LECF_ASPOZ
ID LECF_ASPOZ Reviewed; 310 AA.
AC Q8TGE0;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 45.
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};
OS Aspergillus oryzae (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], PROTEIN SEQUENCE OF 132-146
RP AND 149-163, INDUCTION, AND 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).
CC -!- FUNCTION: Lectin that specifically binds to L-fucose and weakly reacts
CC with mannose and N-acetyl-neuraminic acid (PubMed:12092808). Has
CC strongest preference for the alpha-1,6-fucosylated chain (core fucose)
CC on glycoproteins among alpha-1,2-, alpha-1,3-, alpha-1,4-, and alpha-
CC 1,6-fucosylated chains (By similarity). Binds to fucose residues of IgE
CC in 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 (By
CC similarity). Induces secretion of pro-inflammatory cytokines IL6 and
CC IL8 implicated in ocular diseases such as mycotic keratitis, probably
CC through its interaction with host toll-like receptors TLR2 and TLR4,
CC followed by up-regulation of pro-inflammatory cytokines (By
CC similarity). {ECO:0000250|UniProtKB:Q2UNX8,
CC ECO:0000269|PubMed:12092808}.
CC -!- INDUCTION: Expressed in iron-deficient culture, but repressed in
CC presence of iron (PubMed:12092808). Contains two GGATA sequences at
CC -470 and -193 bp, consensus DNA-binding sites of GATA family
CC transcription factor sreA which regulates siderophore biosynthetic
CC genes and other genes involved in iron homeostasis (PubMed:12092808).
CC {ECO:0000269|PubMed:12092808}.
CC -!- DOMAIN: Has six binding sites that are non-equivalent, and owing to
CC minor differences in amino-acid composition they exhibit a marked
CC difference in specific ligand recognition (By similarity).
CC {ECO:0000250|UniProtKB:Q2UNX8}.
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. AFL is suitable for detecting core fucose on cell surface
CC glycoproteins. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the fungal fucose-specific lectin family.
CC {ECO:0000305}.
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DR EMBL; AB072379; BAB88318.1; -; Genomic_DNA.
DR PIR; JC7853; JC7853.
DR AlphaFoldDB; Q8TGE0; -.
DR SMR; Q8TGE0; -.
DR VEuPathDB; FungiDB:AO090001000189; -.
DR eggNOG; ENOG502SNJJ; Eukaryota.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR InterPro; IPR012475; Fungal_lectin.
DR Pfam; PF07938; Fungal_lectin; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Lectin; Repeat.
FT CHAIN 1..310
FT /note="Fucose-specific lectin"
FT /id="PRO_0000442744"
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..310
FT /note="6"
FT /evidence="ECO:0000305"
FT REGION 1..310
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:0000250|UniProtKB:Q2UNX8"
FT BINDING 37
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 44
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 73
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 85
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 94
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 126
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 138
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 146
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 177
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 189
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 198
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 230
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 242
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 277
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 291
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
SQ SEQUENCE 310 AA; 34482 MW; DA431C8DF83A3692 CRC64;
MSTPGAQEVL FRTGIAAVNS TNHLRVYFQD SHGSIRESLY ESGWANGTAK NVIAKAKLGT
PLAATSKELK NIRVYSLTED NVLQEAAYDS GSGWYNGALA GAKFTVAPYS RIGSVFLAGT
NALQLRIYAQ KTDNTIQEYM WNGDGWKEGT NLGVALPGTG IGVTCWRYTD YDGPSIRVWF
QTDNLKLVQR AYDPHTGWFK ELTTIFDKAP PRCAIAATNF NPGKSSIYMR IYFVNSDNTI
WQVCWDHGQG YHDKRTITPV IQGSEIAIIS WEGPELRLYF QNGTYVSAIS EWSWARHGSQ
LGRRALPPAE
