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P02873

- LEA1_PHAVU

UniProt

P02873 - LEA1_PHAVU

Protein

Alpha-amylase inhibitor 1

Gene

LLP

Organism
Phaseolus vulgaris (Kidney bean) (French bean)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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: InterPro

    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...)2 Publications
    Glycosylationi88 – 881N-linked (GlcNAc...)2 Publications
    Glycosylationi163 – 1631N-linked (GlcNAc...)2 Publications

    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 – 336
    Helixi36 – 383
    Beta strandi39 – 479
    Beta strandi53 – 586
    Beta strandi60 – 7011
    Beta strandi72 – 754
    Turni77 – 793
    Beta strandi84 – 9411
    Beta strandi103 – 1119
    Beta strandi121 – 1266
    Turni127 – 1304
    Beta strandi131 – 1366
    Beta strandi139 – 1457
    Helixi148 – 1503
    Turni151 – 1533
    Beta strandi156 – 1638
    Turni164 – 1674
    Beta strandi168 – 1747
    Turni176 – 1783
    Beta strandi181 – 1877
    Helixi193 – 1953
    Beta strandi196 – 20611
    Helixi209 – 2113
    Beta strandi215 – 22612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    InterProiIPR008985. 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]
    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

    MIMASSKLLS LALFLALLSH ANSATETSFI IDAFNKTNLI LQGDATVSSN    50
    GNLQLSYNSY DSMSRAFYSA PIQIRDSTTG NVASFDTNFT MNIRTHRQAN 100
    SAVGLDFVLV PVQPESKGDT VTVEFDTFLS RISIDVNNND IKSVPWDVHD 150
    YDGQNAEVRI TYNSSTKVFS VSLSNPSTGK SNNVSTTVEL EKEVYDWVSV 200
    GFSATSGAYQ WSYETHDVLS WSFSSKFINL KDQKSERSNI VLNKIL 246
    Length:246
    Mass (Da):27,207
    Last modified:July 21, 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. 1 PublicationCurated
    Sequence conflicti142 – 1421K → E in CAD28835. 1 PublicationCurated
    Sequence conflicti196 – 1961D → N(PubMed:6897567)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01261 Genomic DNA. Translation: AAA33769.1.
    AJ439614 Genomic DNA. Translation: CAD28835.1.
    PIRiA03365. LNFB.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J01261 Genomic DNA. Translation: AAA33769.1 .
    AJ439614 Genomic DNA. Translation: CAD28835.1 .
    PIRi A03365. LNFB.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DHK X-ray 1.85 B 24-246 [» ]
    1VIW X-ray 3.00 B 24-228 [» ]
    ProteinModelPortali P02873.
    SMRi P02873. Positions 24-228.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-88091.

    Protein family/group databases

    Allergomei 2946. Pha v aAI.
    8208. Pha v aAI.0101.

    PTM databases

    UniCarbKBi P02873.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P02873.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. 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 ]
    Pfami PF00139. Lectin_legB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002690. L-type_lectin_plant. 1 hit.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS00308. LECTIN_LEGUME_ALPHA. 1 hit.
    PS00307. LECTIN_LEGUME_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiLEA1_PHAVU
    AccessioniPrimary (citable) accession number: P02873
    Secondary accession number(s): Q8RVY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 101 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