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UniProtKB - P18891 (LECF_ALEAU)

Entry version 83 (25 May 2022)
Sequence version 3 (23 Jan 2007)
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Protein

Fucose-specific lectin

Gene
N/A
Organism
Aleuria aurantia (Orange peel mushroom)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei25beta-L-fucose 1Combined sources2 Publications1
Binding sitei37beta-L-fucose 1Combined sources2 Publications1
Binding sitei78alpha-L-fucose 1Combined sources1 Publication1
Binding sitei78beta-L-fucose 2Combined sources2 Publications1
Binding sitei90alpha-L-fucose 1Combined sources1 Publication1
Binding sitei90beta-L-fucose 2Combined sources2 Publications1
Binding sitei98beta-L-fucose 1Combined sources2 Publications1
Binding sitei102alpha-L-fucose 1; via amide nitrogenCombined sources1 Publication1
Binding sitei102beta-L-fucose 2; via amide nitrogenCombined sources2 Publications1
Binding sitei132beta-L-fucose 3Combined sources1 Publication1
Binding sitei147beta-L-fucose 3Combined sources1 Publication1
Binding sitei154alpha-L-fucose 1Combined sources1 Publication1
Binding sitei154beta-L-fucose 2Combined sources2 Publications1
Binding sitei180alpha-L-fucose 2Combined sources2 Publications1
Binding sitei192alpha-L-fucose 2Combined sources2 Publications1
Binding sitei200beta-L-fucose 3Combined sources1 Publication1
Binding sitei204alpha-L-fucose 2; via amide nitrogenCombined sources2 Publications1
Binding sitei227beta-L-fucose 4Combined sources1 Publication1
Binding sitei239beta-L-fucose 4Combined sources1 Publication1
Binding sitei246alpha-L-fucose 2Combined sources2 Publications1
Binding sitei299beta-L-fucose 4Combined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandLectin

Protein family/group databases

UniLectin database of carbohydrate-binding proteins

More...UniLectini		P18891

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Fucose-specific lectin1 Publication
Alternative name(s):
Aleuria aurantia lectin1 Publication
Short name:
AAL1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAleuria aurantia (Orange peel mushroom)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri5188 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Pezizomycetes › Pezizales › Pyronemataceae › Aleuria

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>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). Identified as one of the several suitable fluorescently labeled lectins that can be used in a combination for the visualization and quantification of extracellular glycoconjugates in dental supragingival biofilms grown for 48 hours in situ in the absence of dietary carbohydrates (PubMed:28748044).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi7Y → R: Impairs homodimerization. 1 Publication1
Mutagenesisi225N → Q: Leads to increased binding to fucosylated glycans. 2 Publications1
Mutagenesisi284S → D: Impairs homodimerization. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000844012 – 313Fucose-specific lectinAdd BLAST312

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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

Keywords - Developmental stagei

Fruiting body

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P18891

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P18891

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P18891

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati5 – 5713 PublicationsAdd BLAST53
Repeati58 – 10923 PublicationsAdd BLAST52
Repeati110 – 16233 PublicationsAdd BLAST53
Repeati163 – 20843 PublicationsAdd BLAST46
Repeati209 – 26053 PublicationsAdd BLAST52
Repeati261 – 30463 PublicationsAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni5 – 3046 X approximate tandem repeats3 PublicationsAdd BLAST300

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<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

Belongs to the fungal fucose-specific lectin family.Curated

Keywords - Domaini

Repeat

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012475, Fungal_lectin

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07938, Fungal_lectin, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P18891-1 [UniParc]FASTAAdd 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i06839A365AA0CAE5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
D00573 mRNA Translation: BAA00451.1
D85776 Genomic DNA Translation: BAA12871.1

Protein sequence database of the Protein Information Resource

More...PIRi		JX0096

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00573 mRNA Translation: BAA00451.1
D85776 Genomic DNA Translation: BAA12871.1
PIRiJX0096

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 entryMethodResolution (Å)ChainPositionsPDBsum
1IUBX-ray2.31A2-313[»]
1IUCX-ray2.24A2-313[»]
1OFZX-ray1.50A/B2-313[»]
5MXCX-ray1.14A1-313[»]
6GKEX-ray1.08A2-313[»]
AlphaFoldDBiP18891
SMRiP18891
ModBaseiSearch...
PDBe-KBiSearch...

Protein family/group databases

UniLectiniP18891

Miscellaneous databases

EvolutionaryTraceiP18891

Family and domain databases

InterProiView protein in InterPro
IPR012475, Fungal_lectin
PfamiView protein in Pfam
PF07938, Fungal_lectin, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLECF_ALEAU
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P18891
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 83 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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