LECF_ALEAU
ID LECF_ALEAU Reviewed; 313 AA.
AC P18891;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Fucose-specific lectin {ECO:0000303|PubMed:2193930};
DE AltName: Full=Aleuria aurantia lectin {ECO:0000303|PubMed:2193930};
DE Short=AAL {ECO:0000303|PubMed:2193930};
OS Aleuria aurantia (Orange peel mushroom).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Pyronemataceae; Aleuria.
OX NCBI_TaxID=5188;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND DEVELOPMENTAL STAGE.
RX PubMed=2193930; DOI=10.1093/oxfordjournals.jbchem.a123024;
RA Fukumori F., Takeuchi N., Hagiwara T., Ohbayashi H., Endo T., Kochibe N.,
RA Nagata Y., Kobata A.;
RT "Primary structure of a fucose-specific lectin obtained from a mushroom,
RT Aleuria aurantia.";
RL J. Biochem. 107:190-196(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ogawa S., Ando A., Nagata Y.;
RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-31, PROTEIN SEQUENCE OF 2-31, AND FUNCTION.
RX PubMed=2666154; DOI=10.1016/0014-5793(89)80709-4;
RA Fukumori F., Takeuchi N., Hagiwara T., Ito K., Kochibe N., Kobata A.,
RA Nagata Y.;
RT "Cloning and expression of a functional fucose-specific lectin from an
RT orange peel mushroom, Aleuria aurantia.";
RL FEBS Lett. 250:153-156(1989).
RN [4]
RP FUNCTION, AND SUBUNIT.
RX PubMed=7397108; DOI=10.1021/bi00554a004;
RA Kochibe N., Furukawa K.;
RT "Purification and properties of a novel fucose-specific hemagglutinin of
RT Aleuria aurantia.";
RL Biochemistry 19:2841-2846(1980).
RN [5]
RP FUNCTION.
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 [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=18493851; DOI=10.1007/s10719-008-9135-7;
RA Olausson J., Tibell L., Jonsson B.H., Paahlsson P.;
RT "Detection of a high affinity binding site in recombinant Aleuria aurantia
RT lectin.";
RL Glycoconj. J. 25:753-762(2008).
RN [7]
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 [8]
RP FUNCTION, AND MUTAGENESIS OF ASN-225.
RX PubMed=21945439; DOI=10.1016/j.bbrc.2011.09.027;
RA Romano P.R., Mackay A., Vong M., DeSa J., Lamontagne A., Comunale M.A.,
RA Hafner J., Block T., Lec R., Mehta A.;
RT "Development of recombinant Aleuria aurantia lectins with altered binding
RT specificities to fucosylated glycans.";
RL Biochem. Biophys. Res. Commun. 414:84-89(2011).
RN [9]
RP SUBUNIT, MUTAGENESIS OF TYR-7 AND SER-284, AND FUNCTION.
RX PubMed=20798114; DOI=10.1093/glycob/cwq129;
RA Olausson J., Astroem E., Jonsson B.H., Tibell L.A., Paahlsson P.;
RT "Production and characterization of a monomeric form and a single-site form
RT of Aleuria aurantia lectin.";
RL Glycobiology 21:34-44(2011).
RN [10]
RP FUNCTION.
RX PubMed=22738968; DOI=10.1271/bbb.110982;
RA Amano K., Katayama H., Saito A., Ando A., Nagata Y.;
RT "Aleuria aurantia lectin exhibits antifungal activity against Mucor
RT racemosus.";
RL Biosci. Biotechnol. Biochem. 76:967-970(2012).
RN [11]
RP FUNCTION.
RX PubMed=22226468; DOI=10.1016/j.jchromb.2011.12.015;
RA Bergstroem M., Astroem E., Paahlsson P., Ohlson S.;
RT "Elucidating the selectivity of recombinant forms of Aleuria aurantia
RT lectin using weak affinity chromatography.";
RL J. Chromatogr. B 885:66-72(2012).
RN [12]
RP BIOTECHNOLOGY.
RX PubMed=22789673; DOI=10.1016/j.jprot.2012.06.027;
RA Ahn Y.H., Shin P.M., Oh N.R., Park G.W., Kim H., Yoo J.S.;
RT "A lectin-coupled, targeted proteomic mass spectrometry (MRM MS) platform
RT for identification of multiple liver cancer biomarkers in human plasma.";
RL J. Proteomics 75:5507-5515(2012).
