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P02873 (LEA1_PHAVU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-amylase inhibitor 1

Short name=Alpha-AI-1
Short name=Alpha-AI1
Alternative name(s):
Lectin
Gene names
Name:LLP
Synonyms:Alpha-AI1
OrganismPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifier3885 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Lectin and alpha-amylase inhibitor. Acts as a defensive protein against insects. Ref.6

Subunit structure

Heterodimer of chain 1 and chain 2. Ref.6

Post-translational modification

Proteolytic processing yields active form.

Biotechnological use

Sold as a diet aid under the name of 'Phaseolamin' or 'Phase 2'.

Sequence similarities

Belongs to the leguminous lectin family.

Ontologies

Keywords
   DomainSignal
   LigandLectin
   Molecular functionAlpha-amylase inhibitor
   PTMGlycoprotein
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functionalpha-amylase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

carbohydrate binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.4 Ref.5 Ref.6
Chain24 – 10077Alpha-amylase inhibitor 1 chain 1
PRO_0000017627
Chain101 – 239139Alpha-amylase inhibitor 1 chain 2
PRO_0000017628
Propeptide240 – 2467
PRO_0000017629

Amino acid modifications

Glycosylation351N-linked (GlcNAc...) Ref.8
Glycosylation881N-linked (GlcNAc...) Ref.8
Glycosylation1631N-linked (GlcNAc...) Ref.8

Experimental info

Sequence conflict301I → N AA sequence Ref.5
Sequence conflict731Q → R in CAD28835. Ref.3
Sequence conflict1421K → E in CAD28835. Ref.3
Sequence conflict1961D → N Ref.2

Secondary structure

.......................................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02873 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: EA56F15EF1F78788

FASTA24627,207
        10         20         30         40         50         60 
MIMASSKLLS LALFLALLSH ANSATETSFI IDAFNKTNLI LQGDATVSSN GNLQLSYNSY 

        70         80         90        100        110        120 
DSMSRAFYSA PIQIRDSTTG NVASFDTNFT MNIRTHRQAN SAVGLDFVLV PVQPESKGDT 

       130        140        150        160        170        180 
VTVEFDTFLS RISIDVNNND IKSVPWDVHD YDGQNAEVRI TYNSSTKVFS VSLSNPSTGK 

       190        200        210        220        230        240 
SNNVSTTVEL EKEVYDWVSV GFSATSGAYQ WSYETHDVLS WSFSSKFINL KDQKSERSNI 


VLNKIL 

« Hide

References

[1]"Structure of a chromosomal Phaseolus vulgaris lectin gene and its transcript."
Hoffman L.M.
J. Mol. Appl. Genet. 2:447-453(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Tendergreen.
[2]"Molecular cloning of Phaseolus vulgaris lectin mRNA and use of cDNA as a probe to estimate lectin transcript levels in various tissues."
Hoffman L.M., Ma Y., Barker R.F.
Nucleic Acids Res. 10:7819-7828(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Tendergreen.
[3]"Arcelin and other members of lectin family in wild Phaseolus vulgaris."
Lioi L., Galasso I., Lanave C., Sparvoli F., Bollini R.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-246.
Tissue: Leaf.
[4]"A lectin gene encodes the alpha-amylase inhibitor of the common bean."
Moreno J., Chrispeels M.J.
Proc. Natl. Acad. Sci. U.S.A. 86:7885-7889(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-34 AND 101-115.
Strain: cv. Greensleeves.
Tissue: Seed.
[5]"Isolation and characterization of the subunits of a heat-labile alpha-amylase inhibitor from Phaseolus vulgaris white kidney bean."
Yamaguchi H.
Biosci. Biotechnol. Biochem. 57:297-302(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-32 AND 101-109.
Strain: cv. Tebo.
Tissue: Seed.
[6]Kluh I., Horn M., Voburka Z.
Submitted (DEC-2003) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 24-99 AND 101-231, FUNCTION, SUBUNIT, GLYCOSYLATION.
Strain: cv. Magna.
Tissue: Seed.
[7]"Location of the active site of the bean alpha-amylase inhibitor and involvement of a Trp, Arg, Tyr triad."
Mirkov T.E., Evans S.V., Wahlstrom J., Gomez L., Young N.M., Chrispeels M.J.
Glycobiology 5:45-50(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[8]"Post-translational processing of two alpha-amylase inhibitors and an arcelin from the common bean, Phaseolus vulgaris."
Young N.M., Thibault P., Watson D.C., Chrispeels M.J.
FEBS Lett. 446:203-206(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING OF C-TERMINAL, GLYCOSYLATION AT ASN-35; ASN-88 AND ASN-163.
[9]"Substrate mimicry in the active center of a mammalian alpha-amylase: structural analysis of an enzyme-inhibitor complex."
Bompard-Gilles C., Rousseau P., Rouge P., Payan F.
Structure 4:1441-1452(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF COMPLEX WITH PIG ALPHA-AMYLASE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01261 Genomic DNA. Translation: AAA33769.1.
AJ439614 Genomic DNA. Translation: CAD28835.1.
PIRLNFB. A03365.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DHKX-ray1.85B24-246[»]
1VIWX-ray3.00B24-228[»]
ProteinModelPortalP02873.
SMRP02873. Positions 24-228.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-88091.

Protein family/group databases

Allergome2946. Pha v aAI.
8208. Pha v aAI.0101.

PTM databases

UniCarbKBP02873.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.200. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02873.

Entry information

Entry nameLEA1_PHAVU
AccessionPrimary (citable) accession number: P02873
Secondary accession number(s): Q8RVY2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 16, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references