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Protein

Agaricus bisporus lectin

Gene
N/A
Organism
Agaricus bisporus (White button mushroom)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Lectin that recognizes O-linked galactose-beta-1,3-N-acetylgalactosamine, a disaccharide (Thomsen-Friedenreich antigen or T-disaccharide), present on cell surface glycoproteins. Can also bind galactose-beta-1,3-N-acetylglucosamine. Does not bind monosaccharides. Can be internalized by clathrin-coated vesicles after binding to surface glycoproteins. After internalization it inhibits nuclear import of nuclear localization signal dependent proteins. Inhibits proliferation of malignant cells without cytotoxicity for normal cells.3 Publications

Miscellaneous

Each monomer has 2 distinct carbohydrate binding sites, one for galactose-beta-1,3-N-acetylgalactosamine and another for galactose-beta-1,3-N-acetylglucosamine.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei48Carbohydrate 1; T-antigen1 Publication1
Binding sitei73Carbohydrate 1; T-antigen1 Publication1
Binding sitei82Carbohydrate 2; N-acetylglucosamine1 Publication1
Binding sitei103Carbohydrate 2; N-acetylglucosamine1 Publication1
Binding sitei114Carbohydrate 2; N-acetylglucosamine1 Publication1

GO - Molecular functioni

Keywordsi

Molecular functionHemagglutinin
LigandLectin

Protein family/group databases

UniLectiniQ00022

Names & Taxonomyi

Protein namesi
Recommended name:
Agaricus bisporus lectin
Short name:
ABL
Alternative name(s):
Agaricus bisporus agglutinin
Short name:
ABA
Gal-beta-1,3-GalNAc-binding lectin
TF antigen-binding lectin
OrganismiAgaricus bisporus (White button mushroom)
Taxonomic identifieri5341 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesAgaricaceaeAgaricus

Pathology & Biotechi

Biotechnological usei

Lectins can be used to recognize and purifiy specific glycoproteins, and for the purification of cells with specific surface glycoproteins. Has potential as anti-proliferative agent. Sold under the name lectin from Agaricus bisporus by Sigma-Aldrich and under the name of Agaricus bisporus (Mushroom) agglutinin (ABA) by USBiological.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00002230942 – 143Agaricus bisporus lectinAdd BLAST142

Proteomic databases

PRIDEiQ00022

Interactioni

Subunit structurei

Homotetramer.1 Publication

Structurei

Secondary structure

1143
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ00022
SMRiQ00022
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00022

Family & Domainsi

Sequence similaritiesi

Belongs to the fungal fruit body lectin family.Curated

Family and domain databases

Gene3Di2.60.270.20, 1 hit
InterProiView protein in InterPro
IPR015926 Cytolysin/lectin
IPR009960 Fruit_body_lectin_fun
PfamiView protein in Pfam
PF07367 FB_lectin, 1 hit
SUPFAMiSSF63724 SSF63724, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q00022-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTYTISIRVY QTTPKGFFRP VERTNWKYAN GGTWDEVRGE YVLTMGGSGT
60 70 80 90 100
SGSLRFVSSD TDESFVATFG VHNYKRWCDI VTNLTNEQTA LVINQEYYGV
110 120 130 140
PIRDQARENQ LTSYNVANAK GRRFAIEYTV TEGDNLKANL IIG
Length:143
Mass (Da):16,185
Last modified:January 23, 2007 - v3
Checksum:i5704CFD273E1FB78
GO

Sequence cautioni

The sequence AAA85813 differs from that shown. Reason: Frameshift at position 134. Frameshift correction allows the C-terminal sequence to be compatible with the results of mass spectrometry and X-ray crystallography.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64S → I in AAA85813 (PubMed:7770537).Curated1
Sequence conflicti134 – 143DNLKANLIIG → IISRPISSSDKCFIRLPSQK S AA sequence (PubMed:7770537).Curated10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14936 mRNA Translation: AAA85813.1 Frameshift.

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14936 mRNA Translation: AAA85813.1 Frameshift.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y2TX-ray1.50A/B2-133[»]
1Y2UX-ray1.85A/B2-143[»]
1Y2VX-ray1.90A/B2-143[»]
1Y2WX-ray1.74A/B2-143[»]
1Y2XX-ray2.36A/B/C/D2-143[»]
ProteinModelPortaliQ00022
SMRiQ00022
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

UniLectiniQ00022

Proteomic databases

PRIDEiQ00022

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ00022

Family and domain databases

Gene3Di2.60.270.20, 1 hit
InterProiView protein in InterPro
IPR015926 Cytolysin/lectin
IPR009960 Fruit_body_lectin_fun
PfamiView protein in Pfam
PF07367 FB_lectin, 1 hit
SUPFAMiSSF63724 SSF63724, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiABL_AGABI
AccessioniPrimary (citable) accession number: Q00022
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 78 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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