LECF_ASPFU
ID LECF_ASPFU Reviewed; 315 AA.
AC Q4WW81;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=AFUA_5G14740;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP FUNCTION.
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 [3]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=27058347; DOI=10.1371/journal.ppat.1005555;
RA Kerr S.C., Fischer G.J., Sinha M., McCabe O., Palmer J.M., Choera T.,
RA Lim F.Y., Wimmerova M., Carrington S.D., Yuan S., Lowell C.A., Oscarson S.,
RA Keller N.P., Fahy J.V.;
RT "FleA expression in Aspergillus fumigatus is recognized by fucosylated
RT structures on mucins and macrophages to prevent lung infection.";
RL PLoS Pathog. 12:E1005555-E1005555(2016).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), DEVELOPMENTAL STAGE, FUNCTION, AND
RP DOMAIN.
RX PubMed=24340081; DOI=10.1371/journal.pone.0083077;
RA Houser J., Komarek J., Kostlanova N., Cioci G., Varrot A., Kerr S.C.,
RA Lahmann M., Balloy V., Fahy J.V., Chignard M., Imberty A., Wimmerova M.;
RT "A soluble fucose-specific lectin from Aspergillus fumigatus
RT conidia-- structure, specificity and possible role in fungal
RT pathogenicity.";
RL PLoS ONE 8:E83077-E83077(2013).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH FUCOSE; GALACTOSE
RP AND N-ACETYL-D-GLUCOSAMINE, DOMAIN, FUNCTION, SUBUNIT, AND BIOTECHNOLOGY.
RX PubMed=25760594; DOI=10.1107/s1399004714026595;
RA Houser J., Komarek J., Cioci G., Varrot A., Imberty A., Wimmerova M.;
RT "Structural insights into Aspergillus fumigatus lectin specificity: AFL
RT binding sites are functionally non-equivalent.";
RL Acta Crystallogr. D 71:442-453(2015).
CC -!- FUNCTION: Multispecific lectin that is able to recognize L-fucose in
CC all possible linkages (PubMed:23695231, PubMed:27058347,
CC PubMed:24340081, PubMed:25760594). These could be found not only in
CC decomposed plant matter in soil, which is the natural environment for
CC A.fumigatus, but also in various epitopes on human tissues
CC (PubMed:25760594). Mediates binding of A.fumigatus conidia to airway
CC mucin in a fucose dependent manner (PubMed:27058347). Stimulates IL-8
CC production by human bronchial cells in a dose-dependent manner,
CC contributing to the inflammatory response observed upon the exposure of
CC a patient to A.fumigatus, and thus might be an important virulence
CC factor involved in an early stage of A.fumigatus infection
CC (PubMed:24340081). {ECO:0000269|PubMed:23695231,
CC ECO:0000269|PubMed:24340081, ECO:0000269|PubMed:25760594,
CC ECO:0000269|PubMed:27058347}.
CC -!- SUBUNIT: Homodimer (PubMed:25760594). {ECO:0000269|PubMed:25760594}.
CC -!- DEVELOPMENTAL STAGE: Expressed in conidia (PubMed:27058347,
CC PubMed:24340081). {ECO:0000269|PubMed:24340081,
CC ECO:0000269|PubMed:27058347}.
CC -!- DOMAIN: AFL adopts the six-bladed beta-propeller fold and contains 6
CC binding sites per monomer, each located between two adjacent blades
CC (PubMed:25760594). The 6 binding sites that are non-equivalent, and
CC owing to minor differences in amino-acid composition they exhibit a
CC marked difference in specific ligand recognition (PubMed:24340081,
CC PubMed:25760594). {ECO:0000269|PubMed:24340081,
CC ECO:0000269|PubMed:25760594}.
CC -!- DISRUPTION PHENOTYPE: Increases lung infection and lung injury by
CC A.fumigatus (PubMed:27058347). {ECO:0000269|PubMed:27058347}.
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 (PubMed:25760594). {ECO:0000305|PubMed:25760594}.
CC -!- SIMILARITY: Belongs to the fungal fucose-specific lectin family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000003; EAL91145.1; -; Genomic_DNA.
DR RefSeq; XP_753183.1; XM_748090.1.
DR PDB; 4AGI; X-ray; 1.60 A; A/B/C/D=1-315.
DR PDB; 4AGT; X-ray; 2.00 A; A/B=1-315.
DR PDB; 4AH4; X-ray; 1.75 A; A/B=1-315.
DR PDB; 4AHA; X-ray; 2.20 A; A/B=1-315.
