Fucose-specific lectin

Functionⁱ

Lectin that specifically binds to L-fucose (PubMed:2193930, PubMed:2666154, PubMed:7397108, PubMed:18493851, PubMed:21945439, PubMed:27650323, PubMed:28800497, PubMed:14503859, PubMed:12732625). Has strongest preference for the alpha-1,6-fucosylated chain (core fucose) on glycoproteins among alpha-1,2-, alpha-1,3-, alpha-1,4-, and alpha-1,6-fucosylated chains (PubMed:17383961, PubMed:19109923, PubMed:20798114, PubMed:22226468). Might play a role in the differentiation of the fruiting body (PubMed:2193930). Exhibits antifungal activity against Mucor racemosus and thus could act as an antifungal protein in natural ecosystems (PubMed:22738968).14 Publications

Sites

Feature key	Position(s)	DescriptionActions	Length
Binding siteⁱ	25	Carbohydrate 1Combined sources2 Publications	1
Binding siteⁱ	37	Carbohydrate 1Combined sources2 Publications	1
Binding siteⁱ	73	FucoseCombined sources1 Publication	1
Binding siteⁱ	78	Carbohydrate 2Combined sources2 Publications	1
Binding siteⁱ	90	Carbohydrate 2Combined sources2 Publications	1
Binding siteⁱ	93	beta-L-fucose 1Combined sources2 Publications	1
Binding siteⁱ	98	Carbohydrate 1Combined sources2 Publications	1
Binding siteⁱ	102	Carbohydrate 2; via amide nitrogenCombined sources2 Publications	1
Binding siteⁱ	105	Carbohydrate 3; via carbonyl oxygenCombined sources	1
Binding siteⁱ	132	Carbohydrate 4Combined sources1 Publication	1
Binding siteⁱ	147	Carbohydrate 4Combined sources1 Publication	1
Binding siteⁱ	150	Carbohydrate 2Combined sources1 Publication	1
Binding siteⁱ	154	Carbohydrate 2Combined sources2 Publications	1
Binding siteⁱ	195	Carbohydrate 4Combined sources1 Publication	1
Binding siteⁱ	200	Carbohydrate 4Combined sources1 Publication	1
Binding siteⁱ	204	Carbohydrate 4; via amide nitrogenCombined sources2 Publications	1
Binding siteⁱ	227	Carbohydrate 3Combined sources1 Publication	1
Binding siteⁱ	239	Carbohydrate 5Combined sources1 Publication	1
Binding siteⁱ	299	Carbohydrate 3Combined sources1 Publication	1

GO - Molecular functionⁱ

carbohydrate binding Source: UniProtKB-KW

Complete GO annotation on QuickGO ...

Keywordsⁱ

Ligand	Lectin

Ligand

Lectin

Protein family/group databases

UniLectinⁱ	P18891

UniLectinⁱ

P18891

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Fucose-specific lectin1 Publication Alternative name(s): Aleuria aurantia lectin1 Publication Short name: AAL1 Publication
Organismⁱ	Aleuria aurantia (Orange peel mushroom)
Taxonomic identifierⁱ	5188 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › Pezizomycetes › Pezizales › Pyronemataceae › Aleuria

Pathology & Biotechⁱ

Biotechnological useⁱ

AAL's binding activity could be used to identify secreted fucosylated glycoproteins that may represent candidate biomarkers for cancer since fucosylation of N-linked glycans has been associated with several types of cancer such as liver cancer (PubMed:22789673, PubMed:24027776, PubMed:27650323).3 Publications

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	7	Y → R: Impairs homodimerization. 1 Publication	1
Mutagenesisⁱ	225	N → Q: Leads to increased binding to fucosylated glycans. 2 Publications	1
Mutagenesisⁱ	284	S → D: Impairs homodimerization. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Initiator methionineⁱ		Removed1 Publication
ChainⁱPRO_0000084401	2 – 313	Fucose-specific lectinAdd BLAST		312

Proteomic databases

PRIDEⁱ	P18891

PRIDEⁱ

P18891

Expressionⁱ

Developmental stageⁱ

AAL is detected in fruiting bodies but not in mycelia (PubMed:2193930).1 Publication

Keywords - Developmental stageⁱ

Fruiting body

Interactionⁱ

Subunit structureⁱ

Forms homodimers (PubMed:2193930, PubMed:7397108, PubMed:20798114, PubMed:12732625). The two AAL monomers are associated via interactions between N-terminal and C-terminal peptides (PubMed:12732625). Tyr-7 interacts via aromatic ring stacking with its counterpart on the other monomer, whereas Ser-284 interacts via hydrogen bonding with Asp-264 on the other monomer (PubMed:12732625).

