LECF_ASPFM
ID LECF_ASPFM Reviewed; 314 AA.
AC Q8NJT4;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Fucose-specific lectin {ECO:0000303|PubMed:23695231};
DE AltName: Full=Aspergillus fumigatus lectin {ECO:0000303|PubMed:23695231};
DE Short=AFL {ECO:0000303|PubMed:23695231};
GN Name=fleA {ECO:0000303|PubMed:23695231}; ORFNames=CDV58_04824;
OS Neosartorya fumigata (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=746128;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=NIH 5233 / ATCC 13073;
RX PubMed=23695231; DOI=10.1007/s10156-013-0614-9;
RA Kuboi S., Ishimaru T., Tamada S., Bernard E.M., Perlin D.S., Armstrong D.;
RT "Molecular characterization of AfuFleA, an L-fucose-specific lectin from
RT Aspergillus fumigatus.";
RL J. Infect. Chemother. 19:1021-1028(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HMR AF 706;
RA Fournier E., Martineau C., Dufresne P.J., De Repentigny L., Dufresne S.F.;
RT "Prevalence of cryptic Aspergillus fumigatus species and azole resistance:
RT a 2000 to 2013 survey in a Montreal hospital.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Multispecific lectin that is able to recognize L-fucose in
CC all possible linkages (PubMed:23695231). These could be found not only
CC in decomposed plant matter in soil, which is the natural environment
CC for A.fumigatus, but also in various epitopes on human tissues (By
CC similarity). Mediates binding of A.fumigatus conidia to airway mucin in
CC a fucose dependent manner (By similarity). Stimulates IL-8 production
CC by human bronchial cells in a dose-dependent manner, contributing to
CC the inflammatory response observed upon the exposure of a patient to
CC A.fumigatus, and thus might be an important virulence factor involved
CC in an early stage of A.fumigatus infection (By similarity).
CC {ECO:0000250|UniProtKB:Q4WW81, ECO:0000269|PubMed:23695231}.
CC -!- SUBUNIT: Homodimer (By similarity). {ECO:0000250|UniProtKB:Q4WW81}.
CC -!- DOMAIN: AFL adopts the six-bladed beta-propeller fold and contains six
CC binding sites per monomer, each located between two adjacent blades (By
CC similarity). The six binding sites that are non-equivalent, and owing
CC to minor differences in amino-acid composition they exhibit a marked
CC difference in specific ligand recognition (By similarity).
CC {ECO:0000250|UniProtKB:Q4WW81}.
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; AF517830; AAM66707.1; -; Genomic_DNA.
DR EMBL; NKHS01000178; OXN04839.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8NJT4; -.
DR SMR; Q8NJT4; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR012475; Fungal_lectin.
DR Pfam; PF07938; Fungal_lectin; 1.
PE 3: Inferred from homology;
KW Lectin; Metal-binding; Repeat; Zinc.
FT CHAIN 1..314
FT /note="Fucose-specific lectin"
FT /id="PRO_0000442746"
FT REPEAT 2..53
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 54..103
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 104..155
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 156..206
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 207..259
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 260..314
FT /note="6"
FT /evidence="ECO:0000305"
FT REGION 2..314
FT /note="6 X approximate tandem repeats"
FT /evidence="ECO:0000305"
FT BINDING 25
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 37
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 44
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 73
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 85
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 94
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 98
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 126
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 138
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 146
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 150
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 177
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 188
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 197
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 229
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 241
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 243
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 281
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
FT BINDING 295
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q4WW81"
SQ SEQUENCE 314 AA; 34520 MW; A1CCAF527E6139BD CRC64;
MSTPGAQQVL FRTGIAAVNS TNHLRVYFQD VYGSIRESLY EGSWANGTEK NVIGNAKLGS
PVAATSKELK HIRVYTLTEG NTLQEFAYDS GTGWYNGGLG GAKFQVAPYS RIAAVFLAGT
DALQLRIYAQ KPDNTIQEYM WNGDGWKEGT NLGGALPGTG IGATSFRYTD YNGPSIRIWF
QTDLKLVQRA YDPHKGWYPD LVTIFDRAPP RTAIAATSFG AGNSSIYMRI YFVNSDNTIW
QVCWDHGKGY HDKGTITPVI QGSEVAIISW GSFANNGPDL RLYFQNGTYI SAVSEWVWNR
AHGSQLGRSA LPPA