RN [13]
RP BIOTECHNOLOGY.
RX PubMed=24027776; DOI=10.1039/c3an01126g;
RA Ahn Y.H., Shin P.M., Kim Y.S., Oh N.R., Ji E.S., Kim K.H., Lee Y.J.,
RA Kim S.H., Yoo J.S.;
RT "Quantitative analysis of aberrant protein glycosylation in liver cancer
RT plasma by AAL-enrichment and MRM mass spectrometry.";
RL Analyst 138:6454-6462(2013).
RN [14]
RP FUNCTION, MUTAGENESIS OF ASN-225, AND BIOTECHNOLOGY.
RX PubMed=27650323; DOI=10.1002/pmic.201600064;
RA Norton P., Comunale M.A., Herrera H., Wang M., Houser J., Wimmerova M.,
RA Romano P.R., Mehta A.;
RT "Development and application of a novel recombinant Aleuria aurantia lectin
RT with enhanced core fucose binding for identification of glycoprotein
RT biomarkers of hepatocellular carcinoma.";
RL Proteomics 16:3126-3136(2016).
RN [15]
RP FUNCTION.
RX PubMed=28800497; DOI=10.1016/j.carres.2017.07.011;
RA Cai D., Xun C., Tang F., Tian X., Yang L., Ding K., Li W., Le Z., Huang W.;
RT "Glycoconjugate probes containing a core-fucosylated N-glycan trisaccharide
RT for fucose lectin identification and purification.";
RL Carbohydr. Res. 449:143-152(2017).
RN [16]
RP BIOTECHNOLOGY.
RX PubMed=28748044; DOI=10.1080/20002297.2017.1345581;
RA Tawakoli P.N., Neu T.R., Busck M.M., Kuhlicke U., Schramm A., Attin T.,
RA Wiedemeier D.B., Schlafer S.;
RT "Visualizing the dental biofilm matrix by means of fluorescence lectin-
RT binding analysis.";
RL J. Oral Microbiol. 9:1345581-1345581(2017).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 2-313 IN COMPLEX WITH
RP ALPHA-L-FUCOSE AND BETA-L-FUCOSE, FUNCTION, AND DOMAIN.
RX PubMed=14503859; DOI=10.1021/bi034983z;
RA Fujihashi M., Peapus D.H., Kamiya N., Nagata Y., Miki K.;
RT "Crystal structure of fucose-specific lectin from Aleuria aurantia binding
RT ligands at three of its five sugar recognition sites.";
RL Biochemistry 42:11093-11099(2003).
RN [18] {ECO:0007744|PDB:1OFZ}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-313 IN COMPLEX WITH
RP ALPHA-L-FUCOSE AND BETA-L-FUCOSE, FUNCTION, AND DOMAIN.
RX PubMed=12732625; DOI=10.1074/jbc.m302642200;
RA Wimmerova M., Mitchell E., Sanchez J.F., Gautier C., Imberty A.;
RT "Crystal structure of fungal lectin: six-bladed beta-propeller fold and
RT novel fucose recognition mode for Aleuria aurantia lectin.";
RL J. Biol. Chem. 278:27059-27067(2003).
CC -!- FUNCTION: Lectin that specifically binds to L-fucose (PubMed:2193930,
CC PubMed:2666154, PubMed:7397108, PubMed:18493851, PubMed:21945439,
CC PubMed:27650323, PubMed:28800497, PubMed:14503859, PubMed:12732625).
CC Has strongest preference for the alpha-1,6-fucosylated chain (core
CC fucose) on glycoproteins among alpha-1,2-, alpha-1,3-, alpha-1,4-, and
CC alpha-1,6-fucosylated chains (PubMed:17383961, PubMed:19109923,
CC PubMed:20798114, PubMed:22226468). Might play a role in the
CC differentiation of the fruiting body (PubMed:2193930). Exhibits
CC antifungal activity against Mucor racemosus and thus could act as an
CC antifungal protein in natural ecosystems (PubMed:22738968).
