092808};
DE AltName: Full=Aspergillus oryzea lectin {ECO:0000303|PubMed:12092808};
DE Short=AOL {ECO:0000303|PubMed:12092808};
GN Name=fleA {ECO:0000303|PubMed:12092808}; ORFNames=AO090001000189;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
RN [2]
RP FUNCTION.
RX PubMed=12092808; DOI=10.1271/bbb.66.1002;
RA Ishida H., Moritani T., Hata Y., Kawato A., Suginami K., Abe Y.,
RA Imayasu S.;
RT "Molecular cloning and overexpression of fleA gene encoding a fucose-
RT specific lectin of Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 66:1002-1008(2002).
RN [3]
RP FUNCTION, SUBUNIT, AND BIOTECHNOLOGY.
RX PubMed=17383961; DOI=10.1074/jbc.m701195200;
RA Matsumura K., Higashida K., Ishida H., Hata Y., Yamamoto K., Shigeta M.,
RA Mizuno-Horikawa Y., Wang X., Miyoshi E., Gu J., Taniguchi N.;
RT "Carbohydrate binding specificity of a fucose-specific lectin from
RT Aspergillus oryzae: a novel probe for core fucose.";
RL J. Biol. Chem. 282:15700-15708(2007).
RN [4]
RP FUNCTION.
RX PubMed=19109923; DOI=10.1016/j.ab.2008.11.044;
RA Matsumura K., Higashida K., Hata Y., Kominami J., Nakamura-Tsuruta S.,
RA Hirabayashi J.;
RT "Comparative analysis of oligosaccharide specificities of fucose-specific
RT lectins from Aspergillus oryzae and Aleuria aurantia using frontal affinity
RT chromatography.";
RL Anal. Biochem. 386:217-221(2009).
RN [5]
RP FUNCTION.
RX PubMed=21790704; DOI=10.1111/j.1365-3083.2011.02598.x;
RA Yamaki K., Yoshino S.;
RT "Aspergillus oryzae lectin induces anaphylactoid oedema and mast cell
RT activation through its interaction with fucose of mast cell-bound non-
RT specific IgE.";
RL Scand. J. Immunol. 74:445-453(2011).
RN [6]
RP BIOTECHNOLOGY.
RX PubMed=21892597; DOI=10.1007/s00253-011-3549-z;
RA Mun J.Y., Lee K.J., Kim Y.J., Kwon O., Kim S.J., Lee S.G., Park W.S.,
RA Heo W.D., Oh D.B.;
RT "Development of fluorescent probes for the detection of fucosylated N-
RT glycans using an Aspergillus oryzae lectin.";
RL Appl. Microbiol. Biotechnol. 93:251-260(2012).
RN [7]
RP FUNCTION.
RX PubMed=28470344; DOI=10.1007/s11010-017-3050-9;
RA Ballal S., Belur S., Laha P., Roy S., Swamy B.M., Inamdar S.R.;
RT "Mitogenic lectins from Cephalosporium curvulum (CSL) and Aspergillus
RT oryzae (AOL) mediate host-pathogen interactions leading to mycotic
RT keratitis.";
RL Mol. Cell. Biochem. 434:209-219(2017).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH SELENO-FUCOSIDES,
RP FUNCTION, AND DOMAIN.
RX PubMed=27318092; DOI=10.1016/j.bbrc.2016.06.069;
RA Makyio H., Shimabukuro J., Suzuki T., Imamura A., Ishida H., Kiso M.,
RA Ando H., Kato R.;
RT "Six independent fucose-binding sites in the crystal structure of
RT Aspergillus oryzae lectin.";
RL Biochem. Biophys. Res. Commun. 477:477-482(2016).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SELENO-FUCOSIDES,
RP FUNCTION, AND DOMAIN.
RX PubMed=28041800; DOI=10.1016/j.bmc.2016.12.021;
RA Shimabukuro J., Makyio H., Suzuki T., Nishikawa Y., Kawasaki M.,
RA Imamura A., Ishida H., Ando H., Kato R., Kiso M.;
RT "Synthesis of seleno-fucose compounds and their application to the X-ray
RT structural determination of carbohydrate-lectin complexes using
RT single/multi-wavelength anomalous dispersion phasing.";
RL Bioorg. Med. Chem. 25:1132-1142(2017).
CC -!- FUNCTION: Lectin that specifically binds to L-fucose and weakly reacts
CC with mannose and N-acetyl-neuraminic acid (PubMed:12092808,
CC PubMed:27318092, PubMed:28041800). Has strongest preference for the
CC alpha-1,6-fucosylated chain (core fucose) on glycoproteins among alpha-
CC 1,2-, alpha-1,3-, alpha-1,4-, and alpha-1,6-fucosylated chains
CC (PubMed:17383961, PubMed:19109923). Binds to fucose residues of IgE in
CC mice and human, causing antigen-independent IgE-mediated mast cell
CC activation and anaphylactoid reactions in mice and is possibly
CC implicated in allergic response to Aspergillus oryzae in humans
CC (PubMed:21790704). Induces secretion of pro-inflammatory cytokines IL6
CC and IL8 implicated in ocular diseases such as mycotic keratitis,
CC probably through its interaction with host toll-like receptors TLR2 and
CC TLR4, followed by up-regulation of pro-inflammatory cytokines
CC (PubMed:28470344). {ECO:0000269|PubMed:12092808,
CC ECO:0000269|PubMed:17383961, ECO:0000269|PubMed:19109923,
CC ECO:0000269|PubMed:21790704, ECO:0000269|PubMed:27318092,
CC ECO:0000269|PubMed:28041800, ECO:0000269|PubMed:28470344}.
