P83886 · ASAL_ALLSA
- ProteinMannose-specific lectin
- GeneLECASAL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids181 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mannose-specific lectin (PubMed:17265166, PubMed:9037141).
Shows agglutinating activity towards rabbit erythrocytes (PubMed:35398454, PubMed:9037141).
However, it does not show agglutinating activity towards human erythrocytes (PubMed:9037141).
Has insecticidal activity against the cotton leafworm S.littoralis and the peach potato aphid M.persicae (PubMed:17147631, PubMed:17265166).
Also displays antiviral activity and therefore may contribute to defense against infections (PubMed:35398454).
Shows agglutinating activity towards rabbit erythrocytes (PubMed:35398454, PubMed:9037141).
However, it does not show agglutinating activity towards human erythrocytes (PubMed:9037141).
Has insecticidal activity against the cotton leafworm S.littoralis and the peach potato aphid M.persicae (PubMed:17147631, PubMed:17265166).
Also displays antiviral activity and therefore may contribute to defense against infections (PubMed:35398454).
Miscellaneous
Has an inhibitory effect on SARS-CoV-2 in Vero E6 cells (IC50=4 ug/ml) (PubMed:35398454).
Viral replication is inhibited by 80% at a concentration of 20 ug/ml, and 50% inhibition is observed at concentrations of 5 ug/ml and 10 ug/ml (PubMed:35398454).
Viral replication is inhibited by 80% at a concentration of 20 ug/ml, and 50% inhibition is observed at concentrations of 5 ug/ml and 10 ug/ml (PubMed:35398454).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 56 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 58 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 60 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 64 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 71 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 72 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 74 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 88 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 90 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 92 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 96 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 103 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 104 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 107 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 114 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 120 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 122 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 124 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 128 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 133 | alpha-D-mannopyranose (UniProtKB | ChEBI) | ||||
Sequence: W |
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | D-mannose binding | |
Molecular Function | protein homodimerization activity | |
Biological Process | cell-cell adhesion | |
Biological Process | defense response to insect | |
Biological Process | defense response to virus | |
Biological Process | regulation of defense response to virus |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameMannose-specific lectin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Asparagales > Amaryllidaceae > Allioideae > Allieae > Allium
Accessions
- Primary accessionP83886
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-30 | |||||
Sequence: MGRTTSSPKAMMRIATVAAILTILASTCMA | ||||||
Chain | PRO_0000064564 | 31-181 | Mannose-specific lectin | |||
Sequence: RNVLTNGEGLYAGQSLDVEQYKFIMQDDCNLVLYEYSTPIWASNTGVTGKNGCRAVMQRDGNFVVYDVNGRPVWASNSVRGNGNYILVLQKDRNVVIYGSDIWSTGTYRRSVGGAVVMAMNGTVDGGSVIGPVVVNQNVTAAIRKVGTGAA | ||||||
Disulfide bond | 59↔83 | |||||
Sequence: CNLVLYEYSTPIWASNTGVTGKNGC |
Keywords
- PTM
Interaction
Structure
Family & Domains
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P83886-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length181
- Mass (Da)19,282
- Last updated2008-01-15 v3
- Checksum4D89A957F75A753D
P83886-2
- Name2
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 2; ABF70332 | ||||
Sequence: R → P | ||||||
Sequence conflict | 32-34 | in Ref. 5; AA sequence | ||||
Sequence: NVL → MIP | ||||||
Sequence conflict | 33 | in Ref. 1; AAB64237, 3; AAW48531 and 4; AAR23523 | ||||
Sequence: V → L | ||||||
Sequence conflict | 47 | in Ref. 1; AA sequence | ||||
Sequence: D → N | ||||||
Sequence conflict | 56-59 | in Ref. 5; AA sequence | ||||
Sequence: QDDC → RPDD | ||||||
Sequence conflict | 98 | in Ref. 6; AA sequence | ||||
Sequence: V → R | ||||||
Sequence conflict | 114 | in Ref. 4; AAR23523 | ||||
Sequence: N → S | ||||||
Sequence conflict | 118 | in Ref. 1; AAB64237 and 4; AAR23523 | ||||
Sequence: V → L | ||||||
Sequence conflict | 121 | in Ref. 1; AAB64237 and 4; AAR23523 | ||||
Sequence: K → E | ||||||
Alternative sequence | VSP_030211 | 138-148 | in isoform 2 | |||
Sequence: YRRSVGGAVVM → LLEHRVPTSFY | ||||||
Alternative sequence | VSP_030212 | 149-181 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 168-169 | in Ref. 2; ABF70332 | ||||
Sequence: NV → KD | ||||||
Sequence conflict | 178 | in Ref. 1; AAB64237 | ||||
Sequence: T → S |
Mass Spectrometry
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U58947 EMBL· GenBank· DDBJ | AAB64237.1 EMBL· GenBank· DDBJ | mRNA | ||
U58948 EMBL· GenBank· DDBJ | AAB64238.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ525625 EMBL· GenBank· DDBJ | ABF70332.1 EMBL· GenBank· DDBJ | mRNA | ||
AY866499 EMBL· GenBank· DDBJ | AAW48531.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AY376827 EMBL· GenBank· DDBJ | AAR23523.1 EMBL· GenBank· DDBJ | mRNA |