4 Publications

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	11 – 16	Combined sources	6
Beta strandⁱ	23 – 30	Combined sources	8
Beta strandⁱ	33 – 41	Combined sources	9
Helixⁱ	51 – 53	Combined sources	3
Beta strandⁱ	54 – 57	Combined sources	4
Beta strandⁱ	65 – 71	Combined sources	7
Beta strandⁱ	74 – 82	Combined sources	9
Beta strandⁱ	87 – 96	Combined sources	10
Beta strandⁱ	98 – 100	Combined sources	3
Helixⁱ	102 – 106	Combined sources	5
Beta strandⁱ	117 – 122	Combined sources	6
Beta strandⁱ	124 – 127	Combined sources	4
Beta strandⁱ	130 – 135	Combined sources	6
Beta strandⁱ	143 – 164	Combined sources	22
Beta strandⁱ	169 – 175	Combined sources	7
Beta strandⁱ	178 – 185	Combined sources	8
Beta strandⁱ	188 – 198	Combined sources	11
Beta strandⁱ	200 – 202	Combined sources	3
Beta strandⁱ	214 – 220	Combined sources	7
Turnⁱ	221 – 224	Combined sources	4
Beta strandⁱ	225 – 231	Combined sources	7
Beta strandⁱ	237 – 246	Combined sources	10
Beta strandⁱ	250 – 252	Combined sources	3
Beta strandⁱ	268 – 272	Combined sources	5
Turnⁱ	273 – 275	Combined sources	3
Beta strandⁱ	276 – 283	Combined sources	8
Turnⁱ	284 – 286	Combined sources	3
Beta strandⁱ	287 – 294	Combined sources	8
Turnⁱ	295 – 297	Combined sources	3
Beta strandⁱ	298 – 301	Combined sources	4

Show more details

3D structure databases

SMRⁱ	P18891
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P18891

EvolutionaryTraceⁱ

P18891

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Repeatⁱ	5 – 57	13 PublicationsAdd BLAST	53
Repeatⁱ	58 – 109	23 PublicationsAdd BLAST	52
Repeatⁱ	110 – 162	33 PublicationsAdd BLAST	53
Repeatⁱ	163 – 208	43 PublicationsAdd BLAST	46
Repeatⁱ	209 – 260	53 PublicationsAdd BLAST	52
Repeatⁱ	261 – 304	63 PublicationsAdd BLAST	44

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	5 – 304	6 X approximate tandem repeats3 PublicationsAdd BLAST		300
Regionⁱ	242 – 246	Fucose bindingCombined sources1 Publication		5

Domainⁱ

AAL adopts the six-bladed beta-propeller fold and contains 5 binding sites per monomer, each located between two adjacent blades (PubMed:14503859, PubMed:12732625). Residues conserved at 5 of the 6 sites, are located on the surface of the AAL and directly contribute to fucose recognition (PubMed:14503859). Because the corresponding residues forming site 6 are not conserved, this site cannot be considered to accommodate fucose molecules (PubMed:14503859). The 5 binding sites that are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition (PubMed:18493851, PubMed:12732625).3 Publications

Sequence similaritiesⁱ

Belongs to the fungal fucose-specific lectin family.Curated

Keywords - Domainⁱ

Repeat

Family and domain databases

InterProⁱ	View protein in InterPro IPR012475 Fungal_lectin
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF07938 Fungal_lectin, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P18891-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPTEFLYTSK IAAISWAATG GRQQRVYFQD LNGKIREAQR GGDNPWTGGS 
        60         70         80         90        100
SQNVIGEAKL FSPLAAVTWK SAQGIQIRVY CVNKDNILSE FVYDGSKWIT 
       110        120        130        140        150
GQLGSVGVKV GSNSKLAALQ WGGSESAPPN IRVYYQKSNG SGSSIHEYVW 
       160        170        180        190        200
SGKWTAGASF GSTVPGTGIG ATAIGPGRLR IYYQATDNKI REHCWDSNSW 
       210        220        230        240        250
YVGGFSASAS AGVSIAAISW GSTPNIRVYW QKGREELYEA AYGGSWNTPG 
       260        270        280        290        300
QIKDASRPTP SLPDTFIAAN SSGNIDISVF FQASGVSLQQ WQWISGKGWS 
       310 
IGAVVPTGTP AGW

Length:313

Mass (Da):33,529

Last modified:January 23, 2007 - v3

Checksum:ⁱ06839A365AA0CAE5

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D00573 mRNA Translation: BAA00451.1 D85776 Genomic DNA Translation: BAA12871.1
PIRⁱ	JX0096

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	D00573 mRNA Translation: BAA00451.1 D85776 Genomic DNA Translation: BAA12871.1
PIRⁱ	JX0096

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1IUB	X-ray	2.31	A	2-313	[»]
	1IUC	X-ray	2.24	A	2-313	[»]
	1OFZ	X-ray	1.50	A/B	2-313	[»]
	5MXC	X-ray	1.14	A	1-313	[»]
	6GKE	X-ray	1.08	A	2-313	[»]
SMRⁱ	P18891
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein family/group databases

UniLectinⁱ	P18891

UniLectinⁱ

P18891

Proteomic databases

PRIDEⁱ	P18891

PRIDEⁱ

P18891

Miscellaneous databases

EvolutionaryTraceⁱ	P18891

EvolutionaryTraceⁱ

P18891

Family and domain databases

InterProⁱ	View protein in InterPro IPR012475 Fungal_lectin
Pfamⁱ	View protein in Pfam PF07938 Fungal_lectin, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	LECF_ALEAU
Accessionⁱ	P18891Primary (citable) accession number: P18891
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
	Last sequence update:	January 23, 2007
	Last modified:	September 18, 2019
	This is version 76 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Fungal Protein Annotation Program

UniProtKB

UniParc

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Supporting data

UniProtKB - P18891 (LECF_ALEAU)

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Protein family/group databases

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Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

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Keywords - Developmental stagei

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Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Family and domain databases

Sequence databases

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Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Miscellaneous databases

Family and domain databases

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Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

Biotechnological useⁱ

PTM / Processingⁱ

Expressionⁱ

Keywords - Developmental stageⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