CC -!- SUBUNIT: Homodimer (PubMed:17383961). {ECO:0000269|PubMed:17383961}.
CC -!- DOMAIN: AOL adopts the six-bladed beta-propeller fold and contains 6
CC binding sites per monomer, each located between two adjacent blades
CC (PubMed:27318092, PubMed:28041800). The 6 binding sites that are non-
CC equivalent, and owing to minor differences in amino-acid composition
CC they exhibit a marked difference in specific ligand recognition
CC (PubMed:27318092, PubMed:28041800). {ECO:0000269|PubMed:27318092,
CC ECO:0000269|PubMed:28041800}.
CC -!- BIOTECHNOLOGY: Lectins have particular value as specific probes for
CC investigating the distribution, structure and biological function of
CC carbohydrate chains on the cell surface of animal, plant, and
CC microorganism because of their specificity for defined carbohydrate
CC structures (PubMed:17383961). FleA is suitable for detecting core
CC fucose on cell surface glycoproteins and/or a useful vehicle for
CC delivery of substances to the inside of cells (PubMed:17383961,
CC PubMed:21892597). {ECO:0000269|PubMed:21892597,
CC ECO:0000305|PubMed:17383961}.
CC -!- SIMILARITY: Belongs to the fungal fucose-specific lectin family.
CC {ECO:0000305}.
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DR EMBL; AP007154; BAE56737.1; -; Genomic_DNA.
DR RefSeq; XP_001818739.1; XM_001818687.2.
DR PDB; 5EO7; X-ray; 2.30 A; A/B/C=2-311.
DR PDB; 5EO8; X-ray; 1.60 A; A=1-311.
DR PDB; 5H47; X-ray; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-311.
DR PDBsum; 5EO7; -.
DR PDBsum; 5EO8; -.
DR PDBsum; 5H47; -.
DR AlphaFoldDB; Q2UNX8; -.
DR SMR; Q2UNX8; -.
DR UniLectin; Q2UNX8; -.
DR EnsemblFungi; BAE56737; BAE56737; AO090001000189.
DR GeneID; 5990710; -.
DR KEGG; aor:AO090001000189; -.
DR VEuPathDB; FungiDB:AO090001000189; -.
DR HOGENOM; CLU_057373_0_0_1; -.
DR OMA; KNGISEW; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0005769; C:early endosome; IDA:AspGD.
DR GO; GO:0043229; C:intracellular organelle; IDA:AspGD.
DR GO; GO:0042806; F:fucose binding; IDA:AspGD.
DR InterPro; IPR012475; Fungal_lectin.
DR Pfam; PF07938; Fungal_lectin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lectin; Reference proteome; Repeat.
FT CHAIN 1..311
FT /note="Fucose-specific lectin"
FT /id="PRO_0000442743"
FT REPEAT 1..53
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 54..103
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 104..151
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 152..209
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 210..256
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 257..311
FT /note="6"
FT /evidence="ECO:0000305"
FT REGION 1..311
FT /note="6 X approximate tandem repeats"
FT /evidence="ECO:0000305"
FT BINDING 25
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 37
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 44
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 73
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 85
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 94
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 126
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 138
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 146
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 177
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 189
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 198
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 230
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 242
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 277
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT BINDING 291
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:27318092,
FT ECO:0000269|PubMed:28041800, ECO:0007744|PDB:5EO8,
FT ECO:0007744|PDB:5H47"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 33..46
FT /evidence="ECO:0007829|PDB:5EO8"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:5EO7"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:5EO8"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:5EO8"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:5EO8"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:5EO7"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:5EO8"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:5EO8"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:5EO8"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:5EO8"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:5EO8"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:5EO8"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:5EO8"
SQ SEQUENCE 311 AA; 34541 MW; 20F3275C3B4CE7E5 CRC64;
MSTPGAQEVL FRTGIAAVNS TNHLRVYFQD SHGSIRESLY ESGWANGTAK NVIAKAKLGT
PLAATSKELK NIRVYSLTED NVLQEAAYDS GSGWYNGALA GAKFTVAPYS RIGSVFLAGT
NALQLRIYAQ KTDNTIQEYM WNGDGWKEGT NLGVALPGTG IGVTCWRYTD YDGPSIRVWF
QTDNLKLVQR AYDPHTGWYK ELTTIFDKAP PRCAIAATNF NPGKSSIYMR IYFVNSDNTI
WQVCWDHGQG YHDKRTITPV IQGSEIAIIS WEGPELRLYF QNGTYVSAIS EWTWGKAHGS
QLGRRALPPA E