CC {ECO:0000269|PubMed:12732625, ECO:0000269|PubMed:14503859,
CC ECO:0000269|PubMed:17383961, ECO:0000269|PubMed:18493851,
CC ECO:0000269|PubMed:19109923, ECO:0000269|PubMed:20798114,
CC ECO:0000269|PubMed:2193930, ECO:0000269|PubMed:21945439,
CC ECO:0000269|PubMed:22226468, ECO:0000269|PubMed:22738968,
CC ECO:0000269|PubMed:2666154, ECO:0000269|PubMed:27650323,
CC ECO:0000269|PubMed:28800497, ECO:0000269|PubMed:7397108}.
CC -!- SUBUNIT: Forms homodimers (PubMed:2193930, PubMed:7397108,
CC PubMed:20798114, PubMed:12732625). The two AAL monomers are associated
CC via interactions between N-terminal and C-terminal peptides
CC (PubMed:12732625). Tyr-7 interacts via aromatic ring stacking with its
CC counterpart on the other monomer, whereas Ser-284 interacts via
CC hydrogen bonding with Asp-264 on the other monomer (PubMed:12732625).
CC {ECO:0000269|PubMed:12732625, ECO:0000269|PubMed:20798114,
CC ECO:0000269|PubMed:2193930, ECO:0000269|PubMed:7397108}.
CC -!- DEVELOPMENTAL STAGE: AAL is detected in fruiting bodies but not in
CC mycelia (PubMed:2193930). {ECO:0000269|PubMed:2193930}.
CC -!- DOMAIN: AAL adopts the six-bladed beta-propeller fold and contains 5
CC binding sites per monomer, each located between two adjacent blades
CC (PubMed:14503859, PubMed:12732625). Residues conserved at 5 of the 6
CC sites, are located on the surface of the AAL and directly contribute to
CC fucose recognition (PubMed:14503859). Because the corresponding
CC residues forming site 6 are not conserved, this site cannot be
CC considered to accommodate fucose molecules (PubMed:14503859). The 5
CC binding sites that are non-equivalent, and owing to minor differences
CC in amino-acid composition they exhibit a marked difference in specific
CC ligand recognition (PubMed:18493851, PubMed:12732625).
CC {ECO:0000269|PubMed:12732625, ECO:0000269|PubMed:14503859,
CC ECO:0000269|PubMed:18493851}.
CC -!- BIOTECHNOLOGY: AAL's binding activity could be used to identify
CC secreted fucosylated glycoproteins that may represent candidate
CC biomarkers for cancer since fucosylation of N-linked glycans has been
CC associated with several types of cancer such as liver cancer
CC (PubMed:22789673, PubMed:24027776, PubMed:27650323). Identified as one
CC of the several suitable fluorescently labeled lectins that can be used
CC in a combination for the visualization and quantification of
CC extracellular glycoconjugates in dental supragingival biofilms grown
CC for 48 hours in situ in the absence of dietary carbohydrates
CC (PubMed:28748044). {ECO:0000269|PubMed:22789673,
CC ECO:0000269|PubMed:24027776, ECO:0000269|PubMed:27650323,
CC ECO:0000269|PubMed:28748044}.
CC -!- SIMILARITY: Belongs to the fungal fucose-specific lectin family.
CC {ECO:0000305}.
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DR EMBL; D00573; BAA00451.1; -; mRNA.
DR EMBL; D85776; BAA12871.1; -; Genomic_DNA.
DR PIR; JX0096; JX0096.
DR PDB; 1IUB; X-ray; 2.31 A; A=2-313.
DR PDB; 1IUC; X-ray; 2.24 A; A=2-313.
DR PDB; 1OFZ; X-ray; 1.50 A; A/B=2-313.
DR PDB; 5MXC; X-ray; 1.14 A; A=1-313.
DR PDB; 6GKE; X-ray; 1.08 A; A=2-313.
DR PDBsum; 1IUB; -.
DR PDBsum; 1IUC; -.
DR PDBsum; 1OFZ; -.
DR PDBsum; 5MXC; -.
DR PDBsum; 6GKE; -.
DR AlphaFoldDB; P18891; -.
DR SMR; P18891; -.
DR UniLectin; P18891; -.