DR PDB; 4C1Y; X-ray; 2.23 A; A/B/C/D=2-315.
DR PDB; 4D4U; X-ray; 1.99 A; A/B=1-315.
DR PDB; 4D52; X-ray; 1.76 A; A/B/C/D=1-315.
DR PDB; 4UOU; X-ray; 2.40 A; A/B/C/D=2-315.
DR PDB; 6Z6C; X-ray; 1.40 A; AAA/BBB=1-315.
DR PDBsum; 4AGI; -.
DR PDBsum; 4AGT; -.
DR PDBsum; 4AH4; -.
DR PDBsum; 4AHA; -.
DR PDBsum; 4C1Y; -.
DR PDBsum; 4D4U; -.
DR PDBsum; 4D52; -.
DR PDBsum; 4UOU; -.
DR PDBsum; 6Z6C; -.
DR AlphaFoldDB; Q4WW81; -.
DR SMR; Q4WW81; -.
DR UniLectin; Q4WW81; -.
DR EnsemblFungi; EAL91145; EAL91145; AFUA_5G14740.
DR GeneID; 3511258; -.
DR KEGG; afm:AFUA_5G14740; -.
DR VEuPathDB; FungiDB:Afu5g14740; -.
DR eggNOG; ENOG502SNJJ; Eukaryota.
DR HOGENOM; CLU_057373_0_0_1; -.
DR InParanoid; Q4WW81; -.
DR OMA; KNGISEW; -.
DR OrthoDB; 1081005at2759; -.
DR PHI-base; PHI:6256; -.
DR PHI-base; PHI:7875; -.
DR Proteomes; UP000002530; Chromosome 5.
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 1: Evidence at protein level;
KW 3D-structure; Lectin; Metal-binding; Reference proteome; Repeat; Zinc.
FT CHAIN 1..315
FT /note="Fucose-specific lectin"
FT /id="PRO_0000442745"
FT REPEAT 2..53
FT /note="1"
FT /evidence="ECO:0000305|PubMed:24340081"
FT REPEAT 54..103
FT /note="2"
FT /evidence="ECO:0000305|PubMed:24340081"
FT REPEAT 104..155
FT /note="3"
FT /evidence="ECO:0000305|PubMed:24340081"
FT REPEAT 156..207
FT /note="4"
FT /evidence="ECO:0000305|PubMed:24340081"
FT REPEAT 208..260
FT /note="5"
FT /evidence="ECO:0000305|PubMed:24340081"
FT REPEAT 261..315
FT /note="6"
FT /evidence="ECO:0000305|PubMed:24340081"
FT REGION 2..315
FT /note="6 X approximate tandem repeats"
FT /evidence="ECO:0000305|PubMed:24340081"
FT BINDING 25
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 37
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 44
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 73
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 85
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 94
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 98
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 126
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 138
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 146
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 150
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 177
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 189
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 198
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 230
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 242
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4D52"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4D52"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4D52"
FT BINDING 282
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT BINDING 296
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="6"
FT /evidence="ECO:0000269|PubMed:25760594,
FT ECO:0007744|PDB:4AGT"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 33..46
FT /evidence="ECO:0007829|PDB:4AGI"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:4AGI"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 81..89
FT /evidence="ECO:0007829|PDB:4AGI"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:4AGI"
FT HELIX 98..102
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 146..154
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4D52"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:4AGI"
FT TURN 194..196
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 215..220
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 238..246
FT /evidence="ECO:0007829|PDB:4AGI"
FT TURN 247..249
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 250..259
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4AGI"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 280..285
FT /evidence="ECO:0007829|PDB:4AGI"
FT TURN 289..292
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:4AGI"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:4AGI"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:4AGI"
SQ SEQUENCE 315 AA; 34661 MW; 22E0C1479074D154 CRC64;
MSTPGAQQVL FRTGIAAVNL TNHLRVYFQD VYGSIRESLY EGSWANGTEK NVIGNAKLGS
PVAATSKELK HIRVYTLTEG NTLQEFAYDS GTGWYNGGLG GAKFQVAPYS RIAAVFLAGT
DALQLRIYAQ KPDNTIQEYM WNGDGWKEGT NLGGALPGTG IGATSFRYTD YNGPSIRIWF
QTDDLKLVQR AYDPHKGWYP DLVTIFDRAP PRTAIAATSF GAGNSSIYMR IYFVNSDNTI
WQVCWDHGKG YHDKGTITPV IQGSEVAIIS WGSFANNGPD LRLYFQNGTY ISAVSEWVWN
RAHGSQLGRS ALPPA
