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Protein

Alpha-amylase inhibitor 1

Gene

LLP

Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Lectin and alpha-amylase inhibitor. Acts as a defensive protein against insects.1 Publication

GO - Molecular functioni

  1. alpha-amylase inhibitor activity Source: UniProtKB-KW
  2. carbohydrate binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Alpha-amylase inhibitor

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-amylase inhibitor 1
Short name:
Alpha-AI-1
Short name:
Alpha-AI1
Alternative name(s):
Lectin
Cleaved into the following 2 chains:
Gene namesi
Name:LLP
Synonyms:Alpha-AI1
OrganismiPhaseolus vulgaris (Kidney bean) (French bean)
Taxonomic identifieri3885 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaePhaseolus

Pathology & Biotechi

Biotechnological usei

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

Protein family/group databases

Allergomei2946. Pha v aAI.
8208. Pha v aAI.0101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23233 PublicationsAdd
BLAST
Chaini24 – 10077Alpha-amylase inhibitor 1 chain 1PRO_0000017627Add
BLAST
Chaini101 – 239139Alpha-amylase inhibitor 1 chain 2PRO_0000017628Add
BLAST
Propeptidei240 – 2467PRO_0000017629

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi35 – 351N-linked (GlcNAc...)1 Publication
Glycosylationi88 – 881N-linked (GlcNAc...)1 Publication
Glycosylationi163 – 1631N-linked (GlcNAc...)1 Publication

Post-translational modificationi

Proteolytic processing yields active form.1 Publication

Keywords - PTMi

Glycoprotein

PTM databases

UniCarbKBiP02873.

Interactioni

Subunit structurei

Heterodimer of chain 1 and chain 2.1 Publication

Protein-protein interaction databases

MINTiMINT-88091.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 336Combined sources
Helixi36 – 383Combined sources
Beta strandi39 – 479Combined sources
Beta strandi53 – 586Combined sources
Beta strandi60 – 7011Combined sources
Beta strandi72 – 754Combined sources
Turni77 – 793Combined sources
Beta strandi84 – 9411Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi121 – 1266Combined sources
Turni127 – 1304Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi139 – 1457Combined sources
Helixi148 – 1503Combined sources
Turni151 – 1533Combined sources
Beta strandi156 – 1638Combined sources
Turni164 – 1674Combined sources
Beta strandi168 – 1747Combined sources
Turni176 – 1783Combined sources
Beta strandi181 – 1877Combined sources
Helixi193 – 1953Combined sources
Beta strandi196 – 20611Combined sources
Helixi209 – 2113Combined sources
Beta strandi215 – 22612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DHKX-ray1.85B24-246[»]
1VIWX-ray3.00B24-228[»]
ProteinModelPortaliP02873.
SMRiP02873. Positions 24-228.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02873.

Family & Domainsi

Sequence similaritiesi

Belongs to the leguminous lectin family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02873-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIMASSKLLS LALFLALLSH ANSATETSFI IDAFNKTNLI LQGDATVSSN
60 70 80 90 100
GNLQLSYNSY DSMSRAFYSA PIQIRDSTTG NVASFDTNFT MNIRTHRQAN
110 120 130 140 150
SAVGLDFVLV PVQPESKGDT VTVEFDTFLS RISIDVNNND IKSVPWDVHD
160 170 180 190 200
YDGQNAEVRI TYNSSTKVFS VSLSNPSTGK SNNVSTTVEL EKEVYDWVSV
210 220 230 240
GFSATSGAYQ WSYETHDVLS WSFSSKFINL KDQKSERSNI VLNKIL
Length:246
Mass (Da):27,207
Last modified:July 20, 1986 - v1
Checksum:iEA56F15EF1F78788
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301I → N AA sequence (PubMed:7763497).Curated
Sequence conflicti73 – 731Q → R in CAD28835 (Ref. 3) Curated
Sequence conflicti142 – 1421K → E in CAD28835 (Ref. 3) Curated
Sequence conflicti196 – 1961D → N (PubMed:6897567).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01261 Genomic DNA. Translation: AAA33769.1.
AJ439614 Genomic DNA. Translation: CAD28835.1.
PIRiA03365. LNFB.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01261 Genomic DNA. Translation: AAA33769.1.
AJ439614 Genomic DNA. Translation: CAD28835.1.
PIRiA03365. LNFB.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DHKX-ray1.85B24-246[»]
1VIWX-ray3.00B24-228[»]
ProteinModelPortaliP02873.
SMRiP02873. Positions 24-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-88091.

Protein family/group databases

Allergomei2946. Pha v aAI.
8208. Pha v aAI.0101.

PTM databases

UniCarbKBiP02873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP02873.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR016363. Lectin.
IPR000985. Lectin_LegA_CS.
IPR019825. Lectin_legB_Mn/Ca_BS.
IPR001220. Legume_lectin_dom.
[Graphical view]
PfamiPF00139. Lectin_legB. 1 hit.
[Graphical view]
PIRSFiPIRSF002690. L-type_lectin_plant. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00308. LECTIN_LEGUME_ALPHA. 1 hit.
PS00307. LECTIN_LEGUME_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure of a chromosomal Phaseolus vulgaris lectin gene and its transcript."
    Hoffman L.M.
    J. Mol. Appl. Genet. 2:447-453(1983) [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(1981) [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 (FEB-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(1988) [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(1992) [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 (NOV-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(1994) [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(1998) [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(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF COMPLEX WITH PIG ALPHA-AMYLASE.

Entry informationi

Entry nameiLEA1_PHAVU
AccessioniPrimary (citable) accession number: P02873
Secondary accession number(s): Q8RVY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: July 20, 1986
Last modified: November 25, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.