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Protein

Fucose-specific lectin

Gene
N/A
Organism
Aleuria aurantia (Orange peel mushroom)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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
Binding sitei25Carbohydrate 1Combined sources2 Publications1
Binding sitei37Carbohydrate 1Combined sources2 Publications1
Binding sitei73FucoseCombined sources1 Publication1
Binding sitei78Carbohydrate 2Combined sources2 Publications1
Binding sitei90Carbohydrate 2Combined sources2 Publications1
Binding sitei93beta-L-fucose 1Combined sources2 Publications1
Binding sitei98Carbohydrate 1Combined sources2 Publications1
Binding sitei102Carbohydrate 2; via amide nitrogenCombined sources2 Publications1
Binding sitei105Carbohydrate 3; via carbonyl oxygenCombined sources1
Binding sitei132Carbohydrate 4Combined sources1 Publication1
Binding sitei147Carbohydrate 4Combined sources1 Publication1
Binding sitei150Carbohydrate 2Combined sources1 Publication1
Binding sitei154Carbohydrate 2Combined sources2 Publications1
Binding sitei195Carbohydrate 4Combined sources1 Publication1
Binding sitei200Carbohydrate 4Combined sources1 Publication1
Binding sitei204Carbohydrate 4; via amide nitrogenCombined sources2 Publications1
Binding sitei227Carbohydrate 3Combined sources1 Publication1
Binding sitei239Carbohydrate 5Combined sources1 Publication1
Binding sitei299Carbohydrate 3Combined sources1 Publication1

GO - Molecular functioni

Keywordsi

LigandLectin

Names & Taxonomyi

Protein namesi
Recommended name:
Fucose-specific lectin1 Publication
Alternative name(s):
Aleuria aurantia lectin1 Publication
Short name:
AAL1 Publication
OrganismiAleuria aurantia (Orange peel mushroom)
Taxonomic identifieri5188 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaPezizomycetesPezizalesPyronemataceaeAleuria

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 keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi7Y → R: Impairs homodimerization. 1 Publication1
Mutagenesisi225N → Q: Leads to increased binding to fucosylated glycans. 2 Publications1
Mutagenesisi284S → D: Impairs homodimerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000844012 – 313Fucose-specific lectinAdd BLAST312

Proteomic databases

PRIDEiP18891

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

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 16Combined sources6
Beta strandi23 – 30Combined sources8
Beta strandi33 – 41Combined sources9
Helixi51 – 53Combined sources3
Beta strandi54 – 57Combined sources4
Beta strandi65 – 71Combined sources7
Beta strandi74 – 82Combined sources9
Beta strandi87 – 96Combined sources10
Beta strandi98 – 100Combined sources3
Helixi102 – 106Combined sources5
Beta strandi117 – 121Combined sources5
Beta strandi124 – 127Combined sources4
Beta strandi130 – 135Combined sources6
Beta strandi143 – 164Combined sources22
Beta strandi169 – 175Combined sources7
Beta strandi178 – 185Combined sources8
Beta strandi188 – 198Combined sources11
Beta strandi200 – 202Combined sources3
Beta strandi214 – 220Combined sources7
Turni221 – 224Combined sources4
Beta strandi225 – 231Combined sources7
Beta strandi237 – 246Combined sources10
Beta strandi250 – 252Combined sources3
Beta strandi268 – 272Combined sources5
Turni273 – 275Combined sources3
Beta strandi276 – 283Combined sources8
Turni284 – 286Combined sources3
Beta strandi287 – 294Combined sources8
Turni295 – 297Combined sources3
Beta strandi298 – 301Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IUBX-ray2.31A2-313[»]
1IUCX-ray2.24A2-313[»]
1OFZX-ray1.50A/B2-313[»]
5MXCX-ray1.14A1-313[»]
ProteinModelPortaliP18891
SMRiP18891
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18891

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Regioni5 – 3046 X approximate tandem repeats3 PublicationsAdd BLAST300
Regioni242 – 246Fucose bindingCombined sources1 Publication5

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

Keywords - Domaini

Repeat

Family and domain databases

InterProiView protein in InterPro
IPR012475 Fungal_lectin
PfamiView 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]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
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
PIRiJX0096

Entry informationi

Entry nameiLECF_ALEAU
AccessioniPrimary (citable) accession number: P18891
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 72 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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