DR EvolutionaryTrace; P18891; -.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0042806; F:fucose binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0030582; P:reproductive fruiting body development; IEP:UniProtKB.
DR InterPro; IPR012475; Fungal_lectin.
DR Pfam; PF07938; Fungal_lectin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Fruiting body; Lectin; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2666154"
FT CHAIN 2..313
FT /note="Fucose-specific lectin"
FT /id="PRO_0000084401"
FT REPEAT 5..57
FT /note="1"
FT /evidence="ECO:0000305|PubMed:12732625,
FT ECO:0000305|PubMed:14503859, ECO:0000305|PubMed:2193930"
FT REPEAT 58..109
FT /note="2"
FT /evidence="ECO:0000305|PubMed:12732625,
FT ECO:0000305|PubMed:14503859, ECO:0000305|PubMed:2193930"
FT REPEAT 110..162
FT /note="3"
FT /evidence="ECO:0000305|PubMed:12732625,
FT ECO:0000305|PubMed:14503859, ECO:0000305|PubMed:2193930"
FT REPEAT 163..208
FT /note="4"
FT /evidence="ECO:0000305|PubMed:12732625,
FT ECO:0000305|PubMed:14503859, ECO:0000305|PubMed:2193930"
FT REPEAT 209..260
FT /note="5"
FT /evidence="ECO:0000305|PubMed:12732625,
FT ECO:0000305|PubMed:14503859, ECO:0000305|PubMed:2193930"
FT REPEAT 261..304
FT /note="6"
FT /evidence="ECO:0000305|PubMed:12732625,
FT ECO:0000305|PubMed:14503859, ECO:0000305|PubMed:2193930"
FT REGION 5..304
FT /note="6 X approximate tandem repeats"
FT /evidence="ECO:0000305|PubMed:12732625,
FT ECO:0000305|PubMed:14503859, ECO:0000305|PubMed:2193930"
FT BINDING 25
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 37
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 78
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 78
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 90
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 90
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 98
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 102
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 102
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUB,
FT ECO:0007744|PDB:1IUC, ECO:0007744|PDB:1OFZ"
FT BINDING 132
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 147
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 154
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 154
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 180
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 192
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 200
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 204
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 227
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 239
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 246
FT /ligand="alpha-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42548"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0000269|PubMed:14503859, ECO:0007744|PDB:1IUC,
FT ECO:0007744|PDB:1OFZ"
FT BINDING 299
FT /ligand="beta-L-fucose"
FT /ligand_id="ChEBI:CHEBI:42589"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:12732625,
FT ECO:0007744|PDB:1OFZ"
FT MUTAGEN 7
FT /note="Y->R: Impairs homodimerization."
FT /evidence="ECO:0000269|PubMed:20798114"
FT MUTAGEN 225
FT /note="N->Q: Leads to increased binding to fucosylated
FT glycans."
FT /evidence="ECO:0000269|PubMed:21945439,
FT ECO:0000269|PubMed:27650323"
FT MUTAGEN 284
FT /note="S->D: Impairs homodimerization."
FT /evidence="ECO:0000269|PubMed:20798114"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:6GKE"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:1OFZ"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6GKE"
FT HELIX 102..106
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:1IUC"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 143..164
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 178..185
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 214..220
FT /evidence="ECO:0007829|PDB:6GKE"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 237..246
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:6GKE"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:6GKE"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:6GKE"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6GKE"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6GKE"
SQ SEQUENCE 313 AA; 33529 MW; 06839A365AA0CAE5 CRC64;
MPTEFLYTSK IAAISWAATG GRQQRVYFQD LNGKIREAQR GGDNPWTGGS SQNVIGEAKL
FSPLAAVTWK SAQGIQIRVY CVNKDNILSE FVYDGSKWIT GQLGSVGVKV GSNSKLAALQ
WGGSESAPPN IRVYYQKSNG SGSSIHEYVW SGKWTAGASF GSTVPGTGIG ATAIGPGRLR
IYYQATDNKI REHCWDSNSW YVGGFSASAS AGVSIAAISW GSTPNIRVYW QKGREELYEA
AYGGSWNTPG QIKDASRPTP SLPDTFIAAN SSGNIDISVF FQASGVSLQQ WQWISGKGWS
IGAVVPTGTP AGW
