LECF_ARTBC
ID LECF_ARTBC Reviewed; 365 AA.
AC D4AL26;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Fucose-specific lectin {ECO:0000250|UniProtKB:P18891};
DE Flags: Precursor;
GN ORFNames=ARB_05022;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- FUNCTION: Probable L-fucose-binding lectin.
CC {ECO:0000250|UniProtKB:P18891}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P18891}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC -!- DOMAIN: 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 -!- SIMILARITY: Belongs to the fungal fucose-specific lectin family.
CC {ECO:0000305}.
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DR EMBL; ABSU01000002; EFE36085.1; -; Genomic_DNA.
DR RefSeq; XP_003016730.1; XM_003016684.1.
DR AlphaFoldDB; D4AL26; -.
DR SMR; D4AL26; -.
DR EnsemblFungi; EFE36085; EFE36085; ARB_05022.
DR GeneID; 9522215; -.
DR KEGG; abe:ARB_05022; -.
DR eggNOG; ENOG502SNJJ; Eukaryota.
DR HOGENOM; CLU_057373_0_0_1; -.
DR OMA; KNGISEW; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Glycoprotein; Lectin; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..365
FT /note="Fucose-specific lectin"
FT /id="PRO_5003054087"
FT REPEAT 22..79
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 80..141
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 142..206
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 207..261
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 262..309
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 310..365
FT /note="6"
FT /evidence="ECO:0000305"
FT REGION 22..365
FT /note="6 X approximate tandem repeats"
FT /evidence="ECO:0000305"
FT BINDING 51
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 63
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 70
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 111
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 123
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 132
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 164
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 176
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 201
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 231
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 283
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="5"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 333
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT BINDING 347
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="6"
FT /evidence="ECO:0000250|UniProtKB:Q2UNX8"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 365 AA; 40297 MW; CCDD3526FCA39D3F CRC64;
MKLLHFTILL QVSLFPASSL AQAGGNNTEV QVQQTLPGTG IAAVNSVNLL RIYSQDTSGG
IREARFEGYW SGGLANDTIA KARANSSIAA ASDDLELYKS SSSTNFLLKI RVYYLLPNNT
LGEAASDSQS RWYTGSLNQY NFQVASHSRL AAVFVPSTQR PRLRIYAQLG DNTIQEFGYD
VSPLSQLEPM FANYLKVGRG WQRLANFGPA LPGTGIAALT YTTGLRRSTT RVYFQTTDRR
VVERVYDNRS WSDGGTVVRT AKPRTPLAAT SFLLTPGNPQ SVRVYYGTED NRILEKGTEG
GTYWYDGAFE HSAIPDSQVA AVDWGNGGVF NIRLYIQDGA FKNGISEWAW FRRSWRRGIL
AIPPA
