LEA1_PHAVU
ID LEA1_PHAVU Reviewed; 246 AA.
AC P02873; Q8RVY2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 134.
DE RecName: Full=Alpha-amylase inhibitor 1;
DE Short=Alpha-AI-1;
DE Short=Alpha-AI1;
DE AltName: Full=Lectin;
DE Contains:
DE RecName: Full=Alpha-amylase inhibitor 1 chain 1;
DE Contains:
DE RecName: Full=Alpha-amylase inhibitor 1 chain 2;
DE Flags: Precursor;
GN Name=LLP; Synonyms=Alpha-AI1;
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Tendergreen;
RX PubMed=6090563;
RA Hoffman L.M.;
RT "Structure of a chromosomal Phaseolus vulgaris lectin gene and its
RT transcript.";
RL J. Mol. Appl. Genet. 2:447-453(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Tendergreen;
RX PubMed=6897567; DOI=10.1093/nar/10.23.7819;
RA Hoffman L.M., Ma Y., Barker R.F.;
RT "Molecular cloning of Phaseolus vulgaris lectin mRNA and use of cDNA as a
RT probe to estimate lectin transcript levels in various tissues.";
RL Nucleic Acids Res. 10:7819-7828(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-246.
RC TISSUE=Leaf;
RA Lioi L., Galasso I., Lanave C., Sparvoli F., Bollini R.;
RT "Arcelin and other members of lectin family in wild Phaseolus vulgaris.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 24-34 AND 101-115.
RC STRAIN=cv. Greensleeves; TISSUE=Seed;
RX PubMed=2682631; DOI=10.1073/pnas.86.20.7885;
RA Moreno J., Chrispeels M.J.;
RT "A lectin gene encodes the alpha-amylase inhibitor of the common bean.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7885-7889(1989).
RN [5]
RP PROTEIN SEQUENCE OF 24-32 AND 101-109.
RC STRAIN=cv. Tebo; TISSUE=Seed;
RX PubMed=7763497; DOI=10.1271/bbb.57.297;
RA Yamaguchi H.;
RT "Isolation and characterization of the subunits of a heat-labile alpha-
RT amylase inhibitor from Phaseolus vulgaris white kidney bean.";
RL Biosci. Biotechnol. Biochem. 57:297-302(1993).
RN [6]
RP PROTEIN SEQUENCE OF 24-99 AND 101-231, FUNCTION, SUBUNIT, AND
RP GLYCOSYLATION.
RC STRAIN=cv. Magna; TISSUE=Seed;
RA Kluh I., Horn M., Voburka Z.;
RL Submitted (DEC-2003) to UniProtKB.
RN [7]
RP CHARACTERIZATION.
RX PubMed=7772866; DOI=10.1093/glycob/5.1.45;
RA Mirkov T.E., Evans S.V., Wahlstrom J., Gomez L., Young N.M.,
RA Chrispeels M.J.;
RT "Location of the active site of the bean alpha-amylase inhibitor and
RT involvement of a Trp, Arg, Tyr triad.";
RL Glycobiology 5:45-50(1995).
RN [8]
RP PROTEOLYTIC PROCESSING OF C-TERMINAL, AND GLYCOSYLATION AT ASN-35; ASN-88
RP AND ASN-163.
RX PubMed=10100643; DOI=10.1016/s0014-5793(99)00212-4;
RA Young N.M., Thibault P., Watson D.C., Chrispeels M.J.;
RT "Post-translational processing of two alpha-amylase inhibitors and an
RT arcelin from the common bean, Phaseolus vulgaris.";
RL FEBS Lett. 446:203-206(1999).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF COMPLEX WITH PIG ALPHA-AMYLASE.
RX PubMed=8994970; DOI=10.1016/s0969-2126(96)00151-7;
RA Bompard-Gilles C., Rousseau P., Rouge P., Payan F.;
RT "Substrate mimicry in the active center of a mammalian alpha-amylase:
RT structural analysis of an enzyme-inhibitor complex.";
RL Structure 4:1441-1452(1996).
CC -!- FUNCTION: Lectin and alpha-amylase inhibitor. Acts as a defensive
CC protein against insects. {ECO:0000269|Ref.6}.
CC -!- SUBUNIT: Heterodimer of chain 1 and chain 2. {ECO:0000269|Ref.6}.
CC -!- PTM: Proteolytic processing yields active form.
CC {ECO:0000269|PubMed:10100643}.
CC -!- BIOTECHNOLOGY: Sold as a diet aid under the name of 'Phaseolamin' or
CC 'Phase 2'.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; J01261; AAA33769.1; -; Genomic_DNA.
DR EMBL; AJ439614; CAD28835.1; -; Genomic_DNA.
DR PIR; A03365; LNFB.
DR PDB; 1DHK; X-ray; 1.85 A; B=24-246.
DR PDB; 1VIW; X-ray; 3.00 A; B=24-228.
DR PDBsum; 1DHK; -.
DR PDBsum; 1VIW; -.
DR AlphaFoldDB; P02873; -.
DR SMR; P02873; -.
DR MINT; P02873; -.
DR Allergome; 2946; Pha v aAI.
DR Allergome; 8208; Pha v aAI.0101.
DR GlyConnect; 26; 7 N-Linked glycans.
DR GlyConnect; 27; 8 N-Linked glycans.
DR iPTMnet; P02873; -.
DR EnsemblPlants; ESW24764; ESW24764; PHAVU_004G158100g.
DR Gramene; ESW24764; ESW24764; PHAVU_004G158100g.
DR EvolutionaryTrace; P02873; -.
DR GO; GO:0015066; F:alpha-amylase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
DR InterPro; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alpha-amylase inhibitor; Direct protein sequencing;
KW Glycoprotein; Lectin; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2682631,
FT ECO:0000269|PubMed:7763497, ECO:0000269|Ref.6"
FT CHAIN 24..100
FT /note="Alpha-amylase inhibitor 1 chain 1"
FT /id="PRO_0000017627"
FT CHAIN 101..239
FT /note="Alpha-amylase inhibitor 1 chain 2"
FT /id="PRO_0000017628"
FT PROPEP 240..246
FT /id="PRO_0000017629"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10100643"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10100643"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10100643"
FT CONFLICT 30
FT /note="I -> N (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="Q -> R (in Ref. 3; CAD28835)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="K -> E (in Ref. 3; CAD28835)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="D -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1DHK"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1DHK"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 84..94
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1DHK"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 131..136
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 139..145
FT /evidence="ECO:0007829|PDB:1DHK"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1DHK"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:1DHK"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1DHK"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:1DHK"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:1DHK"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:1DHK"
FT STRAND 215..226
FT /evidence="ECO:0007829|PDB:1DHK"
SQ SEQUENCE 246 AA; 27207 MW; EA56F15EF1F78788 CRC64;
MIMASSKLLS LALFLALLSH ANSATETSFI IDAFNKTNLI LQGDATVSSN GNLQLSYNSY
DSMSRAFYSA PIQIRDSTTG NVASFDTNFT MNIRTHRQAN SAVGLDFVLV PVQPESKGDT
VTVEFDTFLS RISIDVNNND IKSVPWDVHD YDGQNAEVRI TYNSSTKVFS VSLSNPSTGK
SNNVSTTVEL EKEVYDWVSV GFSATSGAYQ WSYETHDVLS WSFSSKFINL KDQKSERSNI
VLNKIL
